JP2002320474A - タウ蛋白質リン酸化酵素iの結晶、その3次元構造座標、及び3次元構造座標の使用 - Google Patents
タウ蛋白質リン酸化酵素iの結晶、その3次元構造座標、及び3次元構造座標の使用Info
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Abstract
(57)【要約】
【課題】 タウ蛋白質リン酸化酵素I (TPK I)の生物活
性を阻害する化合物の同定、検索、評価、又は設計等に
利用可能なTPK Iの3次元構造等の提供。 【解決手段】 本発明により、タウ蛋白質リン酸化酵素
I結晶、該結晶の調製方法、該結晶のX線回析像の測定
方法、該結晶のX線回析像より得られる3次元構造座
標、該構造座標を含むデータベース若しくは記録媒体、
該構造座標を用いるTPK拮抗薬の設計方法、該設計方法
により得られる物質のスクリーニング方法、該スクリー
ニング方法により得られる薬物分子を有する医薬組成物
の製造方法。
性を阻害する化合物の同定、検索、評価、又は設計等に
利用可能なTPK Iの3次元構造等の提供。 【解決手段】 本発明により、タウ蛋白質リン酸化酵素
I結晶、該結晶の調製方法、該結晶のX線回析像の測定
方法、該結晶のX線回析像より得られる3次元構造座
標、該構造座標を含むデータベース若しくは記録媒体、
該構造座標を用いるTPK拮抗薬の設計方法、該設計方法
により得られる物質のスクリーニング方法、該スクリー
ニング方法により得られる薬物分子を有する医薬組成物
の製造方法。
Description
【0001】
【発明の属する技術分野】本発明は、タウ蛋白質リン酸
化酵素I(以下これを「TPK I」略称することがある) の
結晶、該結晶の調製方法、該結晶のX線回析像の測定方
法、該結晶のX線回析像より得られる3次元構造座標、
該構造座標を含むデータベース若しくは記録媒体、該構
造座標を用いるTPK I拮抗薬の設計方法、該設計方法に
より得られる医薬候補分子のスクリーニング方法、該ス
クリーニング方法により得られる医薬分子を含有する医
薬組成物の製造方法に関する。
化酵素I(以下これを「TPK I」略称することがある) の
結晶、該結晶の調製方法、該結晶のX線回析像の測定方
法、該結晶のX線回析像より得られる3次元構造座標、
該構造座標を含むデータベース若しくは記録媒体、該構
造座標を用いるTPK I拮抗薬の設計方法、該設計方法に
より得られる医薬候補分子のスクリーニング方法、該ス
クリーニング方法により得られる医薬分子を含有する医
薬組成物の製造方法に関する。
【0002】
【従来の技術】アルツハイマー病は初老期 (45〜65
才) に発病する進行性の痴呆で、病理学的にはその脳内
に多数の老人斑と神経原線維変化が認められる。65才
以上の老年期に発症するいわゆる自然老化による老年痴
呆も、病理学的に何ら本質的な差は認められないので、
アルツハイマー型老年痴呆と呼ばれている。この疾患の
患者数は、高齢者人口の増加とともに増え、社会的に重
要な疾患となっている。アルツハイマー病およびアルツ
ハイマー型老年痴呆に特徴的な二つの病理変化(老人斑
と神経原線維変化)の出現量は、知能障害の程度とよく
相関することが知られている。そこで、この二つの病理
変化を生ずる不溶性の蓄積物質を分子レベルで解明し、
この疾患の病因に到達しようという研究が1980年代の前
半頃から行われてきた。この病理変化の一つである神経
原線維変化は、神経細胞内にPHF (paired helical fila
ment) と呼ばれる二重らせん状の繊維状物質が蓄積して
くるものである。その構成成分として、脳に特異的な微
小管結合蛋白質の一種であるタウ蛋白質とユビキチンが
同定された (井原ら (1986) J. Biochem., 99, 1807-18
10 及び Grundke-Iqbalら (1986) Proc. Natl. Acad. S
ci. USA, 83, 4913-4917)。
才) に発病する進行性の痴呆で、病理学的にはその脳内
に多数の老人斑と神経原線維変化が認められる。65才
以上の老年期に発症するいわゆる自然老化による老年痴
呆も、病理学的に何ら本質的な差は認められないので、
アルツハイマー型老年痴呆と呼ばれている。この疾患の
患者数は、高齢者人口の増加とともに増え、社会的に重
要な疾患となっている。アルツハイマー病およびアルツ
ハイマー型老年痴呆に特徴的な二つの病理変化(老人斑
と神経原線維変化)の出現量は、知能障害の程度とよく
相関することが知られている。そこで、この二つの病理
変化を生ずる不溶性の蓄積物質を分子レベルで解明し、
この疾患の病因に到達しようという研究が1980年代の前
半頃から行われてきた。この病理変化の一つである神経
原線維変化は、神経細胞内にPHF (paired helical fila
ment) と呼ばれる二重らせん状の繊維状物質が蓄積して
くるものである。その構成成分として、脳に特異的な微
小管結合蛋白質の一種であるタウ蛋白質とユビキチンが
同定された (井原ら (1986) J. Biochem., 99, 1807-18
10 及び Grundke-Iqbalら (1986) Proc. Natl. Acad. S
ci. USA, 83, 4913-4917)。
【0003】このうちタウ蛋白質は、神経細胞内軸索を
安定化してい微小管の形成を推進することが知られてい
る。さらに、PHF 中に組み込まれたタウ蛋白質は、通常
のタウ蛋白質より強くリン酸化されていることが、PHF
に対するポリクローナル抗体(抗 ptau 抗体:井原ら (1
986) J. Biochem., 99, 1807-1810) や、タウ蛋白質に対
するモノクローナル抗体 (tau-1 抗体:Grundke-Iqbal
ら (1986) Proc. Natl.Acad. Sci. USA, 83, 4913-491
7) を用いて証明された。つまり、異常にリン酸化され
たタウ蛋白質は微小管形成能が低下しているため、微小
管が崩壊し、細胞内軸索輸送に障害が生じ神経細胞死、
痴呆に至ると考えられている。この異常なリン酸化を触
媒する酵素は、内田らにより単離され、タウ蛋白質リン
酸化酵素Iと命名されている (内田ら (1992) 生化学、
第 64 巻、第 5 号、308頁)。遺伝子の解析により、TPK
Iは420個のアミノ酸残基からなる蛋白質であることが
示されている (石黒ら (1993) FEBS Lett. 325, 167-17
2 及び特開平6−253835号公報)。
安定化してい微小管の形成を推進することが知られてい
る。さらに、PHF 中に組み込まれたタウ蛋白質は、通常
のタウ蛋白質より強くリン酸化されていることが、PHF
に対するポリクローナル抗体(抗 ptau 抗体:井原ら (1
986) J. Biochem., 99, 1807-1810) や、タウ蛋白質に対
するモノクローナル抗体 (tau-1 抗体:Grundke-Iqbal
ら (1986) Proc. Natl.Acad. Sci. USA, 83, 4913-491
7) を用いて証明された。つまり、異常にリン酸化され
たタウ蛋白質は微小管形成能が低下しているため、微小
管が崩壊し、細胞内軸索輸送に障害が生じ神経細胞死、
痴呆に至ると考えられている。この異常なリン酸化を触
媒する酵素は、内田らにより単離され、タウ蛋白質リン
酸化酵素Iと命名されている (内田ら (1992) 生化学、
第 64 巻、第 5 号、308頁)。遺伝子の解析により、TPK
Iは420個のアミノ酸残基からなる蛋白質であることが
示されている (石黒ら (1993) FEBS Lett. 325, 167-17
2 及び特開平6−253835号公報)。
【0004】アルツハイマー病を予防または治療する薬
物として、TPK Iの生物活性を阻害する化合物 (拮抗
薬)は有用である。拮抗薬を同定、検索、評価又は設計
するためには、TPK Iの3次元構造座標が必要である。
蛋白質の3次元構造座標を得るには、高純度に精製され
た蛋白質分子を結晶化し、その結晶に単色化されたX線
をあて、得られたX線の回折像をもとに、該蛋白質の3
次元構造を明らかにする必要がある。TPK Iは、一般的
に動物組織からの抽出や遺伝子組換え技術によりバキュ
ロウイルスを用いて生産されており、市場において科学
実験に用いる試薬としても市販されている。しかし、そ
の製造量は少なくX線結晶解析を行うことは不可能であ
り、TPK Iの正確な3次元構造座標は知られていなかっ
た。
物として、TPK Iの生物活性を阻害する化合物 (拮抗
薬)は有用である。拮抗薬を同定、検索、評価又は設計
するためには、TPK Iの3次元構造座標が必要である。
蛋白質の3次元構造座標を得るには、高純度に精製され
た蛋白質分子を結晶化し、その結晶に単色化されたX線
をあて、得られたX線の回折像をもとに、該蛋白質の3
次元構造を明らかにする必要がある。TPK Iは、一般的
に動物組織からの抽出や遺伝子組換え技術によりバキュ
ロウイルスを用いて生産されており、市場において科学
実験に用いる試薬としても市販されている。しかし、そ
の製造量は少なくX線結晶解析を行うことは不可能であ
り、TPK Iの正確な3次元構造座標は知られていなかっ
た。
【0005】
【発明が解決しようとする課題】上記の通り、TPK I単
独もしくはTPK IとATP 類似化合物との複合体そのもの
の3次元構造座標は知られておらず、従って、TPK IとA
TP類似化合物の化学的相互作用の詳細について、3次元
空間における論理的な理解は得られていなかった。すな
わち、他のリン酸化酵素における既知の3次元構造座標
に基づいて TPK Iの3次元構造座標が推定されたとして
も、TPK IとATPとの化学的相互作用の実態の正確な把握
には至らず、3次元空間での TPK IとATPとの化学的相
互作用を考慮に入れた拮抗薬の同定、検索、評価又は設
計はできていなかった。
独もしくはTPK IとATP 類似化合物との複合体そのもの
の3次元構造座標は知られておらず、従って、TPK IとA
TP類似化合物の化学的相互作用の詳細について、3次元
空間における論理的な理解は得られていなかった。すな
わち、他のリン酸化酵素における既知の3次元構造座標
に基づいて TPK Iの3次元構造座標が推定されたとして
も、TPK IとATPとの化学的相互作用の実態の正確な把握
には至らず、3次元空間での TPK IとATPとの化学的相
互作用を考慮に入れた拮抗薬の同定、検索、評価又は設
計はできていなかった。
【0006】本発明は、TPK I拮抗薬の同定、検索、評
価又は設計等に利用可能なTPK Iの3次元構造の提供等
を目的として成されたものである。
価又は設計等に利用可能なTPK Iの3次元構造の提供等
を目的として成されたものである。
【0007】
【課題を解決するための手段】本発明者らは、上記課題
を達成するためにTPK Iを高純度に大量に製造し、TPKI
と ADPとの複合体の結晶を作製し、TPK IとADP又はAMPP
NP(5’−アデニリルイミド二リン酸)複合体の3次元
構造座標を初めて明らかにした。この3次元構造座標に
よってTPK IとADP又はAMPPNPの3次元空間における化学
的な相互作用の詳細を初めて明らかになった。本発明
は、これらの知見に基づいて成し遂げられたものであ
る。即ち、本発明の要旨の第一は、(1)タウ蛋白質リ
ン酸化酵素Iの結晶に存する。この発明の好ましい態様
により、(2)タウ蛋白質リン酸化酵素Iが、タウ蛋白
質リン酸化酵素IとATP類似化合物との複合体である上記
(1)に記載の結晶、(3) ATP類似化合物が、ADP又
はAMPPNPである上記(2)に記載の結晶、(4)結晶が
斜方晶系の空間群対称 P212121 に属する上記(1)〜
(3)のいずれかに記載の結晶、(5)結晶の単位格子
が、a=83±10Å、b=86±10Å、c=178±10Åの大
きさを持つ上記(4)に記載の結晶が提供される。
を達成するためにTPK Iを高純度に大量に製造し、TPKI
と ADPとの複合体の結晶を作製し、TPK IとADP又はAMPP
NP(5’−アデニリルイミド二リン酸)複合体の3次元
構造座標を初めて明らかにした。この3次元構造座標に
よってTPK IとADP又はAMPPNPの3次元空間における化学
的な相互作用の詳細を初めて明らかになった。本発明
は、これらの知見に基づいて成し遂げられたものであ
る。即ち、本発明の要旨の第一は、(1)タウ蛋白質リ
ン酸化酵素Iの結晶に存する。この発明の好ましい態様
により、(2)タウ蛋白質リン酸化酵素Iが、タウ蛋白
質リン酸化酵素IとATP類似化合物との複合体である上記
(1)に記載の結晶、(3) ATP類似化合物が、ADP又
はAMPPNPである上記(2)に記載の結晶、(4)結晶が
斜方晶系の空間群対称 P212121 に属する上記(1)〜
(3)のいずれかに記載の結晶、(5)結晶の単位格子
が、a=83±10Å、b=86±10Å、c=178±10Åの大
きさを持つ上記(4)に記載の結晶が提供される。
【0008】また、この発明の好ましい態様により、
(6)タウ蛋白質リン酸化酵素IとATP類似化合物とが結
合して複合体を形成しており、更にその複合体が結晶学
的な非対称単位中に2分子存在している上記(2)〜
(5)のいずれかに記載の結晶、(7)タウ蛋白質リン
酸化酵素IとATP類似化合物とが、配列番号1に示すヒト
由来のタウ蛋白質リン酸化酵素Iのアミノ酸配列におい
て、Ile62、Gly65、Ser66、Phe67、Gly68、Val70、Ala8
3、Lys85、Glu97、Val110、Leu132、Asp133、Tyr134、V
al135、Glu137、Thr138、Arg141、Asp181、Lys183、Gln
185、Asn186、Leu188、Cys199、Asp200及びその近傍の
アミノ酸残基の全て又はその一部のアミノ酸残基と相互
作用して複合体を形成している上記(2)〜(6)のい
ずれかに記載の結晶が提供される。
(6)タウ蛋白質リン酸化酵素IとATP類似化合物とが結
合して複合体を形成しており、更にその複合体が結晶学
的な非対称単位中に2分子存在している上記(2)〜
(5)のいずれかに記載の結晶、(7)タウ蛋白質リン
酸化酵素IとATP類似化合物とが、配列番号1に示すヒト
由来のタウ蛋白質リン酸化酵素Iのアミノ酸配列におい
て、Ile62、Gly65、Ser66、Phe67、Gly68、Val70、Ala8
3、Lys85、Glu97、Val110、Leu132、Asp133、Tyr134、V
al135、Glu137、Thr138、Arg141、Asp181、Lys183、Gln
185、Asn186、Leu188、Cys199、Asp200及びその近傍の
アミノ酸残基の全て又はその一部のアミノ酸残基と相互
作用して複合体を形成している上記(2)〜(6)のい
ずれかに記載の結晶が提供される。
【0009】本発明の要旨の第二は、(8)精製タウ蛋
白質リン酸化酵素IとATP類似化合物とを沈殿剤の存在下
に結晶化することを特徴とするタウ蛋白質リン酸化酵素
IとATP類似化合物との複合体の結晶の作製方法に存す
る。この発明の好ましい態様により(9)沈殿剤が、ポ
リエチレングリコールである上記(8)に記載の方法が
提供される。
白質リン酸化酵素IとATP類似化合物とを沈殿剤の存在下
に結晶化することを特徴とするタウ蛋白質リン酸化酵素
IとATP類似化合物との複合体の結晶の作製方法に存す
る。この発明の好ましい態様により(9)沈殿剤が、ポ
リエチレングリコールである上記(8)に記載の方法が
提供される。
【0010】本発明の要旨の第三は、(10)上記
(8)又は(9)に記載の方法で得られた結晶を、多価
アルコールを含有する結晶化溶液中で凍結させ、凍結状
態でX線回析データを収集することを特徴とするX線回
折像の測定方法に存する。この発明の好ましい態様によ
り(11)多価アルコールが、D−ソルビトール、ショ
糖またはグリセロールである上記(10)に記載の測定
方法が提供される。
(8)又は(9)に記載の方法で得られた結晶を、多価
アルコールを含有する結晶化溶液中で凍結させ、凍結状
態でX線回析データを収集することを特徴とするX線回
折像の測定方法に存する。この発明の好ましい態様によ
り(11)多価アルコールが、D−ソルビトール、ショ
糖またはグリセロールである上記(10)に記載の測定
方法が提供される。
【0011】本発明の要旨の第四は、(12)上記
(1)〜(7)のいずれかに記載の結晶のX線回折像よ
り得られるタウ蛋白質リン酸化酵素Iの3次元構造座
標、又は、(13)上記(10)又は(11)に記載の
測定方法により得られるタウ蛋白質リン酸化酵素Iの3
次元構造座標に存する。この発明の好ましい態様によ
り、(14)3次元構造座標が、タウ蛋白質リン酸化酵
素IとATP類似化合物との複合体の構造座標である上記
(12)又は(13)に記載の3次元構造座標、(1
5)ATP類似化合物が、ADP又はAMPPNPである上記(1
4)に記載の3次元構造座標が提供される。
(1)〜(7)のいずれかに記載の結晶のX線回折像よ
り得られるタウ蛋白質リン酸化酵素Iの3次元構造座
標、又は、(13)上記(10)又は(11)に記載の
測定方法により得られるタウ蛋白質リン酸化酵素Iの3
次元構造座標に存する。この発明の好ましい態様によ
り、(14)3次元構造座標が、タウ蛋白質リン酸化酵
素IとATP類似化合物との複合体の構造座標である上記
(12)又は(13)に記載の3次元構造座標、(1
5)ATP類似化合物が、ADP又はAMPPNPである上記(1
4)に記載の3次元構造座標が提供される。
【0012】本発明の要旨の第五は、(16)表1に示
されるタウ蛋白質リン酸化酵素IとADPとの複合体の3次
元構造座標に存する。本発明の要旨の第六は、(17)
表3に示されるタウ蛋白質リン酸化酵素IとAMPPNPとの
複合体の3次元構造座標に存する。本発明の要旨の第七
は、(18)上記(16)又は(17)に記載の3次元
構造座標について、各原子の相対的な配置を変化させず
に、3次元空間内で数学的な移動操作を行った結果とし
て得られる3次元構造座標に存する。
されるタウ蛋白質リン酸化酵素IとADPとの複合体の3次
元構造座標に存する。本発明の要旨の第六は、(17)
表3に示されるタウ蛋白質リン酸化酵素IとAMPPNPとの
複合体の3次元構造座標に存する。本発明の要旨の第七
は、(18)上記(16)又は(17)に記載の3次元
構造座標について、各原子の相対的な配置を変化させず
に、3次元空間内で数学的な移動操作を行った結果とし
て得られる3次元構造座標に存する。
【0013】本発明の要旨の第八は、(19)3次元構
造が未知の蛋白質について、上記(16)または(1
7)に記載の3次元構造座標を元に、蛋白質の3次元構
造構築方法により求められたものである蛋白質の3次元
構造座標に存する。この発明の好ましい態様により、
(20)3次元構造構築方法が、分子置換法又はホモロ
ジーモデリングである上記(19)に記載の3次元構造
座標、(21)3次元構造が未知の蛋白質が、ヒト由来
タウ蛋白質リン酸化酵素I のアミノ酸配列に対して20
%以上の相同性を持つ配列を有する蛋白質である上記
(19)に記載の3次元構造座標が提供される。
造が未知の蛋白質について、上記(16)または(1
7)に記載の3次元構造座標を元に、蛋白質の3次元構
造構築方法により求められたものである蛋白質の3次元
構造座標に存する。この発明の好ましい態様により、
(20)3次元構造構築方法が、分子置換法又はホモロ
ジーモデリングである上記(19)に記載の3次元構造
座標、(21)3次元構造が未知の蛋白質が、ヒト由来
タウ蛋白質リン酸化酵素I のアミノ酸配列に対して20
%以上の相同性を持つ配列を有する蛋白質である上記
(19)に記載の3次元構造座標が提供される。
【0014】本発明の要旨の第九は、(22)上記(1
2)〜(21)のいずれかに記載の3次元構造座標の全
部又は一部を含む座標が記録されたデータベース、又
は、(23)上記(12)〜(21)のいずれかに記載
の3次元構造座標の全部又は一部が記録されたコンピュ
ータ読みとり可能な記録媒体に存する。本発明の要旨の
第十は、(24)上記(12)〜(21)のいずれかに
記載の3次元構造座標、又は上記(22)に記載のデー
タベース若しくは上記(23)に記載の記録媒体に含ま
れる構造座標と、薬物候補分子の3次元構造座標との相
互作用に基づいて、タウ蛋白質リン酸化酵素Iの拮抗薬
を同定、検索、評価または設計することを特徴とする薬
物分子の設計方法に存する。
2)〜(21)のいずれかに記載の3次元構造座標の全
部又は一部を含む座標が記録されたデータベース、又
は、(23)上記(12)〜(21)のいずれかに記載
の3次元構造座標の全部又は一部が記録されたコンピュ
ータ読みとり可能な記録媒体に存する。本発明の要旨の
第十は、(24)上記(12)〜(21)のいずれかに
記載の3次元構造座標、又は上記(22)に記載のデー
タベース若しくは上記(23)に記載の記録媒体に含ま
れる構造座標と、薬物候補分子の3次元構造座標との相
互作用に基づいて、タウ蛋白質リン酸化酵素Iの拮抗薬
を同定、検索、評価または設計することを特徴とする薬
物分子の設計方法に存する。
【0015】この発明の好ましい態様により、(25)
タウ蛋白質リン酸化酵素Iの拮抗薬の同定、検索、評価
又は設計が、配列番号1に示すヒト由来のタウ蛋白質リ
ン酸化酵素Iのアミノ酸配列において、Ile62、Gly65、S
er66、Phe67、Gly68、Val70、Ala83、Lys85、Glu97、Va
l110、Leu132、Asp133、Tyr134、Val135、Glu137、Thr1
38、Arg141、Asp181、Lys183、Gln185、Asn186、Leu18
8、Cys199、Asp200及びその近傍のアミノ酸残基の全て
又はその一部のアミノ酸残基の3次元構造座標と薬物候
補分子の3次元構造座標との相互作用に基づいて行われ
る上記(24)に記載の方法が提供される。
タウ蛋白質リン酸化酵素Iの拮抗薬の同定、検索、評価
又は設計が、配列番号1に示すヒト由来のタウ蛋白質リ
ン酸化酵素Iのアミノ酸配列において、Ile62、Gly65、S
er66、Phe67、Gly68、Val70、Ala83、Lys85、Glu97、Va
l110、Leu132、Asp133、Tyr134、Val135、Glu137、Thr1
38、Arg141、Asp181、Lys183、Gln185、Asn186、Leu18
8、Cys199、Asp200及びその近傍のアミノ酸残基の全て
又はその一部のアミノ酸残基の3次元構造座標と薬物候
補分子の3次元構造座標との相互作用に基づいて行われ
る上記(24)に記載の方法が提供される。
【0016】本発明の要旨の第十一は、(26)上記
(24)又は(25)に記載の方法により得られたタウ
蛋白質リン酸化酵素Iの拮抗薬に存する。本発明の要旨
の第十二は、(27)上記(24)又は(25)に記載
の方法により得られたタウ蛋白質リン酸化酵素Iの拮抗
薬について、所望の薬理学的又は生理学的性質を指標と
して医薬としての活性を調べ、所望の活性を有する医薬
候補分子を選択することを特徴とする医薬分子のスクリ
ーニング方法に存する。
(24)又は(25)に記載の方法により得られたタウ
蛋白質リン酸化酵素Iの拮抗薬に存する。本発明の要旨
の第十二は、(27)上記(24)又は(25)に記載
の方法により得られたタウ蛋白質リン酸化酵素Iの拮抗
薬について、所望の薬理学的又は生理学的性質を指標と
して医薬としての活性を調べ、所望の活性を有する医薬
候補分子を選択することを特徴とする医薬分子のスクリ
ーニング方法に存する。
【0017】本発明の要旨の第十三は、(28)上記
(24)又は(25)に記載の方法により得られた医薬
分子と薬学的に許容され得る担体とを配合して製剤化す
ることを特徴とする医薬組成物の製造方法に存する。
(24)又は(25)に記載の方法により得られた医薬
分子と薬学的に許容され得る担体とを配合して製剤化す
ることを特徴とする医薬組成物の製造方法に存する。
【0018】
【発明の実施の形態】以下、本発明を更に詳細に説明す
る。1.X線結晶解析と蛋白質の結晶化 蛋白質の3次元構造を明らかにする手法として、最も一
般的に行われているのは、X線結晶構造解析の手法であ
る。即ち、蛋白質を結晶化し、その結晶に単色化された
X線をあて、得られたX線の回折像をもとに、該蛋白質
の3次元構造を明らかにしていくものである (J. ドレ
ント著, 竹中ら訳 (1998) タンパク質のX線結晶解析
法, シュプリンガー・フェアラーク東京)。結晶化は、
目的の蛋白質溶液に沈殿剤を添加する、又は溶媒量を蒸
発等により減少させる等の操作によって、蛋白質が溶液
状態から非溶解状態になる場合において、ある特定の条
件において、結晶として析出する性質を利用している。
結晶化には高純度に精製された蛋白質が必要である。ま
た、結晶化する条件として、蛋白質濃度、塩濃度、pH、
添加する沈殿剤の種類及び濃度、温度などの物理的およ
び化学的な因子が関与している。更に、沈殿剤添加や溶
媒量の調整による結晶化方法として、バッチ法、透析
法、蒸気拡散法など数多くの手法が知られている(J. ド
レント著, 竹中ら訳 (1998) タンパク質のX線結晶解析
法, シュプリンガー・フェアラーク東京, 1-18)。この
ようにX線結晶解析に適した蛋白質の結晶を得るには、
それぞれの蛋白質において、高純度の蛋白質を得る方法
を確立することと、結晶化における様々な因子や結晶化
手法を最適化することが必要になる。
る。1.X線結晶解析と蛋白質の結晶化 蛋白質の3次元構造を明らかにする手法として、最も一
般的に行われているのは、X線結晶構造解析の手法であ
る。即ち、蛋白質を結晶化し、その結晶に単色化された
X線をあて、得られたX線の回折像をもとに、該蛋白質
の3次元構造を明らかにしていくものである (J. ドレ
ント著, 竹中ら訳 (1998) タンパク質のX線結晶解析
法, シュプリンガー・フェアラーク東京)。結晶化は、
目的の蛋白質溶液に沈殿剤を添加する、又は溶媒量を蒸
発等により減少させる等の操作によって、蛋白質が溶液
状態から非溶解状態になる場合において、ある特定の条
件において、結晶として析出する性質を利用している。
結晶化には高純度に精製された蛋白質が必要である。ま
た、結晶化する条件として、蛋白質濃度、塩濃度、pH、
添加する沈殿剤の種類及び濃度、温度などの物理的およ
び化学的な因子が関与している。更に、沈殿剤添加や溶
媒量の調整による結晶化方法として、バッチ法、透析
法、蒸気拡散法など数多くの手法が知られている(J. ド
レント著, 竹中ら訳 (1998) タンパク質のX線結晶解析
法, シュプリンガー・フェアラーク東京, 1-18)。この
ようにX線結晶解析に適した蛋白質の結晶を得るには、
それぞれの蛋白質において、高純度の蛋白質を得る方法
を確立することと、結晶化における様々な因子や結晶化
手法を最適化することが必要になる。
【0019】2.タウ蛋白質リン酸化酵素I(TPK I)
の発現と精製 まず、目的とするTPK Iを高純度に精製する。TPK Iとし
ては、タウ蛋白質をリン酸化し得る能力有するものであ
れば如何なる配列を有するものであっても良い。具体的
には、例えば、特開平6−253835号公報に開示さ
れているヒト由来の配列を有するものを用いるのが好ま
しい。更に、配列番号1に示すように、上記ヒト由来の
配列のC末端にアミノ酸残基8つからなるヒスチジンタ
グが結合した 428アミノ酸残基からなる融合蛋白質とし
て発現させたものを用いるのがより好ましい。融合蛋白
質の発現は、それ自体既知の方法により行うことができ
る。また、発現させた蛋白質の精製は、アフィニティー
カラム、陽イオン交換カラム及びゲル濾過カラム等のそ
れ自体既知の方法を組み合わせて行うことができる。
の発現と精製 まず、目的とするTPK Iを高純度に精製する。TPK Iとし
ては、タウ蛋白質をリン酸化し得る能力有するものであ
れば如何なる配列を有するものであっても良い。具体的
には、例えば、特開平6−253835号公報に開示さ
れているヒト由来の配列を有するものを用いるのが好ま
しい。更に、配列番号1に示すように、上記ヒト由来の
配列のC末端にアミノ酸残基8つからなるヒスチジンタ
グが結合した 428アミノ酸残基からなる融合蛋白質とし
て発現させたものを用いるのがより好ましい。融合蛋白
質の発現は、それ自体既知の方法により行うことができ
る。また、発現させた蛋白質の精製は、アフィニティー
カラム、陽イオン交換カラム及びゲル濾過カラム等のそ
れ自体既知の方法を組み合わせて行うことができる。
【0020】3.TPK I と ATP 類似化合物との複合体
の結晶 本発明のTPK Iの結晶、例えばヒト由来の TPK I とATP
類似化合物、例えばADP又はAMPPNPとの複合体の結晶
は、以下の様に調製することができる。TPK Iの結晶化
方法としては、バッチ法、透析法、蒸気拡散法などの結
晶化の手法を用いることができる。また、蛋白質濃度、
塩濃度、水素イオン濃度 (pH)、添加する沈殿剤の種
類、温度等の物理的および化学的な因子の決定が必要で
ある。例えば、TPK I とADPとの複合体の結晶化におい
ては、蒸気拡散法を用い、pH6.5、蛋白質濃度 10 mg/m
L、温度 5 ℃の条件下で沈殿剤として 8 〜 12%(w/v)の
ポリエチレングリコール6000を用いてTPK IとADPと
を共結晶させた場合に得られる。
の結晶 本発明のTPK Iの結晶、例えばヒト由来の TPK I とATP
類似化合物、例えばADP又はAMPPNPとの複合体の結晶
は、以下の様に調製することができる。TPK Iの結晶化
方法としては、バッチ法、透析法、蒸気拡散法などの結
晶化の手法を用いることができる。また、蛋白質濃度、
塩濃度、水素イオン濃度 (pH)、添加する沈殿剤の種
類、温度等の物理的および化学的な因子の決定が必要で
ある。例えば、TPK I とADPとの複合体の結晶化におい
ては、蒸気拡散法を用い、pH6.5、蛋白質濃度 10 mg/m
L、温度 5 ℃の条件下で沈殿剤として 8 〜 12%(w/v)の
ポリエチレングリコール6000を用いてTPK IとADPと
を共結晶させた場合に得られる。
【0021】ただし、同一の蛋白質が、異なる条件でも
結晶化し得ることは周知の事実であり、本発明のTPK I
の結晶は、これらの条件で調製されたものに限定される
ものではなく、実質的に本発明と同一の結晶学的定数を
与えるTPK Iの結晶、例えばTPK IとATP類似化合物の複
合体の結晶は、本発明の範囲である かくして得られるTPK Iの結晶は、TPK IとATP類似化合
物が化学量論的に等量の物質量によって結合しているも
の、即ち、1分子のTPK Iと1分子のATP類似化合物とが
結合して、1分子の複合体を形成しているものである。
ここで、本明細書において、「ATP類似化合物」とは、A
TPと共通した化学構造上の特徴を有し、その特徴的化学
構造を用いてTPK IのATP結合部位と相互作用する化合物
を意味する。更に詳述すれば、ATPのγリン酸を除く大
半の部分構造、例えば、塩基、糖、αおよびβリン酸等
が、ADP及びAMPPNPにも共通して存在している。さら
に、後述する結晶構造解析から、ADPおよびAMPPNPの共
通部分構造は、TPK Iの同一部分に同様の相互作用によ
って結合していることが確認されている。従って、ADP
及びAMPPNP等は、全てATP類似化合物に含まれるもので
ある。
結晶化し得ることは周知の事実であり、本発明のTPK I
の結晶は、これらの条件で調製されたものに限定される
ものではなく、実質的に本発明と同一の結晶学的定数を
与えるTPK Iの結晶、例えばTPK IとATP類似化合物の複
合体の結晶は、本発明の範囲である かくして得られるTPK Iの結晶は、TPK IとATP類似化合
物が化学量論的に等量の物質量によって結合しているも
の、即ち、1分子のTPK Iと1分子のATP類似化合物とが
結合して、1分子の複合体を形成しているものである。
ここで、本明細書において、「ATP類似化合物」とは、A
TPと共通した化学構造上の特徴を有し、その特徴的化学
構造を用いてTPK IのATP結合部位と相互作用する化合物
を意味する。更に詳述すれば、ATPのγリン酸を除く大
半の部分構造、例えば、塩基、糖、αおよびβリン酸等
が、ADP及びAMPPNPにも共通して存在している。さら
に、後述する結晶構造解析から、ADPおよびAMPPNPの共
通部分構造は、TPK Iの同一部分に同様の相互作用によ
って結合していることが確認されている。従って、ADP
及びAMPPNP等は、全てATP類似化合物に含まれるもので
ある。
【0022】4.TPK I と ADP の複合体の3次元構造
座標 このようにして得られたTPK Iの結晶、例えばTPK IとAD
Pとの複合体結晶の構造を、X線による結晶構造解析技
術を用いて解析することにより、TPK Iの3次元構造座
標が得られる。例えば、ヒト由来 TPK IとADPとの複合
体の結晶は斜方晶系の空間群 P212121に属するもので、
単位格子としてa軸83±10Å、b軸86±10Å、c軸178
±10Åの大きさを有する。更に、この複合体の結晶を用
いたX線回折による結晶構造解析の手法により、本発明
のTPK IとADPとの複合体の3次元構造座標を得ることが
できる。ここで、蛋白質の3次元構造座標とは、蛋白質
を構成する各原子の空間的な位置関係を示す値であっ
て、三次元空間上で立体構造を記述するものである。各
原子の座標とは、空間上のある点を原点とする互いに垂
直な三方向の相対的な距離であり、タンパク質中に存在
する水素原子を除く原子一つあたりに3個の数字からな
るベクトル量である。
座標 このようにして得られたTPK Iの結晶、例えばTPK IとAD
Pとの複合体結晶の構造を、X線による結晶構造解析技
術を用いて解析することにより、TPK Iの3次元構造座
標が得られる。例えば、ヒト由来 TPK IとADPとの複合
体の結晶は斜方晶系の空間群 P212121に属するもので、
単位格子としてa軸83±10Å、b軸86±10Å、c軸178
±10Åの大きさを有する。更に、この複合体の結晶を用
いたX線回折による結晶構造解析の手法により、本発明
のTPK IとADPとの複合体の3次元構造座標を得ることが
できる。ここで、蛋白質の3次元構造座標とは、蛋白質
を構成する各原子の空間的な位置関係を示す値であっ
て、三次元空間上で立体構造を記述するものである。各
原子の座標とは、空間上のある点を原点とする互いに垂
直な三方向の相対的な距離であり、タンパク質中に存在
する水素原子を除く原子一つあたりに3個の数字からな
るベクトル量である。
【0023】得られたTPK IとADPとの構造座標を後記表
1に示す。表1は、一般的に用いられている蛋白質の3
次元構造座標の表記法であるプロテイン・データ・バン
クの形式に従って記述したものである。表1の1行目以
降、最終行を除いて、各原子の3次元座標を記述してい
る。1列目の ATOM はこの行が原子座標の行であること
を示し、2列目はその原子の順番を、3列目はアミノ酸
残基における原子の区別を、4列目はアミノ酸残基を、
5列目は分子の種類を (同一の種類は一本のポリペプチ
ド鎖であることを示す)、6列目は配列番号1に対応し
たアミノ酸の番号を、7、8、9列目はその原子の座標
(a軸、b軸、c軸方向の順番でÅ単位) を、10列目
は、その原子の占有率 (本発明においてはすべて1.00)
を、11列目はその原子の温度因子を示している。最終
行は、この表の終わりの行であることを示している。
1に示す。表1は、一般的に用いられている蛋白質の3
次元構造座標の表記法であるプロテイン・データ・バン
クの形式に従って記述したものである。表1の1行目以
降、最終行を除いて、各原子の3次元座標を記述してい
る。1列目の ATOM はこの行が原子座標の行であること
を示し、2列目はその原子の順番を、3列目はアミノ酸
残基における原子の区別を、4列目はアミノ酸残基を、
5列目は分子の種類を (同一の種類は一本のポリペプチ
ド鎖であることを示す)、6列目は配列番号1に対応し
たアミノ酸の番号を、7、8、9列目はその原子の座標
(a軸、b軸、c軸方向の順番でÅ単位) を、10列目
は、その原子の占有率 (本発明においてはすべて1.00)
を、11列目はその原子の温度因子を示している。最終
行は、この表の終わりの行であることを示している。
【0024】TPK IとADPとの複合体の結晶から得られた
構造座標を元に、蛋白質の構造を理解するのに一般的に
用いられている表記方法であるリボンモデルで TPK Iの
主鎖を、ボール&スティクモデルでADP分子を表記し
た。その中に結晶学的対称性を持たない最小単位、すな
わち非対称単位内にあるTPK IとADPを図1に、TPK IとA
DPとの複合体を図2に示す。これらの図から理解される
ように、TPK IとADPとの複合体結晶は、非対称単位中に
複合体を2分子、分子A及び分子Bを含んでいる。これ
らの2分子の複合体は、巨視的にみて、非結晶学的な疑
似2回対称軸によって関係づけられる。
構造座標を元に、蛋白質の構造を理解するのに一般的に
用いられている表記方法であるリボンモデルで TPK Iの
主鎖を、ボール&スティクモデルでADP分子を表記し
た。その中に結晶学的対称性を持たない最小単位、すな
わち非対称単位内にあるTPK IとADPを図1に、TPK IとA
DPとの複合体を図2に示す。これらの図から理解される
ように、TPK IとADPとの複合体結晶は、非対称単位中に
複合体を2分子、分子A及び分子Bを含んでいる。これ
らの2分子の複合体は、巨視的にみて、非結晶学的な疑
似2回対称軸によって関係づけられる。
【0025】即ち、分子A及び分子Bは、アミノ酸配列
が同じであり、化学的・生化学的に全く同等のものであ
る。ところが、TPK Iの結晶中では、分子充填の結果と
して隣り合う分子との接触様式が異なる2つの部位・状
態が生じ、結晶中に存在するTPK I分子の半数が部位・
状態Aに、残りの半数が部位・状態Bに存在している。
これを通常「結晶学的に独立な分子Aと分子B」と呼ん
でいる。両者は結晶中での環境の違いを受け、分子の3
次元構造上にも若干の変化がみらる。しかし、この相違
はあくまで結晶内での部位・状態を反映したものであ
り、結晶を溶解して溶液状態にすると両者の区別は全く
つかなくなる。こうした現象および表現方法は、蛋白質
結晶のみならず小分子の分子性結晶でも極めて一般的な
ものである。
が同じであり、化学的・生化学的に全く同等のものであ
る。ところが、TPK Iの結晶中では、分子充填の結果と
して隣り合う分子との接触様式が異なる2つの部位・状
態が生じ、結晶中に存在するTPK I分子の半数が部位・
状態Aに、残りの半数が部位・状態Bに存在している。
これを通常「結晶学的に独立な分子Aと分子B」と呼ん
でいる。両者は結晶中での環境の違いを受け、分子の3
次元構造上にも若干の変化がみらる。しかし、この相違
はあくまで結晶内での部位・状態を反映したものであ
り、結晶を溶解して溶液状態にすると両者の区別は全く
つかなくなる。こうした現象および表現方法は、蛋白質
結晶のみならず小分子の分子性結晶でも極めて一般的な
ものである。
【0026】なお、上記TPK Iの3次元構造座標におい
て、TPK Iの分子AにおけるMet1からGly34までのアミノ
酸残基とSer389 からHis428までのアミノ酸残基、及び
分子Bにおける Met1からAla22までのアミノ酸残基とAl
a387から His428までのアミノ酸残基は、結晶中におい
てもその位置が一定しておらず、X線結晶構造解析にお
いて考慮から除外している。上記した本発明の結晶構造
座標と実質的に一致するものは本発明の範囲である。こ
こで、「実質的に一致する」とは、該構造の主要部分、
具体的にはαヘリックスやβシート構造といった2次構
造を形成している部分や、温度因子が他の部分に比べ低
い値となっている部分において、対応する部分の主鎖ま
たはCα炭素の部分の2乗平均平方根誤差がおよそ2Å
以下である構造を指す。また、各配列の開始部位及び終
了部位も必ずしも厳密に規定されたものでなく、N末端
及び/又はC末端部分に別の蛋白質が結合しているも
の、N末端及び/又はC末端に1個又は複数個のアミノ
酸残基が付加したものなど、TPK Iの活性について実質
的な変化をもたらさないものについても本発明に包含さ
れる。
て、TPK Iの分子AにおけるMet1からGly34までのアミノ
酸残基とSer389 からHis428までのアミノ酸残基、及び
分子Bにおける Met1からAla22までのアミノ酸残基とAl
a387から His428までのアミノ酸残基は、結晶中におい
てもその位置が一定しておらず、X線結晶構造解析にお
いて考慮から除外している。上記した本発明の結晶構造
座標と実質的に一致するものは本発明の範囲である。こ
こで、「実質的に一致する」とは、該構造の主要部分、
具体的にはαヘリックスやβシート構造といった2次構
造を形成している部分や、温度因子が他の部分に比べ低
い値となっている部分において、対応する部分の主鎖ま
たはCα炭素の部分の2乗平均平方根誤差がおよそ2Å
以下である構造を指す。また、各配列の開始部位及び終
了部位も必ずしも厳密に規定されたものでなく、N末端
及び/又はC末端部分に別の蛋白質が結合しているも
の、N末端及び/又はC末端に1個又は複数個のアミノ
酸残基が付加したものなど、TPK Iの活性について実質
的な変化をもたらさないものについても本発明に包含さ
れる。
【0027】本発明により提供される表1に示した構造
座標から、TPK IとADPとの相互作用を特徴づけるアミノ
酸残基を特定することができる。分子Aについて、各残
基間の原子間距離が、ファンデルワールス相互作用して
いる原子として4.0Å以下のものを、静電的な相互作用
をしている原子として3.4Åより大きく5.0Å以下のもの
を、水素結合として3.4Å以下のものを、後記表2に示
す。なお、マグネシウムイオンを介した結合と、水分子
を介した水素結合も示す。表2中、1列目はTPK Iのア
ミノ酸残基(1文字表記)とその番号を、2列目はその
アミノ酸残基の原子を、3列目はADPの原子を、4列目は
それらの原子間距離をÅ単位で、5列目は相互作用の様
式を記述している。なお、相互作用の様式(5列目)
中、VDWはファンデルワールス相互作用を、ESIは静電的
な相互作用を、HYBは水素結合を示している。更に、水
分子の1分子若しくは2分子を介した水素結合に関して
は、原子間距離が2つ又は3つの値になるので、4列目
を更に2つ又は3つに分けてそれぞれの値を示してあ
り、6又は7列目に WMH と記載し、7列目又は8、9
列目に関与している水分子の番号を示してある。また、
マグネシウムイオンを介した結合も同様に、4列目を更
に2つに分けてそれぞれの原子間距離を示してあり、6
列目にMMBと記載し、7列目に関与しているマグネシウ
ムイオンの番号を示してある。更に、マグネシウムイオ
ンと水分子を介した結合についても、4列目を更に3つ
に分けてそれぞれの原子間距離を示してあり、7列目に
MWMBと記載し、8、9列目に関与しているマグネシウム
イオンと水分子の番号を示してある。
座標から、TPK IとADPとの相互作用を特徴づけるアミノ
酸残基を特定することができる。分子Aについて、各残
基間の原子間距離が、ファンデルワールス相互作用して
いる原子として4.0Å以下のものを、静電的な相互作用
をしている原子として3.4Åより大きく5.0Å以下のもの
を、水素結合として3.4Å以下のものを、後記表2に示
す。なお、マグネシウムイオンを介した結合と、水分子
を介した水素結合も示す。表2中、1列目はTPK Iのア
ミノ酸残基(1文字表記)とその番号を、2列目はその
アミノ酸残基の原子を、3列目はADPの原子を、4列目は
それらの原子間距離をÅ単位で、5列目は相互作用の様
式を記述している。なお、相互作用の様式(5列目)
中、VDWはファンデルワールス相互作用を、ESIは静電的
な相互作用を、HYBは水素結合を示している。更に、水
分子の1分子若しくは2分子を介した水素結合に関して
は、原子間距離が2つ又は3つの値になるので、4列目
を更に2つ又は3つに分けてそれぞれの値を示してあ
り、6又は7列目に WMH と記載し、7列目又は8、9
列目に関与している水分子の番号を示してある。また、
マグネシウムイオンを介した結合も同様に、4列目を更
に2つに分けてそれぞれの原子間距離を示してあり、6
列目にMMBと記載し、7列目に関与しているマグネシウ
ムイオンの番号を示してある。更に、マグネシウムイオ
ンと水分子を介した結合についても、4列目を更に3つ
に分けてそれぞれの原子間距離を示してあり、7列目に
MWMBと記載し、8、9列目に関与しているマグネシウム
イオンと水分子の番号を示してある。
【0028】図2に示されているように、TPK Iの結晶
は、2つのドメインから成る。各ドメインの間隙に ADP
があり、ドメインの間隙にある各々のドメイン内のアミ
ノ酸残基がADP を認識している。この認識を特徴づけて
いる TPK Iのアミノ酸残基は、Ile62、Gly65、Ser66、P
he67、Gly68、Val70、Ala83、Lys85、Glu97、Val110、L
eu132、Asp133、Tyr134、Val135、Glu137、Thr138、Arg
141、Asp181、Lys183、Gln185、Asn186、Leu188、Cys19
9、Asp200(表2)であり、これらのアミノ酸残基の空
間的配置をボール&スティクモデルで図3に示した。す
なわち、TPK IとADPの認識(即ち、複合体の形成)は、
これらのアミノ酸残基、及びその近傍のアミノ酸残基の
相互作用で特徴づけられる。なお、後記表1及び表3に
示した構造座標は、結晶内における単位格子の原点を3
次元空間における原点として表記している。本発明の構
造座標をコンピューターによる計算に用いる場合などに
おいて、各原子の相対的な配置を変化させずに、3次元
空間内で並進、回転、対称などの数学的な移動操作を施
した結果として得られる新たな構造座標も本発明の3次
元構造座標の範囲である。
は、2つのドメインから成る。各ドメインの間隙に ADP
があり、ドメインの間隙にある各々のドメイン内のアミ
ノ酸残基がADP を認識している。この認識を特徴づけて
いる TPK Iのアミノ酸残基は、Ile62、Gly65、Ser66、P
he67、Gly68、Val70、Ala83、Lys85、Glu97、Val110、L
eu132、Asp133、Tyr134、Val135、Glu137、Thr138、Arg
141、Asp181、Lys183、Gln185、Asn186、Leu188、Cys19
9、Asp200(表2)であり、これらのアミノ酸残基の空
間的配置をボール&スティクモデルで図3に示した。す
なわち、TPK IとADPの認識(即ち、複合体の形成)は、
これらのアミノ酸残基、及びその近傍のアミノ酸残基の
相互作用で特徴づけられる。なお、後記表1及び表3に
示した構造座標は、結晶内における単位格子の原点を3
次元空間における原点として表記している。本発明の構
造座標をコンピューターによる計算に用いる場合などに
おいて、各原子の相対的な配置を変化させずに、3次元
空間内で並進、回転、対称などの数学的な移動操作を施
した結果として得られる新たな構造座標も本発明の3次
元構造座標の範囲である。
【0029】5.分子置換法によりX線結晶構造解析を
行うための構造座標の使用 本発明のTPK IとADPとの複合体の3次元構造座標、例え
ば後記表1に示す構造座標は、TPK I と有意な相同性を
持つアミノ酸配列を持つ他の蛋白質から得られた結晶な
どのX線結晶構造解析に用いることができる。すなわ
ち、X線結晶構造解析の手法の一つとして一般的に用い
られている分子置換法 (例えば、J. ドレント著, 竹中
ら訳 (1998) タンパク質のX線結晶解析法, シュプリン
ガー・フェアラーク東京, 204-224) において、本発明
のTPK IとADP との複合体の3次元構造座標の全て又は
その一部を使用することで、構造座標が未知の上記蛋白
質の結晶においても、その構造座標を決定する際に、重
原子同型置換法を用いることなく、はるかに迅速にその
結晶のX線回折像より得られる構造因子からその構造座
標を決定しうる。
行うための構造座標の使用 本発明のTPK IとADPとの複合体の3次元構造座標、例え
ば後記表1に示す構造座標は、TPK I と有意な相同性を
持つアミノ酸配列を持つ他の蛋白質から得られた結晶な
どのX線結晶構造解析に用いることができる。すなわ
ち、X線結晶構造解析の手法の一つとして一般的に用い
られている分子置換法 (例えば、J. ドレント著, 竹中
ら訳 (1998) タンパク質のX線結晶解析法, シュプリン
ガー・フェアラーク東京, 204-224) において、本発明
のTPK IとADP との複合体の3次元構造座標の全て又は
その一部を使用することで、構造座標が未知の上記蛋白
質の結晶においても、その構造座標を決定する際に、重
原子同型置換法を用いることなく、はるかに迅速にその
結晶のX線回折像より得られる構造因子からその構造座
標を決定しうる。
【0030】分子置換法を行う際には、分子置換法に用
いるプログラムが動作するように調整されているコンピ
ューターを用いる。該プログラムは、例えばX-PLOR (モ
レキュラーシミュレーション社) や AMORE (CCP4 (Coll
aborative Computational Project, Number 4 (1994) A
cta Cryst. D50, 670-673) のプログラム群の1つ)など
があるが、その他のプログラムを用いても良い。ここ
で、X-PLORは分子置換法、構造精密化等の計算を行うX
線およびNMRによる蛋白質3次元構造解析用統合ソフ
トであり、その詳細はBrunger, A. T. (1992) X-PLOR V
ersion 3.1; ASystem for X-ray Crystallography and
NMR, Yale University Press, New Haven, CT.に記載さ
れている。また、CCP4は、分子置換法、同型置換法、構
造精密化等の計算を行う蛋白質X線結晶構造解析用プロ
グラム群であり、その詳細はThe CCP4 Suit: Programs
for Protein Crystallography (1994) Acta Cryst. D5
0, 760-763.に記載されている。本発明の TPK IとADPと
の複合体の3次元構造座標を用いて分子置換法を適用す
べき結晶としては、TPK Iと有意な相同性を持つアミノ
酸配列を持つ他の蛋白質から得られた結晶や、TPK Iと
結合し得る化合物、例えば AMPPNP やTPK I拮抗薬のリ
ード化合物等のATP類似化合物と TPK I との複合体から
得られた結晶が挙げられる。ここで、有意な相同性と
は、一般に、アミノ酸配列において 20%以上、好ましく
は 30%以上一致している場合をさす。アミノ酸配列の相
同性が20%未満になると導き出された3次元構造座標の
信頼性は低下する。逆にアミノ酸配列の相同性がより高
いほど、容易に目的の3次元構造座標を導き出すことが
できる。ヒトは哺乳類に含まれるために、哺乳類由来の
TPK Iのアミノ酸配列は、ヒト由来のものとそれぞれア
ミノ酸配列の相同性が高いと予想される。従って、哺乳
類由来のそれらについては、正確なアミノ酸配列が決定
されれば、本発明の構造座標を用いて容易に3次元構造
座標を導き出すことができる。
いるプログラムが動作するように調整されているコンピ
ューターを用いる。該プログラムは、例えばX-PLOR (モ
レキュラーシミュレーション社) や AMORE (CCP4 (Coll
aborative Computational Project, Number 4 (1994) A
cta Cryst. D50, 670-673) のプログラム群の1つ)など
があるが、その他のプログラムを用いても良い。ここ
で、X-PLORは分子置換法、構造精密化等の計算を行うX
線およびNMRによる蛋白質3次元構造解析用統合ソフ
トであり、その詳細はBrunger, A. T. (1992) X-PLOR V
ersion 3.1; ASystem for X-ray Crystallography and
NMR, Yale University Press, New Haven, CT.に記載さ
れている。また、CCP4は、分子置換法、同型置換法、構
造精密化等の計算を行う蛋白質X線結晶構造解析用プロ
グラム群であり、その詳細はThe CCP4 Suit: Programs
for Protein Crystallography (1994) Acta Cryst. D5
0, 760-763.に記載されている。本発明の TPK IとADPと
の複合体の3次元構造座標を用いて分子置換法を適用す
べき結晶としては、TPK Iと有意な相同性を持つアミノ
酸配列を持つ他の蛋白質から得られた結晶や、TPK Iと
結合し得る化合物、例えば AMPPNP やTPK I拮抗薬のリ
ード化合物等のATP類似化合物と TPK I との複合体から
得られた結晶が挙げられる。ここで、有意な相同性と
は、一般に、アミノ酸配列において 20%以上、好ましく
は 30%以上一致している場合をさす。アミノ酸配列の相
同性が20%未満になると導き出された3次元構造座標の
信頼性は低下する。逆にアミノ酸配列の相同性がより高
いほど、容易に目的の3次元構造座標を導き出すことが
できる。ヒトは哺乳類に含まれるために、哺乳類由来の
TPK Iのアミノ酸配列は、ヒト由来のものとそれぞれア
ミノ酸配列の相同性が高いと予想される。従って、哺乳
類由来のそれらについては、正確なアミノ酸配列が決定
されれば、本発明の構造座標を用いて容易に3次元構造
座標を導き出すことができる。
【0031】分子置換法の適用については、実際に目的
の結晶のX線回折像から計算された構造因子に分子置換
法を適用し、有意な解が得られることにより判断されう
る。ここで、構造因子(F)とは、電子密度(ρ)をフ
ーリエ変換して得られる物理量であり、構造因子をフー
リエ変換すれば電子密度が得らる。構造因子は複素数
で、F=|F|exp(iφ)の形で表現される。ここで|F|
は振幅、φは位相を示し、|F|は回折X線の強度の平
方根に比例する。φはX線回折実験により直接測定でき
ず、「結晶構造解析」とは、このφを決定することと等
価である。本発明のTPK IとADP の複合体の3次元構造
座標を用いて、分子置換法により TPK IとATP 類似化合
物の1つであるAMPPNPとの複合体の構造座標が、迅速に
決定された。得られた構造座標を、一般的に用いられて
いる蛋白質の3次元構造座標の表記方法に従って示した
ものを後記表3に示す。なお、表3の原子座標の記述様
式は表1と同様である。上記分子置換法により、AMPPNP
以外のATP類似化合物とTPK Iとの複合体の結晶において
も、TPK IとADPとの複合体の3次元構造座標の全部又は
一部を用いて構造解析することができる。この方法によ
り有意な解が得られる構造座標も本発明の範囲である。
の結晶のX線回折像から計算された構造因子に分子置換
法を適用し、有意な解が得られることにより判断されう
る。ここで、構造因子(F)とは、電子密度(ρ)をフ
ーリエ変換して得られる物理量であり、構造因子をフー
リエ変換すれば電子密度が得らる。構造因子は複素数
で、F=|F|exp(iφ)の形で表現される。ここで|F|
は振幅、φは位相を示し、|F|は回折X線の強度の平
方根に比例する。φはX線回折実験により直接測定でき
ず、「結晶構造解析」とは、このφを決定することと等
価である。本発明のTPK IとADP の複合体の3次元構造
座標を用いて、分子置換法により TPK IとATP 類似化合
物の1つであるAMPPNPとの複合体の構造座標が、迅速に
決定された。得られた構造座標を、一般的に用いられて
いる蛋白質の3次元構造座標の表記方法に従って示した
ものを後記表3に示す。なお、表3の原子座標の記述様
式は表1と同様である。上記分子置換法により、AMPPNP
以外のATP類似化合物とTPK Iとの複合体の結晶において
も、TPK IとADPとの複合体の3次元構造座標の全部又は
一部を用いて構造解析することができる。この方法によ
り有意な解が得られる構造座標も本発明の範囲である。
【0032】また、前記したATP 類似化合物とは、表2
及び図3に示した TPK IとADPとの認識を特徴づけるの
アミノ酸残基 Ile62、Gly65、Ser66、Phe67、Gly68、Va
l70、Ala83、Lys85、Glu97、Val110、Leu132、Asp133、
Tyr134、Val135、Glu137、Thr138、Arg141、Asp181、Ly
s183、Gln185、Asn186、Leu188、Cys199、Asp200及びそ
の近傍のアミノ酸残基の全て又は一部からなるATP結合
部位に結合し得る化合物をも意味する。
及び図3に示した TPK IとADPとの認識を特徴づけるの
アミノ酸残基 Ile62、Gly65、Ser66、Phe67、Gly68、Va
l70、Ala83、Lys85、Glu97、Val110、Leu132、Asp133、
Tyr134、Val135、Glu137、Thr138、Arg141、Asp181、Ly
s183、Gln185、Asn186、Leu188、Cys199、Asp200及びそ
の近傍のアミノ酸残基の全て又は一部からなるATP結合
部位に結合し得る化合物をも意味する。
【0033】6.ホモロジーモデリングによる3次元構
造座標の解析 かくして得られる本発明のTPK Iの3次元構造座標、例
えばヒト由来TPK Iの3次元構造座標を用いて、異種の
TPK Iあるいはアミノ酸配列が有意に相同である他の蛋
白質の3次元構造座標をホモロジーモデリング (中村春
木、中井謙太 (1995) バイオテクノロジーのためのコン
ピューター入門、コロナ社、186-204) により推定する
ことができる。ホモロジーモデリングを行う際には、ホ
モロジーモデリングに用いるプログラムが動作するよう
に調整されているコンピューターを用いる。該プログラ
ムは、例えばHOMOLOGYやMODELER (モレキュラーシミュ
レーション社) や SWISS-MODEL(Peitsch (1996) Bioche
m. Soc. Trans. 24, 274-279)などがあるが、その他の
プログラムを用いても良い。
造座標の解析 かくして得られる本発明のTPK Iの3次元構造座標、例
えばヒト由来TPK Iの3次元構造座標を用いて、異種の
TPK Iあるいはアミノ酸配列が有意に相同である他の蛋
白質の3次元構造座標をホモロジーモデリング (中村春
木、中井謙太 (1995) バイオテクノロジーのためのコン
ピューター入門、コロナ社、186-204) により推定する
ことができる。ホモロジーモデリングを行う際には、ホ
モロジーモデリングに用いるプログラムが動作するよう
に調整されているコンピューターを用いる。該プログラ
ムは、例えばHOMOLOGYやMODELER (モレキュラーシミュ
レーション社) や SWISS-MODEL(Peitsch (1996) Bioche
m. Soc. Trans. 24, 274-279)などがあるが、その他の
プログラムを用いても良い。
【0034】まず、例えばヒト由来TPK Iの構造座標を
用いる場合、この座標において、ヒトと哺乳類のTPK I
でアミノ酸残基で一致していない部分の側鎖部分を、哺
乳類の該アミノ酸残基の側鎖に置き換える。この段階
で、立体化学的に各原子が重ならず、エネルギーが最小
になるような側鎖のコンフォーメーションを選択する。
更に、全アミノ酸残基に対して主鎖部分も含めたコンフ
ォーメーションの計算を行い、全体のエネルギーが最小
になるようにする。本発明の TPK IとADPとの複合体の
3次元構造座標を用いてホモロジーモデルを適用すべき
蛋白質としては、他種のTPK Iや、TPK Iと有意な相同性
を持つアミノ酸配列を持つ他の蛋白質、あるいはTPK I
と結合する化合物、例えば AMPPNPやTPK I拮抗薬のリー
ド化合物等のATP 類似化合物と有意に相同な蛋白質との
複合体が挙げられる。
用いる場合、この座標において、ヒトと哺乳類のTPK I
でアミノ酸残基で一致していない部分の側鎖部分を、哺
乳類の該アミノ酸残基の側鎖に置き換える。この段階
で、立体化学的に各原子が重ならず、エネルギーが最小
になるような側鎖のコンフォーメーションを選択する。
更に、全アミノ酸残基に対して主鎖部分も含めたコンフ
ォーメーションの計算を行い、全体のエネルギーが最小
になるようにする。本発明の TPK IとADPとの複合体の
3次元構造座標を用いてホモロジーモデルを適用すべき
蛋白質としては、他種のTPK Iや、TPK Iと有意な相同性
を持つアミノ酸配列を持つ他の蛋白質、あるいはTPK I
と結合する化合物、例えば AMPPNPやTPK I拮抗薬のリー
ド化合物等のATP 類似化合物と有意に相同な蛋白質との
複合体が挙げられる。
【0035】ここで、有意な相同性とは、前記の通り、
一般にアミノ酸配列において 20%以上、好ましくは 30%
以上一致している場合をさす。アミノ酸配列の相同性
が20% 未満になると導き出された3次元構造座標の信頼
性は低下する。逆にアミノ酸配列の相同性がより高いほ
ど、容易に目的の3次元構造座標を導き出すことができ
る。ヒトは哺乳類に含まれるために、哺乳類由来のTPK
I のアミノ酸配列は、ヒト由来のものとそれぞれアミノ
酸配列の相同性が高いと予想される。従って、哺乳類由
来のそれらについては、正確なアミノ酸配列が決定され
れば、本発明による構造座標を用いて容易に3次元構造
座標を導き出すことができる。また、ATP 類似化合物と
は、前記の通りである。上記方法により得られる相同な
蛋白質の推定3次元構造座標も本発明の範囲である。
一般にアミノ酸配列において 20%以上、好ましくは 30%
以上一致している場合をさす。アミノ酸配列の相同性
が20% 未満になると導き出された3次元構造座標の信頼
性は低下する。逆にアミノ酸配列の相同性がより高いほ
ど、容易に目的の3次元構造座標を導き出すことができ
る。ヒトは哺乳類に含まれるために、哺乳類由来のTPK
I のアミノ酸配列は、ヒト由来のものとそれぞれアミノ
酸配列の相同性が高いと予想される。従って、哺乳類由
来のそれらについては、正確なアミノ酸配列が決定され
れば、本発明による構造座標を用いて容易に3次元構造
座標を導き出すことができる。また、ATP 類似化合物と
は、前記の通りである。上記方法により得られる相同な
蛋白質の推定3次元構造座標も本発明の範囲である。
【0036】7.TPK Iの3次元構造座標が記録された
データベース又は記録媒体 かくして得られたTPK Iの3次元構造座標を、コンピュ
ーターが利用可能な所定の形式で適当な記録媒体に格納
することによりTPK Iの3次元構造座標データベース又
は記録媒体が構築できる。本発明においてデータベース
とは、上記構造座標を適当な記録媒体に書き込み、所定
のプログラムに従って検索を行うコンピューターシステ
ムをも意味する。ここで適当な記録媒体としては、例え
ば、フロッピー(登録商標)ディスク、ハードディス
ク、磁気テープ等の磁気媒体;CD-ROM、MO、CD-R、CD-R
W等の光ディスク、半導体メモリ等を挙げることができ
る。
データベース又は記録媒体 かくして得られたTPK Iの3次元構造座標を、コンピュ
ーターが利用可能な所定の形式で適当な記録媒体に格納
することによりTPK Iの3次元構造座標データベース又
は記録媒体が構築できる。本発明においてデータベース
とは、上記構造座標を適当な記録媒体に書き込み、所定
のプログラムに従って検索を行うコンピューターシステ
ムをも意味する。ここで適当な記録媒体としては、例え
ば、フロッピー(登録商標)ディスク、ハードディス
ク、磁気テープ等の磁気媒体;CD-ROM、MO、CD-R、CD-R
W等の光ディスク、半導体メモリ等を挙げることができ
る。
【0037】8.TPK I拮抗薬の分子設計方法 薬物分子設計を行うことができる適当なプログラムが動
作するコンピューターで、得られたTPK Iの構造座標の
全て又は一部、又はそれらが記録されたデータベース若
しくは記録媒体の構造座標を使用して、TPK Iに拮抗す
る薬物分子を同定、検索、評価又は設計する等のTPK I
拮抗薬の分子設計を行うことができる。TPK I拮抗薬の
同定、検索、評価又は設計は、本発明のTPK Iの3次元
構造座標と薬物分子の3次元構造座標との相互作用の有
無やその程度に基づいて行われる。薬物分子との相互作
用の有無やその程度の検討は、例えば配列番号1に示す
ヒト由来TPK Iのアミノ酸配列において、Ile62、Gly6
5、Ser66、Phe67、Gly68、Val70、Ala83、Lys85、Glu9
7、Val110、Leu132、Asp133、Tyr134、Val135、Glu13
7、Thr138、Arg141、Asp181、Lys183、Gln185、Asn18
6、Leu188、Cys199、Asp200及びその近傍のアミノ酸残
基の全て又はその一部のアミノ酸残基の3次元構造座標
を対象として行うのが好ましい。
作するコンピューターで、得られたTPK Iの構造座標の
全て又は一部、又はそれらが記録されたデータベース若
しくは記録媒体の構造座標を使用して、TPK Iに拮抗す
る薬物分子を同定、検索、評価又は設計する等のTPK I
拮抗薬の分子設計を行うことができる。TPK I拮抗薬の
同定、検索、評価又は設計は、本発明のTPK Iの3次元
構造座標と薬物分子の3次元構造座標との相互作用の有
無やその程度に基づいて行われる。薬物分子との相互作
用の有無やその程度の検討は、例えば配列番号1に示す
ヒト由来TPK Iのアミノ酸配列において、Ile62、Gly6
5、Ser66、Phe67、Gly68、Val70、Ala83、Lys85、Glu9
7、Val110、Leu132、Asp133、Tyr134、Val135、Glu13
7、Thr138、Arg141、Asp181、Lys183、Gln185、Asn18
6、Leu188、Cys199、Asp200及びその近傍のアミノ酸残
基の全て又はその一部のアミノ酸残基の3次元構造座標
を対象として行うのが好ましい。
【0038】TPK Iの3次元構造座標と薬物候補分子の
3次元構造座標との相互作に基づいてTPK I拮抗薬の設
計を行う際に用いられるコンピューターとしては、適当
なプログラムが動作するように調整されているコンピュ
ーターであれば特に制限はない。また、コンピューター
の記憶媒体にも特に制限はない。分子設計に用いるプロ
グラムは、例えばモレキュラーシミュレーション社製の
コンピューター・プログラムInsight II等を挙げること
ができる。特に、この目的のために特別に作成されたLu
diやDOCKといったプログラムを単独又は組み合わせて用
いることで、より容易に同定、検索、評価又は設計する
ことができる。また、TPK Iの3次元構造座標と薬物分
子とのドッキング評価は、例えば、NEC社製のBIOCES
(バージョン3.10)を用いて行うことができる。
3次元構造座標との相互作に基づいてTPK I拮抗薬の設
計を行う際に用いられるコンピューターとしては、適当
なプログラムが動作するように調整されているコンピュ
ーターであれば特に制限はない。また、コンピューター
の記憶媒体にも特に制限はない。分子設計に用いるプロ
グラムは、例えばモレキュラーシミュレーション社製の
コンピューター・プログラムInsight II等を挙げること
ができる。特に、この目的のために特別に作成されたLu
diやDOCKといったプログラムを単独又は組み合わせて用
いることで、より容易に同定、検索、評価又は設計する
ことができる。また、TPK Iの3次元構造座標と薬物分
子とのドッキング評価は、例えば、NEC社製のBIOCES
(バージョン3.10)を用いて行うことができる。
【0039】ここで、薬物分子は、既知のものであって
も、新たに合成された新規な化学構造を有する薬物分子
であっても、その三次元構造が得られるものであれば、
いずれの薬物分子も本発明の方法で用いることができ
る。薬物分子の3次元構造座標は、X線結晶解析やモデ
リング等のいずれの方法で得られたものでも良い。3次
元構造座標が決定されているものは、適当なデータベー
ス、例えばCCDC(Cambridge Crystallographic Data Ce
ntre: http://www.ccdc.cam.ac.uk/)やPDB (Protein
Data Bank: http://www.rcsb.org/pdb/)から収得する
ことができる。
も、新たに合成された新規な化学構造を有する薬物分子
であっても、その三次元構造が得られるものであれば、
いずれの薬物分子も本発明の方法で用いることができ
る。薬物分子の3次元構造座標は、X線結晶解析やモデ
リング等のいずれの方法で得られたものでも良い。3次
元構造座標が決定されているものは、適当なデータベー
ス、例えばCCDC(Cambridge Crystallographic Data Ce
ntre: http://www.ccdc.cam.ac.uk/)やPDB (Protein
Data Bank: http://www.rcsb.org/pdb/)から収得する
ことができる。
【0040】更には、特開2000−178209号公
報に記載されている方法によっても、新規なTPK I拮抗
薬を設計することができる。この様に、本発明のTPK I
の3次元構造座標を用いることで、初めてTPK I拮抗薬
のコンピューターによる分子設計が可能となる。ただ
し、本発明の分子設計方法は、これらのプログラムや手
法を用いるものに限定されるものではない。TPK I拮抗
薬の分子設計には、通常、概念的に2つの段階がある。
最初の段階は、リード化合物を見つけだすものであり、
次の段階はリード化合物の最適化である。どちらの段階
も、TPK Iの構造座標を使用して、それ自体既知の方法
により行うことができ、それによりTPK I拮抗薬として
最適な医薬候補分子とすることができる。
報に記載されている方法によっても、新規なTPK I拮抗
薬を設計することができる。この様に、本発明のTPK I
の3次元構造座標を用いることで、初めてTPK I拮抗薬
のコンピューターによる分子設計が可能となる。ただ
し、本発明の分子設計方法は、これらのプログラムや手
法を用いるものに限定されるものではない。TPK I拮抗
薬の分子設計には、通常、概念的に2つの段階がある。
最初の段階は、リード化合物を見つけだすものであり、
次の段階はリード化合物の最適化である。どちらの段階
も、TPK Iの構造座標を使用して、それ自体既知の方法
により行うことができ、それによりTPK I拮抗薬として
最適な医薬候補分子とすることができる。
【0041】9.薬物分子の設計方法により得られるTP
K I拮抗薬及びスクリーニング方法 上記方法により同定、検索、評価又は設計された医薬候
補分子は、その分子の性質に応じて、例えばそれ自体既
知の化学合成法により得ることができる。しかしなが
ら、薬物分子は、天然化合物、合成化合物のいずれでも
良く、また、高分子化合物、低分子化合物のいずれでも
良い。得られた医薬候補分子は、更に、それ自体既知の
方法により、試験管内や生体内における薬理学的または
生理学的試験によりその活性を調べ、所望の活性を有す
る医薬候補分子を選抜することにより実際に医薬として
応用可能なものを得ることができる。かくして得られる
医薬分子は、タウ蛋白質のリン酸化を阻害する作用を有
しており、アルツハイマー病などの中枢神経疾患の優れ
た予防又は治療薬として期待される。
K I拮抗薬及びスクリーニング方法 上記方法により同定、検索、評価又は設計された医薬候
補分子は、その分子の性質に応じて、例えばそれ自体既
知の化学合成法により得ることができる。しかしなが
ら、薬物分子は、天然化合物、合成化合物のいずれでも
良く、また、高分子化合物、低分子化合物のいずれでも
良い。得られた医薬候補分子は、更に、それ自体既知の
方法により、試験管内や生体内における薬理学的または
生理学的試験によりその活性を調べ、所望の活性を有す
る医薬候補分子を選抜することにより実際に医薬として
応用可能なものを得ることができる。かくして得られる
医薬分子は、タウ蛋白質のリン酸化を阻害する作用を有
しており、アルツハイマー病などの中枢神経疾患の優れ
た予防又は治療薬として期待される。
【0042】10.医薬組成物の製造方法 上記スクリーニング方法により選択された薬物分子は、
それ自体単独で前記の疾患等の患者に投与することがで
きるが、これらの有効成分の1種又は2種以上を混合し
て投与することもできる。また、薬理学的に許容される
製剤用添加物等を用いて該物質を医薬品組成物として製
剤化し、これを投与するのが好ましい。例えば、必要に
応じて糖衣を施した錠剤、カプセル剤、顆粒剤、細粒
剤、散剤、丸剤、マイクロカプセル剤、リポソーム製
剤、トローチ、舌下剤、液剤、エリキシル剤、乳剤、懸
濁剤等として経口的に、あるいは無菌の水性液もしくは
油性液として製造した注射剤や、座剤、軟膏、貼付剤等
として非経口的に使用できる。これらは、例えば、該物
質を生理学的に認められる担体、香味剤、賦形剤、ベヒ
クル、防腐剤、安定剤、結合剤などとともに一般に認め
られた製剤実施に要求される単位用量形態で混和し、充
填又は打錠等の当業界で周知の方法を用いて製造するこ
とができる。これらの医薬組成物における有効成分量は
指示された範囲の適当な容量が得られるようにするもの
である。
それ自体単独で前記の疾患等の患者に投与することがで
きるが、これらの有効成分の1種又は2種以上を混合し
て投与することもできる。また、薬理学的に許容される
製剤用添加物等を用いて該物質を医薬品組成物として製
剤化し、これを投与するのが好ましい。例えば、必要に
応じて糖衣を施した錠剤、カプセル剤、顆粒剤、細粒
剤、散剤、丸剤、マイクロカプセル剤、リポソーム製
剤、トローチ、舌下剤、液剤、エリキシル剤、乳剤、懸
濁剤等として経口的に、あるいは無菌の水性液もしくは
油性液として製造した注射剤や、座剤、軟膏、貼付剤等
として非経口的に使用できる。これらは、例えば、該物
質を生理学的に認められる担体、香味剤、賦形剤、ベヒ
クル、防腐剤、安定剤、結合剤などとともに一般に認め
られた製剤実施に要求される単位用量形態で混和し、充
填又は打錠等の当業界で周知の方法を用いて製造するこ
とができる。これらの医薬組成物における有効成分量は
指示された範囲の適当な容量が得られるようにするもの
である。
【0043】例えば、錠剤、カプセル剤等に混和するこ
とができる添加剤としては、ゼラチン、コーンスター
チ、トラガント、アラビアゴム等の結合剤、結晶性セル
ロース等の賦形剤、セルロース、マンニトール、又はラ
クトース等の充填剤、コーンスターチ、ゼラチン、アル
ギン酸等の膨化剤、澱粉、ポリビニルポリピロリドン、
澱粉誘導体、又はナトリウム澱粉グリコラート等の崩壊
剤、ステアリン酸マグネシウム等の滑沢剤、ラウリル硫
酸ナトリウム等の湿潤剤、ショ糖、乳糖又はサッカリン
等の甘味剤、ペパーミント、アカモノ油又はチェリー等
の香味剤等が用いられる。また、錠剤は必要に応じて腸
溶性コーティング剤等を用いてコーティングを施すこと
もできる。カプセルについては、前記の添加剤にさらに
油脂のような液状担体を含有することができる。
とができる添加剤としては、ゼラチン、コーンスター
チ、トラガント、アラビアゴム等の結合剤、結晶性セル
ロース等の賦形剤、セルロース、マンニトール、又はラ
クトース等の充填剤、コーンスターチ、ゼラチン、アル
ギン酸等の膨化剤、澱粉、ポリビニルポリピロリドン、
澱粉誘導体、又はナトリウム澱粉グリコラート等の崩壊
剤、ステアリン酸マグネシウム等の滑沢剤、ラウリル硫
酸ナトリウム等の湿潤剤、ショ糖、乳糖又はサッカリン
等の甘味剤、ペパーミント、アカモノ油又はチェリー等
の香味剤等が用いられる。また、錠剤は必要に応じて腸
溶性コーティング剤等を用いてコーティングを施すこと
もできる。カプセルについては、前記の添加剤にさらに
油脂のような液状担体を含有することができる。
【0044】また例えば、注射剤として用いる無菌医薬
組成物は、注射用水のようなベヒクル中の活性物質、胡
麻油、椰子油等の天然産出植物油等を溶解又は懸濁させ
るなどの通常の製剤実施に従って処方することができ
る。注射用の水性液としては、例えば、生理食塩水、ブ
ドウ糖やその他の補助薬を含む等張液(D−ソルビトー
ル、D−マンニトール、塩化ナトリウム等)等が用いら
れ、適当な溶解補助剤、例えば、アルコール(エタノー
ル等)、ポリアルコール(プロピレングリコール、ポリ
エチレングリコール等)、非イオン性界面活性剤(ポリ
ソルベート80TM、HCO−50等)等と併用するこ
とができる。油性液としては、例えば、ゴマ油、大豆油
等が用いられ、溶解補助剤である安息香酸ベンジル、ベ
ンジルアルコール等と併用することができる。また、上
記の医薬組成物には、例えば、緩衝剤(リン酸塩緩衝
液、酢酸ナトリウム緩衝液等)、無痛化剤(塩化ベンザ
ルコニウム、塩酸プロカイン等)、安定剤(ヒト血清ア
ルブミン、ポリエチレングリコール等)、保存剤(ベン
ジルアルコール、フェノール等)、及び酸化防止剤等を
配合してもよい。かくして調製される注射用の水性液
は、通常、医薬分子を上記のような媒体に溶解させて濾
過滅菌してから、適当な滅菌済みバイアル又はアンプル
に充填して製造される。安定性を高めるために、該医薬
組成物を凍結させた後にバイアル中の水を真空下で除去
してもよい。油性液についても水性液の場合と実質的に
同様に製造できるが、医薬分子を上記媒体に懸濁させた
後にエチレンオキシド等により滅菌することによって好
適に製造できる。
組成物は、注射用水のようなベヒクル中の活性物質、胡
麻油、椰子油等の天然産出植物油等を溶解又は懸濁させ
るなどの通常の製剤実施に従って処方することができ
る。注射用の水性液としては、例えば、生理食塩水、ブ
ドウ糖やその他の補助薬を含む等張液(D−ソルビトー
ル、D−マンニトール、塩化ナトリウム等)等が用いら
れ、適当な溶解補助剤、例えば、アルコール(エタノー
ル等)、ポリアルコール(プロピレングリコール、ポリ
エチレングリコール等)、非イオン性界面活性剤(ポリ
ソルベート80TM、HCO−50等)等と併用するこ
とができる。油性液としては、例えば、ゴマ油、大豆油
等が用いられ、溶解補助剤である安息香酸ベンジル、ベ
ンジルアルコール等と併用することができる。また、上
記の医薬組成物には、例えば、緩衝剤(リン酸塩緩衝
液、酢酸ナトリウム緩衝液等)、無痛化剤(塩化ベンザ
ルコニウム、塩酸プロカイン等)、安定剤(ヒト血清ア
ルブミン、ポリエチレングリコール等)、保存剤(ベン
ジルアルコール、フェノール等)、及び酸化防止剤等を
配合してもよい。かくして調製される注射用の水性液
は、通常、医薬分子を上記のような媒体に溶解させて濾
過滅菌してから、適当な滅菌済みバイアル又はアンプル
に充填して製造される。安定性を高めるために、該医薬
組成物を凍結させた後にバイアル中の水を真空下で除去
してもよい。油性液についても水性液の場合と実質的に
同様に製造できるが、医薬分子を上記媒体に懸濁させた
後にエチレンオキシド等により滅菌することによって好
適に製造できる。
【0045】かくして得られる医薬組成物は安全で低毒
性であるので、前記の疾患等の予防又は治療薬として投
与することができる。該組成物に含まれる前記薬物分子
の投与量は、対象疾患、症状、対象臓器、投与対象、投
与方法等により適宜決定して用いることができる。ま
た、一日の投与量を一〜数回に分けて投与するのが望ま
しい。
性であるので、前記の疾患等の予防又は治療薬として投
与することができる。該組成物に含まれる前記薬物分子
の投与量は、対象疾患、症状、対象臓器、投与対象、投
与方法等により適宜決定して用いることができる。ま
た、一日の投与量を一〜数回に分けて投与するのが望ま
しい。
【0046】
【実施例】以下、実施例を挙げて本発明を更に詳細に説
明するが、本発明は、何らこれに限定されるものではな
い。実施例1 ヒト由来TPK Iの調製 特開平6−253835号公報に記載の方法により調製
したヒト由来 TPK IのcDNAを、C末端にヒスチジンタグ
が結合した融合蛋白質として発現ベクター pET-24a (ノ
バゲン社) に組み込んだ。発現ベクターを電子穿孔法に
より形質転換させた宿主大腸菌 BL21(DE3) を、7 L の
2xYTA とカナマイシン 100 μg/ml及びクロラムフェニ
コール 35 μg/mlを含む培地で、ジャーファーメンター
を用いて、400 rpm で撹拌、5 L/minで通気しつつ 25
℃で培養した。その後、終濃度1.0 mM となるようにイ
ソプロピル-β-D-チオガラクトピラノシド (IPTG) を添
加して、TPK Iの発現を誘導した。更に、25 ℃、5 時間
培養を行い、その培養液を遠心沈降して集菌した。
明するが、本発明は、何らこれに限定されるものではな
い。実施例1 ヒト由来TPK Iの調製 特開平6−253835号公報に記載の方法により調製
したヒト由来 TPK IのcDNAを、C末端にヒスチジンタグ
が結合した融合蛋白質として発現ベクター pET-24a (ノ
バゲン社) に組み込んだ。発現ベクターを電子穿孔法に
より形質転換させた宿主大腸菌 BL21(DE3) を、7 L の
2xYTA とカナマイシン 100 μg/ml及びクロラムフェニ
コール 35 μg/mlを含む培地で、ジャーファーメンター
を用いて、400 rpm で撹拌、5 L/minで通気しつつ 25
℃で培養した。その後、終濃度1.0 mM となるようにイ
ソプロピル-β-D-チオガラクトピラノシド (IPTG) を添
加して、TPK Iの発現を誘導した。更に、25 ℃、5 時間
培養を行い、その培養液を遠心沈降して集菌した。
【0047】菌体をアフィニティーカラム平衡化バッフ
ァー (50 mM Tris-HCl, 200 mM NaCl, 5%(v/v) glycero
l, 5 mM MgCl2, 2.5 mM 2-mercaptoethanol, pH 8.0)
で懸濁し、超音波によって菌体を破砕後、遠心分離によ
って菌体中に可溶性蛋白質として存在している TPK I
を含有する上清を得た。得られた上清を平衡化バッファ
ーで平衡化されたアフィニティーカラムに添加し、TPK
I をカラムに特異的に吸着させた。カラムを、平衡化バ
ッファーによる洗浄を行った後に、200 mM イミダゾー
ルを含む平衡化バッファーのリニアーグラジエントによ
って、カラムに吸着されている TPK I を溶出させた。
溶出された TPK I を含む画分を、陽イオン交換カラム
平衡化バッファー (50 mM MES-NaOH, 100 mM NaCl, 5%
(v/v) glycerol, 5 mM MgCl2, 10 mM DTT, pH 6.0) で
透析してから、平衡化された陽イオン交換カラムに吸着
させた。カラムを、平衡化バッファーによる洗浄を行っ
た後に、1000 mM NaClを含む平衡化バッファーのリニア
ーグラジエントによって、カラムに吸着されている TPK
I を溶出させた。TPK I を含む画分を限外濾過膜で濃
縮してから、50 mM MES-NaOH, 175 mM NaCl, 5%(v/v) g
lycerol, 7 mM MgCl2, 10 mM DTT, pH 6.5で平衡化され
たゲル濾過カラムに添加した。ゲル濾過クロマトグラフ
ィーにより精製された画分を、結晶調製用とした。得ら
れたTPK Iの純度検定は、SDS-PAGE(SDS-ポリアクリル
アミドゲル電気泳動)及び逆相クロマトグラフィーによ
り行った。TPK Iの純度は95%以上、その比活性は、牛
脳やウサギ骨格筋より精製されたTPK Iと同程度であっ
た。また、TPKIの収量は約0.5mgであった。
ァー (50 mM Tris-HCl, 200 mM NaCl, 5%(v/v) glycero
l, 5 mM MgCl2, 2.5 mM 2-mercaptoethanol, pH 8.0)
で懸濁し、超音波によって菌体を破砕後、遠心分離によ
って菌体中に可溶性蛋白質として存在している TPK I
を含有する上清を得た。得られた上清を平衡化バッファ
ーで平衡化されたアフィニティーカラムに添加し、TPK
I をカラムに特異的に吸着させた。カラムを、平衡化バ
ッファーによる洗浄を行った後に、200 mM イミダゾー
ルを含む平衡化バッファーのリニアーグラジエントによ
って、カラムに吸着されている TPK I を溶出させた。
溶出された TPK I を含む画分を、陽イオン交換カラム
平衡化バッファー (50 mM MES-NaOH, 100 mM NaCl, 5%
(v/v) glycerol, 5 mM MgCl2, 10 mM DTT, pH 6.0) で
透析してから、平衡化された陽イオン交換カラムに吸着
させた。カラムを、平衡化バッファーによる洗浄を行っ
た後に、1000 mM NaClを含む平衡化バッファーのリニア
ーグラジエントによって、カラムに吸着されている TPK
I を溶出させた。TPK I を含む画分を限外濾過膜で濃
縮してから、50 mM MES-NaOH, 175 mM NaCl, 5%(v/v) g
lycerol, 7 mM MgCl2, 10 mM DTT, pH 6.5で平衡化され
たゲル濾過カラムに添加した。ゲル濾過クロマトグラフ
ィーにより精製された画分を、結晶調製用とした。得ら
れたTPK Iの純度検定は、SDS-PAGE(SDS-ポリアクリル
アミドゲル電気泳動)及び逆相クロマトグラフィーによ
り行った。TPK Iの純度は95%以上、その比活性は、牛
脳やウサギ骨格筋より精製されたTPK Iと同程度であっ
た。また、TPKIの収量は約0.5mgであった。
【0048】実施例2 TPK IとADPとの複合体結晶の調
製 TPK IとADPとの複合体結晶は、TPK IとADPをハンギング
ドロップ蒸気拡散法により共結晶させて得た。実施例1
で高純度に精製された TPK I を限外濾過膜で蛋白質濃
度を 15 〜 20 mg/mL に調製した。この蛋白質溶液 1.0
μL に、結晶化溶液として 8 〜 12%(w/v) のポリエチ
レングリコール6000と 4 mM ADPを含む pH 6.5 の
0.1 M MES 緩衝溶液を等量加え混合し、表面を疎水的に
なるようにシリコン処理剤により処理したカバーガラス
板上においた。この試料をおいたガラス板を、0.5 mL
の結晶化溶液を入れた気密性のある貯蔵容器に入れ、5
℃で静置した。およそ3〜7日間の静置の後に、試料溶
液中に、大きさが 400μm×200μm×100μm 程度の大き
さの柱状結晶が得られた。
製 TPK IとADPとの複合体結晶は、TPK IとADPをハンギング
ドロップ蒸気拡散法により共結晶させて得た。実施例1
で高純度に精製された TPK I を限外濾過膜で蛋白質濃
度を 15 〜 20 mg/mL に調製した。この蛋白質溶液 1.0
μL に、結晶化溶液として 8 〜 12%(w/v) のポリエチ
レングリコール6000と 4 mM ADPを含む pH 6.5 の
0.1 M MES 緩衝溶液を等量加え混合し、表面を疎水的に
なるようにシリコン処理剤により処理したカバーガラス
板上においた。この試料をおいたガラス板を、0.5 mL
の結晶化溶液を入れた気密性のある貯蔵容器に入れ、5
℃で静置した。およそ3〜7日間の静置の後に、試料溶
液中に、大きさが 400μm×200μm×100μm 程度の大き
さの柱状結晶が得られた。
【0049】実施例3 TPK IとADPとの複合体の結晶構
造解析 実施例2で得られた結晶 (母結晶) を、30% のD−ソル
ビトールを不凍剤として加えた結晶化溶液に浸し、続い
て 100 Kの窒素気流下に入れ、急速凍結した。理化学研
究所播磨 SPring-8の放射光を用いて、100 K窒素気流中
でX線回折データを振動法を用いて収集した。また、1
mMのチオサリチル酸エチル水銀 (EMTS)を含む結晶化溶
液に 1 時間浸漬し、水銀原子を結晶中に含む重原子同
型置換体結晶を得た。その結晶を 30% のD−ソルビト
ールを加えた結晶化溶液中に浸し、続いて 100 K の窒
素気流下に入れ、急速凍結した。100 K 窒素気流中でX
線回折データを振動写真法を用いて収集した。得られた
各々の回折像から、回折強度処理プログラムMOSFLM(Le
slie, A. G. W. (1992) MOSFLM. Daresbury Laborator
y, Warrington, Vol.26.)を用いて回折強度を数値化
し、結晶構造因子を求めた。結晶は、斜方晶系の空間群
対称 P212121 に属し、結晶の格子定数はa=83±10
Å、b=86±10Å、c=178±10Åであった。
造解析 実施例2で得られた結晶 (母結晶) を、30% のD−ソル
ビトールを不凍剤として加えた結晶化溶液に浸し、続い
て 100 Kの窒素気流下に入れ、急速凍結した。理化学研
究所播磨 SPring-8の放射光を用いて、100 K窒素気流中
でX線回折データを振動法を用いて収集した。また、1
mMのチオサリチル酸エチル水銀 (EMTS)を含む結晶化溶
液に 1 時間浸漬し、水銀原子を結晶中に含む重原子同
型置換体結晶を得た。その結晶を 30% のD−ソルビト
ールを加えた結晶化溶液中に浸し、続いて 100 K の窒
素気流下に入れ、急速凍結した。100 K 窒素気流中でX
線回折データを振動写真法を用いて収集した。得られた
各々の回折像から、回折強度処理プログラムMOSFLM(Le
slie, A. G. W. (1992) MOSFLM. Daresbury Laborator
y, Warrington, Vol.26.)を用いて回折強度を数値化
し、結晶構造因子を求めた。結晶は、斜方晶系の空間群
対称 P212121 に属し、結晶の格子定数はa=83±10
Å、b=86±10Å、c=178±10Åであった。
【0050】次に、CCP4 という一連のプログラム群を
用いて、以下の解析を行った。先ず、水銀の同型置換体
結晶と母結晶から得られた各回折点の強度差を用いて、
フーリエ変換の計算を行い、得られた差パターソン図か
ら、これを満足する実空間の水銀原子の単位格子内での
位置を決定した。得られた水銀原子の位置座標から計算
される母結晶の結晶構造因子の位相を用いて、実空間に
おける TPK IとADPとの複合体の結晶の電子密度図を得
た。更に、溶媒領域の電子密度の平滑化、ならびに、非
結晶学的対称性を用いた電子密度の平均化の計算を行
い、分子モデルの構築・修正を行う3次元分子グラフィ
ックスプログラム O(Jones, T. A.ら (1991) Acta Cry
st. A47, 110-119.)を用いて電子密度図上に、TPK Iと
ADPの複合体のアミノ酸残基及び ADP に相当する部位を
同定した。TPK IとADPの複合体は、非対称単位中に2分
子の複合体を含むことが示された。
用いて、以下の解析を行った。先ず、水銀の同型置換体
結晶と母結晶から得られた各回折点の強度差を用いて、
フーリエ変換の計算を行い、得られた差パターソン図か
ら、これを満足する実空間の水銀原子の単位格子内での
位置を決定した。得られた水銀原子の位置座標から計算
される母結晶の結晶構造因子の位相を用いて、実空間に
おける TPK IとADPとの複合体の結晶の電子密度図を得
た。更に、溶媒領域の電子密度の平滑化、ならびに、非
結晶学的対称性を用いた電子密度の平均化の計算を行
い、分子モデルの構築・修正を行う3次元分子グラフィ
ックスプログラム O(Jones, T. A.ら (1991) Acta Cry
st. A47, 110-119.)を用いて電子密度図上に、TPK Iと
ADPの複合体のアミノ酸残基及び ADP に相当する部位を
同定した。TPK IとADPの複合体は、非対称単位中に2分
子の複合体を含むことが示された。
【0051】実施例4 TPK IとADPとの複合体の3次元
構造座標の精密化 次に、X-PLOR (モレキュラーシミュレーション社) を用
いて、各原子位置の精密化を行い、O を用いて水分子の
同定を行った。この操作を繰り返し行い、非対称単位内
に存在する TPK I の2分子共に Ser35 から Ala388 ま
でのアミノ酸残基と各 TPK I 分子に結合した ADP 分子
及び水分子を同定した。この段階で、構造座標の正確さ
の指標とされている R 因子は15 Åから 2.1 Åのブラ
ッグ反射角を持つ回折像から得られる構造因子を用いた
場合、R = 21.8% であった。更に精密化の段階で独立に
精密化の計算に入れなかった構造因子から計算される R
因子( R-free 因子と呼ばれている因子)は R-free =
24,2% であった。更に各原子間の結合距離及び結合角
の理想状態からの2乗平均平方根誤差は、それぞれ 0.0
07 Å及び 1.17 度であった。得られた構造座標は一般
的に用いられている表記法であるプロテイン・データ・
バンクの形式に従って表1に示した。
構造座標の精密化 次に、X-PLOR (モレキュラーシミュレーション社) を用
いて、各原子位置の精密化を行い、O を用いて水分子の
同定を行った。この操作を繰り返し行い、非対称単位内
に存在する TPK I の2分子共に Ser35 から Ala388 ま
でのアミノ酸残基と各 TPK I 分子に結合した ADP 分子
及び水分子を同定した。この段階で、構造座標の正確さ
の指標とされている R 因子は15 Åから 2.1 Åのブラ
ッグ反射角を持つ回折像から得られる構造因子を用いた
場合、R = 21.8% であった。更に精密化の段階で独立に
精密化の計算に入れなかった構造因子から計算される R
因子( R-free 因子と呼ばれている因子)は R-free =
24,2% であった。更に各原子間の結合距離及び結合角
の理想状態からの2乗平均平方根誤差は、それぞれ 0.0
07 Å及び 1.17 度であった。得られた構造座標は一般
的に用いられている表記法であるプロテイン・データ・
バンクの形式に従って表1に示した。
【0052】実施例5 TPK IとADPとの複合体の構造座
標を用いた分子置換法 TPK IとAMPPNPとを実施例2と同様に共結晶させ、TPK I
とAMPPNPとの複合体結晶を得た。この結晶を30 %のD−
ソルビトールを加えた結晶化溶液に浸し、続いて100 K
の窒素気流下に入れ、急速凍結し、100 K窒素気流中で
X線回折データを振動法を用いて収集した。得られた各
々の回折像を、MOSFLMを用いて構造因子に換算した。結
晶は斜方晶系の空間群対称 P212121 に属し、結晶の単
位格子がa=83±10Å、b=86±10Å、c=178±10Å
の大きさを持つことが示された。得られた構造因子と、
表1に示した TPK IとADPの複合体の3次元構造座標と
を用いて分子置換法を行った。この分子置換法には、X-
PLORの中の剛体精密化の方法を用いた。O を用いて AMP
PNP及び水分子の同定を行った後、X-PLOR により各原子
位置を精密化した。計算には、20 Åから1.8 Åのブラ
ッグ反射角を持つ回折像から得られる構造因子を用い
た。R 因子は 21.6%、R-free 因子は 24.2%であった。
これにより、TPK I と AMPPNP の複合体の新たな3次元
構造座標が得られた。得られた構造座標は表3に示し
た。
標を用いた分子置換法 TPK IとAMPPNPとを実施例2と同様に共結晶させ、TPK I
とAMPPNPとの複合体結晶を得た。この結晶を30 %のD−
ソルビトールを加えた結晶化溶液に浸し、続いて100 K
の窒素気流下に入れ、急速凍結し、100 K窒素気流中で
X線回折データを振動法を用いて収集した。得られた各
々の回折像を、MOSFLMを用いて構造因子に換算した。結
晶は斜方晶系の空間群対称 P212121 に属し、結晶の単
位格子がa=83±10Å、b=86±10Å、c=178±10Å
の大きさを持つことが示された。得られた構造因子と、
表1に示した TPK IとADPの複合体の3次元構造座標と
を用いて分子置換法を行った。この分子置換法には、X-
PLORの中の剛体精密化の方法を用いた。O を用いて AMP
PNP及び水分子の同定を行った後、X-PLOR により各原子
位置を精密化した。計算には、20 Åから1.8 Åのブラ
ッグ反射角を持つ回折像から得られる構造因子を用い
た。R 因子は 21.6%、R-free 因子は 24.2%であった。
これにより、TPK I と AMPPNP の複合体の新たな3次元
構造座標が得られた。得られた構造座標は表3に示し
た。
【0053】
【発明の効果】本発明によって提供されるTPK Iの3次
元構造座標を元にして、TPK Iの生物活性を阻害するの
化合物の同定、検索、評価又は設計等のコンピューター
によるTPKI拮抗薬の分子設計が始めて可能となった。し
たがって、本発明は、TPK I拮抗薬等の薬物分子の設計
に極めて有用である。
元構造座標を元にして、TPK Iの生物活性を阻害するの
化合物の同定、検索、評価又は設計等のコンピューター
によるTPKI拮抗薬の分子設計が始めて可能となった。し
たがって、本発明は、TPK I拮抗薬等の薬物分子の設計
に極めて有用である。
【0054】
【表1】表1 TPK IとADPの複合体結晶から得られた3次元構造座標 CRYST 82.930 86.080 178.090 90.00 90.00 90.00 P212121 ATOM 1 CB SER A 35 19.296 42.140 -10.006 1.00 63.79 ATOM 2 OG SER A 35 19.803 43.323 -10.607 1.00 64.73 ATOM 3 C SER A 35 17.651 40.756 -11.289 1.00 62.75 ATOM 4 O SER A 35 16.789 41.299 -10.591 1.00 63.32 ATOM 5 N SER A 35 19.845 41.345 -12.297 1.00 63.23 ATOM 6 CA SER A 35 19.135 41.005 -11.030 1.00 63.19 ATOM 7 N LYS A 36 17.359 39.939 -12.298 1.00 61.72 ATOM 8 CA LYS A 36 15.977 39.615 -12.647 1.00 60.32 ATOM 9 CB LYS A 36 15.919 38.943 -14.022 1.00 60.87 ATOM 10 CG LYS A 36 14.527 38.504 -14.449 1.00 61.29 ATOM 11 CD LYS A 36 14.481 37.007 -14.706 1.00 61.82 ATOM 12 CE LYS A 36 13.727 36.685 -15.988 1.00 62.56 ATOM 13 NZ LYS A 36 14.240 35.448 -16.656 1.00 63.22 ATOM 14 C LYS A 36 15.381 38.689 -11.592 1.00 59.15 ATOM 15 O LYS A 36 15.834 37.554 -11.412 1.00 59.31 ATOM 16 N VAL A 37 14.369 39.180 -10.888 1.00 57.09 ATOM 17 CA VAL A 37 13.723 38.393 -9.851 1.00 54.75 ATOM 18 CB VAL A 37 13.311 39.271 -8.664 1.00 54.38 ATOM 19 CG1 VAL A 37 12.653 38.419 -7.590 1.00 54.21 ATOM 20 CG2 VAL A 37 14.522 39.990 -8.116 1.00 54.12 ATOM 21 C VAL A 37 12.481 37.683 -10.368 1.00 53.34 ATOM 22 O VAL A 37 11.705 38.253 -11.137 1.00 53.51 ATOM 23 N THR A 38 12.310 36.431 -9.951 1.00 50.98 ATOM 24 CA THR A 38 11.148 35.647 -10.337 1.00 48.35 ATOM 25 CB THR A 38 11.548 34.339 -11.030 1.00 48.71 ATOM 26 OG1 THR A 38 12.250 34.634 -12.244 1.00 49.40 ATOM 27 CG2 THR A 38 10.309 33.514 -11.349 1.00 48.47 ATOM 28 C THR A 38 10.366 35.313 -9.069 1.00 46.51 ATOM 29 O THR A 38 10.934 34.846 -8.078 1.00 46.10 ATOM 30 N THR A 39 9.067 35.583 -9.094 1.00 44.07 ATOM 31 CA THR A 39 8.220 35.299 -7.950 1.00 41.64 ATOM 32 CB THR A 39 7.526 36.561 -7.426 1.00 41.92 ATOM 33 OG1 THR A 39 8.517 37.511 -7.016 1.00 42.10 ATOM 34 CG2 THR A 39 6.633 36.223 -6.236 1.00 41.49 ATOM 35 C THR A 39 7.161 34.299 -8.368 1.00 40.07 ATOM 36 O THR A 39 6.534 34.442 -9.420 1.00 40.03 ATOM 37 N VAL A 40 6.980 33.277 -7.541 1.00 37.46 ATOM 38 CA VAL A 40 6.003 32.241 -7.815 1.00 34.88 ATOM 39 CB VAL A 40 6.691 30.919 -8.293 1.00 34.71 ATOM 40 CG1 VAL A 40 7.458 31.160 -9.587 1.00 33.69 ATOM 41 CG2 VAL A 40 7.621 30.388 -7.207 1.00 32.71 ATOM 42 C VAL A 40 5.240 31.956 -6.527 1.00 33.76 ATOM 43 O VAL A 40 5.649 32.376 -5.446 1.00 33.23 ATOM 44 N VAL A 41 4.115 31.264 -6.650 1.00 32.41 ATOM 45 CA VAL A 41 3.342 30.887 -5.486 1.00 31.46 ATOM 46 CB VAL A 41 1.843 31.211 -5.659 1.00 30.82 ATOM 47 CG1 VAL A 41 1.078 30.798 -4.413 1.00 29.52 ATOM 48 CG2 VAL A 41 1.665 32.704 -5.919 1.00 30.08 ATOM 49 C VAL A 41 3.572 29.387 -5.435 1.00 31.22 ATOM 50 O VAL A 41 2.994 28.630 -6.213 1.00 31.36 ATOM 51 N ALA A 42 4.446 28.968 -4.523 1.00 30.90 ATOM 52 CA ALA A 42 4.813 27.567 -4.395 1.00 29.95 ATOM 53 CB ALA A 42 6.337 27.430 -4.477 1.00 29.83 ATOM 54 C ALA A 42 4.302 26.900 -3.135 1.00 29.18 ATOM 55 O ALA A 42 4.170 27.529 -2.089 1.00 28.79 ATOM 56 N THR A 43 4.039 25.605 -3.254 1.00 28.95 ATOM 57 CA THR A 43 3.536 24.800 -2.154 1.00 29.32 ATOM 58 CB THR A 43 2.646 23.674 -2.678 1.00 28.81 ATOM 59 OG1 THR A 43 1.609 24.227 -3.490 1.00 30.16 ATOM 60 CG2 THR A 43 2.032 22.906 -1.538 1.00 28.54 ATOM 61 C THR A 43 4.657 24.151 -1.359 1.00 30.69 ATOM 62 O THR A 43 5.496 23.453 -1.924 1.00 30.05 ATOM 63 N PRO A 44 4.691 24.376 -0.036 1.00 31.82 ATOM 64 CD PRO A 44 3.778 25.227 0.755 1.00 32.37 ATOM 65 CA PRO A 44 5.735 23.770 0.793 1.00 32.81 ATOM 66 CB PRO A 44 5.254 24.025 2.218 1.00 32.36 ATOM 67 CG PRO A 44 4.436 25.277 2.110 1.00 32.56 ATOM 68 C PRO A 44 5.841 22.274 0.478 1.00 34.53 ATOM 69 O PRO A 44 4.827 21.584 0.334 1.00 33.56 ATOM 70 N GLY A 45 7.071 21.782 0.367 1.00 36.16 ATOM 71 CA GLY A 45 7.277 20.384 0.051 1.00 39.12 ATOM 72 C GLY A 45 6.583 19.471 1.032 1.00 41.99 ATOM 73 O GLY A 45 6.020 18.445 0.657 1.00 42.48 ATOM 74 N GLN A 46 6.620 19.848 2.301 1.00 44.81 ATOM 75 CA GLN A 46 5.990 19.052 3.339 1.00 48.00 ATOM 76 CB GLN A 46 7.058 18.413 4.225 1.00 49.53 ATOM 77 CG GLN A 46 8.359 18.136 3.491 1.00 51.89 ATOM 78 CD GLN A 46 8.981 16.820 3.891 1.00 53.63 ATOM 79 OE1 GLN A 46 8.278 15.829 4.129 1.00 54.38 ATOM 80 NE2 GLN A 46 10.311 16.797 3.972 1.00 54.26 ATOM 81 C GLN A 46 5.059 19.903 4.185 1.00 49.05 ATOM 82 O GLN A 46 5.219 21.119 4.291 1.00 49.77 ATOM 83 N GLY A 47 4.080 19.253 4.793 1.00 49.98 ATOM 84 CA GLY A 47 3.146 19.984 5.618 1.00 50.68 ATOM 85 C GLY A 47 1.821 20.145 4.915 1.00 51.20 ATOM 86 O GLY A 47 1.442 19.309 4.091 1.00 51.72 ATOM 87 N PRO A 48 1.097 21.235 5.205 1.00 51.16 ATOM 88 CD PRO A 48 1.483 22.321 6.125 1.00 51.22 ATOM 89 CA PRO A 48 -0.203 21.478 4.581 1.00 50.52 ATOM 90 CB PRO A 48 -0.908 22.381 5.586 1.00 51.22 ATOM 91 CG PRO A 48 0.223 23.159 6.236 1.00 51.26 ATOM 92 C PRO A 48 -0.078 22.136 3.217 1.00 49.63 ATOM 93 O PRO A 48 0.871 22.885 2.964 1.00 49.55 ATOM 94 N ASP A 49 -1.031 21.851 2.336 1.00 48.55 ATOM 95 CA ASP A 49 -1.012 22.451 1.013 1.00 47.40 ATOM 96 CB ASP A 49 -1.967 21.716 0.075 1.00 48.84 ATOM 97 CG ASP A 49 -1.330 20.495 -0.549 1.00 50.20 ATOM 98 OD1 ASP A 49 -0.632 19.764 0.182 1.00 50.75 ATOM 99 OD2 ASP A 49 -1.518 20.264 -1.765 1.00 51.64 ATOM 100 C ASP A 49 -1.423 23.908 1.157 1.00 45.71 ATOM 101 O ASP A 49 -2.549 24.287 0.834 1.00 45.93 ATOM 102 N ARG A 50 -0.495 24.714 1.663 1.00 43.21 ATOM 103 CA ARG A 50 -0.722 26.136 1.866 1.00 40.71 ATOM 104 CB ARG A 50 -0.696 26.465 3.363 1.00 41.13 ATOM 105 CG ARG A 50 -1.861 25.871 4.158 1.00 42.49 ATOM 106 CD ARG A 50 -3.217 26.418 3.694 1.00 43.96 ATOM 107 NE ARG A 50 -4.334 25.698 4.306 1.00 45.37 ATOM 108 CZ ARG A 50 -5.069 24.777 3.684 1.00 46.21 ATOM 109 NH1 ARG A 50 -4.818 24.450 2.422 1.00 46.21 ATOM 110 NH2 ARG A 50 -6.052 24.164 4.331 1.00 46.75 ATOM 111 C ARG A 50 0.361 26.919 1.130 1.00 38.63 ATOM 112 O ARG A 50 1.363 27.339 1.715 1.00 37.78 ATOM 113 N PRO A 51 0.178 27.102 -0.183 1.00 37.11 ATOM 114 CD PRO A 51 -0.949 26.572 -0.967 1.00 36.58 ATOM 115 CA PRO A 51 1.136 27.834 -1.017 1.00 36.61 ATOM 116 CB PRO A 51 0.465 27.871 -2.390 1.00 35.80 ATOM 117 CG PRO A 51 -0.475 26.709 -2.380 1.00 35.90 ATOM 118 C PRO A 51 1.487 29.228 -0.522 1.00 36.63 ATOM 119 O PRO A 51 0.655 29.930 0.053 1.00 36.71 ATOM 120 N GLN A 52 2.733 29.627 -0.756 1.00 36.67 ATOM 121 CA GLN A 52 3.196 30.950 -0.360 1.00 36.58 ATOM 122 CB GLN A 52 4.074 30.860 0.887 1.00 37.80 ATOM 123 CG GLN A 52 5.215 29.863 0.788 1.00 39.72 ATOM 124 CD GLN A 52 5.896 29.665 2.125 1.00 41.34 ATOM 125 OE1 GLN A 52 5.359 28.989 3.004 1.00 41.84 ATOM 126 NE2 GLN A 52 7.075 30.268 2.296 1.00 40.96 ATOM 127 C GLN A 52 3.982 31.564 -1.501 1.00 36.27 ATOM 128 O GLN A 52 4.475 30.859 -2.379 1.00 34.85 ATOM 129 N GLU A 53 4.081 32.886 -1.499 1.00 37.08 ATOM 130 CA GLU A 53 4.822 33.578 -2.539 1.00 38.06 ATOM 131 CB GLU A 53 4.514 35.079 -2.505 1.00 39.91 ATOM 132 CG GLU A 53 3.432 35.522 -3.488 1.00 43.08 ATOM 133 CD GLU A 53 2.444 36.529 -2.889 1.00 45.07 ATOM 134 OE1 GLU A 53 2.559 36.842 -1.679 1.00 46.42 ATOM 135 OE2 GLU A 53 1.552 37.006 -3.631 1.00 44.43 ATOM 136 C GLU A 53 6.301 33.340 -2.255 1.00 37.56 ATOM 137 O GLU A 53 6.751 33.511 -1.124 1.00 37.34 ATOM 138 N VAL A 54 7.046 32.921 -3.273 1.00 36.63 ATOM 139 CA VAL A 54 8.473 32.675 -3.122 1.00 35.82 ATOM 140 CB VAL A 54 8.807 31.162 -3.177 1.00 34.95 ATOM 141 CG1 VAL A 54 10.315 30.960 -3.131 1.00 33.62 ATOM 142 CG2 VAL A 54 8.146 30.440 -2.024 1.00 33.32 ATOM 143 C VAL A 54 9.191 33.379 -4.261 1.00 36.15 ATOM 144 O VAL A 54 8.848 33.191 -5.428 1.00 35.67 ATOM 145 N SER A 55 10.178 34.201 -3.915 1.00 37.16 ATOM 146 CA SER A 55 10.947 34.930 -4.918 1.00 38.31 ATOM 147 CB SER A 55 10.929 36.429 -4.610 1.00 39.15 ATOM 148 OG SER A 55 9.669 37.000 -4.923 1.00 40.75 ATOM 149 C SER A 55 12.389 34.442 -4.956 1.00 38.30 ATOM 150 O SER A 55 12.974 34.131 -3.921 1.00 37.80 ATOM 151 N TYR A 56 12.953 34.376 -6.156 1.00 39.14 ATOM 152 CA TYR A 56 14.329 33.937 -6.331 1.00 40.41 ATOM 153 CB TYR A 56 14.394 32.420 -6.503 1.00 38.94 ATOM 154 CG TYR A 56 13.649 31.893 -7.707 1.00 38.65 ATOM 155 CD1 TYR A 56 12.374 31.341 -7.574 1.00 38.73 ATOM 156 CE1 TYR A 56 11.704 30.811 -8.670 1.00 38.24 ATOM 157 CD2 TYR A 56 14.233 31.905 -8.974 1.00 38.64 ATOM 158 CE2 TYR A 56 13.568 31.377 -10.077 1.00 38.36 ATOM 159 CZ TYR A 56 12.307 30.832 -9.915 1.00 38.49 ATOM 160 OH TYR A 56 11.651 30.304 -10.999 1.00 39.00 ATOM 161 C TYR A 56 14.981 34.615 -7.527 1.00 42.20 ATOM 162 O TYR A 56 14.304 35.114 -8.429 1.00 41.94 ATOM 163 N THR A 57 16.308 34.610 -7.534 1.00 44.46 ATOM 164 CA THR A 57 17.068 35.241 -8.603 1.00 46.40 ATOM 165 CB THR A 57 17.411 36.697 -8.198 1.00 46.65 ATOM 166 OG1 THR A 57 17.965 37.394 -9.319 1.00 47.82 ATOM 167 CG2 THR A 57 18.388 36.707 -7.023 1.00 45.44 ATOM 168 C THR A 57 18.356 34.458 -8.908 1.00 47.52 ATOM 169 O THR A 57 18.556 33.361 -8.382 1.00 47.39 ATOM 170 N ASP A 58 19.206 35.029 -9.761 1.00 48.95 ATOM 171 CA ASP A 58 20.474 34.404 -10.143 1.00 50.41 ATOM 172 CB ASP A 58 21.434 34.377 -8.945 1.00 51.25 ATOM 173 CG ASP A 58 21.794 35.761 -8.449 1.00 52.39 ATOM 174 OD1 ASP A 58 21.820 36.715 -9.264 1.00 52.78 ATOM 175 OD2 ASP A 58 22.062 35.895 -7.242 1.00 52.87 ATOM 176 C ASP A 58 20.274 32.999 -10.671 1.00 51.45 ATOM 177 O ASP A 58 20.993 32.067 -10.311 1.00 50.98 ATOM 178 N THR A 59 19.279 32.884 -11.536 1.00 53.38 ATOM 179 CA THR A 59 18.936 31.605 -12.133 1.00 55.17 ATOM 180 CB THR A 59 17.505 31.629 -12.691 1.00 55.49 ATOM 181 OG1 THR A 59 16.566 31.670 -11.609 1.00 55.42 ATOM 182 CG2 THR A 59 17.233 30.386 -13.525 1.00 55.04 ATOM 183 C THR A 59 19.889 31.226 -13.253 1.00 56.32 ATOM 184 O THR A 59 19.955 31.900 -14.281 1.00 56.78 ATOM 185 N LYS A 60 20.621 30.143 -13.045 1.00 56.89 ATOM 186 CA LYS A 60 21.568 29.664 -14.044 1.00 57.67 ATOM 187 CB LYS A 60 22.991 30.060 -13.661 1.00 58.19 ATOM 188 CG LYS A 60 23.352 29.740 -12.226 1.00 59.23 ATOM 189 CD LYS A 60 24.822 29.997 -11.951 1.00 60.45 ATOM 190 CE LYS A 60 25.711 28.946 -12.620 1.00 61.36 ATOM 191 NZ LYS A 60 27.165 29.300 -12.557 1.00 62.12 ATOM 192 C LYS A 60 21.464 28.150 -14.161 1.00 57.75 ATOM 193 O LYS A 60 21.491 27.439 -13.160 1.00 57.54 ATOM 194 N VAL A 61 21.331 27.669 -15.391 1.00 58.07 ATOM 195 CA VAL A 61 21.230 26.242 -15.643 1.00 58.72 ATOM 196 CB VAL A 61 21.235 25.950 -17.151 1.00 58.04 ATOM 197 CG1 VAL A 61 21.199 24.451 -17.398 1.00 57.97 ATOM 198 CG2 VAL A 61 20.053 26.634 -17.804 1.00 57.57 ATOM 199 C VAL A 61 22.407 25.525 -14.993 1.00 59.48 ATOM 200 O VAL A 61 23.526 26.028 -15.005 1.00 59.45 ATOM 201 N ILE A 62 22.148 24.362 -14.408 1.00 60.60 ATOM 202 CA ILE A 62 23.199 23.593 -13.755 1.00 61.85 ATOM 203 CB ILE A 62 23.167 23.751 -12.210 1.00 61.39 ATOM 204 CG2 ILE A 62 23.284 25.216 -11.837 1.00 61.38 ATOM 205 CG1 ILE A 62 21.890 23.133 -11.638 1.00 61.27 ATOM 206 CD1 ILE A 62 21.958 22.856 -10.147 1.00 60.59 ATOM 207 C ILE A 62 23.071 22.118 -14.089 1.00 63.08 ATOM 208 O ILE A 62 23.466 21.253 -13.304 1.00 63.46 ATOM 209 N GLY A 63 22.516 21.831 -15.259 1.00 64.18 ATOM 210 CA GLY A 63 22.362 20.447 -15.650 1.00 66.00 ATOM 211 C GLY A 63 21.147 20.174 -16.506 1.00 67.29 ATOM 212 O GLY A 63 20.320 21.052 -16.754 1.00 67.25 ATOM 213 N ASN A 64 21.048 18.930 -16.957 1.00 68.58 ATOM 214 CA ASN A 64 19.948 18.497 -17.797 1.00 69.62 ATOM 215 CB ASN A 64 20.342 18.610 -19.268 1.00 69.88 ATOM 216 CG ASN A 64 19.561 19.678 -19.995 1.00 70.72 ATOM 217 OD1 ASN A 64 19.967 20.843 -20.038 1.00 71.03 ATOM 218 ND2 ASN A 64 18.429 19.292 -20.572 1.00 71.04 ATOM 219 C ASN A 64 19.567 17.057 -17.483 1.00 70.11 ATOM 220 O ASN A 64 20.326 16.317 -16.851 1.00 70.66 ATOM 221 N GLY A 65 18.379 16.670 -17.924 1.00 70.12 ATOM 222 CA GLY A 65 17.910 15.320 -17.701 1.00 70.01 ATOM 223 C GLY A 65 17.060 14.904 -18.880 1.00 70.09 ATOM 224 O GLY A 65 16.522 15.762 -19.589 1.00 70.20 ATOM 225 N SER A 66 16.936 13.600 -19.108 1.00 69.87 ATOM 226 CA SER A 66 16.127 13.122 -20.223 1.00 69.26 ATOM 227 CB SER A 66 16.079 11.587 -20.234 1.00 69.24 ATOM 228 OG SER A 66 15.757 11.070 -18.956 1.00 69.45 ATOM 229 C SER A 66 14.716 13.696 -20.093 1.00 68.55 ATOM 230 O SER A 66 14.005 13.861 -21.088 1.00 68.39 ATOM 231 N PHE A 67 14.339 14.032 -18.859 1.00 67.68 ATOM 232 CA PHE A 67 13.014 14.571 -18.560 1.00 66.41 ATOM 233 CB PHE A 67 12.485 13.907 -17.287 1.00 66.89 ATOM 234 CG PHE A 67 12.516 12.405 -17.340 1.00 67.31 ATOM 235 CD1 PHE A 67 13.386 11.684 -16.528 1.00 67.49 ATOM 236 CD2 PHE A 67 11.686 11.709 -18.217 1.00 67.39 ATOM 237 CE1 PHE A 67 13.431 10.291 -16.586 1.00 67.69 ATOM 238 CE2 PHE A 67 11.721 10.316 -18.285 1.00 67.52 ATOM 239 CZ PHE A 67 12.597 9.606 -17.468 1.00 67.78 ATOM 240 C PHE A 67 12.917 16.097 -18.437 1.00 65.01 ATOM 241 O PHE A 67 11.862 16.678 -18.707 1.00 64.69 ATOM 242 N GLY A 68 14.005 16.745 -18.035 1.00 63.50 ATOM 243 CA GLY A 68 13.978 18.192 -17.901 1.00 61.50 ATOM 244 C GLY A 68 15.287 18.816 -17.446 1.00 59.90 ATOM 245 O GLY A 68 16.276 18.120 -17.202 1.00 60.48 ATOM 246 N VAL A 69 15.285 20.140 -17.322 1.00 57.72 ATOM 247 CA VAL A 69 16.469 20.889 -16.906 1.00 55.14 ATOM 248 CB VAL A 69 16.533 22.258 -17.637 1.00 55.45 ATOM 249 CG1 VAL A 69 17.734 23.062 -17.158 1.00 55.48 ATOM 250 CG2 VAL A 69 16.606 22.039 -19.142 1.00 55.83 ATOM 251 C VAL A 69 16.516 21.145 -15.399 1.00 53.10 ATOM 252 O VAL A 69 15.490 21.145 -14.722 1.00 52.58 ATOM 253 N VAL A 70 17.722 21.355 -14.884 1.00 50.61 ATOM 254 CA VAL A 70 17.917 21.644 -13.474 1.00 48.53 ATOM 255 CB VAL A 70 18.767 20.557 -12.781 1.00 47.83 ATOM 256 CG1 VAL A 70 18.943 20.893 -11.309 1.00 46.76 ATOM 257 CG2 VAL A 70 18.108 19.198 -12.947 1.00 47.06 ATOM 258 C VAL A 70 18.649 22.980 -13.398 1.00 47.78 ATOM 259 O VAL A 70 19.706 23.146 -14.004 1.00 47.75 ATOM 260 N TYR A 71 18.075 23.939 -12.676 1.00 46.49 ATOM 261 CA TYR A 71 18.686 25.257 -12.535 1.00 45.07 ATOM 262 CB TYR A 71 17.720 26.388 -12.913 1.00 46.38 ATOM 263 CG TYR A 71 17.000 26.242 -14.226 1.00 47.54 ATOM 264 CD1 TYR A 71 17.311 27.071 -15.305 1.00 48.05 ATOM 265 CE1 TYR A 71 16.642 26.950 -16.519 1.00 48.67 ATOM 266 CD2 TYR A 71 16.000 25.287 -14.390 1.00 48.26 ATOM 267 CE2 TYR A 71 15.322 25.155 -15.599 1.00 49.32 ATOM 268 CZ TYR A 71 15.647 25.988 -16.660 1.00 49.55 ATOM 269 OH TYR A 71 14.977 25.846 -17.857 1.00 50.19 ATOM 270 C TYR A 71 19.071 25.501 -11.105 1.00 43.81 ATOM 271 O TYR A 71 18.626 24.809 -10.197 1.00 43.63 ATOM 272 N GLN A 72 19.903 26.510 -10.910 1.00 42.91 ATOM 273 CA GLN A 72 20.292 26.906 -9.577 1.00 42.23 ATOM 274 CB GLN A 72 21.800 26.908 -9.414 1.00 42.83 ATOM 275 CG GLN A 72 22.212 27.095 -7.973 1.00 43.87 ATOM 276 CD GLN A 72 23.520 27.812 -7.855 1.00 44.77 ATOM 277 OE1 GLN A 72 23.852 28.647 -8.690 1.00 45.68 ATOM 278 NE2 GLN A 72 24.281 27.492 -6.817 1.00 45.85 ATOM 279 C GLN A 72 19.758 28.323 -9.436 1.00 41.68 ATOM 280 O GLN A 72 19.699 29.074 -10.406 1.00 41.25 ATOM 281 N ALA A 73 19.344 28.677 -8.229 1.00 41.10 ATOM 282 CA ALA A 73 18.814 30.004 -7.977 1.00 40.73 ATOM 283 CB ALA A 73 17.330 30.059 -8.317 1.00 40.42 ATOM 284 C ALA A 73 19.034 30.326 -6.526 1.00 40.76 ATOM 285 O ALA A 73 19.337 29.451 -5.717 1.00 41.00 ATOM 286 N LYS A 74 18.884 31.600 -6.198 1.00 41.16 ATOM 287 CA LYS A 74 19.068 32.045 -4.831 1.00 42.08 ATOM 288 CB LYS A 74 20.152 33.121 -4.787 1.00 43.01 ATOM 289 CG LYS A 74 20.406 33.707 -3.415 1.00 44.92 ATOM 290 CD LYS A 74 20.856 35.157 -3.545 1.00 47.50 ATOM 291 CE LYS A 74 22.043 35.471 -2.645 1.00 48.60 ATOM 292 NZ LYS A 74 22.571 36.856 -2.884 1.00 50.28 ATOM 293 C LYS A 74 17.747 32.602 -4.328 1.00 42.13 ATOM 294 O LYS A 74 17.124 33.436 -4.992 1.00 41.82 ATOM 295 N LEU A 75 17.311 32.119 -3.171 1.00 42.49 ATOM 296 CA LEU A 75 16.061 32.583 -2.588 1.00 43.30 ATOM 297 CB LEU A 75 15.646 31.675 -1.430 1.00 41.81 ATOM 298 CG LEU A 75 15.237 30.241 -1.785 1.00 41.13 ATOM 299 CD1 LEU A 75 14.729 29.545 -0.538 1.00 39.52 ATOM 300 CD2 LEU A 75 14.164 30.243 -2.865 1.00 39.87 ATOM 301 C LEU A 75 16.298 33.998 -2.085 1.00 44.36 ATOM 302 O LEU A 75 17.169 34.221 -1.250 1.00 44.21 ATOM 303 N CYS A 76 15.525 34.948 -2.600 1.00 46.03 ATOM 304 CA CYS A 76 15.672 36.352 -2.221 1.00 47.75 ATOM 305 CB CYS A 76 14.608 37.198 -2.908 1.00 46.80 ATOM 306 SG CYS A 76 14.775 37.229 -4.670 1.00 48.31 ATOM 307 C CYS A 76 15.592 36.600 -0.730 1.00 49.06 ATOM 308 O CYS A 76 16.394 37.344 -0.170 1.00 49.57 ATOM 309 N ASP A 77 14.621 35.977 -0.081 1.00 50.93 ATOM 310 CA ASP A 77 14.456 36.189 1.340 1.00 52.59 ATOM 311 CB ASP A 77 13.127 35.593 1.798 1.00 54.68 ATOM 312 CG ASP A 77 11.969 36.566 1.614 1.00 57.01 ATOM 313 OD1 ASP A 77 11.762 37.034 0.467 1.00 57.67 ATOM 314 OD2 ASP A 77 11.275 36.871 2.614 1.00 58.59 ATOM 315 C ASP A 77 15.604 35.669 2.194 1.00 52.59 ATOM 316 O ASP A 77 16.108 36.385 3.059 1.00 53.24 ATOM 317 N SER A 78 16.043 34.443 1.942 1.00 52.13 ATOM 318 CA SER A 78 17.122 33.861 2.735 1.00 50.72 ATOM 319 CB SER A 78 16.773 32.417 3.101 1.00 50.79 ATOM 320 OG SER A 78 16.754 31.593 1.947 1.00 50.55 ATOM 321 C SER A 78 18.502 33.886 2.084 1.00 49.86 ATOM 322 O SER A 78 19.510 33.741 2.767 1.00 50.25 ATOM 323 N GLY A 79 18.555 34.064 0.771 1.00 48.73 ATOM 324 CA GLY A 79 19.840 34.068 0.097 1.00 47.27 ATOM 325 C GLY A 79 20.346 32.643 -0.059 1.00 46.42 ATOM 326 O GLY A 79 21.416 32.406 -0.621 1.00 46.54 ATOM 327 N GLU A 80 19.569 31.686 0.444 1.00 45.29 ATOM 328 CA GLU A 80 19.930 30.277 0.349 1.00 43.84 ATOM 329 CB GLU A 80 18.983 29.425 1.186 1.00 45.45 ATOM 330 CG GLU A 80 19.320 29.390 2.662 1.00 48.05 ATOM 331 CD GLU A 80 18.274 28.649 3.474 1.00 49.84 ATOM 332 OE1 GLU A 80 18.628 28.072 4.527 1.00 51.39 ATOM 333 OE2 GLU A 80 17.094 28.644 3.060 1.00 50.93 ATOM 334 C GLU A 80 19.878 29.803 -1.096 1.00 42.2 ATOM 335 O GLU A 80 19.033 30.242 -1.882 1.00 41.84 ATOM 336 N LEU A 81 20.787 28.899 -1.441 1.00 40.22 ATOM 337 CA LEU A 81 20.846 28.369 -2.792 1.00 37.91 ATOM 338 CB LEU A 81 22.290 28.042 -3.176 1.00 38.56 ATOM 339 CG LEU A 81 23.253 29.220 -3.338 1.00 39.15 ATOM 340 CD1 LEU A 81 24.627 28.680 -3.707 1.00 39.35 ATOM 341 CD2 LEU A 81 22.748 30.177 -4.412 1.00 38.74 ATOM 342 C LEU A 81 19.996 27.121 -2.907 1.00 35.87 ATOM 343 O LEU A 81 19.960 26.290 -1.999 1.00 35.79 ATOM 344 N VAL A 82 19.311 26.998 -4.035 1.00 33.93 ATOM 345 CA VAL A 82 18.456 25.852 -4.282 1.00 31.97 ATOM 346 CB VAL A 82 16.950 26.194 -4.031 1.00 32.11 ATOM 347 CG1 VAL A 82 16.746 26.660 -2.590 1.00 31.34 ATOM 348 CG2 VAL A 82 16.481 27.278 -5.017 1.00 31.41 ATOM 349 C VAL A 82 18.612 25.416 -5.726 1.00 30.97 ATOM 350 O VAL A 82 19.134 26.156 -6.562 1.00 30.39 ATOM 351 N ALA A 83 18.155 24.204 -6.005 1.00 29.95 ATOM 352 CA ALA A 83 18.189 23.651 -7.343 1.00 30.03 ATOM 353 CB ALA A 83 18.892 22.305 -7.337 1.00 29.36 ATOM 354 C ALA A 83 16.730 23.478 -7.739 1.00 30.05 ATOM 355 O ALA A 83 15.925 23.004 -6.948 1.00 30.48 ATOM 356 N ILE A 84 16.379 23.878 -8.950 1.00 30.36 ATOM 357 CA ILE A 84 15.007 23.733 -9.393 1.00 30.27 ATOM 358 CB ILE A 84 14.415 25.074 -9.904 1.00 30.22 ATOM 359 CG2 ILE A 84 12.988 24.855 -10.402 1.00 28.63 ATOM 360 CG1 ILE A 84 14.441 26.125 -8.788 1.00 29.72 ATOM 361 CD1 ILE A 84 13.972 27.501 -9.239 1.00 30.91 ATOM 362 C ILE A 84 14.973 22.724 -10.514 1.00 30.98 ATOM 363 O ILE A 84 15.475 22.981 -11.606 1.00 31.76 ATOM 364 N LYS A 85 14.390 21.565 -10.237 1.00 32.18 ATOM 365 CA LYS A 85 14.277 20.516 -11.235 1.00 33.65 ATOM 366 CB LYS A 85 14.321 19.148 -10.563 1.00 32.83 ATOM 367 CG LYS A 85 14.106 17.989 -11.505 1.00 32.48 ATOM 368 CD LYS A 85 14.433 16.681 -10.790 1.00 32.56 ATOM 369 CE LYS A 85 14.585 15.530 -11.766 1.00 32.82 ATOM 370 NZ LYS A 85 14.704 14.229 -11.044 1.00 32.79 ATOM 371 C LYS A 85 12.952 20.707 -11.970 1.00 35.22 ATOM 372 O LYS A 85 11.876 20.545 -11.391 1.00 34.62 ATOM 373 N LYS A 86 13.044 21.057 -13.247 1.00 37.35 ATOM 374 CA LYS A 86 11.870 21.294 -14.071 1.00 40.15 ATOM 375 CB LYS A 86 12.105 22.521 -14.942 1.00 41.12 ATOM 376 CG LYS A 86 10.853 23.088 -15.550 1.00 42.26 ATOM 377 CD LYS A 86 11.186 24.339 -16.318 1.00 43.25 ATOM 378 CE LYS A 86 9.983 24.843 -17.073 1.00 45.13 ATOM 379 NZ LYS A 86 10.313 26.083 -17.831 1.00 46.92 ATOM 380 C LYS A 86 11.555 20.089 -14.946 1.00 41.86 ATOM 381 O LYS A 86 12.403 19.621 -15.711 1.00 42.56 ATOM 382 N VAL A 87 10.327 19.596 -14.838 1.00 43.19 ATOM 383 CA VAL A 87 9.912 18.429 -15.595 1.00 44.94 ATOM 384 CB VAL A 87 9.882 17.188 -14.669 1.00 44.96 ATOM 385 CG1 VAL A 87 9.096 16.063 -15.311 1.00 45.35 ATOM 386 CG2 VAL A 87 11.305 16.736 -14.368 1.00 45.03 ATOM 387 C VAL A 87 8.540 18.610 -16.245 1.00 46.85 ATOM 388 O VAL A 87 7.640 19.209 -15.659 1.00 46.73 ATOM 389 N LEU A 88 8.391 18.093 -17.462 1.00 48.66 ATOM 390 CA LEU A 88 7.121 18.169 -18.174 1.00 50.56 ATOM 391 CB LEU A 88 7.288 17.643 -19.598 1.00 50.56 ATOM 392 CG LEU A 88 6.188 18.006 -20.594 1.00 50.73 ATOM 393 CD1 LEU A 88 6.355 19.450 -21.053 1.00 50.42 ATOM 394 CD2 LEU A 88 6.255 17.049 -21.778 1.00 50.68 ATOM 395 C LEU A 88 6.125 17.299 -17.410 1.00 52.11 ATOM 396 O LEU A 88 6.382 16.121 -17.167 1.00 52.38 ATOM 397 N GLN A 89 4.994 17.874 -17.021 1.00 54.17 ATOM 398 CA GLN A 89 4.006 17.116 -16.264 1.00 56.49 ATOM 399 CB GLN A 89 3.612 17.885 -14.995 1.00 56.82 ATOM 400 CG GLN A 89 2.880 17.045 -13.951 1.00 57.82 ATOM 401 CD GLN A 89 3.253 15.567 -14.011 1.00 58.69 ATOM 402 OE1 GLN A 89 2.386 14.699 -14.144 1.00 58.95 ATOM 403 NE2 GLN A 89 4.548 15.277 -13.914 1.00 58.51 ATOM 404 C GLN A 89 2.747 16.761 -17.049 1.00 57.83 ATOM 405 O GLN A 89 2.135 17.616 -17.689 1.00 57.48 ATOM 406 N ASP A 90 2.365 15.489 -17.001 1.00 59.76 ATOM 407 CA ASP A 90 1.159 15.050 -17.686 1.00 61.90 ATOM 408 CB ASP A 90 1.088 13.523 -17.763 1.00 63.19 ATOM 409 CG ASP A 90 0.028 13.040 -18.748 1.00 64.51 ATOM 410 OD1 ASP A 90 0.002 11.822 -19.051 1.00 65.36 ATOM 411 OD2 ASP A 90 -0.775 13.882 -19.220 1.00 64.90 ATOM 412 C ASP A 90 -0.024 15.568 -16.883 1.00 62.70 ATOM 413 O ASP A 90 -0.282 15.102 -15.768 1.00 62.79 ATOM 414 N LYS A 91 -0.732 16.538 -17.454 1.00 63.46 ATOM 415 CA LYS A 91 -1.888 17.147 -16.801 1.00 64.12 ATOM 416 CB LYS A 91 -2.612 18.065 -17.788 1.00 64.72 ATOM 417 CG LYS A 91 -2.874 17.427 -19.144 1.00 65.33 ATOM 418 CD LYS A 91 -3.983 18.162 -19.881 1.00 65.98 ATOM 419 CE LYS A 91 -4.743 17.240 -20.823 1.00 66.02 ATOM 420 NZ LYS A 91 -5.183 17.971 -22.047 1.00 66.16 ATOM 421 C LYS A 91 -2.882 16.130 -16.238 1.00 64.04 ATOM 422 O LYS A 91 -3.379 16.286 -15.121 1.00 64.21 ATOM 423 N ARG A 92 -3.154 15.084 -17.013 1.00 63.81 ATOM 424 CA ARG A 92 -4.109 14.052 -16.623 1.00 63.44 ATOM 425 CB ARG A 92 -4.563 13.290 -17.871 1.00 64.87 ATOM 426 CG ARG A 92 -5.463 14.105 -18.795 1.00 66.45 ATOM 427 CD ARG A 92 -6.707 14.591 -18.060 1.00 68.01 ATOM 428 NE ARG A 92 -7.560 13.481 -17.641 1.00 69.37 ATOM 429 CZ ARG A 92 -8.632 13.611 -16.865 1.00 70.09 ATOM 430 NH1 ARG A 92 -8.989 14.809 -16.417 1.00 70.37 ATOM 431 NH2 ARG A 92 -9.355 12.544 -16.544 1.00 70.54 ATOM 432 C ARG A 92 -3.663 13.052 -15.552 1.00 62.34 ATOM 433 O ARG A 92 -4.446 12.188 -15.147 1.00 62.82 ATOM 434 N PHE A 93 -2.422 13.153 -15.088 1.00 60.52 ATOM 435 CA PHE A 93 -1.936 12.222 -14.069 1.00 58.34 ATOM 436 CB PHE A 93 -1.261 11.028 -14.748 1.00 59.11 ATOM 437 CG PHE A 93 -2.054 10.470 -15.897 1.00 60.03 ATOM 438 CD1 PHE A 93 -3.031 9.505 -15.680 1.00 60.45 ATOM 439 CD2 PHE A 93 -1.861 10.948 -17.192 1.00 60.26 ATOM 440 CE1 PHE A 93 -3.809 9.026 -16.737 1.00 60.59 ATOM 441 CE2 PHE A 93 -2.630 10.478 -18.255 1.00 60.24 ATOM 442 CZ PHE A 93 -3.606 9.516 -18.027 1.00 60.41 ATOM 443 C PHE A 93 -0.983 12.896 -13.082 1.00 56.28 ATOM 444 O PHE A 93 -0.363 13.915 -13.402 1.00 56.16 ATOM 445 N LYS A 94 -0.872 12.337 -11.880 1.00 53.35 ATOM 446 CA LYS A 94 0.007 12.936 -10.889 1.00 50.80 ATOM 447 CB LYS A 94 -0.593 12.835 -9.488 1.00 51.37 ATOM 448 CG LYS A 94 -0.113 13.961 -8.551 1.00 52.28 ATOM 449 CD LYS A 94 0.156 15.282 -9.303 1.00 51.90 ATOM 450 CE LYS A 94 1.621 15.722 -9.200 1.00 51.53 ATOM 451 NZ LYS A 94 2.023 16.718 -10.245 1.00 50.30 ATOM 452 C LYS A 94 1.419 12.376 -10.880 1.00 48.15 ATOM 453 O LYS A 94 1.637 11.175 -11.059 1.00 48.29 ATOM 454 N ASN A 95 2.372 13.275 -10.659 1.00 44.47 ATOM 455 CA ASN A 95 3.787 12.948 -10.636 1.00 40.58 ATOM 456 CB ASN A 95 4.593 14.238 -10.559 1.00 40.06 ATOM 457 CG ASN A 95 6.016 14.047 -10.990 1.00 39.51 ATOM 458 OD1 ASN A 95 6.368 14.285 -12.148 1.00 39.59 ATOM 459 ND2 ASN A 95 6.849 13.609 -10.065 1.00 38.42 ATOM 460 C ASN A 95 4.193 12.021 -9.496 1.00 38.13 ATOM 461 O ASN A 95 4.038 12.361 -8.325 1.00 37.22 ATOM 462 N ARG A 96 4.725 10.853 -9.845 1.00 35.69 ATOM 463 CA ARG A 96 5.151 9.882 -8.839 1.00 33.01 ATOM 464 CB ARG A 96 5.480 8.539 -9.497 1.00 33.73 ATOM 465 CG ARG A 96 5.861 7.450 -8.507 1.00 35.14 ATOM 466 CD ARG A 96 6.212 6.142 -9.210 1.00 37.31 ATOM 467 NE ARG A 96 5.027 5.498 -9.769 1.00 39.49 ATOM 468 CZ ARG A 96 5.052 4.471 -10.617 1.00 40.73 ATOM 469 NH1 ARG A 96 6.208 3.957 -11.016 1.00 40.97 ATOM 470 NH2 ARG A 96 3.915 3.960 -11.071 1.00 41.50 ATOM 471 C ARG A 96 6.365 10.389 -8.059 1.00 30.83 ATOM 472 O ARG A 96 6.464 10.192 -6.846 1.00 29.88 ATOM 473 N GLU A 97 7.287 11.042 -8.756 1.00 28.33 ATOM 474 CA GLU A 97 8.476 11.574 -8.112 1.00 27.05 ATOM 475 CB GLU A 97 9.370 12.257 -9.153 1.00 26.60 ATOM 476 CG GLU A 97 10.774 12.588 -8.657 1.00 26.57 ATOM 477 CD GLU A 97 11.619 13.292 -9.715 1.00 26.92 ATOM 478 OE1 GLU A 97 12.699 13.811 -9.368 1.00 26.11 ATOM 479 OE2 GLU A 97 11.203 13.329 -10.895 1.00 27.14 ATOM 480 C GLU A 97 8.067 12.571 -7.027 1.00 26.15 ATOM 481 O GLU A 97 8.560 12.514 -5.899 1.00 25.40 ATOM 482 N LEU A 98 7.160 13.480 -7.374 1.00 25.37 ATOM 483 CA LEU A 98 6.676 14.483 -6.432 1.00 25.35 ATOM 484 CB LEU A 98 5.694 15.428 -7.134 1.00 25.18 ATOM 485 CG LEU A 98 4.927 16.400 -6.230 1.00 24.99 ATOM 486 CD1 LEU A 98 5.893 17.445 -5.673 1.00 24.33 ATOM 487 CD2 LEU A 98 3.819 17.071 -7.014 1.00 24.51 ATOM 488 C LEU A 98 5.985 13.828 -5.236 1.00 26.20 ATOM 489 O LEU A 98 6.253 14.163 -4.079 1.00 25.40 ATOM 490 N GLN A 99 5.094 12.885 -5.521 1.00 26.83 ATOM 491 CA GLN A 99 4.363 12.193 -4.470 1.00 28.35 ATOM 492 CB GLN A 99 3.434 11.147 -5.085 1.00 30.83 ATOM 493 CG GLN A 99 2.331 11.726 -5.964 1.00 35.74 ATOM 494 CD GLN A 99 2.031 13.205 -5.688 1.00 39.16 ATOM 495 OE1 GLN A 99 1.627 13.587 -4.574 1.00 41.25 ATOM 496 NE2 GLN A 99 2.221 14.043 -6.710 1.00 41.32 ATOM 497 C GLN A 99 5.298 11.522 -3.473 1.00 27.45 ATOM 498 O GLN A 99 5.055 11.544 -2.265 1.00 26.38 ATOM 499 N ILE A 100 6.369 10.923 -3.985 1.00 26.98 ATOM 500 CA ILE A 100 7.337 10.245 -3.134 1.00 26.64 ATOM 501 CB ILE A 100 8.256 9.314 -3.974 1.00 27.09 ATOM 502 CG2 ILE A 100 9.553 9.010 -3.220 1.00 26.00 ATOM 503 CG1 ILE A 100 7.513 8.011 -4.282 1.00 27.02 ATOM 504 CD1 ILE A 100 8.130 7.193 -5.408 1.00 27.82 ATOM 505 C ILE A 100 8.175 11.253 -2.347 1.00 26.20 ATOM 506 O ILE A 100 8.351 11.095 -1.146 1.00 25.35 ATOM 507 N MET A 101 8.667 12.293 -3.015 1.00 26.79 ATOM 508 CA MET A 101 9.481 13.317 -2.348 1.00 28.50 ATOM 509 CB MET A 101 9.884 14.415 -3.325 1.00 30.42 ATOM 510 CG MET A 101 10.712 13.965 -4.483 1.00 35.10 ATOM 511 SD MET A 101 12.406 13.851 -4.020 1.00 42.18 ATOM 512 CE MET A 101 12.868 15.519 -3.921 1.00 37.66 ATOM 513 C MET A 101 8.751 13.991 -1.185 1.00 28.39 ATOM 514 O MET A 101 9.343 14.263 -0.147 1.00 27.61 ATOM 515 N ARG A 102 7.469 14.283 -1.381 1.00 28.20 ATOM 516 CA ARG A 102 6.655 14.944 -0.370 1.00 28.67 ATOM 517 CB ARG A 102 5.236 15.143 -0.893 1.00 29.31 ATOM 518 CG ARG A 102 5.141 16.087 -2.069 1.00 30.69 ATOM 519 CD ARG A 102 3.741 16.661 -2.183 1.00 32.57 ATOM 520 NE ARG A 102 3.537 17.713 -1.194 1.00 35.16 ATOM 521 CZ ARG A 102 2.381 18.337 -0.986 1.00 36.54 ATOM 522 NH1 ARG A 102 1.312 18.012 -1.703 1.00 35.80 ATOM 523 NH2 ARG A 102 2.300 19.288 -0.055 1.00 37.48 ATOM 524 C ARG A 102 6.591 14.216 0.964 1.00 28.81 ATOM 525 O ARG A 102 6.411 14.842 2.003 1.00 28.97 ATOM 526 N LYS A 103 6.742 12.899 0.951 1.00 28.71 ATOM 527 CA LYS A 103 6.682 12.158 2.199 1.00 29.30 ATOM 528 CB LYS A 103 5.871 10.880 2.001 1.00 32.14 ATOM 529 CG LYS A 103 6.571 9.817 1.190 1.00 35.30 ATOM 530 CD LYS A 103 5.693 8.574 1.059 1.00 38.30 ATOM 531 CE LYS A 103 4.382 8.873 0.338 1.00 39.76 ATOM 532 NZ LYS A 103 3.683 7.625 -0.098 1.00 41.47 ATOM 533 C LYS A 103 8.036 11.811 2.820 1.00 28.50 ATOM 534 O LYS A 103 8.089 11.256 3.911 1.00 29.22 ATOM 535 N LEU A 104 9.129 12.140 2.141 1.00 27.63 ATOM 536 CA LEU A 104 10.458 11.830 2.668 1.00 26.26 ATOM 537 CB LEU A 104 11.428 11.517 1.523 1.00 25.36 ATOM 538 CG LEU A 104 10.979 10.419 0.561 1.00 25.42 ATOM 539 CD1 LEU A 104 12.009 10.224 -0.540 1.00 25.39 ATOM 540 CD2 LEU A 104 10.766 9.130 1.346 1.00 25.81 ATOM 541 C LEU A 104 11.027 12.964 3.504 1.00 25.89 ATOM 542 O LEU A 104 10.922 14.133 3.141 1.00 26.61 ATOM 543 N ASP A 105 11.632 12.607 4.627 1.00 25.69 ATOM 544 CA ASP A 105 12.241 13.584 5.514 1.00 25.49 ATOM 545 CB ASP A 105 11.214 14.122 6.505 1.00 27.88 ATOM 546 CG ASP A 105 11.817 15.101 7.489 1.00 30.69 ATOM 547 OD1 ASP A 105 12.758 15.832 7.104 1.00 31.65 ATOM 548 OD2 ASP A 105 11.348 15.142 8.650 1.00 33.00 ATOM 549 C ASP A 105 13.369 12.889 6.260 1.00 24.16 ATOM 550 O ASP A 105 13.158 12.303 7.318 1.00 23.70 ATOM 551 N HIS A 106 14.570 12.966 5.690 1.00 22.70 ATOM 552 CA HIS A 106 15.755 12.322 6.257 1.00 20.81 ATOM 553 CB HIS A 106 15.885 10.926 5.655 1.00 19.52 ATOM 554 CG HIS A 106 16.945 10.086 6.280 1.00 19.42 ATOM 555 CD2 HIS A 106 16.874 9.119 7.227 1.00 19.37 ATOM 556 ND1 HIS A 106 18.266 10.149 5.894 1.00 19.39 ATOM 557 CE1 HIS A 106 18.964 9.251 6.569 1.00 18.42 ATOM 558 NE2 HIS A 106 18.145 8.614 7.385 1.00 19.23 ATOM 559 C HIS A 106 16.986 13.172 5.924 1.00 20.12 ATOM 560 O HIS A 106 17.067 13.760 4.839 1.00 18.86 ATOM 561 N CYS A 107 17.941 13.232 6.852 1.00 20.07 ATOM 562 CA CYS A 107 19.142 14.042 6.659 1.00 20.36 ATOM 563 CB CYS A 107 19.970 14.104 7.950 1.00 21.57 ATOM 564 SG CYS A 107 20.468 12.521 8.636 1.00 27.56 ATOM 565 C CYS A 107 20.029 13.603 5.493 1.00 19.73 ATOM 566 O CYS A 107 20.856 14.382 5.015 1.00 19.85 ATOM 567 N ASN A 108 19.850 12.373 5.022 1.00 18.44 ATOM 568 CA ASN A 108 20.649 11.886 3.901 1.00 17.27 ATOM 569 CB ASN A 108 21.322 10.570 4.283 1.00 16.69 ATOM 570 CG ASN A 108 22.319 10.760 5.407 1.00 16.87 ATOM 571 OD1 ASN A 108 23.165 11.656 5.342 1.00 17.95 ATOM 572 ND2 ASN A 108 22.213 9.954 6.447 1.00 14.59 ATOM 573 C ASN A 108 19.880 11.752 2.589 1.00 16.67 ATOM 574 O ASN A 108 20.233 10.956 1.722 1.00 15.69 ATOM 575 N ILE A 109 18.823 12.542 2.453 1.00 16.28 ATOM 576 CA ILE A 109 18.030 12.559 1.231 1.00 17.33 ATOM 577 CB ILE A 109 16.662 11.848 1.417 1.00 17.28 ATOM 578 CG2 ILE A 109 15.821 11.995 0.145 1.00 17.01 ATOM 579 CG1 ILE A 109 16.888 10.358 1.711 1.00 16.92 ATOM 580 CD1 ILE A 109 15.606 9.563 1.969 1.00 16.53 ATOM 581 C ILE A 109 17.807 14.032 0.924 1.00 18.52 ATOM 582 O ILE A 109 17.470 14.798 1.818 1.00 19.05 ATOM 583 N VAL A 110 18.003 14.433 -0.327 1.00 19.25 ATOM 584 CA VAL A 110 17.826 15.830 -0.705 1.00 21.14 ATOM 585 CB VAL A 110 18.182 16.043 -2.210 1.00 21.36 ATOM 586 CG1 VAL A 110 17.051 15.561 -3.114 1.00 21.36 ATOM 587 CG2 VAL A 110 18.500 17.514 -2.460 1.00 23.29 ATOM 588 C VAL A 110 16.396 16.290 -0.389 1.00 22.29 ATOM 589 O VAL A 110 15.418 15.625 -0.728 1.00 20.82 ATOM 590 N ARG A 111 16.282 17.434 0.268 1.00 23.41 ATOM 591 CA ARG A 111 14.980 17.937 0.681 1.00 25.32 ATOM 592 CB ARG A 111 15.139 18.820 1.925 1.00 27.85 ATOM 593 CG ARG A 111 13.829 19.396 2.453 1.00 32.55 ATOM 594 CD ARG A 111 14.052 20.337 3.629 1.00 35.71 ATOM 595 NE ARG A 111 15.079 21.331 3.329 1.00 40.90 ATOM 596 CZ ARG A 111 15.409 22.336 4.138 1.00 42.86 ATOM 597 NH1 ARG A 111 14.787 22.478 5.301 1.00 43.75 ATOM 598 NH2 ARG A 111 16.356 23.202 3.785 1.00 43.98 ATOM 599 C ARG A 111 14.196 18.703 -0.369 1.00 25.34 ATOM 600 O ARG A 111 14.742 19.570 -1.061 1.00 24.64 ATOM 601 N LEU A 112 12.914 18.363 -0.497 1.00 24.77 ATOM 602 CA LEU A 112 12.042 19.078 -1.418 1.00 24.97 ATOM 603 CB LEU A 112 10.865 18.199 -1.853 1.00 23.21 ATOM 604 CG LEU A 112 9.822 18.907 -2.728 1.00 22.16 ATOM 605 CD1 LEU A 112 10.396 19.203 -4.100 1.00 20.15 ATOM 606 CD2 LEU A 112 8.577 18.032 -2.841 1.00 21.36 ATOM 607 C LEU A 112 11.534 20.285 -0.616 1.00 25.61 ATOM 608 O LEU A 112 10.766 20.136 0.335 1.00 25.58 ATOM 609 N ARG A 113 11.986 21.477 -0.979 1.00 26.57 ATOM 610 CA ARG A 113 11.567 22.679 -0.276 1.00 28.47 ATOM 611 CB ARG A 113 12.564 23.797 -0.537 1.00 30.77 ATOM 612 CG ARG A 113 13.865 23.649 0.208 1.00 34.98 ATOM 613 CD ARG A 113 14.568 24.987 0.191 1.00 40.11 ATOM 614 NE ARG A 113 15.769 25.016 1.016 1.00 44.54 ATOM 615 CZ ARG A 113 16.438 26.126 1.302 1.00 46.30 ATOM 616 NH1 ARG A 113 16.017 27.293 0.829 1.00 48.28 ATOM 617 NH2 ARG A 113 17.538 26.066 2.042 1.00 48.41 ATOM 618 C ARG A 113 10.163 23.129 -0.697 1.00 28.17 ATOM 619 O ARG A 113 9.302 23.367 0.144 1.00 27.44 ATOM 620 N TYR A 114 9.955 23.262 -2.003 1.00 27.94 ATOM 621 CA TYR A 114 8.663 23.663 -2.554 1.00 28.54 ATOM 622 CB TYR A 114 8.575 25.178 -2.808 1.00 29.21 ATOM 623 CG TYR A 114 8.939 26.082 -1.661 1.00 30.80 ATOM 624 CD1 TYR A 114 8.019 26.367 -0.653 1.00 31.08 ATOM 625 CE1 TYR A 114 8.354 27.206 0.407 1.00 32.59 ATOM 626 CD2 TYR A 114 10.203 26.663 -1.585 1.00 31.27 ATOM 627 CE2 TYR A 114 10.547 27.501 -0.530 1.00 32.12 ATOM 628 CZ TYR A 114 9.622 27.766 0.462 1.00 32.89 ATOM 629 OH TYR A 114 9.970 28.568 1.527 1.00 34.70 ATOM 630 C TYR A 114 8.530 23.020 -3.916 1.00 28.82 ATOM 631 O TYR A 114 9.461 22.396 -4.429 1.00 28.15 ATOM 632 N PHE A 115 7.355 23.198 -4.500 1.00 28.52 ATOM 633 CA PHE A 115 7.090 22.749 -5.844 1.00 28.59 ATOM 634 CB PHE A 115 6.639 21.278 -5.884 1.00 28.32 ATOM 635 CG PHE A 115 5.282 21.016 -5.296 1.00 28.39 ATOM 636 CD1 PHE A 115 5.146 20.668 -3.957 1.00 28.50 ATOM 637 CD2 PHE A 115 4.146 21.035 -6.100 1.00 28.37 ATOM 638 CE1 PHE A 115 3.893 20.335 -3.424 1.00 28.65 ATOM 639 CE2 PHE A 115 2.895 20.705 -5.574 1.00 28.40 ATOM 640 CZ PHE A 115 2.772 20.353 -4.236 1.00 27.07 ATOM 641 C PHE A 115 6.036 23.706 -6.377 1.00 29.17 ATOM 642 O PHE A 115 5.249 24.266 -5.615 1.00 28.57 ATOM 643 N PHE A 116 6.064 23.943 -7.679 1.00 29.96 ATOM 644 CA PHE A 116 5.108 24.835 -8.302 1.00 31.24 ATOM 645 CB PHE A 116 5.524 26.295 -8.111 1.00 30.51 ATOM 646 CG PHE A 116 6.827 26.655 -8.767 1.00 30.38 ATOM 647 CD1 PHE A 116 8.019 26.621 -8.042 1.00 30.18 ATOM 648 CD2 PHE A 116 6.863 27.064 -10.097 1.00 29.90 ATOM 649 CE1 PHE A 116 9.233 26.993 -8.633 1.00 29.59 ATOM 650 CE2 PHE A 116 8.073 27.439 -10.699 1.00 30.05 ATOM 651 CZ PHE A 116 9.258 27.403 -9.964 1.00 29.89 ATOM 652 C PHE A 116 5.006 24.501 -9.777 1.00 32.82 ATOM 653 O PHE A 116 5.802 23.719 -10.304 1.00 32.75 ATOM 654 N TYR A 117 4.015 25.088 -10.438 1.00 34.67 ATOM 655 CA TYR A 117 3.807 24.846 -11.856 1.00 36.58 ATOM 656 CB TYR A 117 2.390 24.325 -12.089 1.00 35.04 ATOM 657 CG TYR A 117 2.118 23.032 -11.365 1.00 34.14 ATOM 658 CD1 TYR A 117 2.435 21.809 -11.950 1.00 33.63 ATOM 659 CE1 TYR A 117 2.238 20.615 -11.268 1.00 32.81 ATOM 660 CD2 TYR A 117 1.589 23.031 -10.074 1.00 33.44 ATOM 661 CE2 TYR A 117 1.389 21.847 -9.385 1.00 33.14 ATOM 662 CZ TYR A 117 1.718 20.640 -9.988 1.00 33.41 ATOM 663 OH TYR A 117 1.544 19.458 -9.311 1.00 33.01 ATOM 664 C TYR A 117 4.045 26.095 -12.682 1.00 38.53 ATOM 665 O TYR A 117 3.744 27.201 -12.250 1.00 38.88 ATOM 666 N SER A 118 4.614 25.906 -13.865 1.00 41.76 ATOM 667 CA SER A 118 4.883 26.996 -14.788 1.00 45.50 ATOM 668 CB SER A 118 6.349 27.440 -14.695 1.00 45.03 ATOM 669 OG SER A 118 7.248 26.381 -14.970 1.00 45.53 ATOM 670 C SER A 118 4.552 26.470 -16.181 1.00 48.72 ATOM 671 O SER A 118 4.611 25.263 -16.423 1.00 48.84 ATOM 672 N SER A 119 4.190 27.365 -17.093 1.00 52.97 ATOM 673 CA SER A 119 3.815 26.957 -18.447 1.00 57.24 ATOM 674 CB SER A 119 2.644 27.811 -18.951 1.00 57.62 ATOM 675 OG SER A 119 1.454 27.528 -18.234 1.00 58.54 ATOM 676 C SER A 119 4.948 27.023 -19.460 1.00 59.81 ATOM 677 O SER A 119 5.788 27.925 -19.414 1.00 60.18 ATOM 678 N GLY A 120 4.958 26.056 -20.376 1.00 62.68 ATOM 679 CA GLY A 120 5.973 26.015 -21.414 1.00 66.08 ATOM 680 C GLY A 120 5.416 26.661 -22.667 1.00 68.47 ATOM 681 O GLY A 120 4.677 26.024 -23.424 1.00 68.94 ATOM 682 N GLU A 121 5.768 27.928 -22.879 1.00 70.45 ATOM 683 CA GLU A 121 5.292 28.693 -24.030 1.00 72.45 ATOM 684 CB GLU A 121 6.138 29.957 -24.203 1.00 73.21 ATOM 685 CG GLU A 121 5.686 31.111 -23.318 1.00 74.94 ATOM 686 CD GLU A 121 4.978 30.637 -22.053 1.00 75.72 ATOM 687 OE1 GLU A 121 3.732 30.754 -21.979 1.00 76.09 ATOM 688 OE2 GLU A 121 5.671 30.145 -21.134 1.00 76.29 ATOM 689 C GLU A 121 5.267 27.909 -25.336 1.00 73.33 ATOM 690 O GLU A 121 4.466 28.207 -26.225 1.00 73.55 ATOM 691 N LYS A 122 6.133 26.906 -25.449 1.00 74.01 ATOM 692 CA LYS A 122 6.187 26.093 -26.659 1.00 74.73 ATOM 693 CB LYS A 122 7.183 24.942 -26.483 1.00 75.30 ATOM 694 CG LYS A 122 7.577 24.259 -27.785 1.00 75.72 ATOM 695 CD LYS A 122 8.128 22.862 -27.535 1.00 76.10 ATOM 696 CE LYS A 122 8.438 22.156 -28.848 1.00 76.49 ATOM 697 NZ LYS A 122 9.012 20.796 -28.633 1.00 76.53 ATOM 698 C LYS A 122 4.805 25.537 -27.014 1.00 74.71 ATOM 699 O LYS A 122 4.573 25.101 -28.144 1.00 75.10 ATOM 700 N LYS A 123 3.893 25.561 -26.046 1.00 74.16 ATOM 701 CA LYS A 123 2.535 25.066 -26.250 1.00 73.45 ATOM 702 CB LYS A 123 2.567 23.581 -26.627 1.00 73.96 ATOM 703 CG LYS A 123 1.416 23.138 -27.513 1.00 74.86 ATOM 704 CD LYS A 123 1.409 21.628 -27.694 1.00 75.79 ATOM 705 CE LYS A 123 0.005 21.112 -27.992 1.00 76.45 ATOM 706 NZ LYS A 123 0.024 19.792 -28.691 1.00 76.86 ATOM 707 C LYS A 123 1.737 25.252 -24.968 1.00 72.55 ATOM 708 O LYS A 123 2.049 26.124 -24.155 1.00 72.68 ATOM 709 N ASP A 124 0.700 24.439 -24.797 1.00 71.14 ATOM 710 CA ASP A 124 -0.121 24.496 -23.594 1.00 69.71 ATOM 711 CB ASP A 124 -1.568 24.096 -23.907 1.00 70.64 ATOM 712 CG ASP A 124 -1.707 23.415 -25.255 1.00 71.80 ATOM 713 OD1 ASP A 124 -1.458 24.079 -26.286 1.00 72.50 ATOM 714 OD2 ASP A 124 -2.066 22.216 -25.284 1.00 72.62 ATOM 715 C ASP A 124 0.507 23.501 -22.624 1.00 67.95 ATOM 716 O ASP A 124 -0.169 22.905 -21.782 1.00 68.18 ATOM 717 N GLU A 125 1.817 23.326 -22.772 1.00 65.45 ATOM 718 CA GLU A 125 2.597 22.415 -21.945 1.00 62.50 ATOM 719 CB GLU A 125 3.959 22.158 -22.600 1.00 63.41 ATOM 720 CG GLU A 125 4.245 23.050 -23.804 1.00 64.43 ATOM 721 CD GLU A 125 5.703 23.019 -24.232 1.00 65.41 ATOM 722 OE1 GLU A 125 6.125 22.014 -24.848 1.00 66.02 ATOM 723 OE2 GLU A 125 6.427 24.002 -23.954 1.00 65.72 ATOM 724 C GLU A 125 2.795 22.969 -20.535 1.00 59.69 ATOM 725 O GLU A 125 3.137 24.142 -20.355 1.00 58.90 ATOM 726 N VAL A 126 2.579 22.110 -19.543 1.00 56.50 ATOM 727 CA VAL A 126 2.728 22.487 -18.142 1.00 53.07 ATOM 728 CB VAL A 126 1.468 22.148 -17.334 1.00 52.97 ATOM 729 CG1 VAL A 126 1.692 22.467 -15.865 1.00 52.64 ATOM 730 CG2 VAL A 126 0.288 22.929 -17.872 1.00 52.94 ATOM 731 C VAL A 126 3.905 21.768 -17.501 1.00 50.65 ATOM 732 O VAL A 126 4.065 20.555 -17.652 1.00 49.97 ATOM 733 N TYR A 127 4.710 22.530 -16.768 1.00 47.97 ATOM 734 CA TYR A 127 5.884 21.992 -16.097 1.00 45.10 ATOM 735 CB TYR A 127 7.125 22.805 -16.482 1.00 46.92 ATOM 736 CG TYR A 127 7.531 22.642 -17.921 1.00 49.03 ATOM 737 CD1 TYR A 127 7.078 23.528 -18.898 1.00 49.66 ATOM 738 CE1 TYR A 127 7.414 23.352 -20.236 1.00 51.19 ATOM 739 CD2 TYR A 127 8.339 21.576 -18.316 1.00 50.21 ATOM 740 CE2 TYR A 127 8.683 21.391 -19.651 1.00 51.44 ATOM 741 CZ TYR A 127 8.214 22.280 -20.605 1.00 51.77 ATOM 742 OH TYR A 127 8.525 22.080 -21.929 1.00 53.03 ATOM 743 C TYR A 127 5.765 21.977 -14.581 1.00 42.23 ATOM 744 O TYR A 127 5.270 22.925 -13.970 1.00 41.19 ATOM 745 N LEU A 128 6.219 20.879 -13.986 1.00 39.12 ATOM 746 CA LEU A 128 6.241 20.734 -12.542 1.00 35.95 ATOM 747 CB LEU A 128 6.009 19.276 -12.143 1.00 34.35 ATOM 748 CG LEU A 128 6.405 18.893 -10.711 1.00 33.75 ATOM 749 CD1 LEU A 128 5.531 19.621 -9.697 1.00 31.71 ATOM 750 CD2 LEU A 128 6.275 17.382 -10.546 1.00 33.08 ATOM 751 C LEU A 128 7.657 21.163 -12.165 1.00 34.46 ATOM 752 O LEU A 128 8.626 20.687 -12.757 1.00 34.30 ATOM 753 N ASN A 129 7.774 22.076 -11.205 1.00 32.93 ATOM 754 CA ASN A 129 9.074 22.576 -10.761 1.00 30.64 ATOM 755 CB ASN A 129 9.114 24.100 -10.826 1.00 31.15 ATOM 756 CG ASN A 129 9.009 24.624 -12.238 1.00 32.42 ATOM 757 OD1 ASN A 129 10.008 25.045 -12.822 1.00 33.33 ATOM 758 ND2 ASN A 129 7.796 24.603 -12.800 1.00 31.15 ATOM 759 C ASN A 129 9.362 22.160 -9.335 1.00 29.38 ATOM 760 O ASN A 129 8.686 22.607 -8.413 1.00 28.19 ATOM 761 N LEU A 130 10.377 21.320 -9.153 1.00 28.52 ATOM 762 CA LEU A 130 10.754 20.860 -7.820 1.00 27.55 ATOM 763 CB LEU A 130 11.201 19.400 -7.866 1.00 26.98 ATOM 764 CG LEU A 130 10.232 18.416 -8.521 1.00 28.54 ATOM 765 CD1 LEU A 130 10.826 17.013 -8.447 1.00 29.09 ATOM 766 CD2 LEU A 130 8.884 18.457 -7.810 1.00 28.10 ATOM 767 C LEU A 130 11.882 21.719 -7.273 1.00 27.23 ATOM 768 O LEU A 130 12.974 21.765 -7.850 1.00 26.87 ATOM 769 N VAL A 131 11.619 22.405 -6.164 1.00 26.24 ATOM 770 CA VAL A 131 12.635 23.247 -5.559 1.00 25.53 ATOM 771 CB VAL A 131 12.045 24.561 -5.017 1.00 25.90 ATOM 772 CG1 VAL A 131 13.178 25.482 -4.559 1.00 25.00 ATOM 773 CG2 VAL A 131 11.219 25.241 -6.099 1.00 24.51 ATOM 774 C VAL A 131 13.307 22.470 -4.439 1.00 26.08 ATOM 775 O VAL A 131 12.717 22.213 -3.386 1.00 25.19 ATOM 776 N LEU A 132 14.561 22.100 -4.689 1.00 25.98 ATOM 777 CA LEU A 132 15.345 21.311 -3.755 1.00 26.08 ATOM 778 CB LEU A 132 15.894 20.080 -4.477 1.00 25.35 ATOM 779 CG LEU A 132 14.940 19.386 -5.446 1.00 25.52 ATOM 780 CD1 LEU A 132 15.712 18.694 -6.543 1.00 26.70 ATOM 781 CD2 LEU A 132 14.115 18.380 -4.682 1.00 25.39 ATOM 782 C LEU A 132 16.505 22.065 -3.142 1.00 26.43 ATOM 783 O LEU A 132 16.932 23.096 -3.649 1.00 27.38 ATOM 784 N ASP A 133 17.012 21.532 -2.039 1.00 27.37 ATOM 785 CA ASP A 133 18.169 22.113 -1.379 1.00 27.82 ATOM 786 CB ASP A 133 18.533 21.312 -0.130 1.00 29.19 ATOM 787 CG ASP A 133 17.884 21.849 1.114 1.00 30.19 ATOM 788 OD1 ASP A 133 17.952 21.158 2.145 1.00 31.15 ATOM 789 OD2 ASP A 133 17.313 22.961 1.067 1.00 31.65 ATOM 790 C ASP A 133 19.291 21.961 -2.393 1.00 27.56 ATOM 791 O ASP A 133 19.370 20.950 -3.093 1.00 26.15 ATOM 792 N TYR A 134 20.148 22.965 -2.488 1.00 28.00 ATOM 793 CA TYR A 134 21.262 22.877 -3.418 1.00 28.50 ATOM 794 CB TYR A 134 21.645 24.273 -3.911 1.00 29.80 ATOM 795 CG TYR A 134 22.903 24.282 -4.739 1.00 30.67 ATOM 796 CD1 TYR A 134 24.128 24.613 -4.161 1.00 31.26 ATOM 797 CE1 TYR A 134 25.303 24.579 -4.901 1.00 31.62 ATOM 798 CD2 TYR A 134 22.877 23.920 -6.086 1.00 30.39 ATOM 799 CE2 TYR A 134 24.045 23.883 -6.836 1.00 31.56 ATOM 800 CZ TYR A 134 25.257 24.213 -6.227 1.00 31.59 ATOM 801 OH TYR A 134 26.428 24.157 -6.938 1.00 33.16 ATOM 802 C TYR A 134 22.461 22.197 -2.735 1.00 27.38 ATOM 803 O TYR A 134 22.808 22.519 -1.593 1.00 27.26 ATOM 804 N VAL A 135 23.051 21.223 -3.426 1.00 26.58 ATOM 805 CA VAL A 135 24.222 20.501 -2.930 1.00 25.64 ATOM 806 CB VAL A 135 23.914 19.026 -2.658 1.00 25.27 ATOM 807 CG1 VAL A 135 25.068 18.392 -1.888 1.00 24.98 ATOM 808 CG2 VAL A 135 22.637 18.915 -1.846 1.00 24.87 ATOM 809 C VAL A 135 25.273 20.637 -4.028 1.00 25.59 ATOM 810 O VAL A 135 25.034 20.269 -5.170 1.00 24.61 ATOM 811 N PRO A 136 26.466 21.143 -3.678 1.00 25.96 ATOM 812 CD PRO A 136 26.839 21.484 -2.292 1.00 25.46 ATOM 813 CA PRO A 136 27.579 21.371 -4.610 1.00 26.62 ATOM 814 CB PRO A 136 28.618 22.091 -3.752 1.00 25.96 ATOM 815 CG PRO A 136 28.327 21.639 -2.368 1.00 26.30 ATOM 816 C PRO A 136 28.218 20.240 -5.417 1.00 27.21 ATOM 817 O PRO A 136 28.534 20.431 -6.592 1.00 28.56 ATOM 818 N GLU A 137 28.416 19.076 -4.813 1.00 26.62 ATOM 819 CA GLU A 137 29.077 17.979 -5.521 1.00 26.50 ATOM 820 CB GLU A 137 30.414 17.673 -4.833 1.00 27.45 ATOM 821 CG GLU A 137 31.450 18.752 -4.996 1.00 31.28 ATOM 822 CD GLU A 137 31.997 18.798 -6.415 1.00 34.47 ATOM 823 OE1 GLU A 137 32.716 19.766 -6.750 1.00 36.03 ATOM 824 OE2 GLU A 137 31.705 17.864 -7.199 1.00 35.75 ATOM 825 C GLU A 137 28.276 16.686 -5.610 1.00 25.35 ATOM 826 O GLU A 137 27.145 16.605 -5.149 1.00 24.71 ATOM 827 N THR A 138 28.896 15.677 -6.214 1.00 24.38 ATOM 828 CA THR A 138 28.310 14.349 -6.343 1.00 23.52 ATOM 829 CB THR A 138 27.732 14.080 -7.738 1.00 23.34 ATOM 830 OG1 THR A 138 28.803 14.032 -8.684 1.00 24.40 ATOM 831 CG2 THR A 138 26.735 15.159 -8.138 1.00 22.69 ATOM 832 C THR A 138 29.466 13.388 -6.127 1.00 23.53 ATOM 833 O THR A 138 30.630 13.761 -6.302 1.00 23.13 ATOM 834 N VAL A 139 29.148 12.160 -5.742 1.00 22.56 ATOM 835 CA VAL A 139 30.161 11.144 -5.500 1.00 23.28 ATOM 836 CB VAL A 139 29.511 9.837 -4.975 1.00 22.91 ATOM 837 CG1 VAL A 139 30.454 8.655 -5.169 1.00 22.16 ATOM 838 CG2 VAL A 139 29.145 10.003 -3.497 1.00 22.15 ATOM 839 C VAL A 139 30.871 10.868 -6.811 1.00 24.01 ATOM 840 O VAL A 139 32.046 10.499 -6.837 1.00 23.65 ATOM 841 N TYR A 140 30.146 11.053 -7.902 1.00 24.72 ATOM 842 CA TYR A 140 30.704 10.826 -9.222 1.00 27.21 ATOM 843 CB TYR A 140 29.623 11.033 -10.273 1.00 28.10 ATOM 844 CG TYR A 140 30.155 10.977 -11.676 1.00 30.46 ATOM 845 CD1 TYR A 140 30.370 12.144 -12.405 1.00 31.44 ATOM 846 CE1 TYR A 140 30.849 12.097 -13.706 1.00 32.93 ATOM 847 CD2 TYR A 140 30.436 9.759 -12.283 1.00 30.97 ATOM 848 CE2 TYR A 140 30.914 9.700 -13.583 1.00 32.91 ATOM 849 CZ TYR A 140 31.114 10.871 -14.288 1.00 33.09 ATOM 850 OH TYR A 140 31.552 10.813 -15.589 1.00 35.94 ATOM 851 C TYR A 140 31.888 11.756 -9.516 1.00 28.18 ATOM 852 O TYR A 140 32.979 11.298 -9.856 1.00 27.84 ATOM 853 N ARG A 141 31.661 13.060 -9.387 1.00 28.89 ATOM 854 CA ARG A 141 32.696 14.058 -9.646 1.00 30.14 ATOM 855 CB ARG A 141 32.124 15.461 -9.491 1.00 31.89 ATOM 856 CG ARG A 141 31.260 15.918 -10.638 1.00 35.47 ATOM 857 CD ARG A 141 30.595 17.245 -10.281 1.00 39.66 ATOM 858 NE ARG A 141 29.253 17.338 -10.847 1.00 43.83 ATOM 859 CZ ARG A 141 28.265 18.064 -10.330 1.00 45.83 ATOM 860 NH1 ARG A 141 28.461 18.771 -9.220 1.00 46.70 ATOM 861 NH2 ARG A 141 27.079 18.089 -10.930 1.00 47.05 ATOM 862 C ARG A 141 33.885 13.908 -8.710 1.00 29.65 ATOM 863 O ARG A 141 35.027 13.966 -9.143 1.00 29.54 ATOM 864 N VAL A 142 33.607 13.729 -7.425 1.00 29.41 ATOM 865 CA VAL A 142 34.660 13.578 -6.433 1.00 29.62 ATOM 866 CB VAL A 142 34.069 13.459 -5.002 1.00 29.58 ATOM 867 CG1 VAL A 142 35.102 12.893 -4.036 1.00 28.88 ATOM 868 CG2 VAL A 142 33.606 14.845 -4.521 1.00 29.14 ATOM 869 C VAL A 142 35.514 12.359 -6.759 1.00 30.38 ATOM 870 O VAL A 142 36.742 12.458 -6.806 1.00 30.31 ATOM 871 N ALA A 143 34.863 11.221 -6.998 1.00 30.23 ATOM 872 CA ALA A 143 35.573 9.989 -7.338 1.00 30.93 ATOM 873 CB ALA A 143 34.586 8.837 -7.508 1.00 28.80 ATOM 874 C ALA A 143 36.391 10.164 -8.622 1.00 31.66 ATOM 875 O ALA A 143 37.483 9.616 -8.745 1.00 31.55 ATOM 876 N ARG A 144 35.851 10.916 -9.575 1.00 33.11 ATOM 877 CA ARG A 144 36.542 11.155 -10.835 1.00 34.96 ATOM 878 CB ARG A 144 35.632 11.902 -11.805 1.00 35.90 ATOM 879 CG ARG A 144 36.124 11.880 -13.237 1.00 39.00 ATOM 880 CD ARG A 144 35.184 12.639 -14.164 1.00 41.49 ATOM 881 NE ARG A 144 34.745 13.904 -13.580 1.00 44.08 ATOM 882 CZ ARG A 144 33.850 14.715 -14.140 1.00 45.98 ATOM 883 NH1 ARG A 144 33.296 14.389 -15.306 1.00 47.07 ATOM 884 NH2 ARG A 144 33.503 15.850 -13.538 1.00 46.16 ATOM 885 C ARG A 144 37.819 11.957 -10.598 1.00 35.42 ATOM 886 O ARG A 144 38.814 11.762 -11.286 1.00 35.76 ATOM 887 N HIS A 145 37.786 12.858 -9.623 1.00 36.36 ATOM 888 CA HIS A 145 38.957 13.664 -9.302 1.00 36.77 ATOM 889 CB HIS A 145 38.643 14.660 -8.177 1.00 38.31 ATOM 890 CG HIS A 145 39.857 15.133 -7.431 1.00 40.00 ATOM 891 CD2 HIS A 145 40.497 14.620 -6.351 1.00 40.68 ATOM 892 ND1 HIS A 145 40.567 16.258 -7.795 1.00 40.69 ATOM 893 CE1 HIS A 145 41.590 16.418 -6.975 1.00 40.63 ATOM 894 NE2 HIS A 145 41.572 15.438 -6.089 1.00 40.75 ATOM 895 C HIS A 145 40.092 12.748 -8.859 1.00 36.37 ATOM 896 O HIS A 145 41.203 12.821 -9.386 1.00 36.46 ATOM 897 N TYR A 146 39.812 11.892 -7.883 1.00 35.15 ATOM 898 CA TYR A 146 40.824 10.981 -7.384 1.00 34.90 ATOM 899 CB TYR A 146 40.299 10.226 -6.166 1.00 32.11 ATOM 900 CG TYR A 146 40.217 11.095 -4.931 1.00 30.24 ATOM 901 CD1 TYR A 146 39.071 11.847 -4.658 1.00 29.36 ATOM 902 CE1 TYR A 146 39.001 12.680 -3.536 1.00 27.05 ATOM 903 CD2 TYR A 146 41.297 11.196 -4.046 1.00 28.26 ATOM 904 CE2 TYR A 146 41.235 12.022 -2.929 1.00 26.89 ATOM 905 CZ TYR A 146 40.085 12.759 -2.681 1.00 26.99 ATOM 906 OH TYR A 146 40.004 13.558 -1.568 1.00 27.24 ATOM 907 C TYR A 146 41.269 10.007 -8.463 1.00 36.70 ATOM 908 O TYR A 146 42.438 9.625 -8.522 1.00 37.24 ATOM 909 N SER A 147 40.338 9.608 -9.319 1.00 38.06 ATOM 910 CA SER A 147 40.646 8.686 -10.402 1.00 40.06 ATOM 911 CB SER A 147 39.383 8.382 -11.198 1.00 40.16 ATOM 912 OG SER A 147 39.205 6.989 -11.313 1.00 42.19 ATOM 913 C SER A 147 41.682 9.306 -11.330 1.00 41.13 ATOM 914 O SER A 147 42.711 8.701 -11.641 1.00 41.03 ATOM 915 N ARG A 148 41.391 10.525 -11.766 1.00 42.69 ATOM 916 CA ARG A 148 42.267 11.258 -12.660 1.00 44.39 ATOM 917 CB ARG A 148 41.618 12.583 -13.040 1.00 45.02 ATOM 918 CG ARG A 148 40.479 12.434 -14.019 1.00 46.57 ATOM 919 CD ARG A 148 39.630 13.693 -14.059 1.00 49.20 ATOM 920 NE ARG A 148 38.806 13.772 -15.266 1.00 51.11 ATOM 921 CZ ARG A 148 37.864 14.694 -15.474 1.00 52.15 ATOM 922 NH1 ARG A 148 37.619 15.623 -14.553 1.00 51.79 ATOM 923 NH2 ARG A 148 37.165 14.685 -16.605 1.00 52.23 ATOM 924 C ARG A 148 43.630 11.510 -12.025 1.00 45.40 ATOM 925 O ARG A 148 44.661 11.338 -12.675 1.00 46.42 ATOM 926 N ALA A 149 43.636 11.917 -10.759 1.00 45.47 ATOM 927 CA ALA A 149 44.883 12.188 -10.052 1.00 45.59 ATOM 928 CB ALA A 149 44.604 12.971 -8.769 1.00 45.27 ATOM 929 C ALA A 149 45.598 10.891 -9.714 1.00 45.86 ATOM 930 O ALA A 149 46.609 10.902 -9.012 1.00 46.26 ATOM 931 N LYS A 150 45.071 9.776 -10.216 1.00 46.10 ATOM 932 CA LYS A 150 45.650 8.467 -9.945 1.00 46.54 ATOM 933 CB LYS A 150 47.005 8.344 -10.642 1.00 47.99 ATOM 934 CG LYS A 150 47.079 9.095 -11.964 1.00 49.97 ATOM 935 CD LYS A 150 48.168 8.539 -12.866 1.00 51.89 ATOM 936 CE LYS A 150 48.155 9.230 -14.223 1.00 53.41 ATOM 937 NZ LYS A 150 49.481 9.149 -14.912 1.00 55.03 ATOM 938 C LYS A 150 45.809 8.292 -8.433 1.00 46.28 ATOM 939 O LYS A 150 46.779 7.706 -7.956 1.00 46.02 ATOM 940 N GLN A 151 44.839 8.816 -7.691 1.00 45.95 ATOM 941 CA GLN A 151 44.831 8.747 -6.235 1.00 45.47 ATOM 942 CB GLN A 151 44.757 10.158 -5.644 1.00 47.17 ATOM 943 CG GLN A 151 46.092 10.788 -5.322 1.00 49.84 ATOM 944 CD GLN A 151 46.869 9.972 -4.314 1.00 52.18 ATOM 945 OE1 GLN A 151 46.293 9.163 -3.577 1.00 53.98 ATOM 946 NE2 GLN A 151 48.185 10.173 -4.274 1.00 53.18 ATOM 947 C GLN A 151 43.615 7.955 -5.767 1.00 44.73 ATOM 948 O GLN A 151 42.608 7.854 -6.475 1.00 44.73 ATOM 949 N THR A 152 43.713 7.401 -4.566 1.00 43.32 ATOM 950 CA THR A 152 42.619 6.635 -3.977 1.00 42.05 ATOM 951 CB THR A 152 43.149 5.486 -3.091 1.00 43.35 ATOM 952 OG1 THR A 152 43.995 4.624 -3.866 1.00 45.83 ATOM 953 CG2 THR A 152 41.993 4.692 -2.499 1.00 44.54 ATOM 954 C THR A 152 41.822 7.562 -3.065 1.00 39.13 ATOM 955 O THR A 152 42.406 8.390 -2.367 1.00 39.28 ATOM 956 N LEU A 153 40.499 7.443 -3.068 1.00 35.55 ATOM 957 CA LEU A 153 39.703 8.272 -2.170 1.00 32.33 ATOM 958 CB LEU A 153 38.207 8.202 -2.524 1.00 31.29 ATOM 959 CG LEU A 153 37.232 8.780 -1.489 1.00 30.82 ATOM 960 CD1 LEU A 153 37.295 10.299 -1.493 1.00 29.78 ATOM 961 CD2 LEU A 153 35.817 8.307 -1.790 1.00 31.40 ATOM 962 C LEU A 153 39.952 7.692 -0.770 1.00 30.38 ATOM 963 O LEU A 153 39.769 6.484 -0.550 1.00 29.90 ATOM 964 N PRO A 154 40.421 8.528 0.177 1.00 28.46 ATOM 965 CD PRO A 154 40.744 9.959 0.015 1.00 28.42 ATOM 966 CA PRO A 154 40.685 8.063 1.543 1.00 27.51 ATOM 967 CB PRO A 154 40.919 9.352 2.324 1.00 27.43 ATOM 968 CG PRO A 154 41.448 10.306 1.301 1.00 27.37 ATOM 969 C PRO A 154 39.510 7.250 2.091 1.00 27.59 ATOM 970 O PRO A 154 38.348 7.644 1.952 1.00 26.68 ATOM 971 N VAL A 155 39.820 6.113 2.710 1.00 26.80 ATOM 972 CA VAL A 155 38.799 5.232 3.249 1.00 26.31 ATOM 973 CB VAL A 155 39.440 3.993 3.907 1.00 26.95 ATOM 974 CG1 VAL A 155 38.366 2.999 4.310 1.00 27.65 ATOM 975 CG2 VAL A 155 40.387 3.324 2.918 1.00 28.65 ATOM 976 C VAL A 155 37.858 5.904 4.246 1.00 25.84 ATOM 977 O VAL A 155 36.714 5.479 4.408 1.00 26.11 ATOM 978 N ILE A 156 38.320 6.949 4.921 1.00 24.30 ATOM 979 CA ILE A 156 37.452 7.604 5.881 1.00 23.52 ATOM 980 CB ILE A 156 38.189 8.766 6.623 1.00 23.27 ATOM 981 CG2 ILE A 156 38.646 9.822 5.637 1.00 22.62 ATOM 982 CG1 ILE A 156 37.264 9.390 7.669 1.00 23.31 ATOM 983 CD1 ILE A 156 36.464 8.371 8.505 1.00 23.54 ATOM 984 C ILE A 156 36.215 8.119 5.135 1.00 22.92 ATOM 985 O ILE A 156 35.105 8.022 5.647 1.00 22.86 ATOM 986 N TYR A 157 36.410 8.641 3.924 1.00 22.81 ATOM 987 CA TYR A 157 35.299 9.151 3.115 1.00 23.04 ATOM 988 CB TYR A 157 35.803 10.012 1.964 1.00 23.72 ATOM 989 CG TYR A 157 36.464 11.298 2.396 1.00 26.12 ATOM 990 CD1 TYR A 157 37.808 11.528 2.123 1.00 26.89 ATOM 991 CE1 TYR A 157 38.439 12.694 2.534 1.00 28.39 ATOM 992 CD2 TYR A 157 35.756 12.272 3.094 1.00 26.00 ATOM 993 CE2 TYR A 157 36.376 13.447 3.512 1.00 28.59 ATOM 994 CZ TYR A 157 37.724 13.650 3.225 1.00 29.22 ATOM 995 OH TYR A 157 38.355 14.811 3.615 1.00 30.61 ATOM 996 C TYR A 157 34.469 8.010 2.534 1.00 23.09 ATOM 997 O TYR A 157 33.252 8.142 2.368 1.00 23.40 ATOM 998 N VAL A 158 35.117 6.900 2.193 1.00 22.16 ATOM 999 CA VAL A 158 34.378 5.759 1.660 1.00 21.35 ATOM 1000 CB VAL A 158 35.324 4.600 1.259 1.00 21.81 ATOM 1001 CG1 VAL A 158 34.510 3.400 0.769 1.00 22.05 ATOM 1002 CG2 VAL A 158 36.274 5.074 0.158 1.00 22.14 ATOM 1003 C VAL A 158 33.396 5.284 2.740 1.00 20.53 ATOM 1004 O VAL A 158 32.265 4.911 2.438 1.00 19.30 ATOM 1005 N LYS A 159 33.836 5.312 3.999 1.00 19.27 ATOM 1006 CA LYS A 159 32.998 4.907 5.125 1.00 19.85 ATOM 1007 CB LYS A 159 33.825 4.832 6.418 1.00 20.24 ATOM 1008 CG LYS A 159 34.848 3.714 6.437 1.00 21.59 ATOM 1009 CD LYS A 159 35.770 3.817 7.643 1.00 22.00 ATOM 1010 CE LYS A 159 36.592 2.541 7.796 1.00 23.81 ATOM 1011 NZ LYS A 159 37.572 2.586 8.919 1.00 25.18 ATOM 1012 C LYS A 159 31.870 5.917 5.317 1.00 19.48 ATOM 1013 O LYS A 159 30.701 5.547 5.413 1.00 19.97 ATOM 1014 N LEU A 160 32.228 7.195 5.366 1.00 19.05 ATOM 1015 CA LEU A 160 31.249 8.253 5.558 1.00 19.12 ATOM 1016 CB LEU A 160 31.944 9.618 5.588 1.00 18.80 ATOM 1017 CG LEU A 160 32.569 10.021 6.932 1.00 20.26 ATOM 1018 CD1 LEU A 160 33.498 11.233 6.730 1.00 19.31 ATOM 1019 CD2 LEU A 160 31.464 10.348 7.943 1.00 19.28 ATOM 1020 C LEU A 160 30.158 8.276 4.492 1.00 19.64 ATOM 1021 O LEU A 160 28.974 8.328 4.822 1.00 20.10 ATOM 1022 N TYR A 161 30.561 8.252 3.222 1.00 19.28 ATOM 1023 CA TYR A 161 29.616 8.298 2.111 1.00 19.71 ATOM 1024 CB TYR A 161 30.365 8.482 0.779 1.00 21.35 ATOM 1025 CG TYR A 161 31.142 9.781 0.706 1.00 23.77 ATOM 1026 CD1 TYR A 161 30.869 10.818 1.595 1.00 24.89 ATOM 1027 CE1 TYR A 161 31.585 12.006 1.563 1.00 28.54 ATOM 1028 CD2 TYR A 161 32.166 9.964 -0.231 1.00 25.20 ATOM 1029 CE2 TYR A 161 32.900 11.163 -0.273 1.00 26.86 ATOM 1030 CZ TYR A 161 32.598 12.176 0.629 1.00 28.11 ATOM 1031 OH TYR A 161 33.271 13.383 0.609 1.00 32.03 ATOM 1032 C TYR A 161 28.733 7.059 2.036 1.00 19.15 ATOM 1033 O TYR A 161 27.520 7.172 1.864 1.00 18.74 ATOM 1034 N MET A 162 29.338 5.885 2.167 1.00 17.57 ATOM 1035 CA MET A 162 28.586 4.634 2.101 1.00 18.05 ATOM 1036 CB MET A 162 29.556 3.454 1.998 1.00 17.96 ATOM 1037 CG MET A 162 30.296 3.394 0.653 1.00 18.97 ATOM 1038 SD MET A 162 29.215 3.374 -0.806 1.00 21.56 ATOM 1039 CE MET A 162 28.184 1.913 -0.438 1.00 20.30 ATOM 1040 C MET A 162 27.623 4.430 3.277 1.00 16.83 ATOM 1041 O MET A 162 26.528 3.908 3.104 1.00 17.01 ATOM 1042 N TYR A 163 28.037 4.830 4.472 1.00 16.39 ATOM 1043 CA TYR A 163 27.192 4.700 5.653 1.00 15.85 ATOM 1044 CB TYR A 163 27.953 5.159 6.897 1.00 15.59 ATOM 1045 CG TYR A 163 27.106 5.211 8.156 1.00 15.81 ATOM 1046 CD1 TYR A 163 26.440 6.376 8.525 1.00 16.49 ATOM 1047 CE1 TYR A 163 25.689 6.433 9.716 1.00 16.82 ATOM 1048 CD2 TYR A 163 27.001 4.099 8.997 1.00 15.74 ATOM 1049 CE2 TYR A 163 26.263 4.147 10.175 1.00 15.45 ATOM 1050 CZ TYR A 163 25.611 5.315 10.532 1.00 16.15 ATOM 1051 OH TYR A 163 24.896 5.371 11.714 1.00 17.48 ATOM 1052 C TYR A 163 25.944 5.558 5.482 1.00 16.43 ATOM 1053 O TYR A 163 24.825 5.117 5.780 1.00 17.25 ATOM 1054 N GLN A 164 26.139 6.788 5.014 1.00 15.60 ATOM 1055 CA GLN A 164 25.029 7.700 4.806 1.00 15.90 ATOM 1056 CB GLN A 164 25.563 9.106 4.524 1.00 15.39 ATOM 1057 CG GLN A 164 26.264 9.723 5.731 1.00 15.45 ATOM 1058 CD GLN A 164 26.893 11.065 5.420 1.00 17.41 ATOM 1059 OE1 GLN A 164 28.076 11.144 5.054 1.00 18.49 ATOM 1060 NE2 GLN A 164 26.112 12.131 5.554 1.00 14.51 ATOM 1061 C GLN A 164 24.107 7.206 3.680 1.00 16.86 ATOM 1062 O GLN A 164 22.890 7.399 3.743 1.00 16.51 ATOM 1063 N LEU A 165 24.670 6.556 2.663 1.00 16.41 ATOM 1064 CA LEU A 165 23.835 6.029 1.590 1.00 16.98 ATOM 1065 CB LEU A 165 24.700 5.478 0.450 1.00 16.11 ATOM 1066 CG LEU A 165 23.991 4.532 -0.535 1.00 16.68 ATOM 1067 CD1 LEU A 165 22.811 5.255 -1.192 1.00 15.35 ATOM 1068 CD2 LEU A 165 24.987 4.079 -1.599 1.00 15.66 ATOM 1069 C LEU A 165 22.962 4.899 2.171 1.00 17.26 ATOM 1070 O LEU A 165 21.764 4.821 1.896 1.00 17.68 ATOM 1071 N PHE A 166 23.561 4.021 2.972 1.00 17.06 ATOM 1072 CA PHE A 166 22.802 2.928 3.556 1.00 17.54 ATOM 1073 CB PHE A 166 23.750 1.977 4.288 1.00 18.43 ATOM 1074 CG PHE A 166 24.502 1.074 3.361 1.00 18.40 ATOM 1075 CD1 PHE A 166 25.894 1.031 3.379 1.00 20.25 ATOM 1076 CD2 PHE A 166 23.814 0.288 2.435 1.00 19.27 ATOM 1077 CE1 PHE A 166 26.604 0.214 2.478 1.00 20.33 ATOM 1078 CE2 PHE A 166 24.502 -0.533 1.527 1.00 20.56 ATOM 1079 CZ PHE A 166 25.905 -0.570 1.547 1.00 20.56 ATOM 1080 C PHE A 166 21.684 3.433 4.478 1.00 18.11 ATOM 1081 O PHE A 166 20.598 2.845 4.531 1.00 17.58 ATOM 1082 N ARG A 167 21.940 4.530 5.187 1.00 17.44 ATOM 1083 CA ARG A 167 20.927 5.112 6.062 1.00 17.09 ATOM 1084 CB ARG A 167 21.496 6.274 6.871 1.00 15.86 ATOM 1085 CG ARG A 167 22.192 5.846 8.144 1.00 16.59 ATOM 1086 CD ARG A 167 22.353 7.030 9.098 1.00 18.01 ATOM 1087 NE ARG A 167 21.071 7.451 9.662 1.00 17.07 ATOM 1088 CZ ARG A 167 20.852 8.613 10.266 1.00 17.68 ATOM 1089 NH1 ARG A 167 21.839 9.498 10.392 1.00 16.70 ATOM 1090 NH2 ARG A 167 19.648 8.877 10.767 1.00 17.58 ATOM 1091 C ARG A 167 19.777 5.617 5.204 1.00 17.40 ATOM 1092 O ARG A 167 18.613 5.415 5.555 1.00 19.23 ATOM 1093 N SER A 168 20.080 6.270 4.082 1.00 16.51 ATOM 1094 CA SER A 168 19.002 6.759 3.224 1.00 16.24 ATOM 1095 CB SER A 168 19.541 7.660 2.094 1.00 15.85 ATOM 1096 OG SER A 168 20.198 6.919 1.083 1.00 15.67 ATOM 1097 C SER A 168 18.189 5.584 2.647 1.00 16.31 ATOM 1098 O SER A 168 16.970 5.685 2.517 1.00 16.30 ATOM 1099 N LEU A 169 18.850 4.470 2.330 1.00 16.06 ATOM 1100 CA LEU A 169 18.155 3.301 1.787 1.00 16.01 ATOM 1101 CB LEU A 169 19.158 2.318 1.169 1.00 14.70 ATOM 1102 CG LEU A 169 19.911 2.815 -0.079 1.00 15.51 ATOM 1103 CD1 LEU A 169 20.802 1.695 -0.603 1.00 14.31 ATOM 1104 CD2 LEU A 169 18.928 3.295 -1.160 1.00 15.00 ATOM 1105 C LEU A 169 17.314 2.592 2.866 1.00 17.47 ATOM 1106 O LEU A 169 16.212 2.108 2.583 1.00 17.58 ATOM 1107 N ALA A 170 17.831 2.517 4.094 1.00 17.46 ATOM 1108 CA ALA A 170 17.087 1.904 5.195 1.00 17.21 ATOM 1109 CB ALA A 170 17.908 1.937 6.479 1.00 16.12 ATOM 1110 C ALA A 170 15.809 2.733 5.369 1.00 18.02 ATOM 1111 O ALA A 170 14.714 2.202 5.541 1.00 17.57 ATOM 1112 N TYR A 171 15.951 4.048 5.313 1.00 17.60 ATOM 1113 CA TYR A 171 14.797 4.913 5.456 1.00 18.37 ATOM 1114 CB TYR A 171 15.243 6.381 5.504 1.00 17.95 ATOM 1115 CG TYR A 171 14.099 7.359 5.647 1.00 18.41 ATOM 1116 CD1 TYR A 171 13.638 8.074 4.549 1.00 18.33 ATOM 1117 CE1 TYR A 171 12.587 8.972 4.660 1.00 18.84 ATOM 1118 CD2 TYR A 171 13.472 7.566 6.881 1.00 18.79 ATOM 1119 CE2 TYR A 171 12.404 8.474 7.005 1.00 19.73 ATOM 1120 CZ TYR A 171 11.973 9.171 5.888 1.00 19.96 ATOM 1121 OH TYR A 171 10.935 10.084 5.985 1.00 21.91 ATOM 1122 C TYR A 171 13.745 4.703 4.345 1.00 19.72 ATOM 1123 O TYR A 171 12.605 4.339 4.643 1.00 20.72 ATOM 1124 N ILE A 172 14.097 4.902 3.074 1.00 18.13 ATOM 1125 CA ILE A 172 13.081 4.722 2.027 1.00 18.23 ATOM 1126 CB ILE A 172 13.577 5.159 0.607 1.00 17.80 ATOM 1127 CG2 ILE A 172 13.970 6.618 0.640 1.00 17.91 ATOM 1128 CG1 ILE A 172 14.732 4.275 0.119 1.00 17.28 ATOM 1129 CD1 ILE A 172 15.142 4.550 -1.355 1.00 17.39 ATOM 1130 C ILE A 172 12.534 3.300 1.947 1.00 18.37 ATOM 1131 O ILE A 172 11.347 3.099 1.681 1.00 18.46 ATOM 1132 N HIS A 173 13.384 2.314 2.193 1.00 18.18 ATOM 1133 CA HIS A 173 12.943 0.925 2.140 1.00 19.68 ATOM 1134 CB HIS A 173 14.138 -0.019 2.254 1.00 18.63 ATOM 1135 CG HIS A 173 14.968 -0.083 1.008 1.00 19.23 ATOM 1136 CD2 HIS A 173 14.863 0.583 -0.168 1.00 19.15 ATOM 1137 ND1 HIS A 173 16.060 -0.914 0.880 1.00 18.79 ATOM 1138 CE1 HIS A 173 16.592 -0.760 -0.320 1.00 19.72 ATOM 1139 NE2 HIS A 173 15.885 0.144 -0.977 1.00 20.56 ATOM 1140 C HIS A 173 11.931 0.595 3.237 1.00 21.37 ATOM 1141 O HIS A 173 11.135 -0.335 3.085 1.00 21.59 ATOM 1142 N SER A 174 11.959 1.347 4.336 1.00 21.62 ATOM 1143 CA SER A 174 11.028 1.095 5.428 1.00 22.95 ATOM 1144 CB SER A 174 11.475 1.826 6.705 1.00 20.95 ATOM 1145 OG SER A 174 11.297 3.225 6.608 1.00 18.76 ATOM 1146 C SER A 174 9.619 1.516 5.017 1.00 24.60 ATOM 1147 O SER A 174 8.643 1.161 5.670 1.00 27.06 ATOM 1148 N PHE A 175 9.512 2.269 3.927 1.00 25.37 ATOM 1149 CA PHE A 175 8.214 2.698 3.421 1.00 25.33 ATOM 1150 CB PHE A 175 8.259 4.159 2.974 1.00 26.77 ATOM 1151 CG PHE A 175 8.347 5.134 4.107 1.00 29.67 ATOM 1152 CD1 PHE A 175 7.256 5.337 4.952 1.00 31.08 ATOM 1153 CD2 PHE A 175 9.534 5.814 4.366 1.00 29.55 ATOM 1154 CE1 PHE A 175 7.349 6.201 6.049 1.00 32.42 ATOM 1155 CE2 PHE A 175 9.638 6.675 5.453 1.00 31.71 ATOM 1156 CZ PHE A 175 8.546 6.870 6.299 1.00 31.95 ATOM 1157 C PHE A 175 7.844 1.833 2.219 1.00 25.48 ATOM 1158 O PHE A 175 6.827 2.071 1.572 1.00 26.27 ATOM 1159 N GLY A 176 8.671 0.829 1.930 1.00 24.75 ATOM 1160 CA GLY A 176 8.428 -0.047 0.792 1.00 23.82 ATOM 1161 C GLY A 176 8.872 0.578 -0.524 1.00 23.89 ATOM 1162 O GLY A 176 8.609 0.036 -1.603 1.00 23.00 ATOM 1163 N ILE A 177 9.554 1.721 -0.434 1.00 23.47 ATOM 1164 CA ILE A 177 10.027 2.450 -1.615 1.00 22.61 ATOM 1165 CB ILE A 177 9.983 3.981 -1.357 1.00 22.92 ATOM 1166 CG2 ILE A 177 10.534 4.755 -2.550 1.00 20.53 ATOM 1167 CG1 ILE A 177 8.539 4.413 -1.093 1.00 22.77 ATOM 1168 CD1 ILE A 177 8.401 5.874 -0.740 1.00 24.62 ATOM 1169 C ILE A 177 11.442 2.043 -2.036 1.00 22.50 ATOM 1170 O ILE A 177 12.376 2.053 -1.229 1.00 22.15 ATOM 1171 N CYS A 178 11.578 1.676 -3.307 1.00 22.00 ATOM 1172 CA CYS A 178 12.863 1.279 -3.894 1.00 21.34 ATOM 1173 CB CYS A 178 12.703 -0.022 -4.701 1.00 21.72 ATOM 1174 SG CYS A 178 14.236 -0.752 -5.354 1.00 22.67 ATOM 1175 C CYS A 178 13.273 2.424 -4.825 1.00 20.63 ATOM 1176 O CYS A 178 12.469 2.894 -5.632 1.00 19.98 ATOM 1177 N HIS A 179 14.517 2.879 -4.703 1.00 19.37 ATOM 1178 CA HIS A 179 15.000 3.976 -5.530 1.00 17.64 ATOM 1179 CB HIS A 179 16.338 4.484 -4.980 1.00 16.72 ATOM 1180 CG HIS A 179 16.926 5.611 -5.768 1.00 17.12 ATOM 1181 CD2 HIS A 179 17.522 5.631 -6.982 1.00 16.35 ATOM 1182 ND1 HIS A 179 16.906 6.918 -5.326 1.00 17.51 ATOM 1183 CE1 HIS A 179 17.468 7.695 -6.235 1.00 16.31 ATOM 1184 NE2 HIS A 179 17.850 6.937 -7.250 1.00 18.06 ATOM 1185 C HIS A 179 15.135 3.564 -7.005 1.00 17.71 ATOM 1186 O HIS A 179 14.746 4.315 -7.894 1.00 17.07 ATOM 1187 N ARG A 180 15.689 2.375 -7.248 1.00 17.94 ATOM 1188 CA ARG A 180 15.857 1.822 -8.599 1.00 19.30 ATOM 1189 CB ARG A 180 14.501 1.734 -9.298 1.00 18.70 ATOM 1190 CG ARG A 180 13.452 0.947 -8.502 1.00 18.75 ATOM 1191 CD ARG A 180 12.455 0.295 -9.432 1.00 17.91 ATOM 1192 NE ARG A 180 11.589 1.284 -10.064 1.00 19.60 ATOM 1193 CZ ARG A 180 10.575 0.981 -10.869 1.00 19.81 ATOM 1194 NH1 ARG A 180 10.291 -0.288 -11.147 1.00 19.83 ATOM 1195 NH2 ARG A 180 9.832 1.949 -11.385 1.00 20.87 ATOM 1196 C ARG A 180 16.862 2.501 -9.547 1.00 20.48 ATOM 1197 O ARG A 180 16.934 2.149 -10.732 1.00 21.16 ATOM 1198 N ASP A 181 17.632 3.459 -9.041 1.00 19.97 ATOM 1199 CA ASP A 181 18.639 4.125 -9.868 1.00 19.94 ATOM 1200 CB ASP A 181 18.024 5.315 -10.610 1.00 21.38 ATOM 1201 CG ASP A 181 18.869 5.770 -11.788 1.00 23.19 ATOM 1202 OD1 ASP A 181 19.688 4.962 -12.294 1.00 25.22 ATOM 1203 OD2 ASP A 181 18.708 6.935 -12.209 1.00 24.08 ATOM 1204 C ASP A 181 19.807 4.595 -9.008 1.00 18.92 ATOM 1205 O ASP A 181 20.253 5.738 -9.115 1.00 18.65 ATOM 1206 N ILE A 182 20.296 3.712 -8.142 1.00 18.49 ATOM 1207 CA ILE A 182 21.414 4.061 -7.281 1.00 17.66 ATOM 1208 CB ILE A 182 21.537 3.081 -6.084 1.00 17.54 ATOM 1209 CG2 ILE A 182 22.824 3.370 -5.293 1.00 17.12 ATOM 1210 CG1 ILE A 182 20.298 3.192 -5.173 1.00 16.31 ATOM 1211 CD1 ILE A 182 20.090 4.561 -4.519 1.00 14.50 ATOM 1212 C ILE A 182 22.693 4.051 -8.118 1.00 18.20 ATOM 1213 O ILE A 182 23.036 3.043 -8.751 1.00 18.28 ATOM 1214 N LYS A 183 23.367 5.201 -8.145 1.00 18.27 ATOM 1215 CA LYS A 183 24.614 5.380 -8.889 1.00 18.05 ATOM 1216 CB LYS A 183 24.313 5.494 -10.387 1.00 16.98 ATOM 1217 CG LYS A 183 23.503 6.703 -10.772 1.00 17.54 ATOM 1218 CD LYS A 183 23.258 6.681 -12.256 1.00 19.11 ATOM 1219 CE LYS A 183 22.412 7.841 -12.698 1.00 20.89 ATOM 1220 NZ LYS A 183 22.370 7.858 -14.194 1.00 23.60 ATOM 1221 C LYS A 183 25.322 6.639 -8.374 1.00 19.06 ATOM 1222 O LYS A 183 24.678 7.527 -7.799 1.00 19.22 ATOM 1223 N PRO A 184 26.650 6.743 -8.584 1.00 20.23 ATOM 1224 CD PRO A 184 27.506 5.764 -9.282 1.00 20.24 ATOM 1225 CA PRO A 184 27.429 7.899 -8.118 1.00 19.82 ATOM 1226 CB PRO A 184 28.810 7.673 -8.736 1.00 20.33 ATOM 1227 CG PRO A 184 28.892 6.179 -8.878 1.00 20.29 ATOM 1228 C PRO A 184 26.881 9.276 -8.432 1.00 19.71 ATOM 1229 O PRO A 184 27.011 10.185 -7.623 1.00 19.11 ATOM 1230 N GLN A 185 26.270 9.425 -9.599 1.00 20.43 ATOM 1231 CA GLN A 185 25.709 10.700 -10.007 1.00 22.58 ATOM 1232 CB GLN A 185 25.367 10.665 -11.492 1.00 26.30 ATOM 1233 CG GLN A 185 26.587 10.581 -12.368 1.00 32.75 ATOM 1234 CD GLN A 185 26.268 10.007 -13.724 1.00 37.20 ATOM 1235 OE1 GLN A 185 25.536 10.618 -14.518 1.00 39.43 ATOM 1236 NE2 GLN A 185 26.807 8.819 -14.005 1.00 39.10 ATOM 1237 C GLN A 185 24.468 11.106 -9.225 1.00 22.09 ATOM 1238 O GLN A 185 24.104 12.283 -9.198 1.00 21.59 ATOM 1239 N ASN A 186 23.816 10.137 -8.594 1.00 21.33 ATOM 1240 CA ASN A 186 22.616 10.432 -7.817 1.00 21.20 ATOM 1241 CB ASN A 186 21.555 9.355 -8.057 1.00 20.60 ATOM 1242 CG ASN A 186 20.920 9.480 -9.419 1.00 20.54 ATOM 1243 OD1 ASN A 186 20.923 10.556 -10.007 1.00 21.47 ATOM 1244 ND2 ASN A 186 20.375 8.390 -9.930 1.00 20.30 ATOM 1245 C ASN A 186 22.919 10.548 -6.335 1.00 20.28 ATOM 1246 O ASN A 186 22.011 10.531 -5.507 1.00 20.56 ATOM 1247 N LEU A 187 24.199 10.655 -6.002 1.00 19.29 ATOM 1248 CA LEU A 187 24.613 10.801 -4.616 1.00 18.96 ATOM 1249 CB LEU A 187 25.597 9.691 -4.238 1.00 17.20 ATOM 1250 CG LEU A 187 25.117 8.261 -4.494 1.00 17.80 ATOM 1251 CD1 LEU A 187 26.238 7.296 -4.153 1.00 15.47 ATOM 1252 CD2 LEU A 187 23.851 7.960 -3.651 1.00 15.97 ATOM 1253 C LEU A 187 25.278 12.165 -4.480 1.00 19.50 ATOM 1254 O LEU A 187 26.449 12.323 -4.839 1.00 19.44 ATOM 1255 N LEU A 188 24.527 13.146 -3.973 1.00 20.01 ATOM 1256 CA LEU A 188 25.039 14.507 -3.802 1.00 20.09 ATOM 1257 CB LEU A 188 23.886 15.506 -3.697 1.00 19.13 ATOM 1258 CG LEU A 188 22.816 15.384 -4.789 1.00 19.65 ATOM 1259 CD1 LEU A 188 21.723 16.418 -4.550 1.00 18.29 ATOM 1260 CD2 LEU A 188 23.431 15.569 -6.158 1.00 19.48 ATOM 1261 C LEU A 188 25.937 14.612 -2.580 1.00 20.88 ATOM 1262 O LEU A 188 25.732 13.921 -1.584 1.00 20.36 ATOM 1263 N LEU A 189 26.927 15.496 -2.661 1.00 21.45 ATOM 1264 CA LEU A 189 27.888 15.669 -1.583 1.00 23.35 ATOM 1265 CB LEU A 189 29.227 15.014 -1.949 1.00 23.80 ATOM 1266 CG LEU A 189 29.432 13.512 -2.017 1.00 25.29 ATOM 1267 CD1 LEU A 189 30.837 13.225 -2.564 1.00 24.98 ATOM 1268 CD2 LEU A 189 29.247 12.918 -0.620 1.00 26.50 ATOM 1269 C LEU A 189 28.226 17.106 -1.253 1.00 24.52 ATOM 1270 O LEU A 189 28.345 17.947 -2.139 1.00 24.12 ATOM 1271 N ASP A 190 28.398 17.372 0.032 1.00 26.25 ATOM 1272 CA ASP A 190 28.844 18.679 0.471 1.00 29.31 ATOM 1273 CB ASP A 190 27.960 19.255 1.568 1.00 30.69 ATOM 1274 CG ASP A 190 28.393 20.653 1.974 1.00 32.98 ATOM 1275 OD1 ASP A 190 29.532 21.047 1.647 1.00 34.35 ATOM 1276 OD2 ASP A 190 27.601 21.359 2.618 1.00 34.45 ATOM 1277 C ASP A 190 30.208 18.303 1.047 1.00 30.51 ATOM 1278 O ASP A 190 30.301 17.857 2.188 1.00 30.36 ATOM 1279 N PRO A 191 31.279 18.455 0.248 1.00 31.85 ATOM 1280 CD PRO A 191 31.206 18.991 -1.122 1.00 32.82 ATOM 1281 CA PRO A 191 32.666 18.136 0.628 1.00 32.61 ATOM 1282 CB PRO A 191 33.505 18.658 -0.546 1.00 32.95 ATOM 1283 CG PRO A 191 32.587 19.562 -1.328 1.00 33.73 ATOM 1284 C PRO A 191 33.161 18.684 1.962 1.00 32.44 ATOM 1285 O PRO A 191 33.895 17.999 2.675 1.00 33.71 ATOM 1286 N ASP A 192 32.763 19.903 2.307 1.00 32.07 ATOM 1287 CA ASP A 192 33.210 20.501 3.557 1.00 31.81 ATOM 1288 CB ASP A 192 32.835 21.981 3.604 1.00 34.19 ATOM 1289 CG ASP A 192 33.626 22.816 2.608 1.00 36.96 ATOM 1290 OD1 ASP A 192 33.214 23.978 2.377 1.00 38.74 ATOM 1291 OD2 ASP A 192 34.646 22.316 2.058 1.00 37.11 ATOM 1292 C ASP A 192 32.648 19.810 4.788 1.00 30.64 ATOM 1293 O ASP A 192 33.359 19.612 5.777 1.00 30.73 ATOM 1294 N THR A 193 31.371 19.450 4.740 1.00 28.24 ATOM 1295 CA THR A 193 30.744 18.793 5.878 1.00 26.36 ATOM 1296 CB THR A 193 29.300 19.285 6.057 1.00 26.47 ATOM 1297 OG1 THR A 193 28.516 18.869 4.934 1.00 26.88 ATOM 1298 CG2 THR A 193 29.270 20.813 6.156 1.00 26.37 ATOM 1299 C THR A 193 30.744 17.272 5.754 1.00 24.79 ATOM 1300 O THR A 193 30.481 16.571 6.726 1.00 24.39 ATOM 1301 N ALA A 194 31.062 16.776 4.564 1.00 23.40 ATOM 1302 CA ALA A 194 31.082 15.336 4.280 1.00 23.13 ATOM 1303 CB ALA A 194 32.008 14.611 5.253 1.00 21.95 ATOM 1304 C ALA A 194 29.673 14.720 4.326 1.00 22.99 ATOM 1305 O ALA A 194 29.511 13.518 4.538 1.00 23.06 ATOM 1306 N VAL A 195 28.658 15.555 4.117 1.00 22.67 ATOM 1307 CA VAL A 195 27.270 15.107 4.120 1.00 21.84 ATOM 1308 CB VAL A 195 26.314 16.277 4.495 1.00 21.88 ATOM 1309 CG1 VAL A 195 24.846 15.866 4.283 1.00 22.52 ATOM 1310 CG2 VAL A 195 26.539 16.680 5.943 1.00 20.79 ATOM 1311 C VAL A 195 26.891 14.570 2.737 1.00 21.90 ATOM 1312 O VAL A 195 27.211 15.182 1.719 1.00 22.00 ATOM 1313 N LEU A 196 26.236 13.411 2.707 1.00 20.93 ATOM 1314 CA LEU A 196 25.795 12.815 1.451 1.00 19.65 ATOM 1315 CB LEU A 196 26.238 11.343 1.341 1.00 18.62 ATOM 1316 CG LEU A 196 25.743 10.564 0.100 1.00 18.70 ATOM 1317 CD1 LEU A 196 26.791 9.521 -0.316 1.00 19.21 ATOM 1318 CD2 LEU A 196 24.410 9.883 0.387 1.00 17.18 ATOM 1319 C LEU A 196 24.274 12.877 1.436 1.00 19.23 ATOM 1320 O LEU A 196 23.631 12.643 2.460 1.00 18.55 ATOM 1321 N LYS A 197 23.704 13.197 0.281 1.00 19.05 ATOM 1322 CA LYS A 197 22.258 13.262 0.137 1.00 18.80 ATOM 1323 CB LYS A 197 21.778 14.713 0.087 1.00 19.75 ATOM 1324 CG LYS A 197 21.889 15.432 1.420 1.00 22.81 ATOM 1325 CD LYS A 197 21.310 16.824 1.349 1.00 24.26 ATOM 1326 CE LYS A 197 21.509 17.560 2.663 1.00 24.65 ATOM 1327 NZ LYS A 197 21.243 16.672 3.824 1.00 26.14 ATOM 1328 C LYS A 197 21.824 12.539 -1.127 1.00 18.50 ATOM 1329 O LYS A 197 22.237 12.880 -2.231 1.00 18.47 ATOM 1330 N LEU A 198 20.997 11.519 -0.952 1.00 18.48 ATOM 1331 CA LEU A 198 20.472 10.757 -2.071 1.00 18.14 ATOM 1332 CB LEU A 198 19.740 9.526 -1.546 1.00 17.24 ATOM 1333 CG LEU A 198 19.054 8.652 -2.585 1.00 17.91 ATOM 1334 CD1 LEU A 198 20.076 8.120 -3.587 1.00 17.92 ATOM 1335 CD2 LEU A 198 18.338 7.515 -1.848 1.00 17.52 ATOM 1336 C LEU A 198 19.507 11.653 -2.844 1.00 18.06 ATOM 1337 O LEU A 198 18.744 12.410 -2.249 1.00 18.45 ATOM 1338 N CYS A 199 19.553 11.587 -4.167 1.00 18.39 ATOM 1339 CA CYS A 199 18.666 12.399 -4.987 1.00 19.96 ATOM 1340 CB CYS A 199 19.394 13.668 -5.467 1.00 21.39 ATOM 1341 SG CYS A 199 20.530 13.422 -6.864 1.00 24.07 ATOM 1342 C CYS A 199 18.110 11.640 -6.190 1.00 20.23 ATOM 1343 O CYS A 199 18.391 10.456 -6.391 1.00 20.19 ATOM 1344 N ASP A 200 17.299 12.339 -6.973 1.00 21.17 ATOM 1345 CA ASP A 200 16.687 11.791 -8.174 1.00 22.22 ATOM 1346 CB ASP A 200 17.765 11.360 -9.162 1.00 23.30 ATOM 1347 CG ASP A 200 17.195 10.994 -10.520 1.00 26.30 ATOM 1348 OD1 ASP A 200 15.957 11.080 -10.710 1.00 28.28 ATOM 1349 OD2 ASP A 200 17.987 10.617 -11.401 1.00 28.20 ATOM 1350 C ASP A 200 15.746 10.625 -7.923 1.00 22.14 ATOM 1351 O ASP A 200 16.118 9.461 -8.084 1.00 22.48 ATOM 1352 N PHE A 201 14.511 10.941 -7.551 1.00 22.71 ATOM 1353 CA PHE A 201 13.525 9.900 -7.297 1.00 22.47 ATOM 1354 CB PHE A 201 12.733 10.257 -6.037 1.00 21.47 ATOM 1355 CG PHE A 201 13.534 10.068 -4.777 1.00 21.56 ATOM 1356 CD1 PHE A 201 14.420 11.052 -4.349 1.00 21.10 ATOM 1357 CD2 PHE A 201 13.492 8.865 -4.085 1.00 21.02 ATOM 1358 CE1 PHE A 201 15.253 10.838 -3.265 1.00 20.29 ATOM 1359 CE2 PHE A 201 14.323 8.644 -2.998 1.00 20.60 ATOM 1360 CZ PHE A 201 15.206 9.633 -2.590 1.00 20.67 ATOM 1361 C PHE A 201 12.624 9.668 -8.509 1.00 22.93 ATOM 1362 O PHE A 201 11.494 9.183 -8.390 1.00 22.94 ATOM 1363 N GLY A 202 13.160 10.003 -9.680 1.00 22.62 ATOM 1364 CA GLY A 202 12.429 9.826 -10.918 1.00 22.92 ATOM 1365 C GLY A 202 12.149 8.378 -11.279 1.00 23.57 ATOM 1366 O GLY A 202 11.256 8.108 -12.077 1.00 24.65 ATOM 1367 N SER A 203 12.900 7.439 -10.710 1.00 23.52 ATOM 1368 CA SER A 203 12.679 6.024 -11.000 1.00 23.27 ATOM 1369 CB SER A 203 13.988 5.330 -11.398 1.00 23.26 ATOM 1370 OG SER A 203 14.521 5.859 -12.599 1.00 25.03 ATOM 1371 C SER A 203 12.122 5.285 -9.793 1.00 23.00 ATOM 1372 O SER A 203 11.804 4.103 -9.892 1.00 23.92 ATOM 1373 N ALA A 204 12.015 5.969 -8.657 1.00 23.06 ATOM 1374 CA ALA A 204 11.539 5.331 -7.434 1.00 23.36 ATOM 1375 CB ALA A 204 11.687 6.283 -6.255 1.00 22.51 ATOM 1376 C ALA A 204 10.109 4.823 -7.524 1.00 23.71 ATOM 1377 O ALA A 204 9.273 5.387 -8.224 1.00 23.31 ATOM 1378 N LYS A 205 9.839 3.746 -6.799 1.00 25.43 ATOM 1379 CA LYS A 205 8.512 3.141 -6.791 1.00 26.50 ATOM 1380 CB LYS A 205 8.324 2.287 -8.047 1.00 26.50 ATOM 1381 CG LYS A 205 6.949 1.655 -8.188 1.00 26.83 ATOM 1382 CD LYS A 205 6.714 1.221 -9.629 1.00 27.32 ATOM 1383 CE LYS A 205 5.249 0.905 -9.879 1.00 28.01 ATOM 1384 NZ LYS A 205 4.941 -0.456 -9.428 1.00 27.00 ATOM 1385 C LYS A 205 8.295 2.268 -5.569 1.00 27.59 ATOM 1386 O LYS A 205 9.207 1.573 -5.105 1.00 26.88 ATOM 1387 N GLN A 206 7.084 2.312 -5.034 1.00 28.78 ATOM 1388 CA GLN A 206 6.769 1.466 -3.904 1.00 30.86 ATOM 1389 CB GLN A 206 5.472 1.932 -3.244 1.00 33.54 ATOM 1390 CG GLN A 206 4.704 0.810 -2.574 1.00 37.54 ATOM 1391 CD GLN A 206 4.262 1.176 -1.185 1.00 39.58 ATOM 1392 OE1 GLN A 206 4.284 2.351 -0.810 1.00 41.99 ATOM 1393 NE2 GLN A 206 3.857 0.176 -0.405 1.00 40.19 ATOM 1394 C GLN A 206 6.592 0.068 -4.507 1.00 30.74 ATOM 1395 O GLN A 206 5.768 -0.126 -5.397 1.00 30.43 ATOM 1396 N LEU A 207 7.379 -0.897 -4.045 1.00 30.44 ATOM 1397 CA LEU A 207 7.284 -2.250 -4.570 1.00 31.81 ATOM 1398 CB LEU A 207 8.658 -2.919 -4.592 1.00 29.58 ATOM 1399 CG LEU A 207 9.732 -2.211 -5.423 1.00 28.37 ATOM 1400 CD1 LEU A 207 10.972 -3.073 -5.478 1.00 27.44 ATOM 1401 CD2 LEU A 207 9.205 -1.921 -6.821 1.00 26.93 ATOM 1402 C LEU A 207 6.334 -3.068 -3.721 1.00 34.09 ATOM 1403 O LEU A 207 6.496 -3.147 -2.504 1.00 35.13 ATOM 1404 N VAL A 208 5.344 -3.670 -4.371 1.00 35.76 ATOM 1405 CA VAL A 208 4.344 -4.486 -3.689 1.00 37.93 ATOM 1406 CB VAL A 208 2.923 -4.009 -4.050 1.00 38.12 ATOM 1407 CG1 VAL A 208 1.887 -4.767 -3.234 1.00 38.32 ATOM 1408 CG2 VAL A 208 2.810 -2.512 -3.810 1.00 37.94 ATOM 1409 C VAL A 208 4.496 -5.954 -4.081 1.00 39.60 ATOM 1410 O VAL A 208 4.355 -6.311 -5.256 1.00 39.70 ATOM 1411 N ARG A 209 4.794 -6.798 -3.097 1.00 41.68 ATOM 1412 CA ARG A 209 4.974 -8.228 -3.333 1.00 44.15 ATOM 1413 CB ARG A 209 4.956 -8.973 -1.995 1.00 46.88 ATOM 1414 CG ARG A 209 4.916 -10.490 -2.112 1.00 50.91 ATOM 1415 CD ARG A 209 6.255 -11.034 -2.575 1.00 54.81 ATOM 1416 NE ARG A 209 6.375 -12.479 -2.388 1.00 58.25 ATOM 1417 CZ ARG A 209 7.437 -13.189 -2.762 1.00 59.97 ATOM 1418 NH1 ARG A 209 8.470 -12.585 -3.343 1.00 61.06 ATOM 1419 NH2 ARG A 209 7.471 -14.503 -2.557 1.00 60.60 ATOM 1420 C ARG A 209 3.881 -8.774 -4.258 1.00 43.98 ATOM 1421 O ARG A 209 2.693 -8.559 -4.020 1.00 44.25 ATOM 1422 N GLY A 210 4.286 -9.461 -5.323 1.00 43.86 ATOM 1423 CA GLY A 210 3.314 -10.014 -6.249 1.00 43.26 ATOM 1424 C GLY A 210 2.957 -9.115 -7.418 1.00 43.22 ATOM 1425 O GLY A 210 2.348 -9.566 -8.385 1.00 43.46 ATOM 1426 N GLU A 211 3.312 -7.838 -7.330 1.00 42.96 ATOM 1427 CA GLU A 211 3.034 -6.899 -8.416 1.00 43.03 ATOM 1428 CB GLU A 211 2.707 -5.522 -7.854 1.00 44.77 ATOM 1429 CG GLU A 211 1.262 -5.368 -7.427 1.00 48.04 ATOM 1430 CD GLU A 211 1.013 -4.055 -6.711 1.00 49.98 ATOM 1431 OE1 GLU A 211 1.826 -3.114 -6.894 1.00 51.02 ATOM 1432 OE2 GLU A 211 0.009 -3.966 -5.966 1.00 51.59 ATOM 1433 C GLU A 211 4.277 -6.813 -9.299 1.00 41.60 ATOM 1434 O GLU A 211 5.370 -6.531 -8.813 1.00 42.23 ATOM 1435 N PRO A 212 4.130 -7.052 -10.608 1.00 40.00 ATOM 1436 CD PRO A 212 2.916 -7.386 -11.373 1.00 39.58 ATOM 1437 CA PRO A 212 5.312 -6.983 -11.471 1.00 38.42 ATOM 1438 CB PRO A 212 4.848 -7.650 -12.764 1.00 38.22 ATOM 1439 CG PRO A 212 3.397 -7.358 -12.807 1.00 38.96 ATOM 1440 C PRO A 212 5.808 -5.563 -11.706 1.00 36.44 ATOM 1441 O PRO A 212 5.032 -4.613 -11.682 1.00 36.32 ATOM 1442 N ASN A 213 7.110 -5.435 -11.936 1.00 34.28 ATOM 1443 CA ASN A 213 7.721 -4.142 -12.199 1.00 31.93 ATOM 1444 CB ASN A 213 8.443 -3.662 -10.948 1.00 31.18 ATOM 1445 CG ASN A 213 7.482 -3.241 -9.863 1.00 30.77 ATOM 1446 OD1 ASN A 213 6.844 -2.183 -9.950 1.00 30.53 ATOM 1447 ND2 ASN A 213 7.361 -4.067 -8.838 1.00 29.67 ATOM 1448 C ASN A 213 8.692 -4.267 -13.375 1.00 31.05 ATOM 1449 O ASN A 213 9.202 -5.357 -13.652 1.00 30.47 ATOM 1450 N VAL A 214 8.939 -3.160 -14.071 1.00 29.87 ATOM 1451 CA VAL A 214 9.837 -3.190 -15.216 1.00 29.51 ATOM 1452 CB VAL A 214 9.783 -1.886 -16.009 1.00 29.53 ATOM 1453 CG1 VAL A 214 8.388 -1.685 -16.524 1.00 29.69 ATOM 1454 CG2 VAL A 214 10.224 -0.724 -15.151 1.00 28.88 ATOM 1455 C VAL A 214 11.281 -3.464 -14.837 1.00 29.76 ATOM 1456 O VAL A 214 11.795 -2.936 -13.851 1.00 29.50 ATOM 1457 N SER A 215 11.936 -4.291 -15.643 1.00 29.47 ATOM 1458 CA SER A 215 13.318 -4.654 -15.394 1.00 29.11 ATOM 1459 CB SER A 215 13.563 -6.091 -15.843 1.00 29.25 ATOM 1460 OG SER A 215 13.468 -6.173 -17.250 1.00 30.52 ATOM 1461 C SER A 215 14.304 -3.731 -16.098 1.00 28.22 ATOM 1462 O SER A 215 15.510 -3.920 -15.962 1.00 29.03 ATOM 1463 N TYR A 216 13.815 -2.741 -16.843 1.00 26.59 ATOM 1464 CA TYR A 216 14.738 -1.848 -17.532 1.00 26.31 ATOM 1465 CB TYR A 216 14.244 -1.515 -18.950 1.00 26.79 ATOM 1466 CG TYR A 216 12.816 -1.059 -19.033 1.00 28.06 ATOM 1467 CD1 TYR A 216 12.480 0.276 -18.839 1.00 28.12 ATOM 1468 CE1 TYR A 216 11.153 0.698 -18.925 1.00 29.86 ATOM 1469 CD2 TYR A 216 11.797 -1.964 -19.313 1.00 28.25 ATOM 1470 CE2 TYR A 216 10.472 -1.553 -19.401 1.00 29.50 ATOM 1471 CZ TYR A 216 10.159 -0.225 -19.207 1.00 29.50 ATOM 1472 OH TYR A 216 8.849 0.177 -19.300 1.00 31.51 ATOM 1473 C TYR A 216 15.113 -0.557 -16.802 1.00 25.47 ATOM 1474 O TYR A 216 15.584 0.392 -17.428 1.00 25.03 ATOM 1475 N ILE A 217 14.909 -0.509 -15.486 1.00 23.99 ATOM 1476 CA ILE A 217 15.313 0.668 -14.727 1.00 22.74 ATOM 1477 CB ILE A 217 14.412 0.917 -13.457 1.00 22.17 ATOM 1478 CG2 ILE A 217 13.275 1.876 -13.815 1.00 21.23 ATOM 1479 CG1 ILE A 217 13.838 -0.396 -12.919 1.00 20.89 ATOM 1480 CD1 ILE A 217 14.873 -1.319 -12.279 1.00 20.06 ATOM 1481 C ILE A 217 16.754 0.389 -14.288 1.00 22.90 ATOM 1482 O ILE A 217 17.262 -0.716 -14.504 1.00 21.91 ATOM 1483 N CYS A 218 17.408 1.386 -13.693 1.00 23.48 ATOM 1484 CA CYS A 218 18.779 1.270 -13.194 1.00 24.21 ATOM 1485 CB CYS A 218 18.961 -0.022 -12.409 1.00 24.07 ATOM 1486 SG CYS A 218 20.291 0.083 -11.203 1.00 27.51 ATOM 1487 C CYS A 218 19.845 1.359 -14.274 1.00 24.97 ATOM 1488 O CYS A 218 19.775 0.680 -15.295 1.00 24.75 ATOM 1489 N SER A 219 20.843 2.202 -14.032 1.00 25.88 ATOM 1490 CA SER A 219 21.920 2.417 -14.988 1.00 27.49 ATOM 1491 CB SER A 219 22.675 3.698 -14.647 1.00 27.73 ATOM 1492 OG SER A 219 21.759 4.761 -14.463 1.00 31.62 ATOM 1493 C SER A 219 22.911 1.278 -15.088 1.00 27.94 ATOM 1494 O SER A 219 23.211 0.619 -14.103 1.00 26.89 ATOM 1495 N ARG A 220 23.423 1.072 -16.298 1.00 29.74 ATOM 1496 CA ARG A 220 24.413 0.029 -16.576 1.00 31.72 ATOM 1497 CB ARG A 220 24.894 0.138 -18.030 1.00 35.21 ATOM 1498 CG ARG A 220 25.539 1.487 -18.378 1.00 39.92 ATOM 1499 CD ARG A 220 26.458 1.376 -19.599 1.00 44.70 ATOM 1500 NE ARG A 220 27.474 2.432 -19.630 1.00 49.09 ATOM 1501 CZ ARG A 220 28.535 2.434 -20.439 1.00 50.77 ATOM 1502 NH1 ARG A 220 29.402 3.443 -20.391 1.00 51.24 ATOM 1503 NH2 ARG A 220 28.725 1.434 -21.300 1.00 51.08 ATOM 1504 C ARG A 220 25.606 0.181 -15.638 1.00 30.83 ATOM 1505 O ARG A 220 26.051 1.302 -15.355 1.00 31.44 ATOM 1506 N TYR A 221 26.122 -0.956 -15.189 1.00 29.34 ATOM 1507 CA TYR A 221 27.250 -1.064 -14.256 1.00 28.35 ATOM 1508 CB TYR A 221 28.118 0.202 -14.202 1.00 30.46 ATOM 1509 CG TYR A 221 28.937 0.503 -15.431 1.00 33.38 ATOM 1510 CD1 TYR A 221 28.767 -0.224 -16.613 1.00 33.73 ATOM 1511 CE1 TYR A 221 29.483 0.099 -17.765 1.00 35.76 ATOM 1512 CD2 TYR A 221 29.852 1.563 -15.427 1.00 34.31 ATOM 1513 CE2 TYR A 221 30.573 1.896 -16.571 1.00 35.52 ATOM 1514 CZ TYR A 221 30.382 1.161 -17.735 1.00 36.36 ATOM 1515 OH TYR A 221 31.080 1.489 -18.872 1.00 38.86 ATOM 1516 C TYR A 221 26.725 -1.306 -12.843 1.00 26.15 ATOM 1517 O TYR A 221 27.349 -2.029 -12.076 1.00 26.02 ATOM 1518 N TYR A 222 25.576 -0.703 -12.518 1.00 24.16 ATOM 1519 CA TYR A 222 24.977 -0.803 -11.174 1.00 22.84 ATOM 1520 CB TYR A 222 24.657 0.618 -10.659 1.00 21.48 ATOM 1521 CG TYR A 222 25.834 1.562 -10.822 1.00 20.65 ATOM 1522 CD1 TYR A 222 26.894 1.546 -9.920 1.00 20.76 ATOM 1523 CE1 TYR A 222 28.037 2.319 -10.132 1.00 20.88 ATOM 1524 CD2 TYR A 222 25.939 2.390 -11.945 1.00 21.81 ATOM 1525 CE2 TYR A 222 27.078 3.171 -12.171 1.00 21.39 ATOM 1526 CZ TYR A 222 28.126 3.125 -11.261 1.00 21.87 ATOM 1527 OH TYR A 222 29.272 3.858 -11.493 1.00 22.01 ATOM 1528 C TYR A 222 23.738 -1.693 -11.085 1.00 21.82 ATOM 1529 O TYR A 222 23.141 -1.829 -10.017 1.00 20.30 ATOM 1530 N ARG A 223 23.373 -2.310 -12.206 1.00 22.30 ATOM 1531 CA ARG A 223 22.196 -3.184 -12.285 1.00 22.75 ATOM 1532 CB ARG A 223 21.807 -3.414 -13.753 1.00 24.24 ATOM 1533 CG ARG A 223 21.099 -2.244 -14.397 1.00 27.38 ATOM 1534 CD ARG A 223 21.172 -2.303 -15.901 1.00 30.59 ATOM 1535 NE ARG A 223 20.438 -3.433 -16.472 1.00 34.37 ATOM 1536 CZ ARG A 223 19.114 -3.554 -16.467 1.00 35.85 ATOM 1537 NH1 ARG A 223 18.352 -2.617 -15.918 1.00 36.58 ATOM 1538 NH2 ARG A 223 18.544 -4.609 -17.036 1.00 37.68 ATOM 1539 C ARG A 223 22.400 -4.542 -11.622 1.00 21.76 ATOM 1540 O ARG A 223 23.378 -5.233 -11.909 1.00 22.00 ATOM 1541 N ALA A 224 21.476 -4.924 -10.742 1.00 20.83 ATOM 1542 CA ALA A 224 21.553 -6.223 -10.073 1.00 20.37 ATOM 1543 CB ALA A 224 20.445 -6.349 -9.025 1.00 19.21 ATOM 1544 C ALA A 224 21.396 -7.307 -11.143 1.00 20.70 ATOM 1545 O ALA A 224 20.741 -7.089 -12.164 1.00 19.59 ATOM 1546 N PRO A 225 22.024 -8.477 -10.939 1.00 21.01 ATOM 1547 CD PRO A 225 22.888 -8.826 -9.804 1.00 20.71 ATOM 1548 CA PRO A 225 21.923 -9.568 -11.920 1.00 21.49 ATOM 1549 CB PRO A 225 22.706 -10.717 -11.276 1.00 21.54 ATOM 1550 CG PRO A 225 22.888 -10.326 -9.837 1.00 21.30 ATOM 1551 C PRO A 225 20.485 -9.960 -12.271 1.00 22.38 ATOM 1552 O PRO A 225 20.165 -10.177 -13.443 1.00 22.51 ATOM 1553 N GLU A 226 19.608 -10.041 -11.275 1.00 22.20 ATOM 1554 CA GLU A 226 18.231 -10.407 -11.564 1.00 22.73 ATOM 1555 CB GLU A 226 17.372 -10.441 -10.290 1.00 22.66 ATOM 1556 CG GLU A 226 17.313 -9.143 -9.488 1.00 23.95 ATOM 1557 CD GLU A 226 18.298 -9.139 -8.341 1.00 23.60 ATOM 1558 OE1 GLU A 226 19.403 -9.685 -8.510 1.00 24.14 ATOM 1559 OE2 GLU A 226 17.977 -8.593 -7.270 1.00 24.79 ATOM 1560 C GLU A 226 17.631 -9.447 -12.582 1.00 23.08 ATOM 1561 O GLU A 226 16.762 -9.842 -13.366 1.00 23.12 ATOM 1562 N LEU A 227 18.096 -8.195 -12.588 1.00 22.59 ATOM 1563 CA LEU A 227 17.594 -7.203 -13.543 1.00 22.96 ATOM 1564 CB LEU A 227 18.006 -5.774 -13.137 1.00 22.04 ATOM 1565 CG LEU A 227 17.363 -5.127 -11.896 1.00 21.34 ATOM 1566 CD1 LEU A 227 17.933 -3.723 -11.733 1.00 19.62 ATOM 1567 CD2 LEU A 227 15.833 -5.066 -12.030 1.00 20.79 ATOM 1568 C LEU A 227 18.146 -7.515 -14.940 1.00 23.39 ATOM 1569 O LEU A 227 17.423 -7.464 -15.937 1.00 23.76 ATOM 1570 N ILE A 228 19.431 -7.831 -15.013 1.00 23.46 ATOM 1571 CA ILE A 228 20.027 -8.157 -16.293 1.00 24.68 ATOM 1572 CB ILE A 228 21.540 -8.441 -16.151 1.00 24.25 ATOM 1573 CG2 ILE A 228 22.117 -8.862 -17.492 1.00 24.89 ATOM 1574 CG1 ILE A 228 22.261 -7.173 -15.672 1.00 24.65 ATOM 1575 CD1 ILE A 228 23.630 -7.419 -15.100 1.00 23.37 ATOM 1576 C ILE A 228 19.303 -9.387 -16.843 1.00 25.24 ATOM 1577 O ILE A 228 19.045 -9.477 -18.040 1.00 25.57 ATOM 1578 N PHE A 229 18.963 -10.321 -15.956 1.00 26.21 ATOM 1579 CA PHE A 229 18.255 -11.543 -16.341 1.00 26.72 ATOM 1580 CB PHE A 229 18.376 -12.599 -15.242 1.00 26.49 ATOM 1581 CG PHE A 229 19.692 -13.311 -15.227 1.00 27.25 ATOM 1582 CD1 PHE A 229 20.440 -13.395 -14.058 1.00 28.34 ATOM 1583 CD2 PHE A 229 20.180 -13.915 -16.374 1.00 29.24 ATOM 1584 CE1 PHE A 229 21.654 -14.070 -14.030 1.00 28.68 ATOM 1585 CE2 PHE A 229 21.399 -14.598 -16.360 1.00 30.26 ATOM 1586 CZ PHE A 229 22.136 -14.675 -15.185 1.00 30.14 ATOM 1587 C PHE A 229 16.773 -11.292 -16.627 1.00 27.34 ATOM 1588 O PHE A 229 16.017 -12.232 -16.837 1.00 28.32 ATOM 1589 N GLY A 230 16.354 -10.031 -16.596 1.00 27.35 ATOM 1590 CA GLY A 230 14.972 -9.694 -16.899 1.00 27.67 ATOM 1591 C GLY A 230 13.862 -9.977 -15.899 1.00 28.73 ATOM 1592 O GLY A 230 12.693 -9.994 -16.279 1.00 28.61 ATOM 1593 N ALA A 231 14.192 -10.181 -14.627 1.00 29.15 ATOM 1594 CA ALA A 231 13.164 -10.450 -13.624 1.00 28.54 ATOM 1595 CB ALA A 231 13.809 -10.820 -12.296 1.00 28.69 ATOM 1596 C ALA A 231 12.259 -9.244 -13.436 1.00 28.92 ATOM 1597 O ALA A 231 12.702 -8.099 -13.551 1.00 28.38 ATOM 1598 N THR A 232 10.984 -9.508 -13.161 1.00 29.06 ATOM 1599 CA THR A 232 10.008 -8.448 -12.923 1.00 29.20 ATOM 1600 CB THR A 232 8.828 -8.529 -13.894 1.00 29.35 ATOM 1601 OG1 THR A 232 8.226 -9.824 -13.791 1.00 29.80 ATOM 1602 CG2 THR A 232 9.292 -8.278 -15.322 1.00 28.94 ATOM 1603 C THR A 232 9.468 -8.581 -11.499 1.00 28.89 ATOM 1604 O THR A 232 8.626 -7.805 -11.069 1.00 28.88 ATOM 1605 N ASP A 233 9.966 -9.570 -10.771 1.00 28.95 ATOM 1606 CA ASP A 233 9.537 -9.793 -9.401 1.00 29.85 ATOM 1607 CB ASP A 233 9.126 -11.255 -9.221 1.00 32.20 ATOM 1608 CG ASP A 233 10.288 -12.207 -9.399 1.00 34.94 ATOM 1609 OD1 ASP A 233 11.334 -11.786 -9.945 1.00 36.97 ATOM 1610 OD2 ASP A 233 10.159 -13.381 -8.993 1.00 36.65 ATOM 1611 C ASP A 233 10.649 -9.445 -8.410 1.00 28.90 ATOM 1612 O ASP A 233 10.726 -10.017 -7.323 1.00 28.78 ATOM 1613 N TYR A 234 11.513 -8.506 -8.782 1.00 27.36 ATOM 1614 CA TYR A 234 12.608 -8.109 -7.907 1.00 25.85 ATOM 1615 CB TYR A 234 13.655 -7.312 -8.696 1.00 23.62 ATOM 1616 CG TYR A 234 13.104 -6.076 -9.367 1.00 21.48 ATOM 1617 CD1 TYR A 234 12.967 -4.873 -8.663 1.00 20.36 ATOM 1618 CE1 TYR A 234 12.461 -3.719 -9.288 1.00 19.82 ATOM 1619 CD2 TYR A 234 12.726 -6.101 -10.705 1.00 20.32 ATOM 1620 CE2 TYR A 234 12.223 -4.959 -11.336 1.00 20.65 ATOM 1621 CZ TYR A 234 12.092 -3.773 -10.625 1.00 19.85 ATOM 1622 OH TYR A 234 11.573 -2.659 -11.256 1.00 19.95 ATOM 1623 C TYR A 234 12.114 -7.287 -6.714 1.00 25.08 ATOM 1624 O TYR A 234 11.000 -6.764 -6.716 1.00 24.68 ATOM 1625 N THR A 235 12.972 -7.172 -5.708 1.00 25.71 ATOM 1626 CA THR A 235 12.673 -6.443 -4.477 1.00 25.40 ATOM 1627 CB THR A 235 12.837 -7.356 -3.272 1.00 25.34 ATOM 1628 OG1 THR A 235 14.212 -7.757 -3.184 1.00 25.12 ATOM 1629 CG2 THR A 235 11.968 -8.600 -3.428 1.00 24.91 ATOM 1630 C THR A 235 13.629 -5.264 -4.282 1.00 25.46 ATOM 1631 O THR A 235 14.451 -4.959 -5.148 1.00 25.48 ATOM 1632 N SER A 236 13.531 -4.628 -3.120 1.00 24.25 ATOM 1633 CA SER A 236 14.363 -3.478 -2.797 1.00 23.86 ATOM 1634 CB SER A 236 13.892 -2.854 -1.474 1.00 24.26 ATOM 1635 OG SER A 236 12.691 -2.122 -1.671 1.00 26.82 ATOM 1636 C SER A 236 15.845 -3.839 -2.706 1.00 22.38 ATOM 1637 O SER A 236 16.705 -2.953 -2.682 1.00 22.00 ATOM 1638 N SER A 237 16.146 -5.133 -2.641 1.00 20.73 ATOM 1639 CA SER A 237 17.532 -5.568 -2.559 1.00 20.19 ATOM 1640 CB SER A 237 17.619 -7.078 -2.305 1.00 19.88 ATOM 1641 OG SER A 237 16.901 -7.806 -3.289 1.00 22.89 ATOM 1642 C SER A 237 18.307 -5.214 -3.833 1.00 19.59 ATOM 1643 O SER A 237 19.518 -5.399 -3.885 1.00 19.64 ATOM 1644 N ILE A 238 17.626 -4.726 -4.867 1.00 19.10 ATOM 1645 CA ILE A 238 18.356 -4.351 -6.073 1.00 19.28 ATOM 1646 CB ILE A 238 17.425 -4.113 -7.303 1.00 19.67 ATOM 1647 CG2 ILE A 238 16.611 -5.370 -7.606 1.00 20.20 ATOM 1648 CG1 ILE A 238 16.485 -2.931 -7.050 1.00 19.35 ATOM 1649 CD1 ILE A 238 15.886 -2.358 -8.325 1.00 19.21 ATOM 1650 C ILE A 238 19.136 -3.061 -5.762 1.00 19.30 ATOM 1651 O ILE A 238 20.162 -2.787 -6.390 1.00 18.66 ATOM 1652 N ASP A 239 18.655 -2.280 -4.788 1.00 18.86 ATOM 1653 CA ASP A 239 19.335 -1.038 -4.398 1.00 18.14 ATOM 1654 CB ASP A 239 18.459 -0.164 -3.493 1.00 17.57 ATOM 1655 CG ASP A 239 17.409 0.635 -4.254 1.00 17.96 ATOM 1656 OD1 ASP A 239 16.482 1.137 -3.582 1.00 18.29 ATOM 1657 OD2 ASP A 239 17.492 0.773 -5.497 1.00 17.36 ATOM 1658 C ASP A 239 20.596 -1.392 -3.615 1.00 18.30 ATOM 1659 O ASP A 239 21.585 -0.654 -3.642 1.00 18.02 ATOM 1660 N VAL A 240 20.553 -2.509 -2.895 1.00 18.31 ATOM 1661 CA VAL A 240 21.713 -2.927 -2.109 1.00 19.32 ATOM 1662 CB VAL A 240 21.337 -4.025 -1.091 1.00 19.56 ATOM 1663 CG1 VAL A 240 22.577 -4.549 -0.421 1.00 19.57 ATOM 1664 CG2 VAL A 240 20.384 -3.453 -0.048 1.00 18.91 ATOM 1665 C VAL A 240 22.827 -3.423 -3.037 1.00 19.47 ATOM 1666 O VAL A 240 24.016 -3.195 -2.784 1.00 19.72 ATOM 1667 N TRP A 241 22.452 -4.094 -4.120 1.00 18.91 ATOM 1668 CA TRP A 241 23.462 -4.547 -5.066 1.00 18.66 ATOM 1669 CB TRP A 241 22.827 -5.366 -6.196 1.00 18.84 ATOM 1670 CG TRP A 241 23.789 -5.659 -7.318 1.00 19.23 ATOM 1671 CD2 TRP A 241 24.530 -6.873 -7.517 1.00 19.98 ATOM 1672 CE2 TRP A 241 25.332 -6.692 -8.671 1.00 20.27 ATOM 1673 CE3 TRP A 241 24.598 -8.097 -6.834 1.00 20.38 ATOM 1674 CD1 TRP A 241 24.157 -4.816 -8.330 1.00 19.46 ATOM 1675 NE1 TRP A 241 25.087 -5.429 -9.149 1.00 19.93 ATOM 1676 CZ2 TRP A 241 26.187 -7.689 -9.155 1.00 20.49 ATOM 1677 CZ3 TRP A 241 25.450 -9.088 -7.316 1.00 19.84 ATOM 1678 CH2 TRP A 241 26.232 -8.874 -8.465 1.00 20.78 ATOM 1679 C TRP A 241 24.102 -3.272 -5.642 1.00 18.02 ATOM 1680 O TRP A 241 25.329 -3.146 -5.682 1.00 17.77 ATOM 1681 N SER A 242 23.260 -2.335 -6.088 1.00 17.01 ATOM 1682 CA SER A 242 23.737 -1.072 -6.653 1.00 17.50 ATOM 1683 CB SER A 242 22.573 -0.135 -6.972 1.00 17.69 ATOM 1684 OG SER A 242 21.819 -0.625 -8.062 1.00 18.11 ATOM 1685 C SER A 242 24.688 -0.367 -5.698 1.00 17.50 ATOM 1686 O SER A 242 25.723 0.153 -6.119 1.00 17.78 ATOM 1687 N ALA A 243 24.330 -0.340 -4.414 1.00 17.48 ATOM 1688 CA ALA A 243 25.171 0.291 -3.400 1.00 17.79 ATOM 1689 CB ALA A 243 24.462 0.274 -2.046 1.00 17.16 ATOM 1690 C ALA A 243 26.517 -0.448 -3.308 1.00 18.48 ATOM 1691 O ALA A 243 27.573 0.172 -3.166 1.00 18.62 ATOM 1692 N GLY A 244 26.473 -1.773 -3.397 1.00 18.76 ATOM 1693 CA GLY A 244 27.691 -2.561 -3.337 1.00 19.29 ATOM 1694 C GLY A 244 28.606 -2.238 -4.503 1.00 20.22 ATOM 1695 O GLY A 244 29.824 -2.270 -4.369 1.00 21.53 ATOM 1696 N CYS A 245 28.021 -1.932 -5.657 1.00 20.67 ATOM 1697 CA CYS A 245 28.803 -1.589 -6.847 1.00 19.99 ATOM 1698 CB CYS A 245 27.894 -1.513 -8.075 1.00 19.97 ATOM 1699 SG CYS A 245 27.318 -3.133 -8.677 1.00 21.55 ATOM 1700 C CYS A 245 29.486 -0.241 -6.640 1.00 20.15 ATOM 1701 O CYS A 245 30.599 -0.019 -7.123 1.00 19.66 ATOM 1702 N VAL A 246 28.811 0.662 -5.929 1.00 19.48 ATOM 1703 CA VAL A 246 29.378 1.981 -5.649 1.00 18.83 ATOM 1704 CB VAL A 246 28.309 2.946 -5.051 1.00 18.67 ATOM 1705 CG1 VAL A 246 28.958 4.283 -4.640 1.00 17.82 ATOM 1706 CG2 VAL A 246 27.215 3.206 -6.084 1.00 17.01 ATOM 1707 C VAL A 246 30.558 1.835 -4.674 1.00 19.39 ATOM 1708 O VAL A 246 31.610 2.436 -4.876 1.00 19.24 ATOM 1709 N LEU A 247 30.385 1.030 -3.627 1.00 19.52 ATOM 1710 CA LEU A 247 31.453 0.812 -2.652 1.00 20.75 ATOM 1711 CB LEU A 247 30.993 -0.159 -1.553 1.00 20.36 ATOM 1712 CG LEU A 247 32.073 -0.753 -0.629 1.00 20.88 ATOM 1713 CD1 LEU A 247 32.733 0.349 0.194 1.00 19.39 ATOM 1714 CD2 LEU A 247 31.451 -1.812 0.283 1.00 20.20 ATOM 1715 C LEU A 247 32.698 0.245 -3.335 1.00 21.54 ATOM 1716 O LEU A 247 33.804 0.765 -3.162 1.00 22.16 ATOM 1717 N ALA A 248 32.519 -0.821 -4.109 1.00 21.65 ATOM 1718 CA ALA A 248 33.642 -1.451 -4.803 1.00 22.26 ATOM 1719 CB ALA A 248 33.159 -2.679 -5.569 1.00 21.78 ATOM 1720 C ALA A 248 34.336 -0.476 -5.750 1.00 22.37 ATOM 1721 O ALA A 248 35.560 -0.466 -5.860 1.00 22.61 ATOM 1722 N GLU A 249 33.550 0.353 -6.427 1.00 22.90 ATOM 1723 CA GLU A 249 34.088 1.338 -7.360 1.00 22.59 ATOM 1724 CB GLU A 249 32.941 1.995 -8.123 1.00 22.99 ATOM 1725 CG GLU A 249 33.351 3.155 -9.010 1.00 23.72 ATOM 1726 CD GLU A 249 32.307 3.481 -10.066 1.00 24.47 ATOM 1727 OE1 GLU A 249 31.304 2.729 -10.194 1.00 24.23 ATOM 1728 OE2 GLU A 249 32.496 4.493 -10.773 1.00 23.60 ATOM 1729 C GLU A 249 34.906 2.408 -6.634 1.00 23.38 ATOM 1730 O GLU A 249 35.905 2.902 -7.164 1.00 22.93 ATOM 1731 N LEU A 250 34.478 2.772 -5.426 1.00 23.90 ATOM 1732 CA LEU A 250 35.196 3.784 -4.647 1.00 24.93 ATOM 1733 CB LEU A 250 34.346 4.271 -3.467 1.00 23.60 ATOM 1734 CG LEU A 250 33.160 5.160 -3.848 1.00 22.62 ATOM 1735 CD1 LEU A 250 32.420 5.599 -2.589 1.00 22.07 ATOM 1736 CD2 LEU A 250 33.659 6.370 -4.636 1.00 21.28 ATOM 1737 C LEU A 250 36.499 3.190 -4.134 1.00 25.50 ATOM 1738 O LEU A 250 37.484 3.899 -3.966 1.00 26.47 ATOM 1739 N LEU A 251 36.489 1.882 -3.889 1.00 25.98 ATOM 1740 CA LEU A 251 37.662 1.162 -3.407 1.00 26.98 ATOM 1741 CB LEU A 251 37.246 -0.177 -2.787 1.00 26.26 ATOM 1742 CG LEU A 251 36.480 -0.163 -1.458 1.00 27.16 ATOM 1743 CD1 LEU A 251 36.069 -1.582 -1.071 1.00 25.53 ATOM 1744 CD2 LEU A 251 37.356 0.450 -0.373 1.00 27.26 ATOM 1745 C LEU A 251 38.631 0.898 -4.560 1.00 27.87 ATOM 1746 O LEU A 251 39.836 1.070 -4.412 1.00 28.96 ATOM 1747 N LEU A 252 38.086 0.498 -5.708 1.00 28.22 ATOM 1748 CA LEU A 252 38.865 0.175 -6.902 1.00 28.42 ATOM 1749 CB LEU A 252 38.052 -0.718 -7.829 1.00 28.83 ATOM 1750 CG LEU A 252 37.954 -2.196 -7.487 1.00 29.88 ATOM 1751 CD1 LEU A 252 36.839 -2.821 -8.320 1.00 30.60 ATOM 1752 CD2 LEU A 252 39.293 -2.878 -7.762 1.00 30.35 ATOM 1753 C LEU A 252 39.348 1.356 -7.722 1.00 28.81 ATOM 1754 O LEU A 252 40.435 1.309 -8.284 1.00 29.68 ATOM 1755 N GLY A 253 38.540 2.404 -7.810 1.00 28.22 ATOM 1756 CA GLY A 253 38.928 3.551 -8.604 1.00 27.21 ATOM 1757 C GLY A 253 38.275 3.497 -9.973 1.00 27.99 ATOM 1758 O GLY A 253 38.513 4.361 -10.812 1.00 28.10 ATOM 1759 N GLN A 254 37.442 2.483 -10.200 1.00 28.10 ATOM 1760 CA GLN A 254 36.735 2.326 -11.473 1.00 28.87 ATOM 1761 CB GLN A 254 37.690 1.775 -12.535 1.00 31.05 ATOM 1762 CG GLN A 254 38.429 0.540 -12.079 1.00 33.99 ATOM 1763 CD GLN A 254 39.382 0.017 -13.129 1.00 37.46 ATOM 1764 OE1 GLN A 254 40.352 0.683 -13.485 1.00 39.90 ATOM 1765 NE2 GLN A 254 39.111 -1.183 -13.634 1.00 38.54 ATOM 1766 C GLN A 254 35.558 1.360 -11.286 1.00 27.62 ATOM 1767 O GLN A 254 35.543 0.574 -10.336 1.00 27.54 ATOM 1768 N PRO A 255 34.565 1.394 -12.190 1.00 26.74 ATOM 1769 CD PRO A 255 34.441 2.244 -13.390 1.00 25.53 ATOM 1770 CA PRO A 255 33.421 0.482 -12.038 1.00 26.42 ATOM 1771 CB PRO A 255 32.589 0.721 -13.301 1.00 25.76 ATOM 1772 CG PRO A 255 32.993 2.090 -13.768 1.00 25.99 ATOM 1773 C PRO A 255 33.884 -0.968 -11.920 1.00 26.68 ATOM 1774 O PRO A 255 34.813 -1.381 -12.609 1.00 26.61 ATOM 1775 N ILE A 256 33.247 -1.744 -11.052 1.00 26.91 ATOM 1776 CA ILE A 256 33.648 -3.136 -10.893 1.00 26.57 ATOM 1777 CB ILE A 256 33.365 -3.650 -9.457 1.00 26.96 ATOM 1778 CG2 ILE A 256 31.864 -3.634 -9.169 1.00 26.59 ATOM 1779 CG1 ILE A 256 33.947 -5.060 -9.297 1.00 27.26 ATOM 1780 CD1 ILE A 256 34.059 -5.532 -7.851 1.00 28.11 ATOM 1781 C ILE A 256 33.037 -4.118 -11.898 1.00 26.53 ATOM 1782 O ILE A 256 33.615 -5.173 -12.146 1.00 26.76 ATOM 1783 N PHE A 257 31.883 -3.788 -12.474 1.00 25.80 ATOM 1784 CA PHE A 257 31.237 -4.679 -13.441 1.00 26.08 ATOM 1785 CB PHE A 257 29.968 -5.307 -12.850 1.00 24.92 ATOM 1786 CG PHE A 257 30.207 -6.143 -11.613 1.00 24.36 ATOM 1787 CD1 PHE A 257 29.385 -5.998 -10.496 1.00 22.84 ATOM 1788 CD2 PHE A 257 31.249 -7.075 -11.567 1.00 24.50 ATOM 1789 CE1 PHE A 257 29.590 -6.759 -9.355 1.00 22.66 ATOM 1790 CE2 PHE A 257 31.468 -7.849 -10.424 1.00 23.16 ATOM 1791 CZ PHE A 257 30.634 -7.688 -9.314 1.00 23.85 ATOM 1792 C PHE A 257 30.864 -3.940 -14.717 1.00 26.92 ATOM 1793 O PHE A 257 29.685 -3.803 -15.043 1.00 27.09 ATOM 1794 N PRO A 258 31.868 -3.453 -15.462 1.00 28.14 ATOM 1795 CD PRO A 258 33.316 -3.554 -15.196 1.00 28.28 ATOM 1796 CA PRO A 258 31.595 -2.730 -16.704 1.00 28.04 ATOM 1797 CB PRO A 258 32.925 -2.066 -17.026 1.00 28.36 ATOM 1798 CG PRO A 258 33.938 -3.010 -16.460 1.00 28.23 ATOM 1799 C PRO A 258 31.157 -3.704 -17.786 1.00 28.93 ATOM 1800 O PRO A 258 31.248 -4.923 -17.610 1.00 28.79 ATOM 1801 N GLY A 259 30.672 -3.160 -18.896 1.00 29.64 ATOM 1802 CA GLY A 259 30.220 -3.985 -20.001 1.00 30.69 ATOM 1803 C GLY A 259 29.184 -3.230 -20.801 1.00 32.07 ATOM 1804 O GLY A 259 28.269 -2.640 -20.227 1.00 32.61 ATOM 1805 N ASP A 260 29.317 -3.244 -22.124 1.00 32.98 ATOM 1806 CA ASP A 260 28.371 -2.531 -22.977 1.00 33.51 ATOM 1807 CB ASP A 260 29.021 -2.201 -24.325 1.00 36.79 ATOM 1808 CG ASP A 260 30.004 -1.032 -24.231 1.00 39.83 ATOM 1809 OD1 ASP A 260 29.846 -0.168 -23.331 1.00 41.46 ATOM 1810 OD2 ASP A 260 30.940 -0.980 -25.061 1.00 42.06 ATOM 1811 C ASP A 260 27.078 -3.316 -23.189 1.00 32.34 ATOM 1812 O ASP A 260 26.042 -2.746 -23.525 1.00 31.95 ATOM 1813 N SER A 261 27.137 -4.625 -22.984 1.00 31.05 ATOM 1814 CA SER A 261 25.960 -5.469 -23.132 1.00 29.58 ATOM 1815 CB SER A 261 26.164 -6.481 -24.256 1.00 29.19 ATOM 1816 OG SER A 261 27.061 -7.504 -23.853 1.00 30.14 ATOM 1817 C SER A 261 25.704 -6.224 -21.836 1.00 28.94 ATOM 1818 O SER A 261 26.599 -6.360 -20.998 1.00 28.29 ATOM 1819 N GLY A 262 24.477 -6.713 -21.681 1.00 28.19 ATOM 1820 CA GLY A 262 24.136 -7.480 -20.502 1.00 27.81 ATOM 1821 C GLY A 262 25.048 -8.683 -20.385 1.00 27.93 ATOM 1822 O GLY A 262 25.450 -9.057 -19.289 1.00 27.42 ATOM 1823 N VAL A 263 25.385 -9.294 -21.517 1.00 28.62 ATOM 1824 CA VAL A 263 26.269 -10.463 -21.514 1.00 29.55 ATOM 1825 CB VAL A 263 26.450 -11.054 -22.944 1.00 30.52 ATOM 1826 CG1 VAL A 263 27.501 -12.174 -22.918 1.00 31.18 ATOM 1827 CG2 VAL A 263 25.126 -11.590 -23.462 1.00 30.73 ATOM 1828 C VAL A 263 27.657 -10.121 -20.965 1.00 29.37 ATOM 1829 O VAL A 263 28.234 -10.885 -20.181 1.00 29.63 ATOM 1830 N ASP A 264 28.196 -8.981 -21.388 1.00 29.19 ATOM 1831 CA ASP A 264 29.513 -8.553 -20.933 1.00 29.52 ATOM 1832 CB ASP A 264 29.954 -7.319 -21.704 1.00 31.73 ATOM 1833 CG ASP A 264 30.146 -7.603 -23.177 1.00 34.85 ATOM 1834 OD1 ASP A 264 30.037 -6.654 -23.985 1.00 37.15 ATOM 1835 OD2 ASP A 264 30.403 -8.780 -23.521 1.00 35.48 ATOM 1836 C ASP A 264 29.513 -8.256 -19.440 1.00 29.16 ATOM 1837 O ASP A 264 30.456 -8.604 -18.727 1.00 29.34 ATOM 1838 N GLN A 265 28.456 -7.603 -18.976 1.00 28.02 ATOM 1839 CA GLN A 265 28.314 -7.279 -17.567 1.00 27.92 ATOM 1840 CB GLN A 265 27.033 -6.476 -17.342 1.00 27.99 ATOM 1841 CG GLN A 265 27.172 -5.010 -17.732 1.00 30.08 ATOM 1842 CD GLN A 265 25.837 -4.333 -17.985 1.00 30.90 ATOM 1843 OE1 GLN A 265 25.740 -3.427 -18.807 1.00 34.27 ATOM 1844 NE2 GLN A 265 24.808 -4.765 -17.281 1.00 30.80 ATOM 1845 C GLN A 265 28.273 -8.559 -16.737 1.00 27.56 ATOM 1846 O GLN A 265 28.917 -8.643 -15.693 1.00 27.69 ATOM 1847 N LEU A 266 27.518 -9.553 -17.208 1.00 27.61 ATOM 1848 CA LEU A 266 27.396 -10.832 -16.508 1.00 28.01 ATOM 1849 CB LEU A 266 26.316 -11.695 -17.165 1.00 27.79 ATOM 1850 CG LEU A 266 24.890 -11.246 -16.824 1.00 28.73 ATOM 1851 CD1 LEU A 266 23.895 -11.923 -17.743 1.00 29.09 ATOM 1852 CD2 LEU A 266 24.573 -11.579 -15.374 1.00 28.66 ATOM 1853 C LEU A 266 28.723 -11.589 -16.468 1.00 28.53 ATOM 1854 O LEU A 266 29.034 -12.271 -15.491 1.00 28.53 ATOM 1855 N VAL A 267 29.512 -11.464 -17.527 1.00 29.33 ATOM 1856 CA VAL A 267 30.808 -12.131 -17.571 1.00 30.43 ATOM 1857 CB VAL A 267 31.454 -12.017 -18.985 1.00 30.93 ATOM 1858 CG1 VAL A 267 32.936 -12.362 -18.919 1.00 31.15 ATOM 1859 CG2 VAL A 267 30.731 -12.942 -19.964 1.00 30.11 ATOM 1860 C VAL A 267 31.734 -11.499 -16.526 1.00 31.36 ATOM 1861 O VAL A 267 32.556 -12.181 -15.914 1.00 31.34 ATOM 1862 N GLU A 268 31.598 -10.192 -16.322 1.00 31.56 ATOM 1863 CA GLU A 268 32.419 -9.495 -15.341 1.00 31.48 ATOM 1864 CB GLU A 268 32.281 -7.982 -15.514 1.00 32.62 ATOM 1865 CG GLU A 268 32.899 -7.451 -16.790 1.00 33.66 ATOM 1866 CD GLU A 268 34.350 -7.868 -16.951 1.00 35.13 ATOM 1867 OE1 GLU A 268 35.057 -7.990 -15.929 1.00 35.75 ATOM 1868 OE2 GLU A 268 34.786 -8.079 -18.102 1.00 37.22 ATOM 1869 C GLU A 268 31.981 -9.893 -13.933 1.00 31.02 ATOM 1870 O GLU A 268 32.805 -10.016 -13.027 1.00 30.57 ATOM 1871 N ILE A 269 30.677 -10.095 -13.758 1.00 30.25 ATOM 1872 CA ILE A 269 30.143 -10.486 -12.462 1.00 29.81 ATOM 1873 CB ILE A 269 28.591 -10.424 -12.440 1.00 28.30 ATOM 1874 CG2 ILE A 269 28.049 -11.025 -11.143 1.00 27.55 ATOM 1875 CG1 ILE A 269 28.131 -8.971 -12.567 1.00 26.87 ATOM 1876 CD1 ILE A 269 26.631 -8.816 -12.593 1.00 24.21 ATOM 1877 C ILE A 269 30.598 -11.913 -12.168 1.00 31.18 ATOM 1878 O ILE A 269 31.059 -12.208 -11.069 1.00 30.99 ATOM 1879 N ILE A 270 30.476 -12.791 -13.158 1.00 32.16 ATOM 1880 CA ILE A 270 30.882 -14.186 -12.993 1.00 33.71 ATOM 1881 CB ILE A 270 30.524 -15.034 -14.247 1.00 32.76 ATOM 1882 CG2 ILE A 270 31.291 -16.360 -14.230 1.00 33.16 ATOM 1883 CG1 ILE A 270 29.019 -15.305 -14.266 1.00 32.09 ATOM 1884 CD1 ILE A 270 28.479 -15.704 -15.618 1.00 30.87 ATOM 1885 C ILE A 270 32.381 -14.308 -12.715 1.00 34.56 ATOM 1886 O ILE A 270 32.805 -15.164 -11.940 1.00 35.67 ATOM 1887 N LYS A 271 33.183 -13.450 -13.336 1.00 35.44 ATOM 1888 CA LYS A 271 34.620 -13.504 -13.118 1.00 36.89 ATOM 1889 CB LYS A 271 35.333 -12.440 -13.952 1.00 37.91 ATOM 1890 CG LYS A 271 35.328 -12.734 -15.444 1.00 40.02 ATOM 1891 CD LYS A 271 36.511 -12.095 -16.138 1.00 41.88 ATOM 1892 CE LYS A 271 36.151 -11.668 -17.547 1.00 43.60 ATOM 1893 NZ LYS A 271 36.962 -10.487 -17.958 1.00 45.70 ATOM 1894 C LYS A 271 34.936 -13.302 -11.643 1.00 37.49 ATOM 1895 O LYS A 271 35.868 -13.911 -11.104 1.00 37.95 ATOM 1896 N VAL A 272 34.150 -12.459 -10.981 1.00 36.79 ATOM 1897 CA VAL A 272 34.381 -12.191 -9.571 1.00 36.34 ATOM 1898 CB VAL A 272 33.981 -10.746 -9.192 1.00 35.35 ATOM 1899 CG1 VAL A 272 34.190 -10.525 -7.701 1.00 35.18 ATOM 1900 CG2 VAL A 272 34.804 -9.753 -9.984 1.00 34.67 ATOM 1901 C VAL A 272 33.644 -13.149 -8.645 1.00 36.74 ATOM 1902 O VAL A 272 34.242 -13.709 -7.734 1.00 36.89 ATOM 1903 N LEU A 273 32.351 -13.340 -8.879 1.00 37.32 ATOM 1904 CA LEU A 273 31.544 -14.211 -8.030 1.00 38.11 ATOM 1905 CB LEU A 273 30.095 -13.718 -7.985 1.00 37.10 ATOM 1906 CG LEU A 273 29.781 -12.269 -7.587 1.00 36.57 ATOM 1907 CD1 LEU A 273 28.272 -12.105 -7.433 1.00 34.94 ATOM 1908 CD2 LEU A 273 30.482 -11.928 -6.302 1.00 36.22 ATOM 1909 C LEU A 273 31.529 -15.678 -8.434 1.00 39.24 ATOM 1910 O LEU A 273 31.057 -16.515 -7.676 1.00 39.89 ATOM 1911 N GLY A 274 32.037 -15.997 -9.616 1.00 40.27 ATOM 1912 CA GLY A 274 32.007 -17.380 -10.052 1.00 41.51 ATOM 1913 C GLY A 274 30.662 -17.641 -10.697 1.00 42.56 ATOM 1914 O GLY A 274 29.745 -16.833 -10.559 1.00 42.73 ATOM 1915 N THR A 275 30.531 -18.762 -11.397 1.00 43.71 ATOM 1916 CA THR A 275 29.278 -19.089 -12.073 1.00 44.99 ATOM 1917 CB THR A 275 29.443 -20.348 -12.966 1.00 45.10 ATOM 1918 OG1 THR A 275 30.510 -20.130 -13.900 1.00 44.99 ATOM 1919 CG2 THR A 275 28.161 -20.632 -13.742 1.00 44.55 ATOM 1920 C THR A 275 28.126 -19.295 -11.093 1.00 45.79 ATOM 1921 O THR A 275 28.272 -19.956 -10.071 1.00 45.97 ATOM 1922 N PRO A 276 26.957 -18.714 -11.393 1.00 46.52 ATOM 1923 CD PRO A 276 26.625 -17.878 -12.557 1.00 46.44 ATOM 1924 CA PRO A 276 25.816 -18.873 -10.492 1.00 47.61 ATOM 1925 CB PRO A 276 24.813 -17.840 -10.998 1.00 46.99 ATOM 1926 CG PRO A 276 25.128 -17.708 -12.443 1.00 46.61 ATOM 1927 C PRO A 276 25.228 -20.276 -10.497 1.00 49.29 ATOM 1928 O PRO A 276 25.040 -20.891 -11.543 1.00 49.59 ATOM 1929 N THR A 277 24.938 -20.765 -9.301 1.00 50.79 ATOM 1930 CA THR A 277 24.342 -22.074 -9.095 1.00 51.74 ATOM 1931 CB THR A 277 24.151 -22.302 -7.584 1.00 51.68 ATOM 1932 OG1 THR A 277 25.238 -23.092 -7.094 1.00 52.44 ATOM 1933 CG2 THR A 277 22.833 -22.979 -7.276 1.00 51.87 ATOM 1934 C THR A 277 22.995 -22.087 -9.804 1.00 52.69 ATOM 1935 O THR A 277 22.477 -21.033 -10.167 1.00 53.00 ATOM 1936 N ARG A 278 22.429 -23.272 -10.009 1.00 54.03 ATOM 1937 CA ARG A 278 21.133 -23.368 -10.670 1.00 55.18 ATOM 1938 CB ARG A 278 20.778 -24.832 -10.952 1.00 57.07 ATOM 1939 CG ARG A 278 20.205 -25.084 -12.350 1.00 59.51 ATOM 1940 CD ARG A 278 19.930 -26.573 -12.566 1.00 62.14 ATOM 1941 NE ARG A 278 18.887 -26.824 -13.562 1.00 64.29 ATOM 1942 CZ ARG A 278 18.294 -28.004 -13.745 1.00 65.24 ATOM 1943 NH1 ARG A 278 18.640 -29.050 -12.999 1.00 65.55 ATOM 1944 NH2 ARG A 278 17.362 -28.146 -14.681 1.00 65.54 ATOM 1945 C ARG A 278 20.078 -22.733 -9.772 1.00 54.85 ATOM 1946 O ARG A 278 19.167 -22.059 -10.255 1.00 54.75 ATOM 1947 N GLU A 279 20.211 -22.947 -8.463 1.00 54.84 ATOM 1948 CA GLU A 279 19.277 -22.386 -7.487 1.00 54.92 ATOM 1949 CB GLU A 279 19.542 -22.956 -6.085 1.00 56.19 ATOM 1950 CG GLU A 279 18.346 -23.683 -5.458 1.00 58.68 ATOM 1951 CD GLU A 279 17.233 -22.742 -4.981 1.00 60.41 ATOM 1952 OE1 GLU A 279 16.454 -22.242 -5.828 1.00 61.14 ATOM 1953 OE2 GLU A 279 17.133 -22.506 -3.753 1.00 61.09 ATOM 1954 C GLU A 279 19.421 -20.866 -7.453 1.00 54.12 ATOM 1955 O GLU A 279 18.431 -20.143 -7.360 1.00 54.01 ATOM 1956 N GLN A 280 20.660 -20.387 -7.527 1.00 53.08 ATOM 1957 CA GLN A 280 20.920 -18.955 -7.521 1.00 51.81 ATOM 1958 CB GLN A 280 22.422 -18.690 -7.532 1.00 50.15 ATOM 1959 CG GLN A 280 23.050 -18.865 -6.174 1.00 48.50 ATOM 1960 CD GLN A 280 24.549 -18.764 -6.211 1.00 48.01 ATOM 1961 OE1 GLN A 280 25.183 -19.078 -7.215 1.00 47.59 ATOM 1962 NE2 GLN A 280 25.133 -18.321 -5.109 1.00 48.21 ATOM 1963 C GLN A 280 20.266 -18.320 -8.737 1.00 52.06 ATOM 1964 O GLN A 280 19.626 -17.278 -8.628 1.00 51.97 ATOM 1965 N ILE A 281 20.421 -18.951 -9.895 1.00 52.45 ATOM 1966 CA ILE A 281 19.812 -18.435 -11.113 1.00 53.52 ATOM 1967 CB ILE A 281 20.152 -19.321 -12.329 1.00 53.41 ATOM 1968 CG2 ILE A 281 19.191 -19.029 -13.474 1.00 53.45 ATOM 1969 CG1 ILE A 281 21.593 -19.062 -12.771 1.00 53.37 ATOM 1970 CD1 ILE A 281 22.189 -20.171 -13.610 1.00 53.74 ATOM 1971 C ILE A 281 18.297 -18.400 -10.925 1.00 54.21 ATOM 1972 O ILE A 281 17.628 -17.451 -11.330 1.00 53.95 ATOM 1973 N ARG A 282 17.772 -19.447 -10.297 1.00 55.57 ATOM 1974 CA ARG A 282 16.345 -19.572 -10.031 1.00 57.00 ATOM 1975 CB ARG A 282 16.065 -20.958 -9.440 1.00 58.98 ATOM 1976 CG ARG A 282 14.601 -21.274 -9.173 1.00 61.62 ATOM 1977 CD ARG A 282 14.470 -22.513 -8.281 1.00 64.34 ATOM 1978 NE ARG A 282 13.213 -22.540 -7.527 1.00 66.44 ATOM 1979 CZ ARG A 282 12.975 -23.332 -6.480 1.00 67.38 ATOM 1980 NH1 ARG A 282 13.910 -24.176 -6.050 1.00 67.68 ATOM 1981 NH2 ARG A 282 11.797 -23.288 -5.864 1.00 67.37 ATOM 1982 C ARG A 282 15.899 -18.477 -9.062 1.00 57.12 ATOM 1983 O ARG A 282 14.790 -17.959 -9.164 1.00 56.76 ATOM 1984 N GLU A 283 16.779 -18.135 -8.124 1.00 57.77 ATOM 1985 CA GLU A 283 16.514 -17.092 -7.132 1.00 58.69 ATOM 1986 CB GLU A 283 17.653 -17.031 -6.112 1.00 59.00 ATOM 1987 CG GLU A 283 17.922 -18.327 -5.393 1.00 60.19 ATOM 1988 CD GLU A 283 17.239 -18.390 -4.049 1.00 61.36 ATOM 1989 OE1 GLU A 283 17.768 -19.082 -3.149 1.00 61.80 ATOM 1990 OE2 GLU A 283 16.173 -17.748 -3.890 1.00 61.75 ATOM 1991 C GLU A 283 16.379 -15.717 -7.790 1.00 59.05 ATOM 1992 O GLU A 283 15.526 -14.913 -7.411 1.00 58.67 ATOM 1993 N MET A 284 17.234 -15.450 -8.770 1.00 59.56 ATOM 1994 CA MET A 284 17.215 -14.180 -9.476 1.00 60.75 ATOM 1995 CB MET A 284 18.500 -14.021 -10.276 1.00 58.76 ATOM 1996 CG MET A 284 19.736 -14.100 -9.424 1.00 56.89 ATOM 1997 SD MET A 284 21.234 -14.132 -10.384 1.00 54.22 ATOM 1998 CE MET A 284 22.192 -13.257 -9.380 1.00 55.51 ATOM 1999 C MET A 284 16.018 -14.066 -10.406 1.00 62.94 ATOM 2000 O MET A 284 15.229 -13.128 -10.308 1.00 62.46 ATOM 2001 N ASN A 285 15.895 -15.028 -11.314 1.00 66.31 ATOM 2002 CA ASN A 285 14.801 -15.052 -12.278 1.00 69.68 ATOM 2003 CB ASN A 285 15.070 -14.086 -13.433 1.00 69.30 ATOM 2004 CG ASN A 285 13.939 -14.057 -14.439 1.00 69.18 ATOM 2005 OD1 ASN A 285 14.156 -14.173 -15.646 1.00 68.45 ATOM 2006 ND2 ASN A 285 12.717 -13.904 -13.942 1.00 69.18 ATOM 2007 C ASN A 285 14.658 -16.454 -12.836 1.00 72.45 ATOM 2008 O ASN A 285 15.437 -16.874 -13.698 1.00 72.35 ATOM 2009 N PRO A 286 13.655 -17.200 -12.354 1.00 75.40 ATOM 2010 CD PRO A 286 12.667 -16.783 -11.337 1.00 75.67 ATOM 2011 CA PRO A 286 13.431 -18.572 -12.825 1.00 77.92 ATOM 2012 CB PRO A 286 12.568 -19.190 -11.730 1.00 77.54 ATOM 2013 CG PRO A 286 11.821 -18.017 -11.136 1.00 76.81 ATOM 2014 C PRO A 286 12.743 -18.604 -14.190 1.00 80.26 ATOM 2015 O PRO A 286 11.636 -19.128 -14.321 1.00 80.53 ATOM 2016 N ASN A 287 13.405 -18.050 -15.203 1.00 82.85 ATOM 2017 CA ASN A 287 12.826 -18.008 -16.538 1.00 85.53 ATOM 2018 CB ASN A 287 11.965 -16.749 -16.686 1.00 85.83 ATOM 2019 CG ASN A 287 10.850 -16.674 -15.651 1.00 86.37 ATOM 2020 OD1 ASN A 287 9.816 -17.335 -15.784 1.00 86.55 ATOM 2021 ND2 ASN A 287 11.055 -15.869 -14.613 1.00 86.43 ATOM 2022 C ASN A 287 13.843 -18.065 -17.676 1.00 87.37 ATOM 2023 O ASN A 287 13.851 -19.022 -18.450 1.00 87.75 ATOM 2024 N TYR A 288 14.695 -17.044 -17.773 1.00 89.39 ATOM 2025 CA TYR A 288 15.700 -16.954 -18.838 1.00 91.09 ATOM 2026 CB TYR A 288 16.783 -15.946 -18.462 1.00 91.89 ATOM 2027 CG TYR A 288 16.460 -14.561 -18.961 1.00 93.14 ATOM 2028 CD1 TYR A 288 15.142 -14.099 -18.977 1.00 93.86 ATOM 2029 CE1 TYR A 288 14.832 -12.820 -19.427 1.00 94.34 ATOM 2030 CD2 TYR A 288 17.461 -13.708 -19.413 1.00 93.63 ATOM 2031 CE2 TYR A 288 17.161 -12.425 -19.865 1.00 94.25 ATOM 2032 CZ TYR A 288 15.847 -11.989 -19.865 1.00 94.58 ATOM 2033 OH TYR A 288 15.547 -10.711 -20.258 1.00 95.25 ATOM 2034 C TYR A 288 16.343 -18.261 -19.276 1.00 91.78 ATOM 2035 O TYR A 288 16.968 -18.971 -18.484 1.00 92.00 ATOM 2036 N THR A 289 16.194 -18.540 -20.567 1.00 92.31 ATOM 2037 CA THR A 289 16.692 -19.754 -21.201 1.00 92.74 ATOM 2038 CB THR A 289 16.210 -19.809 -22.660 1.00 92.74 ATOM 2039 OG1 THR A 289 15.274 -18.747 -22.886 1.00 92.59 ATOM 2040 CG2 THR A 289 15.539 -21.144 -22.950 1.00 92.56 ATOM 2041 C THR A 289 18.203 -19.996 -21.175 1.00 93.09 ATOM 2042 O THR A 289 18.663 -20.951 -20.547 1.00 93.21 ATOM 2043 N GLU A 290 18.970 -19.150 -21.861 1.00 93.33 ATOM 2044 CA GLU A 290 20.425 -19.309 -21.915 1.00 93.40 ATOM 2045 CB GLU A 290 21.102 -18.037 -22.438 1.00 93.56 ATOM 2046 CG GLU A 290 22.498 -18.242 -23.013 1.00 93.62 ATOM 2047 CD GLU A 290 22.680 -17.565 -24.366 1.00 93.62 ATOM 2048 OE1 GLU A 290 23.416 -16.554 -24.433 1.00 93.25 ATOM 2049 OE2 GLU A 290 22.090 -18.042 -25.361 1.00 93.29 ATOM 2050 C GLU A 290 21.018 -19.655 -20.562 1.00 93.35 ATOM 2051 O GLU A 290 20.953 -18.870 -19.613 1.00 93.77 ATOM 2052 N PHE A 291 21.588 -20.848 -20.483 1.00 92.98 ATOM 2053 CA PHE A 291 22.219 -21.312 -19.264 1.00 92.64 ATOM 2054 CB PHE A 291 21.505 -22.566 -18.739 1.00 93.01 ATOM 2055 CG PHE A 291 20.302 -22.270 -17.867 1.00 93.34 ATOM 2056 CD1 PHE A 291 19.674 -23.294 -17.161 1.00 93.26 ATOM 2057 CD2 PHE A 291 19.799 -20.973 -17.749 1.00 93.55 ATOM 2058 CE1 PHE A 291 18.562 -23.033 -16.351 1.00 93.28 ATOM 2059 CE2 PHE A 291 18.687 -20.702 -16.940 1.00 93.46 ATOM 2060 CZ PHE A 291 18.069 -21.734 -16.241 1.00 93.26 ATOM 2061 C PHE A 291 23.660 -21.625 -19.644 1.00 92.17 ATOM 2062 O PHE A 291 24.415 -22.205 -18.863 1.00 92.33 ATOM 2063 N LYS A 292 24.026 -21.223 -20.860 1.00 91.33 ATOM 2064 CA LYS A 292 25.370 -21.438 -21.388 1.00 90.60 ATOM 2065 CB LYS A 292 25.332 -21.493 -22.923 1.00 90.94 ATOM 2066 CG LYS A 292 26.684 -21.263 -23.610 1.00 91.32 ATOM 2067 CD LYS A 292 26.511 -20.750 -25.042 1.00 91.45 ATOM 2068 CE LYS A 292 27.552 -21.343 -25.991 1.00 91.47 ATOM 2069 NZ LYS A 292 27.256 -22.758 -26.365 1.00 91.37 ATOM 2070 C LYS A 292 26.303 -20.321 -20.939 1.00 89.78 ATOM 2071 O LYS A 292 26.348 -19.257 -21.551 1.00 89.68 ATOM 2072 N PHE A 293 27.044 -20.564 -19.865 1.00 88.95 ATOM 2073 CA PHE A 293 27.971 -19.566 -19.358 1.00 88.18 ATOM 2074 CB PHE A 293 27.284 -18.668 -18.327 1.00 88.18 ATOM 2075 CG PHE A 293 27.135 -17.243 -18.779 1.00 88.17 ATOM 2076 CD1 PHE A 293 25.877 -16.653 -18.869 1.00 88.08 ATOM 2077 CD2 PHE A 293 28.253 -16.497 -19.147 1.00 88.07 ATOM 2078 CE1 PHE A 293 25.734 -15.343 -19.323 1.00 87.81 ATOM 2079 CE2 PHE A 293 28.121 -15.187 -19.602 1.00 87.83 ATOM 2080 CZ PHE A 293 26.859 -14.609 -19.690 1.00 87.87 ATOM 2081 C PHE A 293 29.204 -20.200 -18.744 1.00 87.60 ATOM 2082 O PHE A 293 29.106 -20.977 -17.794 1.00 87.64 ATOM 2083 N PRO A 294 30.387 -19.877 -19.292 1.00 87.09 ATOM 2084 CD PRO A 294 30.558 -18.980 -20.445 1.00 87.12 ATOM 2085 CA PRO A 294 31.675 -20.396 -18.822 1.00 86.49 ATOM 2086 CB PRO A 294 32.690 -19.349 -19.297 1.00 86.74 ATOM 2087 CG PRO A 294 31.926 -18.408 -20.224 1.00 87.04 ATOM 2088 C PRO A 294 31.727 -20.602 -17.310 1.00 85.69 ATOM 2089 O PRO A 294 31.500 -19.672 -16.534 1.00 85.43 ATOM 2090 N GLN A 295 32.020 -21.834 -16.904 1.00 84.81 ATOM 2091 CA GLN A 295 32.109 -22.178 -15.491 1.00 83.80 ATOM 2092 CB GLN A 295 32.067 -23.697 -15.301 1.00 84.16 ATOM 2093 CG GLN A 295 31.676 -24.466 -16.547 1.00 84.67 ATOM 2094 CD GLN A 295 30.251 -24.182 -16.968 1.00 85.14 ATOM 2095 OE1 GLN A 295 29.946 -24.098 -18.161 1.00 85.32 ATOM 2096 NE2 GLN A 295 29.366 -24.029 -15.987 1.00 84.99 ATOM 2097 C GLN A 295 33.406 -21.637 -14.916 1.00 82.70 ATOM 2098 O GLN A 295 34.451 -22.277 -15.019 1.00 82.69 ATOM 2099 N ILE A 296 33.337 -20.454 -14.320 1.00 81.37 ATOM 2100 CA ILE A 296 34.512 -19.842 -13.726 1.00 79.91 ATOM 2101 CB ILE A 296 34.623 -18.344 -14.115 1.00 79.58 ATOM 2102 CG2 ILE A 296 35.280 -17.551 -12.998 1.00 79.45 ATOM 2103 CG1 ILE A 296 35.450 -18.202 -15.395 1.00 79.37 ATOM 2104 CD1 ILE A 296 34.656 -18.394 -16.667 1.00 79.21 ATOM 2105 C ILE A 296 34.412 -19.980 -12.215 1.00 79.24 ATOM 2106 O ILE A 296 33.329 -19.865 -11.640 1.00 79.10 ATOM 2107 N LYS A 297 35.544 -20.255 -11.580 1.00 78.33 ATOM 2108 CA LYS A 297 35.583 -20.396 -10.136 1.00 77.33 ATOM 2109 CB LYS A 297 36.867 -21.118 -9.708 1.00 78.29 ATOM 2110 CG LYS A 297 38.156 -20.345 -10.000 1.00 79.18 ATOM 2111 CD LYS A 297 38.680 -20.641 -11.403 1.00 79.95 ATOM 2112 CE LYS A 297 39.435 -19.449 -11.981 1.00 80.70 ATOM 2113 NZ LYS A 297 39.384 -19.419 -13.475 1.00 80.69 ATOM 2114 C LYS A 297 35.543 -18.995 -9.538 1.00 76.21 ATOM 2115 O LYS A 297 36.005 -18.033 -10.158 1.00 75.99 ATOM 2116 N ALA A 298 34.984 -18.882 -8.340 1.00 74.88 ATOM 2117 CA ALA A 298 34.895 -17.593 -7.670 1.00 73.38 ATOM 2118 CB ALA A 298 34.234 -17.758 -6.314 1.00 73.14 ATOM 2119 C ALA A 298 36.287 -16.997 -7.504 1.00 72.43 ATOM 2120 O ALA A 298 37.205 -17.670 -7.032 1.00 72.41 ATOM 2121 N HIS A 299 36.440 -15.740 -7.904 1.00 71.22 ATOM 2122 CA HIS A 299 37.716 -15.043 -7.784 1.00 70.07 ATOM 2123 CB HIS A 299 37.783 -13.901 -8.801 1.00 71.16 ATOM 2124 CG HIS A 299 39.133 -13.263 -8.909 1.00 72.25 ATOM 2125 CD2 HIS A 299 39.512 -12.055 -9.391 1.00 72.99 ATOM 2126 ND1 HIS A 299 40.287 -13.886 -8.487 1.00 72.80 ATOM 2127 CE1 HIS A 299 41.320 -13.091 -8.704 1.00 73.20 ATOM 2128 NE2 HIS A 299 40.877 -11.973 -9.252 1.00 73.47 ATOM 2129 C HIS A 299 37.850 -14.491 -6.360 1.00 68.56 ATOM 2130 O HIS A 299 37.057 -13.651 -5.931 1.00 68.70 ATOM 2131 N PRO A 300 38.862 -14.956 -5.611 1.00 66.96 ATOM 2132 CD PRO A 300 39.885 -15.931 -6.027 1.00 66.80 ATOM 2133 CA PRO A 300 39.079 -14.496 -4.235 1.00 65.20 ATOM 2134 CB PRO A 300 40.497 -14.980 -3.899 1.00 65.73 ATOM 2135 CG PRO A 300 41.062 -15.546 -5.191 1.00 66.14 ATOM 2136 C PRO A 300 38.936 -12.982 -4.106 1.00 63.43 ATOM 2137 O PRO A 300 39.783 -12.221 -4.585 1.00 63.29 ATOM 2138 N TRP A 301 37.853 -12.563 -3.457 1.00 61.07 ATOM 2139 CA TRP A 301 37.548 -11.153 -3.250 1.00 58.44 ATOM 2140 CB TRP A 301 36.442 -11.011 -2.204 1.00 55.34 ATOM 2141 CG TRP A 301 35.057 -10.936 -2.777 1.00 51.88 ATOM 2142 CD2 TRP A 301 34.495 -9.856 -3.531 1.00 50.16 ATOM 2143 CE2 TRP A 301 33.160 -10.204 -3.830 1.00 49.38 ATOM 2144 CE3 TRP A 301 34.992 -8.625 -3.982 1.00 49.12 ATOM 2145 CD1 TRP A 301 34.068 -11.871 -2.656 1.00 50.77 ATOM 2146 NE1 TRP A 301 32.924 -11.438 -3.284 1.00 49.57 ATOM 2147 CZ2 TRP A 301 32.312 -9.368 -4.560 1.00 48.88 ATOM 2148 CZ3 TRP A 301 34.147 -7.793 -4.709 1.00 48.75 ATOM 2149 CH2 TRP A 301 32.822 -8.169 -4.991 1.00 48.62 ATOM 2150 C TRP A 301 38.766 -10.336 -2.821 1.00 58.53 ATOM 2151 O TRP A 301 38.834 -9.133 -3.086 1.00 58.66 ATOM 2152 N THR A 302 39.725 -10.983 -2.160 1.00 58.39 ATOM 2153 CA THR A 302 40.927 -10.288 -1.709 1.00 57.93 ATOM 2154 CB THR A 302 41.743 -11.140 -0.714 1.00 58.11 ATOM 2155 OG1 THR A 302 40.952 -11.402 0.451 1.00 58.10 ATOM 2156 CG2 THR A 302 43.007 -10.400 -0.292 1.00 57.74 ATOM 2157 C THR A 302 41.823 -9.903 -2.882 1.00 57.47 ATOM 2158 O THR A 302 42.447 -8.840 -2.861 1.00 57.95 ATOM 2159 N LYS A 303 41.883 -10.757 -3.903 1.00 56.58 ATOM 2160 CA LYS A 303 42.709 -10.470 -5.077 1.00 55.92 ATOM 2161 CB LYS A 303 43.003 -11.756 -5.862 1.00 57.91 ATOM 2162 CG LYS A 303 43.997 -11.562 -7.023 1.00 59.78 ATOM 2163 CD LYS A 303 44.539 -12.887 -7.562 1.00 61.05 ATOM 2164 CE LYS A 303 45.070 -12.729 -8.991 1.00 62.29 ATOM 2165 NZ LYS A 303 44.847 -13.942 -9.846 1.00 62.80 ATOM 2166 C LYS A 303 42.047 -9.448 -6.003 1.00 54.29 ATOM 2167 O LYS A 303 42.654 -8.984 -6.968 1.00 54.25 ATOM 2168 N VAL A 304 40.802 -9.095 -5.698 1.00 52.51 ATOM 2169 CA VAL A 304 40.058 -8.130 -6.500 1.00 50.09 ATOM 2170 CB VAL A 304 38.541 -8.200 -6.192 1.00 50.03 ATOM 2171 CG1 VAL A 304 37.813 -7.076 -6.906 1.00 49.34 ATOM 2172 CG2 VAL A 304 37.983 -9.549 -6.613 1.00 49.55 ATOM 2173 C VAL A 304 40.531 -6.702 -6.245 1.00 49.09 ATOM 2174 O VAL A 304 40.625 -5.901 -7.171 1.00 48.32 ATOM 2175 N PHE A 305 40.836 -6.383 -4.991 1.00 48.06 ATOM 2176 CA PHE A 305 41.270 -5.035 -4.644 1.00 47.44 ATOM 2177 CB PHE A 305 40.492 -4.543 -3.420 1.00 45.51 ATOM 2178 CG PHE A 305 38.995 -4.627 -3.570 1.00 43.24 ATOM 2179 CD1 PHE A 305 38.286 -5.686 -3.021 1.00 42.01 ATOM 2180 CD2 PHE A 305 38.292 -3.633 -4.245 1.00 42.64 ATOM 2181 CE1 PHE A 305 36.904 -5.753 -3.137 1.00 41.72 ATOM 2182 CE2 PHE A 305 36.908 -3.693 -4.366 1.00 41.08 ATOM 2183 CZ PHE A 305 36.216 -4.753 -3.811 1.00 40.73 ATOM 2184 C PHE A 305 42.773 -4.914 -4.367 1.00 48.45 ATOM 2185 O PHE A 305 43.464 -5.917 -4.175 1.00 48.87 ATOM 2186 N ARG A 306 43.274 -3.680 -4.347 1.00 49.05 ATOM 2187 CA ARG A 306 44.686 -3.445 -4.070 1.00 50.04 ATOM 2188 CB ARG A 306 44.992 -1.943 -4.076 1.00 50.67 ATOM 2189 CG ARG A 306 44.557 -1.200 -2.830 1.00 52.79 ATOM 2190 CD ARG A 306 44.692 0.309 -3.009 1.00 54.75 ATOM 2191 NE ARG A 306 44.602 1.021 -1.734 1.00 57.42 ATOM 2192 CZ ARG A 306 43.539 0.994 -0.930 1.00 58.93 ATOM 2193 NH1 ARG A 306 42.463 0.285 -1.266 1.00 59.80 ATOM 2194 NH2 ARG A 306 43.546 1.678 0.211 1.00 59.12 ATOM 2195 C ARG A 306 45.017 -4.059 -2.708 1.00 50.43 ATOM 2196 O ARG A 306 44.128 -4.299 -1.889 1.00 50.38 ATOM 2197 N PRO A 307 46.304 -4.335 -2.451 1.00 50.96 ATOM 2198 CD PRO A 307 47.451 -4.113 -3.346 1.00 50.83 ATOM 2199 CA PRO A 307 46.716 -4.934 -1.175 1.00 50.90 ATOM 2200 CB PRO A 307 48.221 -5.159 -1.352 1.00 50.89 ATOM 2201 CG PRO A 307 48.451 -5.097 -2.838 1.00 50.66 ATOM 2202 C PRO A 307 46.397 -4.125 0.085 1.00 50.88 ATOM 2203 O PRO A 307 46.087 -4.694 1.130 1.00 50.95 ATOM 2204 N ARG A 308 46.468 -2.804 -0.012 1.00 51.08 ATOM 2205 CA ARG A 308 46.198 -1.940 1.136 1.00 51.57 ATOM 2206 CB ARG A 308 46.591 -0.501 0.804 1.00 54.11 ATOM 2207 CG ARG A 308 48.065 -0.294 0.518 1.00 57.19 ATOM 2208 CD ARG A 308 48.293 1.091 -0.071 1.00 59.97 ATOM 2209 NE ARG A 308 49.692 1.504 0.015 1.00 62.62 ATOM 2210 CZ ARG A 308 50.193 2.580 -0.589 1.00 64.03 ATOM 2211 NH1 ARG A 308 51.482 2.881 -0.457 1.00 64.47 ATOM 2212 NH2 ARG A 308 49.403 3.357 -1.327 1.00 64.38 ATOM 2213 C ARG A 308 44.741 -1.944 1.616 1.00 50.21 ATOM 2214 O ARG A 308 44.457 -1.584 2.762 1.00 50.31 ATOM 2215 N THR A 309 43.827 -2.339 0.733 1.00 48.02 ATOM 2216 CA THR A 309 42.397 -2.375 1.033 1.00 45.46 ATOM 2217 CB THR A 309 41.634 -3.031 -0.126 1.00 45.12 ATOM 2218 OG1 THR A 309 41.979 -2.367 -1.347 1.00 44.74 ATOM 2219 CG2 THR A 309 40.131 -2.929 0.092 1.00 45.08 ATOM 2220 C THR A 309 42.014 -3.081 2.334 1.00 43.85 ATOM 2221 O THR A 309 42.315 -4.256 2.527 1.00 43.86 ATOM 2222 N PRO A 310 41.323 -2.365 3.240 1.00 42.66 ATOM 2223 CD PRO A 310 40.910 -0.960 3.066 1.00 41.69 ATOM 2224 CA PRO A 310 40.883 -2.906 4.532 1.00 41.41 ATOM 2225 CB PRO A 310 40.115 -1.746 5.168 1.00 41.33 ATOM 2226 CG PRO A 310 40.591 -0.532 4.452 1.00 41.26 ATOM 2227 C PRO A 310 40.008 -4.151 4.385 1.00 40.60 ATOM 2228 O PRO A 310 39.039 -4.149 3.634 1.00 40.70 ATOM 2229 N PRO A 311 40.337 -5.229 5.113 1.00 40.13 ATOM 2230 CD PRO A 311 41.458 -5.340 6.061 1.00 40.03 ATOM 2231 CA PRO A 311 39.569 -6.477 5.045 1.00 39.20 ATOM 2232 CB PRO A 311 40.235 -7.375 6.089 1.00 39.18 ATOM 2233 CG PRO A 311 41.009 -6.452 6.962 1.00 39.75 ATOM 2234 C PRO A 311 38.082 -6.303 5.319 1.00 38.35 ATOM 2235 O PRO A 311 37.258 -7.007 4.741 1.00 38.67 ATOM 2236 N GLU A 312 37.733 -5.378 6.205 1.00 37.44 ATOM 2237 CA GLU A 312 36.324 -5.150 6.512 1.00 36.82 ATOM 2238 CB GLU A 312 36.189 -4.189 7.692 1.00 38.52 ATOM 2239 CG GLU A 312 36.579 -4.807 9.033 1.00 41.17 ATOM 2240 CD GLU A 312 35.830 -6.102 9.332 1.00 44.23 ATOM 2241 OE1 GLU A 312 36.167 -6.772 10.336 1.00 45.98 ATOM 2242 OE2 GLU A 312 34.901 -6.458 8.570 1.00 45.73 ATOM 2243 C GLU A 312 35.574 -4.609 5.286 1.00 34.88 ATOM 2244 O GLU A 312 34.407 -4.932 5.074 1.00 33.91 ATOM 2245 N ALA A 313 36.258 -3.797 4.484 1.00 33.25 ATOM 2246 CA ALA A 313 35.669 -3.247 3.270 1.00 32.87 ATOM 2247 CB ALA A 313 36.619 -2.240 2.634 1.00 31.93 ATOM 2248 C ALA A 313 35.378 -4.383 2.283 1.00 32.85 ATOM 2249 O ALA A 313 34.317 -4.422 1.662 1.00 32.85 ATOM 2250 N ILE A 314 36.325 -5.308 2.138 1.00 32.41 ATOM 2251 CA ILE A 314 36.159 -6.434 1.225 1.00 31.87 ATOM 2252 CB ILE A 314 37.471 -7.246 1.112 1.00 32.08 ATOM 2253 CG2 ILE A 314 37.272 -8.454 0.203 1.00 31.93 ATOM 2254 CG1 ILE A 314 38.580 -6.348 0.560 1.00 32.29 ATOM 2255 CD1 ILE A 314 39.956 -7.000 0.520 1.00 32.54 ATOM 2256 C ILE A 314 35.033 -7.343 1.720 1.00 31.81 ATOM 2257 O ILE A 314 34.188 -7.796 0.938 1.00 32.25 ATOM 2258 N ALA A 315 35.021 -7.597 3.025 1.00 31.07 ATOM 2259 CA ALA A 315 34.001 -8.437 3.640 1.00 29.99 ATOM 2260 CB ALA A 315 34.287 -8.584 5.118 1.00 30.39 ATOM 2261 C ALA A 315 32.601 -7.853 3.430 1.00 29.37 ATOM 2262 O ALA A 315 31.673 -8.569 3.067 1.00 29.64 ATOM 2263 N LEU A 316 32.449 -6.551 3.667 1.00 28.33 ATOM 2264 CA LEU A 316 31.160 -5.889 3.474 1.00 27.29 ATOM 2265 CB LEU A 316 31.269 -4.400 3.813 1.00 25.04 ATOM 2266 CG LEU A 316 30.086 -3.526 3.391 1.00 23.75 ATOM 2267 CD1 LEU A 316 28.798 -4.069 4.008 1.00 22.33 ATOM 2268 CD2 LEU A 316 30.339 -2.086 3.818 1.00 21.01 ATOM 2269 C LEU A 316 30.748 -6.053 2.007 1.00 27.97 ATOM 2270 O LEU A 316 29.594 -6.350 1.691 1.00 27.37 ATOM 2271 N CYS A 317 31.713 -5.869 1.115 1.00 28.25 ATOM 2272 CA CYS A 317 31.466 -5.998 -0.308 1.00 29.36 ATOM 2273 CB CYS A 317 32.761 -5.820 -1.075 1.00 31.37 ATOM 2274 SG CYS A 317 32.803 -4.354 -2.031 1.00 36.53 ATOM 2275 C CYS A 317 30.883 -7.350 -0.677 1.00 29.17 ATOM 2276 O CYS A 317 29.881 -7.429 -1.384 1.00 28.79 ATOM 2277 N SER A 318 31.520 -8.415 -0.203 1.00 29.07 ATOM 2278 CA SER A 318 31.067 -9.761 -0.520 1.00 29.12 ATOM 2279 CB SER A 318 32.062 -10.779 0.022 1.00 29.59 ATOM 2280 OG SER A 318 31.989 -10.834 1.431 1.00 32.54 ATOM 2281 C SER A 318 29.675 -10.067 0.008 1.00 28.68 ATOM 2282 O SER A 318 29.020 -10.993 -0.465 1.00 28.79 ATOM 2283 N ARG A 319 29.214 -9.281 0.976 1.00 28.69 ATOM 2284 CA ARG A 319 27.892 -9.484 1.572 1.00 28.07 ATOM 2285 CB ARG A 319 27.947 -9.189 3.075 1.00 29.62 ATOM 2286 CG ARG A 319 28.896 -10.105 3.837 1.00 32.04 ATOM 2287 CD ARG A 319 28.400 -11.536 3.828 1.00 34.28 ATOM 2288 NE ARG A 319 27.173 -11.670 4.610 1.00 37.49 ATOM 2289 CZ ARG A 319 25.965 -11.876 4.087 1.00 38.41 ATOM 2290 NH1 ARG A 319 25.806 -11.977 2.770 1.00 38.63 ATOM 2291 NH2 ARG A 319 24.909 -11.972 4.884 1.00 39.57 ATOM 2292 C ARG A 319 26.800 -8.641 0.919 1.00 26.48 ATOM 2293 O ARG A 319 25.622 -8.770 1.246 1.00 26.54 ATOM 2294 N LEU A 320 27.200 -7.770 0.004 1.00 25.66 ATOM 2295 CA LEU A 320 26.252 -6.920 -0.713 1.00 24.64 ATOM 2296 CB LEU A 320 26.768 -5.473 -0.800 1.00 22.87 ATOM 2297 CG LEU A 320 26.961 -4.705 0.508 1.00 22.19 ATOM 2298 CD1 LEU A 320 27.640 -3.376 0.218 1.00 22.54 ATOM 2299 CD2 LEU A 320 25.623 -4.472 1.176 1.00 21.58 ATOM 2300 C LEU A 320 26.097 -7.474 -2.124 1.00 24.27 ATOM 2301 O LEU A 320 24.988 -7.595 -2.647 1.00 23.44 ATOM 2302 N LEU A 321 27.229 -7.800 -2.737 1.00 24.66 ATOM 2303 CA LEU A 321 27.232 -8.325 -4.089 1.00 24.87 ATOM 2304 CB LEU A 321 28.521 -7.895 -4.786 1.00 23.28 ATOM 2305 CG LEU A 321 28.691 -6.366 -4.823 1.00 22.89 ATOM 2306 CD1 LEU A 321 30.074 -5.988 -5.371 1.00 21.50 ATOM 2307 CD2 LEU A 321 27.593 -5.758 -5.691 1.00 20.89 ATOM 2308 C LEU A 321 27.072 -9.848 -4.078 1.00 26.22 ATOM 2309 O LEU A 321 28.019 -10.596 -4.331 1.00 26.31 ATOM 2310 N GLU A 322 25.853 -10.283 -3.766 1.00 27.62 ATOM 2311 CA GLU A 322 25.493 -11.699 -3.701 1.00 29.11 ATOM 2312 CB GLU A 322 24.892 -12.057 -2.328 1.00 30.25 ATOM 2313 CG GLU A 322 25.812 -11.853 -1.130 1.00 33.30 ATOM 2314 CD GLU A 322 26.439 -13.151 -0.626 1.00 35.74 ATOM 2315 OE1 GLU A 322 26.438 -14.153 -1.379 1.00 37.26 ATOM 2316 OE2 GLU A 322 26.937 -13.170 0.524 1.00 36.65 ATOM 2317 C GLU A 322 24.442 -11.988 -4.764 1.00 28.95 ATOM 2318 O GLU A 322 23.523 -11.184 -4.970 1.00 28.37 ATOM 2319 N TYR A 323 24.564 -13.141 -5.420 1.00 29.18 ATOM 2320 CA TYR A 323 23.609 -13.549 -6.454 1.00 29.42 ATOM 2321 CB TYR A 323 24.012 -14.907 -7.058 1.00 29.65 ATOM 2322 CG TYR A 323 25.126 -14.870 -8.091 1.00 29.52 ATOM 2323 CD1 TYR A 323 25.037 -14.061 -9.223 1.00 29.69 ATOM 2324 CE1 TYR A 323 26.031 -14.064 -10.192 1.00 30.10 ATOM 2325 CD2 TYR A 323 26.246 -15.682 -7.957 1.00 29.91 ATOM 2326 CE2 TYR A 323 27.246 -15.693 -8.923 1.00 30.51 ATOM 2327 CZ TYR A 323 27.130 -14.883 -10.037 1.00 30.32 ATOM 2328 OH TYR A 323 28.113 -14.895 -10.998 1.00 31.51 ATOM 2329 C TYR A 323 22.174 -13.658 -5.908 1.00 29.51 ATOM 2330 O TYR A 323 21.241 -13.080 -6.467 1.00 29.81 ATOM 2331 N THR A 324 21.990 -14.403 -4.823 1.00 29.61 ATOM 2332 CA THR A 324 20.652 -14.569 -4.255 1.00 29.99 ATOM 2333 CB THR A 324 20.609 -15.717 -3.222 1.00 30.24 ATOM 2334 OG1 THR A 324 21.099 -16.920 -3.824 1.00 30.90 ATOM 2335 CG2 THR A 324 19.194 -15.948 -2.748 1.00 30.60 ATOM 2336 C THR A 324 20.218 -13.282 -3.583 1.00 29.96 ATOM 2337 O THR A 324 20.766 -12.892 -2.553 1.00 30.30 ATOM 2338 N PRO A 325 19.222 -12.599 -4.158 1.00 29.97 ATOM 2339 CD PRO A 325 18.502 -12.963 -5.391 1.00 30.20 ATOM 2340 CA PRO A 325 18.737 -11.338 -3.587 1.00 29.85 ATOM 2341 CB PRO A 325 17.445 -11.072 -4.353 1.00 29.84 ATOM 2342 CG PRO A 325 17.670 -11.727 -5.682 1.00 30.85 ATOM 2343 C PRO A 325 18.525 -11.330 -2.072 1.00 29.94 ATOM 2344 O PRO A 325 18.975 -10.414 -1.385 1.00 29.77 ATOM 2345 N THR A 326 17.850 -12.351 -1.554 1.00 29.34 ATOM 2346 CA THR A 326 17.563 -12.434 -0.128 1.00 28.33 ATOM 2347 CB THR A 326 16.552 -13.566 0.177 1.00 28.98 ATOM 2348 OG1 THR A 326 17.080 -14.817 -0.273 1.00 30.12 ATOM 2349 CG2 THR A 326 15.234 -13.306 -0.525 1.00 28.95 ATOM 2350 C THR A 326 18.798 -12.647 0.725 1.00 27.40 ATOM 2351 O THR A 326 18.757 -12.420 1.930 1.00 27.88 ATOM 2352 N ALA A 327 19.895 -13.081 0.111 1.00 26.59 ATOM 2353 CA ALA A 327 21.135 -13.303 0.849 1.00 25.75 ATOM 2354 CB ALA A 327 22.021 -14.275 0.108 1.00 25.26 ATOM 2355 C ALA A 327 21.909 -12.006 1.104 1.00 26.09 ATOM 2356 O ALA A 327 22.834 -11.981 1.918 1.00 26.56 ATOM 2357 N ARG A 328 21.547 -10.929 0.412 1.00 25.25 ATOM 2358 CA ARG A 328 22.248 -9.658 0.612 1.00 24.36 ATOM 2359 CB ARG A 328 21.943 -8.702 -0.543 1.00 23.53 ATOM 2360 CG ARG A 328 22.336 -9.262 -1.902 1.00 23.40 ATOM 2361 CD ARG A 328 21.817 -8.423 -3.062 1.00 23.34 ATOM 2362 NE ARG A 328 21.887 -9.188 -4.302 1.00 22.87 ATOM 2363 CZ ARG A 328 21.074 -9.021 -5.337 1.00 22.96 ATOM 2364 NH1 ARG A 328 20.113 -8.104 -5.300 1.00 22.19 ATOM 2365 NH2 ARG A 328 21.206 -9.800 -6.402 1.00 22.10 ATOM 2366 C ARG A 328 21.874 -8.991 1.937 1.00 23.54 ATOM 2367 O ARG A 328 20.750 -9.121 2.420 1.00 23.40 ATOM 2368 N LEU A 329 22.829 -8.282 2.528 1.00 23.07 ATOM 2369 CA LEU A 329 22.582 -7.560 3.771 1.00 22.45 ATOM 2370 CB LEU A 329 23.816 -6.767 4.195 1.00 22.20 ATOM 2371 CG LEU A 329 25.078 -7.493 4.621 1.00 21.95 ATOM 2372 CD1 LEU A 329 26.107 -6.471 5.085 1.00 21.08 ATOM 2373 CD2 LEU A 329 24.740 -8.470 5.730 1.00 23.39 ATOM 2374 C LEU A 329 21.486 -6.545 3.500 1.00 22.27 ATOM 2375 O LEU A 329 21.319 -6.095 2.367 1.00 21.79 ATOM 2376 N THR A 330 20.724 -6.185 4.522 1.00 21.92 ATOM 2377 CA THR A 330 19.716 -5.154 4.334 1.00 21.71 ATOM 2378 CB THR A 330 18.622 -5.236 5.390 1.00 22.23 ATOM 2379 OG1 THR A 330 19.223 -5.084 6.678 1.00 22.32 ATOM 2380 CG2 THR A 330 17.899 -6.580 5.330 1.00 22.15 ATOM 2381 C THR A 330 20.509 -3.860 4.586 1.00 21.41 ATOM 2382 O THR A 330 21.614 -3.908 5.132 1.00 21.43 ATOM 2383 N PRO A 331 19.978 -2.700 4.163 1.00 20.90 ATOM 2384 CD PRO A 331 18.746 -2.469 3.392 1.00 20.49 ATOM 2385 CA PRO A 331 20.711 -1.452 4.405 1.00 21.80 ATOM 2386 CB PRO A 331 19.759 -0.376 3.873 1.00 21.00 ATOM 2387 CG PRO A 331 18.952 -1.087 2.839 1.00 21.05 ATOM 2388 C PRO A 331 21.069 -1.241 5.887 1.00 22.35 ATOM 2389 O PRO A 331 22.199 -0.869 6.216 1.00 22.26 ATOM 2390 N LEU A 332 20.110 -1.487 6.780 1.00 23.27 ATOM 2391 CA LEU A 332 20.354 -1.305 8.212 1.00 23.33 ATOM 2392 CB LEU A 332 19.074 -1.564 9.017 1.00 23.16 ATOM 2393 CG LEU A 332 18.968 -0.854 10.373 1.00 23.52 ATOM 2394 CD1 LEU A 332 19.041 0.661 10.200 1.00 23.08 ATOM 2395 CD2 LEU A 332 17.650 -1.247 11.035 1.00 23.98 ATOM 2396 C LEU A 332 21.484 -2.212 8.691 1.00 24.19 ATOM 2397 O LEU A 332 22.347 -1.779 9.454 1.00 23.46 ATOM 2398 N GLU A 333 21.491 -3.463 8.235 1.00 24.09 ATOM 2399 CA GLU A 333 22.549 -4.393 8.614 1.00 24.63 ATOM 2400 CB GLU A 333 22.298 -5.776 8.014 1.00 25.80 ATOM 2401 CG GLU A 333 21.221 -6.561 8.728 1.00 29.30 ATOM 2402 CD GLU A 333 20.780 -7.800 7.963 1.00 30.58 ATOM 2403 OE1 GLU A 333 21.287 -8.039 6.844 1.00 30.44 ATOM 2404 OE2 GLU A 333 19.921 -8.538 8.487 1.00 31.75 ATOM 2405 C GLU A 333 23.892 -3.880 8.107 1.00 24.62 ATOM 2406 O GLU A 333 24.915 -4.026 8.783 1.00 24.93 ATOM 2407 N ALA A 334 23.889 -3.294 6.909 1.00 23.62 ATOM 2408 CA ALA A 334 25.119 -2.757 6.326 1.00 23.39 ATOM 2409 CB ALA A 334 24.846 -2.202 4.912 1.00 22.18 ATOM 2410 C ALA A 334 25.655 -1.654 7.241 1.00 22.66 ATOM 2411 O ALA A 334 26.845 -1.620 7.557 1.00 23.19 ATOM 2412 N CYS A 335 24.762 -0.770 7.679 1.00 22.54 ATOM 2413 CA CYS A 335 25.129 0.332 8.569 1.00 22.05 ATOM 2414 CB CYS A 335 23.884 1.130 8.972 1.00 21.30 ATOM 2415 SG CYS A 335 23.228 2.271 7.717 1.00 22.11 ATOM 2416 C CYS A 335 25.817 -0.195 9.836 1.00 22.30 ATOM 2417 O CYS A 335 26.748 0.430 10.353 1.00 21.25 ATOM 2418 N ALA A 336 25.351 -1.345 10.325 1.00 22.60 ATOM 2419 CA ALA A 336 25.899 -1.953 11.538 1.00 23.08 ATOM 2420 CB ALA A 336 24.845 -2.839 12.200 1.00 22.79 ATOM 2421 C ALA A 336 27.179 -2.758 11.314 1.00 23.44 ATOM 2422 O ALA A 336 27.773 -3.251 12.274 1.00 23.78 ATOM 2423 N HIS A 337 27.609 -2.873 10.058 1.00 23.79 ATOM 2424 CA HIS A 337 28.814 -3.630 9.715 1.00 24.28 ATOM 2425 CB HIS A 337 28.941 -3.738 8.192 1.00 24.17 ATOM 2426 CG HIS A 337 29.978 -4.718 7.743 1.00 24.21 ATOM 2427 CD2 HIS A 337 31.329 -4.621 7.682 1.00 23.94 ATOM 2428 ND1 HIS A 337 29.666 -5.991 7.316 1.00 23.60 ATOM 2429 CE1 HIS A 337 30.777 -6.637 7.013 1.00 23.54 ATOM 2430 NE2 HIS A 337 31.802 -5.829 7.226 1.00 23.92 ATOM 2431 C HIS A 337 30.116 -3.059 10.297 1.00 25.19 ATOM 2432 O HIS A 337 30.273 -1.844 10.448 1.00 25.48 ATOM 2433 N SER A 338 31.058 -3.949 10.597 1.00 25.89 ATOM 2434 CA SER A 338 32.352 -3.576 11.170 1.00 27.12 ATOM 2435 CB SER A 338 33.232 -4.819 11.311 1.00 28.44 ATOM 2436 OG SER A 338 32.794 -5.609 12.405 1.00 32.67 ATOM 2437 C SER A 338 33.113 -2.519 10.384 1.00 26.71 ATOM 2438 O SER A 338 33.888 -1.748 10.957 1.00 27.47 ATOM 2439 N PHE A 339 32.908 -2.490 9.072 1.00 25.58 ATOM 2440 CA PHE A 339 33.591 -1.519 8.231 1.00 24.70 ATOM 2441 CB PHE A 339 33.153 -1.687 6.767 1.00 24.04 ATOM 2442 CG PHE A 339 33.776 -0.692 5.818 1.00 24.45 ATOM 2443 CD1 PHE A 339 35.163 -0.623 5.661 1.00 24.33 ATOM 2444 CD2 PHE A 339 32.974 0.182 5.078 1.00 23.95 ATOM 2445 CE1 PHE A 339 35.750 0.305 4.781 1.00 24.16 ATOM 2446 CE2 PHE A 339 33.545 1.115 4.194 1.00 23.58 ATOM 2447 CZ PHE A 339 34.941 1.177 4.046 1.00 24.01 ATOM 2448 C PHE A 339 33.298 -0.103 8.708 1.00 24.08 ATOM 2449 O PHE A 339 34.128 0.789 8.572 1.00 24.84 ATOM 2450 N PHE A 340 32.128 0.102 9.299 1.00 23.40 ATOM 2451 CA PHE A 340 31.759 1.436 9.751 1.00 22.79 ATOM 2452 CB PHE A 340 30.270 1.668 9.462 1.00 20.66 ATOM 2453 CG PHE A 340 29.911 1.541 7.995 1.00 19.46 ATOM 2454 CD1 PHE A 340 30.428 2.441 7.059 1.00 18.50 ATOM 2455 CD2 PHE A 340 29.066 0.522 7.550 1.00 18.23 ATOM 2456 CE1 PHE A 340 30.112 2.333 5.699 1.00 18.38 ATOM 2457 CE2 PHE A 340 28.740 0.401 6.199 1.00 18.74 ATOM 2458 CZ PHE A 340 29.266 1.312 5.266 1.00 18.74 ATOM 2459 C PHE A 340 32.079 1.742 11.217 1.00 22.96 ATOM 2460 O PHE A 340 31.692 2.789 11.732 1.00 23.00 ATOM 2461 N ASP A 341 32.808 0.846 11.879 1.00 23.75 ATOM 2462 CA ASP A 341 33.164 1.035 13.289 1.00 24.15 ATOM 2463 CB ASP A 341 33.960 -0.166 13.796 1.00 24.77 ATOM 2464 CG ASP A 341 33.083 -1.382 14.044 1.00 26.09 ATOM 2465 OD1 ASP A 341 31.840 -1.246 14.032 1.00 27.07 ATOM 2466 OD2 ASP A 341 33.640 -2.476 14.248 1.00 26.43 ATOM 2467 C ASP A 341 33.946 2.314 13.584 1.00 24.32 ATOM 2468 O ASP A 341 33.766 2.915 14.633 1.00 25.00 ATOM 2469 N GLU A 342 34.815 2.740 12.679 1.00 24.28 ATOM 2470 CA GLU A 342 35.568 3.968 12.924 1.00 24.64 ATOM 2471 CB GLU A 342 36.530 4.266 11.769 1.00 25.71 ATOM 2472 CG GLU A 342 37.227 5.620 11.906 1.00 27.82 ATOM 2473 CD GLU A 342 38.337 5.842 10.881 1.00 29.59 ATOM 2474 OE1 GLU A 342 38.373 5.128 9.855 1.00 30.15 ATOM 2475 OE2 GLU A 342 39.177 6.743 11.103 1.00 31.30 ATOM 2476 C GLU A 342 34.630 5.164 13.100 1.00 24.28 ATOM 2477 O GLU A 342 34.908 6.079 13.882 1.00 24.02 ATOM 2478 N LEU A 343 33.526 5.165 12.361 1.00 23.69 ATOM 2479 CA LEU A 343 32.567 6.261 12.443 1.00 22.99 ATOM 2480 CB LEU A 343 31.474 6.088 11.390 1.00 22.13 ATOM 2481 CG LEU A 343 31.892 5.991 9.928 1.00 21.74 ATOM 2482 CD1 LEU A 343 30.637 6.062 9.060 1.00 21.29 ATOM 2483 CD2 LEU A 343 32.860 7.107 9.591 1.00 20.81 ATOM 2484 C LEU A 343 31.917 6.354 13.822 1.00 23.03 ATOM 2485 O LEU A 343 31.484 7.430 14.243 1.00 23.45 ATOM 2486 N ARG A 344 31.844 5.222 14.514 1.00 23.67 ATOM 2487 CA ARG A 344 31.243 5.169 15.841 1.00 25.09 ATOM 2488 CB ARG A 344 30.594 3.796 16.053 1.00 24.22 ATOM 2489 CG ARG A 344 29.287 3.625 15.283 1.00 23.41 ATOM 2490 CD ARG A 344 28.681 2.237 15.461 1.00 23.17 ATOM 2491 NE ARG A 344 29.353 1.223 14.640 1.00 23.97 ATOM 2492 CZ ARG A 344 28.939 0.827 13.438 1.00 23.50 ATOM 2493 NH1 ARG A 344 27.849 1.354 12.894 1.00 23.16 ATOM 2494 NH2 ARG A 344 29.600 -0.119 12.787 1.00 23.92 ATOM 2495 C ARG A 344 32.256 5.476 16.959 1.00 27.26 ATOM 2496 O ARG A 344 31.920 5.451 18.153 1.00 27.54 ATOM 2497 N ASP A 345 33.489 5.779 16.562 1.00 28.67 ATOM 2498 CA ASP A 345 34.555 6.123 17.505 1.00 29.91 ATOM 2499 CB ASP A 345 35.914 6.037 16.808 1.00 31.64 ATOM 2500 CG ASP A 345 37.083 6.248 17.764 1.00 32.68 ATOM 2501 OD1 ASP A 345 37.038 7.174 18.601 1.00 33.71 ATOM 2502 OD2 ASP A 345 38.053 5.479 17.672 1.00 33.86 ATOM 2503 C ASP A 345 34.325 7.549 17.990 1.00 30.47 ATOM 2504 O ASP A 345 34.235 8.472 17.189 1.00 30.11 ATOM 2505 N PRO A 346 34.267 7.755 19.313 1.00 31.27 ATOM 2506 CD PRO A 346 34.446 6.753 20.376 1.00 31.52 ATOM 2507 CA PRO A 346 34.041 9.094 19.863 1.00 32.02 ATOM 2508 CB PRO A 346 34.016 8.864 21.375 1.00 32.33 ATOM 2509 CG PRO A 346 34.779 7.602 21.573 1.00 31.36 ATOM 2510 C PRO A 346 35.052 10.171 19.466 1.00 33.03 ATOM 2511 O PRO A 346 34.731 11.362 19.498 1.00 33.40 ATOM 2512 N ASN A 347 36.264 9.775 19.085 1.00 33.67 ATOM 2513 CA ASN A 347 37.273 10.769 18.706 1.00 34.30 ATOM 2514 CB ASN A 347 38.638 10.386 19.276 1.00 35.59 ATOM 2515 CG ASN A 347 38.581 10.060 20.743 1.00 36.27 ATOM 2516 OD1 ASN A 347 39.024 8.993 21.168 1.00 38.22 ATOM 2517 ND2 ASN A 347 38.034 10.972 21.531 1.00 36.66 ATOM 2518 C ASN A 347 37.425 11.002 17.206 1.00 33.96 ATOM 2519 O ASN A 347 38.258 11.795 16.787 1.00 34.42 ATOM 2520 N VAL A 348 36.627 10.322 16.393 1.00 33.52 ATOM 2521 CA VAL A 348 36.724 10.489 14.948 1.00 32.27 ATOM 2522 CB VAL A 348 35.725 9.560 14.208 1.00 32.27 ATOM 2523 CG1 VAL A 348 34.300 10.128 14.299 1.00 31.89 ATOM 2524 CG2 VAL A 348 36.149 9.400 12.760 1.00 31.87 ATOM 2525 C VAL A 348 36.475 11.938 14.530 1.00 31.76 ATOM 2526 O VAL A 348 35.638 12.634 15.101 1.00 31.27 ATOM 2527 N LYS A 349 37.222 12.382 13.527 1.00 31.48 ATOM 2528 CA LYS A 349 37.099 13.736 13.013 1.00 31.06 ATOM 2529 CB LYS A 349 38.167 14.633 13.642 1.00 32.87 ATOM 2530 CG LYS A 349 37.895 15.005 15.082 1.00 34.36 ATOM 2531 CD LYS A 349 37.117 16.302 15.159 1.00 36.82 ATOM 2532 CE LYS A 349 36.859 16.704 16.602 1.00 38.50 ATOM 2533 NZ LYS A 349 35.708 15.951 17.193 1.00 40.04 ATOM 2534 C LYS A 349 37.284 13.718 11.502 1.00 30.23 ATOM 2535 O LYS A 349 37.806 12.756 10.947 1.00 29.88 ATOM 2536 N LEU A 350 36.854 14.779 10.835 1.00 29.60 ATOM 2537 CA LEU A 350 37.011 14.858 9.390 1.00 29.27 ATOM 2538 CB LEU A 350 36.003 15.838 8.784 1.00 28.04 ATOM 2539 CG LEU A 350 34.508 15.530 8.945 1.00 28.23 ATOM 2540 CD1 LEU A 350 33.702 16.565 8.180 1.00 26.85 ATOM 2541 CD2 LEU A 350 34.201 14.124 8.434 1.00 26.89 ATOM 2542 C LEU A 350 38.428 15.339 9.073 1.00 30.30 ATOM 2543 O LEU A 350 39.034 16.081 9.853 1.00 30.40 ATOM 2544 N PRO A 351 38.984 14.895 7.936 1.00 30.45 ATOM 2545 CD PRO A 351 38.402 13.929 6.982 1.00 30.41 ATOM 2546 CA PRO A 351 40.332 15.303 7.538 1.00 30.21 ATOM 2547 CB PRO A 351 40.475 14.725 6.131 1.00 30.65 ATOM 2548 CG PRO A 351 39.597 13.495 6.169 1.00 30.79 ATOM 2549 C PRO A 351 40.520 16.818 7.579 1.00 29.87 ATOM 2550 O PRO A 351 41.636 17.295 7.755 1.00 29.87 ATOM 2551 N ASN A 352 39.436 17.576 7.427 1.00 29.32 ATOM 2552 CA ASN A 352 39.551 19.031 7.466 1.00 29.11 ATOM 2553 CB ASN A 352 38.526 19.701 6.535 1.00 29.24 ATOM 2554 CG ASN A 352 37.080 19.534 6.997 1.00 30.10 ATOM 2555 OD1 ASN A 352 36.163 20.016 6.332 1.00 32.01 ATOM 2556 ND2 ASN A 352 36.868 18.862 8.121 1.00 29.82 ATOM 2557 C ASN A 352 39.443 19.596 8.872 1.00 28.52 ATOM 2558 O ASN A 352 39.367 20.803 9.055 1.00 28.55 ATOM 2559 N GLY A 353 39.453 18.718 9.866 1.00 28.89 ATOM 2560 CA GLY A 353 39.380 19.172 11.242 1.00 30.80 ATOM 2561 C GLY A 353 37.987 19.290 11.826 1.00 31.69 ATOM 2562 O GLY A 353 37.836 19.323 13.040 1.00 32.01 ATOM 2563 N ARG A 354 36.973 19.366 10.969 1.00 32.90 ATOM 2564 CA ARG A 354 35.579 19.477 11.411 1.00 33.77 ATOM 2565 CB ARG A 354 34.682 19.828 10.229 1.00 35.25 ATOM 2566 CG ARG A 354 34.847 21.215 9.670 1.00 38.26 ATOM 2567 CD ARG A 354 33.626 21.551 8.830 1.00 40.90 ATOM 2568 NE ARG A 354 33.828 22.686 7.932 1.00 42.74 ATOM 2569 CZ ARG A 354 32.837 23.453 7.487 1.00 43.86 ATOM 2570 NH1 ARG A 354 31.588 23.203 7.863 1.00 44.12 ATOM 2571 NH2 ARG A 354 33.087 24.461 6.662 1.00 44.53 ATOM 2572 C ARG A 354 35.052 18.180 12.027 1.00 33.51 ATOM 2573 O ARG A 354 35.623 17.106 11.830 1.00 33.11 ATOM 2574 N ASP A 355 33.958 18.280 12.776 1.00 33.71 ATOM 2575 CA ASP A 355 33.357 17.088 13.370 1.00 33.94 ATOM 2576 CB ASP A 355 32.349 17.446 14.461 1.00 36.94 ATOM 2577 CG ASP A 355 32.986 18.146 15.640 1.00 39.64 ATOM 2578 OD1 ASP A 355 34.076 17.711 16.077 1.00 41.43 ATOM 2579 OD2 ASP A 355 32.388 19.132 16.128 1.00 41.60 ATOM 2580 C ASP A 355 32.605 16.391 12.251 1.00 32.21 ATOM 2581 O ASP A 355 32.291 17.001 11.226 1.00 31.66 ATOM 2582 N THR A 356 32.318 15.114 12.444 1.00 30.64 ATOM 2583 CA THR A 356 31.580 14.366 11.439 1.00 29.42 ATOM 2584 CB THR A 356 31.523 12.874 11.806 1.00 29.69 ATOM 2585 OG1 THR A 356 31.211 12.748 13.198 1.00 29.98 ATOM 2586 CG2 THR A 356 32.861 12.194 11.526 1.00 28.88 ATOM 2587 C THR A 356 30.153 14.917 11.418 1.00 28.03 ATOM 2588 O THR A 356 29.709 15.552 12.378 1.00 27.48 ATOM 2589 N PRO A 357 29.423 14.705 10.318 1.00 26.71 ATOM 2590 CD PRO A 357 29.817 14.011 9.075 1.00 26.53 ATOM 2591 CA PRO A 357 28.048 15.211 10.265 1.00 25.97 ATOM 2592 CB PRO A 357 27.702 15.154 8.779 1.00 26.08 ATOM 2593 CG PRO A 357 28.570 14.055 8.234 1.00 26.10 ATOM 2594 C PRO A 357 27.147 14.303 11.105 1.00 25.06 ATOM 2595 O PRO A 357 27.630 13.383 11.756 1.00 25.15 ATOM 2596 N ALA A 358 25.844 14.565 11.103 1.00 25.63 ATOM 2597 CA ALA A 358 24.893 13.739 11.857 1.00 24.88 ATOM 2598 CB ALA A 358 23.476 14.286 11.669 1.00 25.51 ATOM 2599 C ALA A 358 24.982 12.292 11.348 1.00 24.39 ATOM 2600 O ALA A 358 24.920 12.056 10.137 1.00 25.35 ATOM 2601 N LEU A 359 25.138 11.337 12.262 1.00 22.91 ATOM 2602 CA LEU A 359 25.261 9.924 11.888 1.00 22.31 ATOM 2603 CB LEU A 359 26.726 9.470 11.998 1.00 21.71 ATOM 2604 CG LEU A 359 27.802 10.075 11.093 1.00 22.23 ATOM 2605 CD1 LEU A 359 29.163 9.522 11.503 1.00 21.73 ATOM 2606 CD2 LEU A 359 27.511 9.752 9.641 1.00 21.26 ATOM 2607 C LEU A 359 24.432 8.974 12.744 1.00 21.46 ATOM 2608 O LEU A 359 24.232 7.813 12.381 1.00 20.64 ATOM 2609 N PHE A 360 23.955 9.456 13.884 1.00 22.39 ATOM 2610 CA PHE A 360 23.223 8.585 14.799 1.00 22.82 ATOM 2611 CB PHE A 360 24.053 8.407 16.078 1.00 23.12 ATOM 2612 CG PHE A 360 25.521 8.165 15.819 1.00 23.77 ATOM 2613 CD1 PHE A 360 26.469 9.114 16.178 1.00 23.35 ATOM 2614 CD2 PHE A 360 25.947 6.999 15.192 1.00 22.69 ATOM 2615 CE1 PHE A 360 27.824 8.906 15.911 1.00 24.37 ATOM 2616 CE2 PHE A 360 27.291 6.781 14.921 1.00 23.42 ATOM 2617 CZ PHE A 360 28.233 7.733 15.278 1.00 23.87 ATOM 2618 C PHE A 360 21.800 8.985 15.175 1.00 22.95 ATOM 2619 O PHE A 360 21.207 8.392 16.083 1.00 22.94 ATOM 2620 N ASN A 361 21.240 9.970 14.484 1.00 23.01 ATOM 2621 CA ASN A 361 19.896 10.408 14.806 1.00 23.16 ATOM 2622 CB ASN A 361 19.704 11.875 14.403 1.00 22.59 ATOM 2623 CG ASN A 361 20.036 12.139 12.949 1.00 24.48 ATOM 2624 OD1 ASN A 361 19.573 13.128 12.376 1.00 26.66 ATOM 2625 ND2 ASN A 361 20.834 11.269 12.342 1.00 22.12 ATOM 2626 C ASN A 361 18.837 9.514 14.166 1.00 23.24 ATOM 2627 O ASN A 361 17.982 9.971 13.416 1.00 24.15 ATOM 2628 N PHE A 362 18.905 8.228 14.479 1.00 23.80 ATOM 2629 CA PHE A 362 17.954 7.261 13.955 1.00 24.09 ATOM 2630 CB PHE A 362 18.416 5.842 14.266 1.00 23.71 ATOM 2631 CG PHE A 362 19.580 5.395 13.450 1.00 24.20 ATOM 2632 CD1 PHE A 362 19.387 4.820 12.190 1.00 23.54 ATOM 2633 CD2 PHE A 362 20.873 5.562 13.926 1.00 23.42 ATOM 2634 CE1 PHE A 362 20.481 4.419 11.414 1.00 23.75 ATOM 2635 CE2 PHE A 362 21.971 5.167 13.163 1.00 24.04 ATOM 2636 CZ PHE A 362 21.773 4.595 11.902 1.00 23.60 ATOM 2637 C PHE A 362 16.569 7.445 14.558 1.00 24.35 ATOM 2638 O PHE A 362 16.436 7.789 15.735 1.00 24.19 ATOM 2639 N THR A 363 15.543 7.205 13.746 1.00 24.73 ATOM 2640 CA THR A 363 14.161 7.285 14.204 1.00 24.37 ATOM 2641 CB THR A 363 13.270 8.098 13.231 1.00 23.80 ATOM 2642 OG1 THR A 363 13.232 7.450 11.954 1.00 23.71 ATOM 2643 CG2 THR A 363 13.816 9.514 13.047 1.00 22.10 ATOM 2644 C THR A 363 13.628 5.851 14.286 1.00 25.71 ATOM 2645 O THR A 363 14.263 4.899 13.808 1.00 25.74 ATOM 2646 N THR A 364 12.462 5.696 14.897 1.00 26.55 ATOM 2647 CA THR A 364 11.829 4.388 15.033 1.00 27.31 ATOM 2648 CB THR A 364 10.507 4.505 15.811 1.00 27.73 ATOM 2649 OG1 THR A 364 10.797 4.832 17.177 1.00 30.28 ATOM 2650 CG2 THR A 364 9.734 3.197 15.756 1.00 28.52 ATOM 2651 C THR A 364 11.542 3.803 13.650 1.00 26.91 ATOM 2652 O THR A 364 11.767 2.614 13.402 1.00 26.81 ATOM 2653 N GLN A 365 11.035 4.651 12.761 1.00 26.87 ATOM 2654 CA GLN A 365 10.721 4.260 11.390 1.00 27.20 ATOM 2655 CB GLN A 365 10.216 5.480 10.619 1.00 28.26 ATOM 2656 CG GLN A 365 9.987 5.243 9.129 1.00 30.43 ATOM 2657 CD GLN A 365 8.814 4.322 8.855 1.00 30.85 ATOM 2658 OE1 GLN A 365 7.850 4.288 9.616 1.00 33.33 ATOM 2659 NE2 GLN A 365 8.890 3.571 7.769 1.00 31.20 ATOM 2660 C GLN A 365 11.965 3.691 10.702 1.00 27.13 ATOM 2661 O GLN A 365 11.930 2.618 10.104 1.00 27.20 ATOM 2662 N GLU A 366 13.071 4.418 10.806 1.00 27.05 ATOM 2663 CA GLU A 366 14.334 4.007 10.196 1.00 26.31 ATOM 2664 CB GLU A 366 15.380 5.104 10.413 1.00 26.31 ATOM 2665 CG GLU A 366 16.535 5.053 9.442 1.00 27.51 ATOM 2666 CD GLU A 366 17.501 6.203 9.633 1.00 28.60 ATOM 2667 OE1 GLU A 366 18.615 6.127 9.072 1.00 28.52 ATOM 2668 OE2 GLU A 366 17.145 7.174 10.345 1.00 28.51 ATOM 2669 C GLU A 366 14.869 2.677 10.725 1.00 25.75 ATOM 2670 O GLU A 366 15.457 1.896 9.976 1.00 25.34 ATOM 2671 N LEU A 367 14.659 2.414 12.013 1.00 25.43 ATOM 2672 CA LEU A 367 15.141 1.176 12.628 1.00 25.07 ATOM 2673 CB LEU A 367 15.522 1.440 14.091 1.00 24.13 ATOM 2674 CG LEU A 367 16.746 2.336 14.350 1.00 24.81 ATOM 2675 CD1 LEU A 367 16.638 2.974 15.752 1.00 25.13 ATOM 2676 CD2 LEU A 367 18.012 1.515 14.232 1.00 22.65 ATOM 2677 C LEU A 367 14.141 0.019 12.588 1.00 25.39 ATOM 2678 O LEU A 367 14.468 -1.096 12.976 1.00 24.28 ATOM 2679 N SER A 368 12.936 0.289 12.100 1.00 26.87 ATOM 2680 CA SER A 368 11.867 -0.704 12.071 1.00 28.57 ATOM 2681 CB SER A 368 10.634 -0.126 11.370 1.00 28.66 ATOM 2682 OG SER A 368 10.867 0.096 9.999 1.00 29.53 ATOM 2683 C SER A 368 12.172 -2.087 11.516 1.00 30.08 ATOM 2684 O SER A 368 11.614 -3.076 11.997 1.00 30.91 ATOM 2685 N SER A 369 13.055 -2.182 10.529 1.00 30.65 ATOM 2686 CA SER A 369 13.380 -3.489 9.958 1.00 30.93 ATOM 2687 CB SER A 369 14.183 -3.321 8.666 1.00 30.91 ATOM 2688 OG SER A 369 15.572 -3.261 8.947 1.00 30.39 ATOM 2689 C SER A 369 14.165 -4.390 10.910 1.00 31.61 ATOM 2690 O SER A 369 14.346 -5.576 10.631 1.00 32.09 ATOM 2691 N ASN A 370 14.637 -3.840 12.028 1.00 31.18 ATOM 2692 CA ASN A 370 15.419 -4.629 12.984 1.00 30.53 ATOM 2693 CB ASN A 370 16.648 -5.216 12.277 1.00 30.57 ATOM 2694 CG ASN A 370 17.325 -6.312 13.076 1.00 30.92 ATOM 2695 OD1 ASN A 370 17.179 -6.396 14.293 1.00 31.80 ATOM 2696 ND2 ASN A 370 18.077 -7.159 12.388 1.00 31.35 ATOM 2697 C ASN A 370 15.850 -3.730 14.145 1.00 30.50 ATOM 2698 O ASN A 370 17.036 -3.408 14.301 1.00 30.12 ATOM 2699 N PRO A 371 14.882 -3.315 14.981 1.00 30.38 ATOM 2700 CD PRO A 371 13.452 -3.678 14.872 1.00 29.83 ATOM 2701 CA PRO A 371 15.141 -2.444 16.135 1.00 29.46 ATOM 2702 CB PRO A 371 13.842 -2.515 16.934 1.00 29.23 ATOM 2703 CG PRO A 371 12.793 -2.785 15.893 1.00 30.10 ATOM 2704 C PRO A 371 16.377 -2.771 16.986 1.00 29.14 ATOM 2705 O PRO A 371 17.119 -1.871 17.373 1.00 28.76 ATOM 2706 N PRO A 372 16.613 -4.061 17.294 1.00 28.72 ATOM 2707 CD PRO A 372 15.791 -5.232 16.939 1.00 28.85 ATOM 2708 CA PRO A 372 17.780 -4.435 18.109 1.00 28.21 ATOM 2709 CB PRO A 372 17.752 -5.966 18.109 1.00 28.51 ATOM 2710 CG PRO A 372 16.315 -6.311 17.852 1.00 28.82 ATOM 2711 C PRO A 372 19.135 -3.898 17.646 1.00 28.43 ATOM 2712 O PRO A 372 20.088 -3.858 18.426 1.00 27.80 ATOM 2713 N LEU A 373 19.233 -3.497 16.383 1.00 28.36 ATOM 2714 CA LEU A 373 20.487 -2.972 15.857 1.00 28.66 ATOM 2715 CB LEU A 373 20.404 -2.830 14.332 1.00 28.26 ATOM 2716 CG LEU A 373 20.486 -4.138 13.544 1.00 29.30 ATOM 2717 CD1 LEU A 373 20.483 -3.829 12.052 1.00 29.60 ATOM 2718 CD2 LEU A 373 21.746 -4.915 13.933 1.00 29.73 ATOM 2719 C LEU A 373 20.860 -1.624 16.484 1.00 28.94 ATOM 2720 O LEU A 373 22.018 -1.214 16.421 1.00 29.03 ATOM 2721 N ALA A 374 19.881 -0.940 17.079 1.00 29.90 ATOM 2722 CA ALA A 374 20.116 0.365 17.715 1.00 30.31 ATOM 2723 CB ALA A 374 18.854 0.837 18.433 1.00 29.35 ATOM 2724 C ALA A 374 21.270 0.281 18.704 1.00 30.75 ATOM 2725 O ALA A 374 21.994 1.248 18.920 1.00 31.22 ATOM 2726 N THR A 375 21.430 -0.894 19.298 1.00 31.79 ATOM 2727 CA THR A 375 22.482 -1.159 20.271 1.00 31.96 ATOM 2728 CB THR A 375 22.359 -2.593 20.789 1.00 32.56 ATOM 2729 OG1 THR A 375 21.291 -2.646 21.741 1.00 34.71 ATOM 2730 CG2 THR A 375 23.646 -3.051 21.438 1.00 33.54 ATOM 2731 C THR A 375 23.850 -0.963 19.646 1.00 31.80 ATOM 2732 O THR A 375 24.806 -0.581 20.320 1.00 31.35 ATOM 2733 N ILE A 376 23.947 -1.246 18.352 1.00 31.59 ATOM 2734 CA ILE A 376 25.204 -1.068 17.641 1.00 31.24 ATOM 2735 CB ILE A 376 25.412 -2.143 16.553 1.00 31.87 ATOM 2736 CG2 ILE A 376 26.688 -1.852 15.770 1.00 31.98 ATOM 2737 CG1 ILE A 376 25.499 -3.524 17.190 1.00 31.35 ATOM 2738 CD1 ILE A 376 25.205 -4.638 16.220 1.00 31.43 ATOM 2739 C ILE A 376 25.244 0.292 16.951 1.00 30.67 ATOM 2740 O ILE A 376 26.257 0.993 17.008 1.00 30.93 ATOM 2741 N LEU A 377 24.131 0.661 16.321 1.00 29.30 ATOM 2742 CA LEU A 377 24.035 1.905 15.563 1.00 27.78 ATOM 2743 CB LEU A 377 22.759 1.891 14.727 1.00 26.16 ATOM 2744 CG LEU A 377 22.733 0.747 13.711 1.00 25.87 ATOM 2745 CD1 LEU A 377 21.316 0.605 13.155 1.00 25.75 ATOM 2746 CD2 LEU A 377 23.736 1.010 12.595 1.00 25.28 ATOM 2747 C LEU A 377 24.143 3.219 16.321 1.00 27.71 ATOM 2748 O LEU A 377 24.595 4.217 15.756 1.00 27.25 ATOM 2749 N ILE A 378 23.711 3.237 17.577 1.00 27.35 ATOM 2750 CA ILE A 378 23.815 4.445 18.384 1.00 27.54 ATOM 2751 CB ILE A 378 22.460 4.841 19.020 1.00 28.16 ATOM 2752 CG2 ILE A 378 22.587 6.189 19.725 1.00 27.35 ATOM 2753 CG1 ILE A 378 21.380 4.919 17.936 1.00 27.46 ATOM 2754 CD1 ILE A 378 20.074 5.533 18.403 1.00 28.33 ATOM 2755 C ILE A 378 24.823 4.125 19.472 1.00 28.37 ATOM 2756 O ILE A 378 24.495 3.469 20.463 1.00 28.81 ATOM 2757 N PRO A 379 26.078 4.572 19.294 1.00 28.70 ATOM 2758 CD PRO A 379 26.569 5.354 18.148 1.00 28.43 ATOM 2759 CA PRO A 379 27.135 4.317 20.279 1.00 29.12 ATOM 2760 CB PRO A 379 28.409 4.802 19.578 1.00 28.54 ATOM 2761 CG PRO A 379 27.947 5.776 18.578 1.00 28.60 ATOM 2762 C PRO A 379 26.898 5.009 21.626 1.00 29.54 ATOM 2763 O PRO A 379 26.135 5.966 21.721 1.00 29.25 ATOM 2764 N PRO A 380 27.557 4.524 22.685 1.00 30.70 ATOM 2765 CD PRO A 380 28.491 3.381 22.648 1.00 30.59 ATOM 2766 CA PRO A 380 27.429 5.075 24.041 1.00 31.58 ATOM 2767 CB PRO A 380 28.571 4.412 24.805 1.00 30.83 ATOM 2768 CG PRO A 380 28.761 3.106 24.109 1.00 30.67 ATOM 2769 C PRO A 380 27.471 6.592 24.161 1.00 32.40 ATOM 2770 O PRO A 380 26.656 7.188 24.860 1.00 32.47 ATOM 2771 N HIS A 381 28.416 7.214 23.469 1.00 33.92 ATOM 2772 CA HIS A 381 28.578 8.661 23.531 1.00 35.45 ATOM 2773 CB HIS A 381 29.985 9.033 23.067 1.00 34.52 ATOM 2774 CG HIS A 381 30.196 8.842 21.599 1.00 33.86 ATOM 2775 CD2 HIS A 381 30.117 9.716 20.567 1.00 32.78 ATOM 2776 ND1 HIS A 381 30.482 7.615 21.041 1.00 33.26 ATOM 2777 CE1 HIS A 381 30.569 7.740 19.729 1.00 33.30 ATOM 2778 NE2 HIS A 381 30.352 9.006 19.417 1.00 32.76 ATOM 2779 C HIS A 381 27.586 9.471 22.719 1.00 37.30 ATOM 2780 O HIS A 381 27.437 10.668 22.945 1.00 37.57 ATOM 2781 N ALA A 382 26.905 8.830 21.778 1.00 39.82 ATOM 2782 CA ALA A 382 25.978 9.540 20.901 1.00 43.01 ATOM 2783 CB ALA A 382 25.737 8.713 19.641 1.00 42.21 ATOM 2784 C ALA A 382 24.639 9.975 21.482 1.00 45.66 ATOM 2785 O ALA A 382 24.055 9.298 22.327 1.00 45.54 ATOM 2786 N ARG A 383 24.169 11.122 21.003 1.00 49.46 ATOM 2787 CA ARG A 383 22.885 11.691 21.392 1.00 53.77 ATOM 2788 CB ARG A 383 21.759 10.888 20.735 1.00 53.90 ATOM 2789 CG ARG A 383 21.812 10.867 19.216 1.00 54.31 ATOM 2790 CD ARG A 383 20.661 10.052 18.639 1.00 54.99 ATOM 2791 NE ARG A 383 19.386 10.774 18.578 1.00 55.06 ATOM 2792 CZ ARG A 383 19.244 12.029 18.154 1.00 54.95 ATOM 2793 NH1 ARG A 383 20.298 12.729 17.745 1.00 55.15 ATOM 2794 NH2 ARG A 383 18.039 12.579 18.108 1.00 54.85 ATOM 2795 C ARG A 383 22.610 11.801 22.888 1.00 56.92 ATOM 2796 O ARG A 383 21.449 11.840 23.303 1.00 57.60 ATOM 2797 N ILE A 384 23.661 11.851 23.701 1.00 60.62 ATOM 2798 CA ILE A 384 23.481 11.965 25.145 1.00 64.06 ATOM 2799 CB ILE A 384 24.820 11.770 25.898 1.00 63.86 ATOM 2800 CG2 ILE A 384 24.683 12.222 27.340 1.00 64.12 ATOM 2801 CG1 ILE A 384 25.230 10.299 25.864 1.00 63.80 ATOM 2802 CD1 ILE A 384 24.162 9.362 26.373 1.00 64.09 ATOM 2803 C ILE A 384 22.923 13.351 25.462 1.00 66.76 ATOM 2804 O ILE A 384 23.591 14.368 25.237 1.00 67.37 ATOM 2805 N GLN A 385 21.692 13.387 25.970 1.00 69.52 ATOM 2806 CA GLN A 385 21.050 14.653 26.314 1.00 71.89 ATOM 2807 CB GLN A 385 20.316 15.217 25.081 1.00 72.31 ATOM 2808 CG GLN A 385 18.821 14.934 25.007 1.00 73.26 ATOM 2809 CD GLN A 385 18.036 16.105 24.437 1.00 73.93 ATOM 2810 OE1 GLN A 385 17.319 15.964 23.444 1.00 74.66 ATOM 2811 NE2 GLN A 385 18.173 17.271 25.064 1.00 73.73 ATOM 2812 C GLN A 385 20.103 14.540 27.513 1.00 73.14 ATOM 2813 O GLN A 385 19.155 13.749 27.507 1.00 73.36 ATOM 2814 N ALA A 386 20.381 15.333 28.546 1.00 74.64 ATOM 2815 CA ALA A 386 19.569 15.353 29.762 1.00 75.87 ATOM 2816 CB ALA A 386 20.422 15.771 30.937 1.00 75.49 ATOM 2817 C ALA A 386 18.384 16.308 29.604 1.00 76.91 ATOM 2818 O ALA A 386 18.251 16.969 28.583 1.00 76.95 ATOM 2819 N ALA A 387 17.524 16.380 30.617 1.00 78.25 ATOM 2820 CA ALA A 387 16.341 17.235 30.557 1.00 79.51 ATOM 2821 CB ALA A 387 15.097 16.425 30.885 1.00 79.22 ATOM 2822 C ALA A 387 16.478 18.418 31.502 1.00 80.50 ATOM 2823 O ALA A 387 15.505 18.850 32.137 1.00 80.95 ATOM 2824 N ALA A 388 17.696 18.941 31.603 1.00 81.43 ATOM 2825 CA ALA A 388 17.984 20.078 32.466 1.00 82.41 ATOM 2826 CB ALA A 388 17.392 21.362 31.846 1.00 82.37 ATOM 2827 C ALA A 388 17.487 19.929 33.933 1.00 82.88 ATOM 2828 O ALA A 388 16.276 20.150 34.153 1.00 83.22 ATOM 2829 OT ALA A 388 18.278 19.605 34.853 1.00 83.19 ATOM 2830 CB PHE B 523 43.133 -31.642 -26.564 1.00 92.80 ATOM 2831 CG PHE B 523 42.528 -32.859 -27.241 1.00 93.32 ATOM 2832 CD1 PHE B 523 41.831 -32.754 -28.447 1.00 93.51 ATOM 2833 CD2 PHE B 523 42.647 -34.117 -26.649 1.00 93.42 ATOM 2834 CE1 PHE B 523 41.262 -33.880 -29.049 1.00 93.57 ATOM 2835 CE2 PHE B 523 42.083 -35.247 -27.243 1.00 93.48 ATOM 2836 CZ PHE B 523 41.389 -35.128 -28.445 1.00 93.53 ATOM 2837 C PHE B 523 44.442 -30.632 -28.461 1.00 92.26 ATOM 2838 O PHE B 523 44.659 -31.741 -28.955 1.00 92.33 ATOM 2839 N PHE B 523 42.004 -30.093 -28.151 1.00 92.33 ATOM 2840 CA PHE B 523 43.294 -30.411 -27.475 1.00 92.38 ATOM 2841 N GLY B 524 45.175 -29.558 -28.740 1.00 92.03 ATOM 2842 CA GLY B 524 46.299 -29.632 -29.656 1.00 91.68 ATOM 2843 C GLY B 524 47.522 -28.941 -29.081 1.00 91.47 ATOM 2844 O GLY B 524 47.556 -28.615 -27.893 1.00 91.52 ATOM 2845 N SER B 525 48.525 -28.705 -29.921 1.00 91.10 ATOM 2846 CA SER B 525 49.753 -28.055 -29.476 1.00 90.63 ATOM 2847 CB SER B 525 50.721 -29.105 -28.931 1.00 90.68 ATOM 2848 OG SER B 525 50.935 -30.132 -29.885 1.00 90.66 ATOM 2849 C SER B 525 50.431 -27.279 -30.601 1.00 90.30 ATOM 2850 O SER B 525 50.070 -27.413 -31.771 1.00 90.40 ATOM 2851 N MET B 526 51.420 -26.470 -30.237 1.00 89.85 ATOM 2852 CA MET B 526 52.157 -25.676 -31.214 1.00 89.41 ATOM 2853 CB MET B 526 51.941 -24.182 -30.967 1.00 89.37 ATOM 2854 CG MET B 526 50.560 -23.812 -30.469 1.00 89.34 ATOM 2855 SD MET B 526 50.494 -22.070 -30.046 1.00 89.44 ATOM 2856 CE MET B 526 51.815 -21.968 -28.820 1.00 89.46 ATOM 2857 C MET B 526 53.652 -25.975 -31.161 1.00 89.11 ATOM 2858 O MET B 526 54.109 -26.800 -30.367 1.00 89.12 ATOM 2859 N LYS B 527 54.406 -25.291 -32.014 1.00 88.58 ATOM 2860 CA LYS B 527 55.850 -25.462 -32.080 1.00 88.00 ATOM 2861 CB LYS B 527 56.216 -26.447 -33.195 1.00 87.35 ATOM 2862 CG LYS B 527 55.714 -27.863 -32.960 1.00 86.66 ATOM 2863 CD LYS B 527 56.830 -28.881 -33.118 1.00 86.15 ATOM 2864 CE LYS B 527 56.293 -30.302 -33.118 1.00 85.63 ATOM 2865 NZ LYS B 527 56.160 -30.848 -34.497 1.00 85.10 ATOM 2866 C LYS B 527 56.510 -24.113 -32.338 1.00 88.03 ATOM 2867 O LYS B 527 56.422 -23.565 -33.437 1.00 87.95 ATOM 2868 N VAL B 528 57.169 -23.584 -31.313 1.00 88.27 ATOM 2869 CA VAL B 528 57.844 -22.295 -31.407 1.00 88.57 ATOM 2870 CB VAL B 528 57.700 -21.507 -30.088 1.00 88.31 ATOM 2871 CG1 VAL B 528 58.159 -20.077 -30.285 1.00 88.44 ATOM 2872 CG2 VAL B 528 56.257 -21.546 -29.613 1.00 88.19 ATOM 2873 C VAL B 528 59.334 -22.451 -31.722 1.00 88.91 ATOM 2874 O VAL B 528 59.991 -23.366 -31.228 1.00 88.95 ATOM 2875 N SER B 529 59.856 -21.552 -32.550 1.00 89.33 ATOM 2876 CA SER B 529 61.266 -21.575 -32.925 1.00 89.94 ATOM 2877 CB SER B 529 61.496 -22.547 -34.090 1.00 89.80 ATOM 2878 OG SER B 529 60.858 -22.106 -35.277 1.00 89.63 ATOM 2879 C SER B 529 61.703 -20.168 -33.321 1.00 90.51 ATOM 2880 O SER B 529 60.990 -19.199 -33.065 1.00 90.58 ATOM 2881 N ARG B 530 62.875 -20.057 -33.938 1.00 91.17 ATOM 2882 CA ARG B 530 63.392 -18.760 -34.368 1.00 91.77 ATOM 2883 CB ARG B 530 64.518 -18.294 -33.440 1.00 92.00 ATOM 2884 CG ARG B 530 64.047 -17.740 -32.106 1.00 92.49 ATOM 2885 CD ARG B 530 65.224 -17.504 -31.173 1.00 93.11 ATOM 2886 NE ARG B 530 64.821 -17.461 -29.769 1.00 93.84 ATOM 2887 CZ ARG B 530 65.653 -17.224 -28.758 1.00 94.20 ATOM 2888 NH1 ARG B 530 66.942 -17.007 -28.993 1.00 94.27 ATOM 2889 NH2 ARG B 530 65.197 -17.202 -27.511 1.00 94.28 ATOM 2890 C ARG B 530 63.922 -18.861 -35.790 1.00 92.00 ATOM 2891 O ARG B 530 65.066 -19.265 -36.002 1.00 92.07 ATOM 2892 N ASP B 531 63.085 -18.497 -36.760 1.00 92.16 ATOM 2893 CA ASP B 531 63.468 -18.554 -38.168 1.00 92.35 ATOM 2894 CB ASP B 531 62.474 -17.761 -39.023 1.00 93.03 ATOM 2895 CG ASP B 531 61.637 -18.656 -39.928 1.00 93.76 ATOM 2896 OD1 ASP B 531 61.479 -18.317 -41.122 1.00 94.05 ATOM 2897 OD2 ASP B 531 61.137 -19.698 -39.445 1.00 94.12 ATOM 2898 C ASP B 531 64.874 -18.007 -38.372 1.00 92.07 ATOM 2899 O ASP B 531 65.774 -18.724 -38.816 1.00 92.33 ATOM 2900 N LYS B 532 65.059 -16.734 -38.044 1.00 91.42 ATOM 2901 CA LYS B 532 66.359 -16.089 -38.174 1.00 90.66 ATOM 2902 CB LYS B 532 66.789 -16.027 -39.643 1.00 90.93 ATOM 2903 CG LYS B 532 65.811 -15.305 -40.551 1.00 91.30 ATOM 2904 CD LYS B 532 66.526 -14.729 -41.762 1.00 91.46 ATOM 2905 CE LYS B 532 65.623 -14.730 -42.986 1.00 91.66 ATOM 2906 NZ LYS B 532 66.369 -14.368 -44.222 1.00 91.76 ATOM 2907 C LYS B 532 66.280 -14.686 -37.592 1.00 89.88 ATOM 2908 O LYS B 532 65.207 -14.076 -37.574 1.00 89.89 ATOM 2909 N ASP B 533 67.420 -14.185 -37.119 1.00 88.75 ATOM 2910 CA ASP B 533 67.510 -12.858 -36.509 1.00 87.35 ATOM 2911 CB ASP B 533 66.824 -11.802 -37.389 1.00 87.91 ATOM 2912 CG ASP B 533 67.203 -11.921 -38.855 1.00 88.56 ATOM 2913 OD1 ASP B 533 68.306 -11.463 -39.228 1.00 89.05 ATOM 2914 OD2 ASP B 533 66.394 -12.470 -39.636 1.00 89.00 ATOM 2915 C ASP B 533 66.850 -12.881 -35.129 1.00 85.85 ATOM 2916 O ASP B 533 66.566 -11.833 -34.545 1.00 85.91 ATOM 2917 N GLY B 534 66.618 -14.086 -34.613 1.00 83.92 ATOM 2918 CA GLY B 534 65.981 -14.232 -33.317 1.00 81.06 ATOM 2919 C GLY B 534 64.472 -14.197 -33.468 1.00 78.92 ATOM 2920 O GLY B 534 63.735 -14.340 -32.490 1.00 79.01 ATOM 2921 N SER B 535 64.019 -14.010 -34.707 1.00 76.46 ATOM 2922 CA SER B 535 62.596 -13.942 -35.026 1.00 73.87 ATOM 2923 CB SER B 535 62.398 -13.743 -36.531 1.00 74.31 ATOM 2924 OG SER B 535 61.078 -13.308 -36.811 1.00 74.71 ATOM 2925 C SER B 535 61.851 -15.192 -34.589 1.00 71.71 ATOM 2926 O SER B 535 62.118 -16.287 -35.087 1.00 71.91 ATOM 2927 N LYS B 536 60.912 -15.020 -33.664 1.00 68.67 ATOM 2928 CA LYS B 536 60.120 -16.132 -33.156 1.00 65.60 ATOM 2929 CB LYS B 536 59.459 -15.747 -31.831 1.00 65.80 ATOM 2930 CG LYS B 536 58.526 -16.809 -31.266 1.00 65.95 ATOM 2931 CD LYS B 536 57.831 -16.318 -30.000 1.00 66.37 ATOM 2932 CE LYS B 536 56.613 -17.172 -29.665 1.00 66.43 ATOM 2933 NZ LYS B 536 56.659 -17.681 -28.265 1.00 66.44 ATOM 2934 C LYS B 536 59.052 -16.549 -34.166 1.00 63.39 ATOM 2935 O LYS B 536 58.282 -15.719 -34.656 1.00 63.49 ATOM 2936 N VAL B 537 59.018 -17.842 -34.473 1.00 60.14 ATOM 2937 CA VAL B 537 58.054 -18.392 -35.414 1.00 56.66 ATOM 2938 CB VAL B 537 58.765 -19.020 -36.625 1.00 56.66 ATOM 2939 CG1 VAL B 537 57.768 -19.790 -37.481 1.00 56.15 ATOM 2940 CG2 VAL B 537 59.448 -17.940 -37.433 1.00 56.19 ATOM 2941 C VAL B 537 57.215 -19.466 -34.731 1.00 54.42 ATOM 2942 O VAL B 537 57.755 -20.374 -34.098 1.00 54.10 ATOM 2943 N THR B 538 55.897 -19.351 -34.852 1.00 51.51 ATOM 2944 CA THR B 538 54.993 -20.326 -34.255 1.00 49.08 ATOM 2945 CB THR B 538 53.848 -19.651 -33.481 1.00 48.82 ATOM 2946 OG1 THR B 538 54.392 -18.809 -32.459 1.00 49.27 ATOM 2947 CG2 THR B 538 52.960 -20.701 -32.832 1.00 48.10 ATOM 2948 C THR B 538 54.383 -21.187 -35.350 1.00 47.45 ATOM 2949 O THR B 538 53.794 -20.679 -36.303 1.00 46.88 ATOM 2950 N THR B 539 54.542 -22.496 -35.221 1.00 45.49 ATOM 2951 CA THR B 539 53.987 -23.405 -36.206 1.00 43.21 ATOM 2952 CB THR B 539 55.059 -24.321 -36.804 1.00 42.95 ATOM 2953 OG1 THR B 539 55.977 -23.531 -37.570 1.00 42.60 ATOM 2954 CG2 THR B 539 54.411 -25.372 -37.718 1.00 42.31 ATOM 2955 C THR B 539 52.931 -24.248 -35.536 1.00 42.02 ATOM 2956 O THR B 539 53.165 -24.829 -34.475 1.00 41.30 ATOM 2957 N VAL B 540 51.762 -24.294 -36.165 1.00 40.75 ATOM 2958 CA VAL B 540 50.632 -25.055 -35.654 1.00 39.17 ATOM 2959 CB VAL B 540 49.533 -24.110 -35.109 1.00 38.90 ATOM 2960 CG1 VAL B 540 50.107 -23.187 -34.049 1.00 38.69 ATOM 2961 CG2 VAL B 540 48.956 -23.285 -36.247 1.00 38.41 ATOM 2962 C VAL B 540 50.029 -25.877 -36.785 1.00 38.51 ATOM 2963 O VAL B 540 50.329 -25.651 -37.957 1.00 37.57 ATOM 2964 N VAL B 541 49.184 -26.834 -36.423 1.00 37.92 ATOM 2965 CA VAL B 541 48.497 -27.661 -37.403 1.00 37.80 ATOM 2966 CB VAL B 541 48.694 -29.180 -37.115 1.00 37.91 ATOM 2967 CG1 VAL B 541 47.824 -30.023 -38.050 1.00 37.20 ATOM 2968 CG2 VAL B 541 50.160 -29.549 -37.298 1.00 37.37 ATOM 2969 C VAL B 541 47.032 -27.266 -37.253 1.00 37.61 ATOM 2970 O VAL B 541 46.393 -27.572 -36.243 1.00 37.20 ATOM 2971 N ALA B 542 46.514 -26.564 -38.257 1.00 37.90 ATOM 2972 CA ALA B 542 45.138 -26.077 -38.237 1.00 37.77 ATOM 2973 CB ALA B 542 45.134 -24.576 -38.496 1.00 37.82 ATOM 2974 C ALA B 542 44.184 -26.758 -39.211 1.00 38.02 ATOM 2975 O ALA B 542 44.595 -27.293 -40.238 1.00 37.47 ATOM 2976 N THR B 543 42.898 -26.711 -38.875 1.00 38.45 ATOM 2977 CA THR B 543 41.847 -27.285 -39.704 1.00 39.99 ATOM 2978 CB THR B 543 40.716 -27.849 -38.846 1.00 39.89 ATOM 2979 OG1 THR B 543 41.235 -28.883 -38.007 1.00 41.34 ATOM 2980 CG2 THR B 543 39.604 -28.411 -39.722 1.00 39.91 ATOM 2981 C THR B 543 41.259 -26.197 -40.593 1.00 41.22 ATOM 2982 O THR B 543 40.855 -25.141 -40.105 1.00 40.87 ATOM 2983 N PRO B 544 41.192 -26.443 -41.911 1.00 42.46 ATOM 2984 CD PRO B 544 41.609 -27.660 -42.626 1.00 42.47 ATOM 2985 CA PRO B 544 40.637 -25.437 -42.823 1.00 43.74 ATOM 2986 CB PRO B 544 40.558 -26.170 -44.158 1.00 43.64 ATOM 2987 CG PRO B 544 41.615 -27.227 -44.059 1.00 42.96 ATOM 2988 C PRO B 544 39.271 -24.947 -42.348 1.00 45.18 ATOM 2989 O PRO B 544 38.445 -25.737 -41.881 1.00 44.99 ATOM 2990 N GLY B 545 39.044 -23.640 -42.464 1.00 46.85 ATOM 2991 CA GLY B 545 37.784 -23.062 -42.033 1.00 49.09 ATOM 2992 C GLY B 545 36.572 -23.507 -42.830 1.00 50.82 ATOM 2993 O GLY B 545 35.534 -23.832 -42.254 1.00 50.84 ATOM 2994 N GLN B 546 36.699 -23.536 -44.153 1.00 52.62 ATOM 2995 CA GLN B 546 35.587 -23.929 -45.004 1.00 54.97 ATOM 2996 CB GLN B 546 35.284 -22.812 -46.007 1.00 56.09 ATOM 2997 CG GLN B 546 33.974 -22.996 -46.777 1.00 57.43 ATOM 2998 CD GLN B 546 32.753 -22.531 -45.993 1.00 58.07 ATOM 2999 OE1 GLN B 546 31.622 -22.947 -46.272 1.00 58.23 ATOM 3000 NE2 GLN B 546 32.977 -21.664 -45.007 1.00 57.97 ATOM 3001 C GLN B 546 35.772 -25.251 -45.750 1.00 56.02 ATOM 3002 O GLN B 546 34.848 -26.066 -45.802 1.00 56.80 ATOM 3003 N GLY B 547 36.953 -25.470 -46.324 1.00 56.56 ATOM 3004 CA GLY B 547 37.189 -26.700 -47.068 1.00 57.50 ATOM 3005 C GLY B 547 37.084 -27.976 -46.244 1.00 57.85 ATOM 3006 O GLY B 547 36.747 -27.914 -45.061 1.00 58.63 ATOM 3007 N PRO B 548 37.350 -29.155 -46.845 1.00 57.59 ATOM 3008 CD PRO B 548 37.721 -29.351 -48.258 1.00 57.38 ATOM 3009 CA PRO B 548 37.276 -30.428 -46.110 1.00 56.96 ATOM 3010 CB PRO B 548 37.432 -31.483 -47.201 1.00 57.23 ATOM 3011 CG PRO B 548 38.166 -30.782 -48.301 1.00 57.37 ATOM 3012 C PRO B 548 38.388 -30.509 -45.065 1.00 56.46 ATOM 3013 O PRO B 548 39.407 -29.828 -45.194 1.00 56.59 ATOM 3014 N ASP B 549 38.195 -31.341 -44.039 1.00 55.85 ATOM 3015 CA ASP B 549 39.175 -31.486 -42.957 1.00 54.80 ATOM 3016 CB ASP B 549 38.617 -32.358 -41.828 1.00 55.20 ATOM 3017 CG ASP B 549 39.535 -32.396 -40.609 1.00 55.83 ATOM 3018 OD1 ASP B 549 40.548 -31.658 -40.588 1.00 55.83 ATOM 3019 OD2 ASP B 549 39.243 -33.165 -39.668 1.00 56.40 ATOM 3020 C ASP B 549 40.526 -32.044 -43.377 1.00 53.81 ATOM 3021 O ASP B 549 40.810 -33.226 -43.196 1.00 54.04 ATOM 3022 N ARG B 550 41.355 -31.179 -43.937 1.00 52.31 ATOM 3023 CA ARG B 550 42.689 -31.560 -44.354 1.00 51.14 ATOM 3024 CB ARG B 550 42.889 -31.263 -45.835 1.00 52.36 ATOM 3025 CG ARG B 550 42.562 -32.428 -46.733 1.00 54.25 ATOM 3026 CD ARG B 550 42.620 -32.007 -48.183 1.00 56.31 ATOM 3027 NE ARG B 550 41.556 -32.632 -48.958 1.00 57.86 ATOM 3028 CZ ARG B 550 41.244 -32.288 -50.200 1.00 58.61 ATOM 3029 NH1 ARG B 550 41.921 -31.318 -50.806 1.00 58.87 ATOM 3030 NH2 ARG B 550 40.261 -32.915 -50.833 1.00 58.94 ATOM 3031 C ARG B 550 43.594 -30.675 -43.520 1.00 49.32 ATOM 3032 O ARG B 550 43.826 -29.515 -43.865 1.00 48.97 ATOM 3033 N PRO B 551 44.127 -31.209 -42.413 1.00 47.64 ATOM 3034 CD PRO B 551 44.015 -32.576 -41.876 1.00 47.20 ATOM 3035 CA PRO B 551 44.993 -30.360 -41.594 1.00 46.26 ATOM 3036 CB PRO B 551 45.477 -31.290 -40.479 1.00 46.50 ATOM 3037 CG PRO B 551 44.503 -32.426 -40.464 1.00 47.29 ATOM 3038 C PRO B 551 46.140 -29.781 -42.391 1.00 45.16 ATOM 3039 O PRO B 551 46.709 -30.443 -43.258 1.00 44.55 ATOM 3040 N GLN B 552 46.462 -28.527 -42.115 1.00 44.51 ATOM 3041 CA GLN B 552 47.574 -27.885 -42.786 1.00 44.06 ATOM 3042 CB GLN B 552 47.094 -26.853 -43.807 1.00 45.99 ATOM 3043 CG GLN B 552 45.786 -26.174 -43.470 1.00 49.35 ATOM 3044 CD GLN B 552 45.407 -25.126 -44.509 1.00 51.73 ATOM 3045 OE1 GLN B 552 46.280 -24.512 -45.144 1.00 53.24 ATOM 3046 NE2 GLN B 552 44.104 -24.916 -44.693 1.00 52.47 ATOM 3047 C GLN B 552 48.452 -27.223 -41.744 1.00 42.65 ATOM 3048 O GLN B 552 47.989 -26.823 -40.677 1.00 42.02 ATOM 3049 N GLU B 553 49.734 -27.145 -42.054 1.00 41.57 ATOM 3050 CA GLU B 553 50.698 -26.540 -41.166 1.00 41.12 ATOM 3051 CB GLU B 553 52.088 -27.090 -41.475 1.00 41.37 ATOM 3052 CG GLU B 553 52.856 -27.558 -40.271 1.00 42.74 ATOM 3053 CD GLU B 553 54.113 -28.305 -40.654 1.00 43.42 ATOM 3054 OE1 GLU B 553 54.915 -27.760 -41.439 1.00 44.33 ATOM 3055 OE2 GLU B 553 54.301 -29.439 -40.170 1.00 44.92 ATOM 3056 C GLU B 553 50.668 -25.041 -41.420 1.00 40.42 ATOM 3057 O GLU B 553 50.714 -24.602 -42.565 1.00 40.46 ATOM 3058 N VAL B 554 50.585 -24.259 -40.354 1.00 40.10 ATOM 3059 CA VAL B 554 50.554 -22.806 -40.479 1.00 39.53 ATOM 3060 CB VAL B 554 49.160 -22.243 -40.093 1.00 39.17 ATOM 3061 CG1 VAL B 554 49.122 -20.733 -40.317 1.00 39.27 ATOM 3062 CG2 VAL B 554 48.076 -22.926 -40.914 1.00 38.58 ATOM 3063 C VAL B 554 51.616 -22.194 -39.566 1.00 39.36 ATOM 3064 O VAL B 554 51.677 -22.500 -38.374 1.00 39.10 ATOM 3065 N SER B 555 52.455 -21.335 -40.133 1.00 39.71 ATOM 3066 CA SER B 555 53.514 -20.680 -39.372 1.00 40.66 ATOM 3067 CB SER B 555 54.881 -21.070 -39.933 1.00 41.41 ATOM 3068 OG SER B 555 55.144 -22.445 -39.715 1.00 43.21 ATOM 3069 C SER B 555 53.354 -19.166 -39.438 1.00 40.90 ATOM 3070 O SER B 555 53.125 -18.600 -40.509 1.00 40.53 ATOM 3071 N TYR B 556 53.486 -18.507 -38.295 1.00 41.77 ATOM 3072 CA TYR B 556 53.339 -17.059 -38.254 1.00 43.25 ATOM 3073 CB TYR B 556 51.895 -16.687 -37.920 1.00 41.08 ATOM 3074 CG TYR B 556 51.383 -17.326 -36.657 1.00 39.07 ATOM 3075 CD1 TYR B 556 50.588 -18.462 -36.708 1.00 37.86 ATOM 3076 CE1 TYR B 556 50.084 -19.036 -35.549 1.00 37.92 ATOM 3077 CD2 TYR B 556 51.669 -16.778 -35.410 1.00 38.45 ATOM 3078 CE2 TYR B 556 51.169 -17.344 -34.245 1.00 37.88 ATOM 3079 CZ TYR B 556 50.376 -18.472 -34.324 1.00 37.76 ATOM 3080 OH TYR B 556 49.865 -19.037 -33.185 1.00 38.17 ATOM 3081 C TYR B 556 54.272 -16.387 -37.264 1.00 45.16 ATOM 3082 O TYR B 556 54.803 -17.023 -36.348 1.00 44.99 ATOM 3083 N THR B 557 54.446 -15.083 -37.456 1.00 47.21 ATOM 3084 CA THR B 557 55.322 -14.276 -36.622 1.00 49.73 ATOM 3085 CB THR B 557 56.662 -14.033 -37.336 1.00 50.09 ATOM 3086 OG1 THR B 557 56.424 -13.295 -38.540 1.00 50.37 ATOM 3087 CG2 THR B 557 57.326 -15.351 -37.702 1.00 50.49 ATOM 3088 C THR B 557 54.699 -12.915 -36.319 1.00 51.00 ATOM 3089 O THR B 557 53.568 -12.631 -36.720 1.00 51.26 ATOM 3090 N ASP B 558 55.459 -12.080 -35.612 1.00 52.73 ATOM 3091 CA ASP B 558 55.044 -10.727 -35.249 1.00 54.49 ATOM 3092 CB ASP B 558 55.106 -9.809 -36.468 1.00 54.68 ATOM 3093 CG ASP B 558 56.477 -9.793 -37.110 1.00 55.18 ATOM 3094 OD1 ASP B 558 57.479 -9.671 -36.373 1.00 55.21 ATOM 3095 OD2 ASP B 558 56.546 -9.898 -38.353 1.00 55.52 ATOM 3096 C ASP B 558 53.659 -10.656 -34.634 1.00 55.88 ATOM 3097 O ASP B 558 52.825 -9.860 -35.053 1.00 55.79 ATOM 3098 N THR B 559 53.430 -11.494 -33.624 1.00 58.08 ATOM 3099 CA THR B 559 52.148 -11.544 -32.945 1.00 59.82 ATOM 3100 CB THR B 559 51.990 -12.870 -32.174 1.00 60.54 ATOM 3101 OG1 THR B 559 51.848 -13.950 -33.101 1.00 60.92 ATOM 3102 CG2 THR B 559 50.766 -12.827 -31.274 1.00 60.42 ATOM 3103 C THR B 559 51.967 -10.387 -31.969 1.00 60.56 ATOM 3104 O THR B 559 52.687 -10.276 -30.977 1.00 61.14 ATOM 3105 N LYS B 560 50.996 -9.525 -32.260 1.00 60.93 ATOM 3106 CA LYS B 560 50.703 -8.380 -31.404 1.00 61.31 ATOM 3107 CB LYS B 560 51.243 -7.086 -32.028 1.00 61.52 ATOM 3108 CG LYS B 560 50.743 -6.793 -33.430 1.00 62.42 ATOM 3109 CD LYS B 560 51.851 -6.197 -34.289 1.00 63.57 ATOM 3110 CE LYS B 560 51.368 -4.975 -35.074 1.00 64.37 ATOM 3111 NZ LYS B 560 52.286 -4.621 -36.208 1.00 64.56 ATOM 3112 C LYS B 560 49.196 -8.262 -31.181 1.00 61.40 ATOM 3113 O LYS B 560 48.407 -8.431 -32.114 1.00 61.36 ATOM 3114 N VAL B 561 48.798 -7.981 -29.942 1.00 61.05 ATOM 3115 CA VAL B 561 47.386 -7.841 -29.609 1.00 60.99 ATOM 3116 CB VAL B 561 47.183 -7.647 -28.095 1.00 60.15 ATOM 3117 CG1 VAL B 561 45.703 -7.524 -27.785 1.00 59.35 ATOM 3118 CG2 VAL B 561 47.793 -8.813 -27.335 1.00 59.71 ATOM 3119 C VAL B 561 46.752 -6.661 -30.339 1.00 61.47 ATOM 3120 O VAL B 561 47.322 -5.575 -30.393 1.00 61.17 ATOM 3121 N ILE B 562 45.575 -6.887 -30.914 1.00 62.34 ATOM 3122 CA ILE B 562 44.860 -5.839 -31.632 1.00 63.76 ATOM 3123 CB ILE B 562 44.847 -6.077 -33.168 1.00 63.41 ATOM 3124 CG2 ILE B 562 46.266 -6.094 -33.708 1.00 63.45 ATOM 3125 CG1 ILE B 562 44.121 -7.384 -33.496 1.00 63.03 ATOM 3126 CD1 ILE B 562 43.702 -7.498 -34.946 1.00 61.88 ATOM 3127 C ILE B 562 43.422 -5.796 -31.145 1.00 64.84 ATOM 3128 O ILE B 562 42.560 -5.178 -31.765 1.00 64.81 ATOM 3129 N GLY B 563 43.172 -6.462 -30.026 1.00 66.49 ATOM 3130 CA GLY B 563 41.833 -6.490 -29.477 1.00 68.63 ATOM 3131 C GLY B 563 41.766 -7.253 -28.172 1.00 70.21 ATOM 3132 O GLY B 563 42.737 -7.883 -27.745 1.00 70.24 ATOM 3133 N ASN B 564 40.607 -7.192 -27.530 1.00 71.83 ATOM 3134 CA ASN B 564 40.408 -7.883 -26.269 1.00 73.56 ATOM 3135 CB ASN B 564 41.262 -7.249 -25.167 1.00 74.35 ATOM 3136 CG ASN B 564 41.875 -8.285 -24.239 1.00 75.58 ATOM 3137 OD1 ASN B 564 43.099 -8.398 -24.136 1.00 76.11 ATOM 3138 ND2 ASN B 564 41.022 -9.051 -23.560 1.00 75.83 ATOM 3139 C ASN B 564 38.944 -7.852 -25.868 1.00 74.07 ATOM 3140 O ASN B 564 38.270 -6.830 -25.998 1.00 74.36 ATOM 3141 N GLY B 565 38.458 -8.991 -25.391 1.00 74.53 ATOM 3142 CA GLY B 565 37.078 -9.095 -24.964 1.00 74.80 ATOM 3143 C GLY B 565 37.014 -9.900 -23.684 1.00 75.03 ATOM 3144 O GLY B 565 38.030 -10.431 -23.227 1.00 74.76 ATOM 3145 N SER B 566 35.824 -9.990 -23.102 1.00 75.46 ATOM 3146 CA SER B 566 35.644 -10.739 -21.864 1.00 75.74 ATOM 3147 CB SER B 566 34.209 -10.580 -21.344 1.00 76.21 ATOM 3148 OG SER B 566 33.309 -10.183 -22.368 1.00 76.26 ATOM 3149 C SER B 566 35.946 -12.217 -22.083 1.00 75.49 ATOM 3150 O SER B 566 36.217 -12.952 -21.132 1.00 75.55 ATOM 3151 N PHE B 567 35.911 -12.639 -23.345 1.00 75.20 ATOM 3152 CA PHE B 567 36.159 -14.034 -23.705 1.00 74.61 ATOM 3153 CB PHE B 567 35.265 -14.425 -24.889 1.00 76.01 ATOM 3154 CG PHE B 567 33.809 -14.066 -24.699 1.00 77.57 ATOM 3155 CD1 PHE B 567 32.981 -13.851 -25.798 1.00 78.18 ATOM 3156 CD2 PHE B 567 33.265 -13.943 -23.418 1.00 78.26 ATOM 3157 CE1 PHE B 567 31.631 -13.518 -25.624 1.00 78.73 ATOM 3158 CE2 PHE B 567 31.919 -13.611 -23.233 1.00 78.52 ATOM 3159 CZ PHE B 567 31.102 -13.398 -24.335 1.00 78.72 ATOM 3160 C PHE B 567 37.620 -14.363 -24.020 1.00 73.21 ATOM 3161 O PHE B 567 38.097 -15.453 -23.689 1.00 73.13 ATOM 3162 N GLY B 568 38.332 -13.435 -24.654 1.00 71.41 ATOM 3163 CA GLY B 568 39.727 -13.690 -24.977 1.00 68.78 ATOM 3164 C GLY B 568 40.486 -12.525 -25.587 1.00 66.86 ATOM 3165 O GLY B 568 40.183 -11.360 -25.321 1.00 67.03 ATOM 3166 N VAL B 569 41.478 -12.845 -26.412 1.00 64.50 ATOM 3167 CA VAL B 569 42.296 -11.829 -27.058 1.00 62.20 ATOM 3168 CB VAL B 569 43.708 -11.806 -26.463 1.00 62.15 ATOM 3169 CG1 VAL B 569 44.528 -10.704 -27.114 1.00 62.37 ATOM 3170 CG2 VAL B 569 43.629 -11.607 -24.964 1.00 62.69 ATOM 3171 C VAL B 569 42.434 -12.040 -28.560 1.00 60.50 ATOM 3172 O VAL B 569 42.570 -13.169 -29.030 1.00 60.58 ATOM 3173 N VAL B 570 42.402 -10.940 -29.306 1.00 57.97 ATOM 3174 CA VAL B 570 42.549 -10.988 -30.751 1.00 55.76 ATOM 3175 CB VAL B 570 41.485 -10.122 -31.455 1.00 54.87 ATOM 3176 CG1 VAL B 570 41.569 -10.313 -32.957 1.00 54.01 ATOM 3177 CG2 VAL B 570 40.102 -10.491 -30.953 1.00 54.16 ATOM 3178 C VAL B 570 43.938 -10.458 -31.101 1.00 55.17 ATOM 3179 O VAL B 570 44.269 -9.315 -30.788 1.00 54.87 ATOM 3180 N TYR B 571 44.753 -11.296 -31.737 1.00 53.94 ATOM 3181 CA TYR B 571 46.102 -10.898 -32.124 1.00 52.76 ATOM 3182 CB TYR B 571 47.124 -11.983 -31.790 1.00 52.78 ATOM 3183 CG TYR B 571 47.097 -12.498 -30.382 1.00 53.28 ATOM 3184 CD1 TYR B 571 47.969 -11.988 -29.421 1.00 53.40 ATOM 3185 CE1 TYR B 571 47.995 -12.501 -28.132 1.00 53.88 ATOM 3186 CD2 TYR B 571 46.244 -13.535 -30.020 1.00 53.48 ATOM 3187 CE2 TYR B 571 46.258 -14.058 -28.733 1.00 54.19 ATOM 3188 CZ TYR B 571 47.139 -13.537 -27.792 1.00 54.54 ATOM 3189 OH TYR B 571 47.169 -14.058 -26.517 1.00 55.51 ATOM 3190 C TYR B 571 46.224 -10.656 -33.608 1.00 51.98 ATOM 3191 O TYR B 571 45.393 -11.103 -34.399 1.00 52.03 ATOM 3192 N GLN B 572 47.272 -9.934 -33.980 1.00 51.30 ATOM 3193 CA GLN B 572 47.560 -9.713 -35.380 1.00 50.74 ATOM 3194 CB GLN B 572 47.858 -8.254 -35.701 1.00 51.11 ATOM 3195 CG GLN B 572 47.950 -8.027 -37.206 1.00 51.70 ATOM 3196 CD GLN B 572 48.851 -6.871 -37.593 1.00 52.65 ATOM 3197 OE1 GLN B 572 49.951 -6.714 -37.059 1.00 53.02 ATOM 3198 NE2 GLN B 572 48.390 -6.056 -38.536 1.00 52.78 ATOM 3199 C GLN B 572 48.822 -10.535 -35.561 1.00 50.22 ATOM 3200 O GLN B 572 49.711 -10.512 -34.711 1.00 49.84 ATOM 3201 N ALA B 573 48.888 -11.284 -36.649 1.00 49.60 ATOM 3202 CA ALA B 573 50.049 -12.109 -36.913 1.00 49.08 ATOM 3203 CB ALA B 573 49.801 -13.544 -36.440 1.00 49.09 ATOM 3204 C ALA B 573 50.328 -12.082 -38.396 1.00 48.89 ATOM 3205 O ALA B 573 49.437 -11.815 -39.207 1.00 48.60 ATOM 3206 N LYS B 574 51.580 -12.344 -38.743 1.00 48.47 ATOM 3207 CA LYS B 574 51.980 -12.361 -40.132 1.00 48.77 ATOM 3208 CB LYS B 574 53.211 -11.483 -40.330 1.00 48.91 ATOM 3209 CG LYS B 574 53.518 -11.187 -41.783 1.00 50.08 ATOM 3210 CD LYS B 574 54.984 -10.852 -41.970 1.00 51.20 ATOM 3211 CE LYS B 574 55.382 -9.634 -41.147 1.00 51.58 ATOM 3212 NZ LYS B 574 56.832 -9.327 -41.297 1.00 52.30 ATOM 3213 C LYS B 574 52.288 -13.797 -40.539 1.00 48.78 ATOM 3214 O LYS B 574 53.026 -14.504 -39.845 1.00 48.79 ATOM 3215 N LEU B 575 51.699 -14.226 -41.650 1.00 48.33 ATOM 3216 CA LEU B 575 51.920 -15.566 -42.160 1.00 48.27 ATOM 3217 CB LEU B 575 50.899 -15.888 -43.249 1.00 46.49 ATOM 3218 CG LEU B 575 49.466 -16.065 -42.746 1.00 45.30 ATOM 3219 CD1 LEU B 575 48.617 -16.638 -43.860 1.00 45.12 ATOM 3220 CD2 LEU B 575 49.442 -16.967 -41.525 1.00 43.88 ATOM 3221 C LEU B 575 53.334 -15.601 -42.717 1.00 49.25 ATOM 3222 O LEU B 575 53.689 -14.805 -43.581 1.00 49.55 ATOM 3223 N CYS B 576 54.132 -16.534 -42.212 1.00 50.52 ATOM 3224 CA CYS B 576 55.528 -16.664 -42.600 1.00 51.93 ATOM 3225 CB CYS B 576 56.118 -17.917 -41.970 1.00 51.45 ATOM 3226 SG CYS B 576 56.502 -17.667 -40.258 1.00 52.08 ATOM 3227 C CYS B 576 55.873 -16.653 -44.075 1.00 53.29 ATOM 3228 O CYS B 576 56.834 -16.000 -44.486 1.00 54.31 ATOM 3229 N ASP B 577 55.111 -17.365 -44.887 1.00 54.27 ATOM 3230 CA ASP B 577 55.449 -17.396 -46.294 1.00 55.52 ATOM 3231 CB ASP B 577 55.177 -18.791 -46.843 1.00 56.77 ATOM 3232 CG ASP B 577 56.228 -19.785 -46.390 1.00 57.98 ATOM 3233 OD1 ASP B 577 57.422 -19.544 -46.678 1.00 58.98 ATOM 3234 OD2 ASP B 577 55.872 -20.789 -45.734 1.00 58.69 ATOM 3235 C ASP B 577 54.780 -16.322 -47.131 1.00 55.78 ATOM 3236 O ASP B 577 55.461 -15.538 -47.793 1.00 56.18 ATOM 3237 N SER B 578 53.455 -16.265 -47.096 1.00 55.43 ATOM 3238 CA SER B 578 52.744 -15.262 -47.873 1.00 54.75 ATOM 3239 CB SER B 578 51.236 -15.514 -47.813 1.00 55.03 ATOM 3240 OG SER B 578 50.742 -15.362 -46.495 1.00 55.44 ATOM 3241 C SER B 578 53.053 -13.860 -47.362 1.00 54.27 ATOM 3242 O SER B 578 52.973 -12.887 -48.110 1.00 54.30 ATOM 3243 N GLY B 579 53.422 -13.764 -46.088 1.00 53.59 ATOM 3244 CA GLY B 579 53.712 -12.469 -45.498 1.00 52.51 ATOM 3245 C GLY B 579 52.394 -11.806 -45.159 1.00 51.54 ATOM 3246 O GLY B 579 52.338 -10.716 -44.602 1.00 51.84 ATOM 3247 N GLU B 580 51.319 -12.499 -45.506 1.00 50.70 ATOM 3248 CA GLU B 580 49.964 -12.032 -45.275 1.00 49.57 ATOM 3249 CB GLU B 580 48.974 -13.053 -45.814 1.00 50.73 ATOM 3250 CG GLU B 580 48.084 -12.534 -46.898 1.00 52.21 ATOM 3251 CD GLU B 580 47.243 -13.631 -47.496 1.00 53.36 ATOM 3252 OE1 GLU B 580 46.116 -13.331 -47.935 1.00 54.82 ATOM 3253 OE2 GLU B 580 47.706 -14.792 -47.524 1.00 53.57 ATOM 3254 C GLU B 580 49.664 -11.810 -43.809 1.00 48.09 ATOM 3255 O GLU B 580 50.130 -12.552 -42.947 1.00 48.52 ATOM 3256 N LEU B 581 48.869 -10.786 -43.531 1.00 46.18 ATOM 3257 CA LEU B 581 48.484 -10.488 -42.163 1.00 44.19 ATOM 3258 CB LEU B 581 48.328 -8.980 -41.968 1.00 44.42 ATOM 3259 CG LEU B 581 49.620 -8.190 -41.765 1.00 44.92 ATOM 3260 CD1 LEU B 581 49.303 -6.707 -41.764 1.00 44.82 ATOM 3261 CD2 LEU B 581 50.272 -8.592 -40.453 1.00 44.84 ATOM 3262 C LEU B 581 47.151 -11.177 -41.917 1.00 42.42 ATOM 3263 O LEU B 581 46.344 -11.322 -42.833 1.00 42.11 ATOM 3264 N VAL B 582 46.934 -11.619 -40.687 1.00 40.26 ATOM 3265 CA VAL B 582 45.690 -12.275 -40.321 1.00 38.61 ATOM 3266 CB VAL B 582 45.772 -13.843 -40.410 1.00 38.15 ATOM 3267 CG1 VAL B 582 46.147 -14.282 -41.825 1.00 36.99 ATOM 3268 CG2 VAL B 582 46.770 -14.382 -39.391 1.00 37.47 ATOM 3269 C VAL B 582 45.431 -11.897 -38.884 1.00 37.86 ATOM 3270 O VAL B 582 46.286 -11.308 -38.232 1.00 37.67 ATOM 3271 N ALA B 583 44.247 -12.230 -38.395 1.00 37.41 ATOM 3272 CA ALA B 583 43.891 -11.947 -37.016 1.00 37.05 ATOM 3273 CB ALA B 583 42.643 -11.076 -36.964 1.00 36.51 ATOM 3274 C ALA B 583 43.618 -13.300 -36.381 1.00 36.99 ATOM 3275 O ALA B 583 43.115 -14.204 -37.045 1.00 37.55 ATOM 3276 N ILE B 584 43.957 -13.450 -35.109 1.00 36.68 ATOM 3277 CA ILE B 584 43.718 -14.708 -34.429 1.00 37.15 ATOM 3278 CB ILE B 584 45.040 -15.408 -34.030 1.00 37.68 ATOM 3279 CG2 ILE B 584 44.738 -16.693 -33.266 1.00 36.71 ATOM 3280 CG1 ILE B 584 45.870 -15.709 -35.280 1.00 37.59 ATOM 3281 CD1 ILE B 584 47.287 -16.130 -34.969 1.00 37.96 ATOM 3282 C ILE B 584 42.907 -14.470 -33.175 1.00 37.82 ATOM 3283 O ILE B 584 43.424 -13.962 -32.178 1.00 37.77 ATOM 3284 N LYS B 585 41.630 -14.829 -33.230 1.00 38.60 ATOM 3285 CA LYS B 585 40.752 -14.662 -32.080 1.00 39.70 ATOM 3286 CB LYS B 585 39.292 -14.492 -32.535 1.00 38.60 ATOM 3287 CG LYS B 585 38.297 -14.258 -31.401 1.00 37.34 ATOM 3288 CD LYS B 585 36.904 -13.926 -31.928 1.00 37.19 ATOM 3289 CE LYS B 585 35.928 -13.641 -30.789 1.00 36.87 ATOM 3290 NZ LYS B 585 34.631 -13.076 -31.267 1.00 36.41 ATOM 3291 C LYS B 585 40.896 -15.886 -31.180 1.00 41.09 ATOM 3292 O LYS B 585 40.502 -16.995 -31.541 1.00 40.73 ATOM 3293 N LYS B 586 41.481 -15.673 -30.009 1.00 43.27 ATOM 3294 CA LYS B 586 41.693 -16.739 -29.045 1.00 45.63 ATOM 3295 CB LYS B 586 43.069 -16.585 -28.401 1.00 46.13 ATOM 3296 CG LYS B 586 43.454 -17.715 -27.470 1.00 47.05 ATOM 3297 CD LYS B 586 44.909 -17.585 -27.060 1.00 47.67 ATOM 3298 CE LYS B 586 45.466 -18.921 -26.612 1.00 48.89 ATOM 3299 NZ LYS B 586 46.956 -18.968 -26.700 1.00 49.62 ATOM 3300 C LYS B 586 40.611 -16.689 -27.979 1.00 47.23 ATOM 3301 O LYS B 586 40.460 -15.688 -27.285 1.00 47.49 ATOM 3302 N VAL B 587 39.865 -17.782 -27.851 1.00 49.38 ATOM 3303 CA VAL B 587 38.776 -17.875 -26.888 1.00 51.10 ATOM 3304 CB VAL B 587 37.413 -17.852 -27.622 1.00 50.74 ATOM 3305 CG1 VAL B 587 36.333 -18.476 -26.762 1.00 51.23 ATOM 3306 CG2 VAL B 587 37.047 -16.425 -27.978 1.00 50.50 ATOM 3307 C VAL B 587 38.879 -19.154 -26.056 1.00 52.83 ATOM 3308 O VAL B 587 39.272 -20.203 -26.564 1.00 52.68 ATOM 3309 N LEU B 588 38.531 -19.060 -24.775 1.00 54.87 ATOM 3310 CA LEU B 588 38.572 -20.223 -23.898 1.00 56.99 ATOM 3311 CB LEU B 588 38.334 -19.811 -22.446 1.00 56.93 ATOM 3312 CG LEU B 588 38.692 -20.862 -21.395 1.00 56.78 ATOM 3313 CD1 LEU B 588 40.133 -20.679 -20.954 1.00 56.38 ATOM 3314 CD2 LEU B 588 37.747 -20.734 -20.213 1.00 57.30 ATOM 3315 C LEU B 588 37.483 -21.190 -24.348 1.00 58.69 ATOM 3316 O LEU B 588 36.327 -20.800 -24.526 1.00 58.82 ATOM 3317 N GLN B 589 37.855 -22.451 -24.536 1.00 60.90 ATOM 3318 CA GLN B 589 36.903 -23.452 -24.991 1.00 62.94 ATOM 3319 CB GLN B 589 37.537 -24.330 -26.074 1.00 63.31 ATOM 3320 CG GLN B 589 36.563 -25.315 -26.703 1.00 64.14 ATOM 3321 CD GLN B 589 35.187 -24.706 -26.932 1.00 64.73 ATOM 3322 OE1 GLN B 589 34.163 -25.277 -26.543 1.00 64.50 ATOM 3323 NE2 GLN B 589 35.158 -23.535 -27.564 1.00 65.31 ATOM 3324 C GLN B 589 36.377 -24.337 -23.874 1.00 64.32 ATOM 3325 O GLN B 589 37.149 -24.886 -23.088 1.00 64.81 ATOM 3326 N ASP B 590 35.053 -24.470 -23.820 1.00 65.80 ATOM 3327 CA ASP B 590 34.388 -25.304 -22.824 1.00 67.31 ATOM 3328 CB ASP B 590 32.949 -24.811 -22.599 1.00 68.05 ATOM 3329 CG ASP B 590 32.319 -25.379 -21.329 1.00 69.33 ATOM 3330 OD1 ASP B 590 31.236 -24.888 -20.927 1.00 69.65 ATOM 3331 OD2 ASP B 590 32.902 -26.315 -20.733 1.00 69.92 ATOM 3332 C ASP B 590 34.367 -26.746 -23.336 1.00 67.97 ATOM 3333 O ASP B 590 33.736 -27.043 -24.353 1.00 68.15 ATOM 3334 N LYS B 591 35.065 -27.637 -22.638 1.00 68.65 ATOM 3335 CA LYS B 591 35.106 -29.041 -23.035 1.00 69.26 ATOM 3336 CB LYS B 591 36.055 -29.824 -22.114 1.00 69.42 ATOM 3337 CG LYS B 591 37.543 -29.619 -22.410 1.00 69.57 ATOM 3338 CD LYS B 591 38.116 -28.410 -21.668 1.00 69.75 ATOM 3339 CE LYS B 591 38.122 -28.622 -20.158 1.00 69.82 ATOM 3340 NZ LYS B 591 36.778 -28.384 -19.555 1.00 69.62 ATOM 3341 C LYS B 591 33.696 -29.640 -22.965 1.00 69.37 ATOM 3342 O LYS B 591 33.453 -30.743 -23.456 1.00 69.62 ATOM 3343 N ARG B 592 32.770 -28.895 -22.363 1.00 69.30 ATOM 3344 CA ARG B 592 31.381 -29.326 -22.207 1.00 69.00 ATOM 3345 CB ARG B 592 30.645 -28.363 -21.270 1.00 69.99 ATOM 3346 CG ARG B 592 29.242 -28.800 -20.879 1.00 71.70 ATOM 3347 CD ARG B 592 29.162 -30.285 -20.549 1.00 73.42 ATOM 3348 NE ARG B 592 27.834 -30.676 -20.073 1.00 75.05 ATOM 3349 CZ ARG B 592 27.568 -31.826 -19.455 1.00 75.87 ATOM 3350 NH1 ARG B 592 28.539 -32.705 -19.234 1.00 76.20 ATOM 3351 NH2 ARG B 592 26.330 -32.101 -19.057 1.00 76.31 ATOM 3352 C ARG B 592 30.610 -29.454 -23.526 1.00 68.14 ATOM 3353 O ARG B 592 30.129 -30.536 -23.858 1.00 68.42 ATOM 3354 N PHE B 593 30.474 -28.353 -24.264 1.00 66.93 ATOM 3355 CA PHE B 593 29.768 -28.373 -25.550 1.00 65.45 ATOM 3356 CB PHE B 593 28.477 -27.538 -25.498 1.00 66.45 ATOM 3357 CG PHE B 593 28.027 -27.169 -24.106 1.00 67.42 ATOM 3358 CD1 PHE B 593 27.113 -27.971 -23.421 1.00 67.74 ATOM 3359 CD2 PHE B 593 28.480 -25.998 -23.497 1.00 67.83 ATOM 3360 CE1 PHE B 593 26.653 -27.612 -22.148 1.00 67.97 ATOM 3361 CE2 PHE B 593 28.027 -25.628 -22.222 1.00 67.99 ATOM 3362 CZ PHE B 593 27.111 -26.437 -21.549 1.00 68.00 ATOM 3363 C PHE B 593 30.648 -27.834 -26.681 1.00 63.84 ATOM 3364 O PHE B 593 31.807 -27.469 -26.464 1.00 64.09 ATOM 3365 N LYS B 594 30.091 -27.785 -27.889 1.00 61.40 ATOM 3366 CA LYS B 594 30.824 -27.276 -29.046 1.00 58.74 ATOM 3367 CB LYS B 594 30.260 -27.859 -30.346 1.00 60.00 ATOM 3368 CG LYS B 594 30.117 -29.375 -30.341 1.00 61.87 ATOM 3369 CD LYS B 594 30.170 -29.951 -31.752 1.00 63.27 ATOM 3370 CE LYS B 594 29.593 -31.363 -31.790 1.00 64.19 ATOM 3371 NZ LYS B 594 28.892 -31.659 -33.078 1.00 64.92 ATOM 3372 C LYS B 594 30.718 -25.758 -29.093 1.00 56.00 ATOM 3373 O LYS B 594 29.776 -25.174 -28.549 1.00 55.44 ATOM 3374 N ASN B 595 31.686 -25.119 -29.743 1.00 52.69 ATOM 3375 CA ASN B 595 31.675 -23.668 -29.856 1.00 48.94 ATOM 3376 CB ASN B 595 33.059 -23.153 -30.224 1.00 48.39 ATOM 3377 CG ASN B 595 33.170 -21.668 -30.052 1.00 48.01 ATOM 3378 OD1 ASN B 595 33.456 -21.186 -28.961 1.00 48.25 ATOM 3379 ND2 ASN B 595 32.930 -20.927 -31.124 1.00 47.46 ATOM 3380 C ASN B 595 30.661 -23.223 -30.911 1.00 46.45 ATOM 3381 O ASN B 595 30.777 -23.582 -32.086 1.00 45.47 ATOM 3382 N ARG B 596 29.670 -22.444 -30.482 1.00 43.73 ATOM 3383 CA ARG B 596 28.625 -21.966 -31.383 1.00 41.00 ATOM 3384 CB ARG B 596 27.490 -21.331 -30.588 1.00 41.35 ATOM 3385 CG ARG B 596 26.304 -20.948 -31.438 1.00 42.82 ATOM 3386 CD ARG B 596 25.197 -20.329 -30.595 1.00 44.47 ATOM 3387 NE ARG B 596 24.492 -21.331 -29.801 1.00 46.21 ATOM 3388 CZ ARG B 596 23.760 -21.056 -28.722 1.00 47.21 ATOM 3389 NH1 ARG B 596 23.630 -19.800 -28.298 1.00 47.18 ATOM 3390 NH2 ARG B 596 23.152 -22.041 -28.066 1.00 47.44 ATOM 3391 C ARG B 596 29.149 -20.967 -32.406 1.00 38.80 ATOM 3392 O ARG B 596 28.697 -20.956 -33.548 1.00 38.32 ATOM 3393 N GLU B 597 30.100 -20.134 -31.994 1.00 36.41 ATOM 3394 CA GLU B 597 30.682 -19.138 -32.885 1.00 34.56 ATOM 3395 CB GLU B 597 31.659 -18.253 -32.107 1.00 33.75 ATOM 3396 CG GLU B 597 32.405 -17.226 -32.953 1.00 33.98 ATOM 3397 CD GLU B 597 33.178 -16.215 -32.105 1.00 34.70 ATOM 3398 OE1 GLU B 597 33.733 -15.247 -32.673 1.00 33.20 ATOM 3399 OE2 GLU B 597 33.229 -16.393 -30.867 1.00 34.89 ATOM 3400 C GLU B 597 31.402 -19.840 -34.039 1.00 33.99 ATOM 3401 O GLU B 597 31.220 -19.488 -35.203 1.00 32.69 ATOM 3402 N LEU B 598 32.212 -20.842 -33.704 1.00 33.66 ATOM 3403 CA LEU B 598 32.955 -21.610 -34.698 1.00 33.80 ATOM 3404 CB LEU B 598 33.863 -22.626 -34.002 1.00 33.84 ATOM 3405 CG LEU B 598 34.503 -23.678 -34.908 1.00 33.05 ATOM 3406 CD1 LEU B 598 35.452 -23.000 -35.875 1.00 33.10 ATOM 3407 CD2 LEU B 598 35.250 -24.695 -34.064 1.00 33.14 ATOM 3408 C LEU B 598 32.004 -22.351 -35.639 1.00 34.21 ATOM 3409 O LEU B 598 32.164 -22.313 -36.862 1.00 33.78 ATOM 3410 N GLN B 599 31.014 -23.025 -35.062 1.00 34.14 ATOM 3411 CA GLN B 599 30.050 -23.775 -35.850 1.00 34.97 ATOM 3412 CB GLN B 599 29.025 -24.431 -34.924 1.00 36.61 ATOM 3413 CG GLN B 599 29.615 -25.441 -33.915 1.00 40.88 ATOM 3414 CD GLN B 599 30.943 -26.079 -34.361 1.00 43.72 ATOM 3415 OE1 GLN B 599 31.057 -26.627 -35.472 1.00 45.15 ATOM 3416 NE2 GLN B 599 31.951 -26.016 -33.485 1.00 45.02 ATOM 3417 C GLN B 599 29.344 -22.880 -36.867 1.00 34.56 ATOM 3418 O GLN B 599 29.086 -23.288 -38.000 1.00 33.90 ATOM 3419 N ILE B 600 29.039 -21.651 -36.461 1.00 34.40 ATOM 3420 CA ILE B 600 28.365 -20.705 -37.340 1.00 33.47 ATOM 3421 CB ILE B 600 27.768 -19.527 -36.525 1.00 33.33 ATOM 3422 CG2 ILE B 600 27.540 -18.312 -37.425 1.00 32.72 ATOM 3423 CG1 ILE B 600 26.457 -19.975 -35.866 1.00 32.42 ATOM 3424 CD1 ILE B 600 25.972 -19.065 -34.757 1.00 31.94 ATOM 3425 C ILE B 600 29.337 -20.173 -38.387 1.00 33.40 ATOM 3426 O ILE B 600 29.032 -20.158 -39.574 1.00 32.98 ATOM 3427 N MET B 601 30.515 -19.752 -37.946 1.00 34.16 ATOM 3428 CA MET B 601 31.518 -19.213 -38.858 1.00 35.77 ATOM 3429 CB MET B 601 32.772 -18.804 -38.084 1.00 36.64 ATOM 3430 CG MET B 601 32.550 -17.683 -37.087 1.00 38.71 ATOM 3431 SD MET B 601 33.517 -16.214 -37.433 1.00 40.71 ATOM 3432 CE MET B 601 35.019 -16.880 -37.979 1.00 41.30 ATOM 3433 C MET B 601 31.918 -20.198 -39.951 1.00 36.31 ATOM 3434 O MET B 601 32.214 -19.801 -41.078 1.00 36.21 ATOM 3435 N ARG B 602 31.930 -21.483 -39.611 1.00 36.60 ATOM 3436 CA ARG B 602 32.316 -22.520 -40.560 1.00 36.69 ATOM 3437 CB ARG B 602 32.428 -23.864 -39.848 1.00 37.44 ATOM 3438 CG ARG B 602 33.592 -23.915 -38.880 1.00 38.74 ATOM 3439 CD ARG B 602 33.725 -25.294 -38.292 1.00 39.44 ATOM 3440 NE ARG B 602 34.306 -26.201 -39.265 1.00 40.02 ATOM 3441 CZ ARG B 602 34.522 -27.487 -39.035 1.00 40.55 ATOM 3442 NH1 ARG B 602 34.201 -28.019 -37.856 1.00 40.31 ATOM 3443 NH2 ARG B 602 35.057 -28.239 -39.985 1.00 41.40 ATOM 3444 C ARG B 602 31.384 -22.654 -41.748 1.00 36.34 ATOM 3445 O ARG B 602 31.811 -23.068 -42.817 1.00 36.59 ATOM 3446 N LYS B 603 30.116 -22.304 -41.577 1.00 36.10 ATOM 3447 CA LYS B 603 29.194 -22.418 -42.692 1.00 36.16 ATOM 3448 CB LYS B 603 27.855 -22.986 -42.208 1.00 37.64 ATOM 3449 CG LYS B 603 27.109 -22.152 -41.197 1.00 39.77 ATOM 3450 CD LYS B 603 25.888 -22.913 -40.682 1.00 41.51 ATOM 3451 CE LYS B 603 26.277 -23.896 -39.572 1.00 43.64 ATOM 3452 NZ LYS B 603 25.346 -25.077 -39.456 1.00 45.18 ATOM 3453 C LYS B 603 28.976 -21.119 -43.473 1.00 35.27 ATOM 3454 O LYS B 603 28.228 -21.099 -44.451 1.00 35.61 ATOM 3455 N LEU B 604 29.644 -20.043 -43.068 1.00 33.83 ATOM 3456 CA LEU B 604 29.484 -18.764 -43.756 1.00 32.65 ATOM 3457 CB LEU B 604 29.519 -17.609 -42.750 1.00 32.41 ATOM 3458 CG LEU B 604 28.518 -17.707 -41.595 1.00 31.95 ATOM 3459 CD1 LEU B 604 28.627 -16.480 -40.718 1.00 31.69 ATOM 3460 CD2 LEU B 604 27.109 -17.864 -42.148 1.00 31.63 ATOM 3461 C LEU B 604 30.528 -18.515 -44.836 1.00 32.27 ATOM 3462 O LEU B 604 31.719 -18.754 -44.641 1.00 31.99 ATOM 3463 N ASP B 605 30.064 -18.017 -45.974 1.00 32.21 ATOM 3464 CA ASP B 605 30.942 -17.702 -47.096 1.00 32.71 ATOM 3465 CB ASP B 605 31.063 -18.911 -48.026 1.00 34.76 ATOM 3466 CG ASP B 605 31.999 -18.657 -49.184 1.00 36.92 ATOM 3467 OD1 ASP B 605 32.856 -17.749 -49.068 1.00 38.15 ATOM 3468 OD2 ASP B 605 31.876 -19.362 -50.213 1.00 38.42 ATOM 3469 C ASP B 605 30.314 -16.522 -47.837 1.00 31.85 ATOM 3470 O ASP B 605 29.428 -16.706 -48.673 1.00 32.05 ATOM 3471 N HIS B 606 30.773 -15.311 -47.515 1.00 29.98 ATOM 3472 CA HIS B 606 30.234 -14.094 -48.111 1.00 27.99 ATOM 3473 CB HIS B 606 29.016 -13.637 -47.302 1.00 26.92 ATOM 3474 CG HIS B 606 28.198 -12.583 -47.975 1.00 25.49 ATOM 3475 CD2 HIS B 606 27.026 -12.660 -48.651 1.00 25.17 ATOM 3476 ND1 HIS B 606 28.542 -11.251 -47.960 1.00 24.78 ATOM 3477 CE1 HIS B 606 27.620 -10.549 -48.597 1.00 24.65 ATOM 3478 NE2 HIS B 606 26.688 -11.383 -49.025 1.00 24.55 ATOM 3479 C HIS B 606 31.303 -13.004 -48.120 1.00 27.67 ATOM 3480 O HIS B 606 32.115 -12.911 -47.200 1.00 27.11 ATOM 3481 N CYS B 607 31.293 -12.171 -49.155 1.00 27.70 ATOM 3482 CA CYS B 607 32.289 -11.112 -49.289 1.00 28.00 ATOM 3483 CB CYS B 607 32.221 -10.507 -50.702 1.00 29.83 ATOM 3484 SG CYS B 607 30.576 -9.886 -51.227 1.00 34.31 ATOM 3485 C CYS B 607 32.203 -10.001 -48.239 1.00 26.74 ATOM 3486 O CYS B 607 33.150 -9.234 -48.072 1.00 26.61 ATOM 3487 N ASN B 608 31.075 -9.912 -47.538 1.00 25.79 ATOM 3488 CA ASN B 608 30.898 -8.886 -46.508 1.00 24.37 ATOM 3489 CB ASN B 608 29.632 -8.077 -46.788 1.00 23.51 ATOM 3490 CG ASN B 608 29.737 -7.284 -48.080 1.00 23.36 ATOM 3491 OD1 ASN B 608 30.691 -6.523 -48.273 1.00 23.56 ATOM 3492 ND2 ASN B 608 28.777 -7.470 -48.976 1.00 21.39 ATOM 3493 C ASN B 608 30.863 -9.473 -45.101 1.00 24.51 ATOM 3494 O ASN B 608 30.263 -8.908 -44.183 1.00 23.87 ATOM 3495 N ILE B 609 31.513 -10.619 -44.945 1.00 23.91 ATOM 3496 CA ILE B 609 31.609 -11.301 -43.663 1.00 23.93 ATOM 3497 CB ILE B 609 30.666 -12.534 -43.602 1.00 23.60 ATOM 3498 CG2 ILE B 609 30.960 -13.369 -42.348 1.00 22.89 ATOM 3499 CG1 ILE B 609 29.211 -12.062 -43.628 1.00 22.15 ATOM 3500 CD1 ILE B 609 28.201 -13.156 -43.439 1.00 23.21 ATOM 3501 C ILE B 609 33.061 -11.744 -43.573 1.00 24.59 ATOM 3502 O ILE B 609 33.598 -12.337 -44.514 1.00 24.48 ATOM 3503 N VAL B 610 33.708 -11.442 -42.457 1.00 24.98 ATOM 3504 CA VAL B 610 35.108 -11.799 -42.300 1.00 26.44 ATOM 3505 CB VAL B 610 35.667 -11.268 -40.952 1.00 26.34 ATOM 3506 CG1 VAL B 610 35.082 -12.055 -39.777 1.00 25.75 ATOM 3507 CG2 VAL B 610 37.192 -11.322 -40.976 1.00 26.89 ATOM 3508 C VAL B 610 35.284 -13.314 -42.420 1.00 27.37 ATOM 3509 O VAL B 610 34.536 -14.086 -41.827 1.00 26.41 ATOM 3510 N ARG B 611 36.276 -13.722 -43.203 1.00 28.86 ATOM 3511 CA ARG B 611 36.543 -15.134 -43.448 1.00 30.89 ATOM 3512 CB ARG B 611 37.252 -15.302 -44.801 1.00 32.83 ATOM 3513 CG ARG B 611 37.537 -16.760 -45.184 1.00 36.04 ATOM 3514 CD ARG B 611 38.233 -16.883 -46.538 1.00 37.80 ATOM 3515 NE ARG B 611 39.456 -16.091 -46.583 1.00 41.57 ATOM 3516 CZ ARG B 611 40.426 -16.247 -47.486 1.00 44.18 ATOM 3517 NH1 ARG B 611 40.317 -17.174 -48.434 1.00 44.86 ATOM 3518 NH2 ARG B 611 41.509 -15.471 -47.443 1.00 44.75 ATOM 3519 C ARG B 611 37.348 -15.870 -42.390 1.00 30.87 ATOM 3520 O ARG B 611 38.358 -15.371 -41.895 1.00 30.69 ATOM 3521 N LEU B 612 36.883 -17.068 -42.056 1.00 31.47 ATOM 3522 CA LEU B 612 37.577 -17.929 -41.108 1.00 32.71 ATOM 3523 CB LEU B 612 36.583 -18.820 -40.347 1.00 32.10 ATOM 3524 CG LEU B 612 37.214 -19.922 -39.481 1.00 31.99 ATOM 3525 CD1 LEU B 612 37.872 -19.290 -38.272 1.00 31.69 ATOM 3526 CD2 LEU B 612 36.169 -20.938 -39.054 1.00 31.83 ATOM 3527 C LEU B 612 38.510 -18.804 -41.959 1.00 33.82 ATOM 3528 O LEU B 612 38.056 -19.725 -42.642 1.00 33.80 ATOM 3529 N ARG B 613 39.801 -18.499 -41.944 1.00 34.45 ATOM 3530 CA ARG B 613 40.760 -19.282 -42.716 1.00 36.20 ATOM 3531 CB ARG B 613 42.118 -18.608 -42.671 1.00 37.09 ATOM 3532 CG ARG B 613 42.143 -17.295 -43.404 1.00 38.99 ATOM 3533 CD ARG B 613 43.559 -16.944 -43.759 1.00 41.53 ATOM 3534 NE ARG B 613 43.638 -15.671 -44.457 1.00 43.86 ATOM 3535 CZ ARG B 613 44.704 -15.268 -45.141 1.00 44.90 ATOM 3536 NH1 ARG B 613 44.693 -14.088 -45.750 1.00 45.55 ATOM 3537 NH2 ARG B 613 45.778 -16.046 -45.215 1.00 45.35 ATOM 3538 C ARG B 613 40.841 -20.687 -42.133 1.00 36.81 ATOM 3539 O ARG B 613 40.614 -21.677 -42.831 1.00 37.14 ATOM 3540 N TYR B 614 41.180 -20.771 -40.851 1.00 37.38 ATOM 3541 CA TYR B 614 41.231 -22.051 -40.158 1.00 38.05 ATOM 3542 CB TYR B 614 42.491 -22.861 -40.494 1.00 38.92 ATOM 3543 CG TYR B 614 43.586 -22.079 -41.140 1.00 39.59 ATOM 3544 CD1 TYR B 614 43.915 -22.284 -42.481 1.00 40.08 ATOM 3545 CE1 TYR B 614 44.892 -21.527 -43.103 1.00 40.67 ATOM 3546 CD2 TYR B 614 44.267 -21.105 -40.430 1.00 40.51 ATOM 3547 CE2 TYR B 614 45.251 -20.338 -41.043 1.00 41.26 ATOM 3548 CZ TYR B 614 45.554 -20.553 -42.376 1.00 41.18 ATOM 3549 OH TYR B 614 46.518 -19.784 -42.977 1.00 43.14 ATOM 3550 C TYR B 614 41.189 -21.822 -38.675 1.00 37.73 ATOM 3551 O TYR B 614 41.241 -20.691 -38.206 1.00 37.82 ATOM 3552 N PHE B 615 41.088 -22.915 -37.940 1.00 37.63 ATOM 3553 CA PHE B 615 41.043 -22.860 -36.498 1.00 38.17 ATOM 3554 CB PHE B 615 39.607 -23.005 -36.013 1.00 37.07 ATOM 3555 CG PHE B 615 38.963 -24.303 -36.405 1.00 37.31 ATOM 3556 CD1 PHE B 615 38.438 -24.480 -37.687 1.00 37.36 ATOM 3557 CD2 PHE B 615 38.845 -25.340 -35.484 1.00 37.41 ATOM 3558 CE1 PHE B 615 37.800 -25.670 -38.044 1.00 36.82 ATOM 3559 CE2 PHE B 615 38.211 -26.535 -35.829 1.00 37.62 ATOM 3560 CZ PHE B 615 37.686 -26.699 -37.112 1.00 37.41 ATOM 3561 C PHE B 615 41.895 -23.990 -35.942 1.00 39.47 ATOM 3562 O PHE B 615 42.154 -24.987 -36.622 1.00 39.40 ATOM 3563 N PHE B 616 42.334 -23.826 -34.704 1.00 40.25 ATOM 3564 CA PHE B 616 43.151 -24.826 -34.056 1.00 41.09 ATOM 3565 CB PHE B 616 44.607 -24.704 -34.522 1.00 40.36 ATOM 3566 CG PHE B 616 45.271 -23.405 -34.144 1.00 39.49 ATOM 3567 CD1 PHE B 616 45.305 -22.345 -35.037 1.00 39.10 ATOM 3568 CD2 PHE B 616 45.887 -23.251 -32.905 1.00 39.55 ATOM 3569 CE1 PHE B 616 45.942 -21.151 -34.710 1.00 38.68 ATOM 3570 CE2 PHE B 616 46.527 -22.059 -32.569 1.00 39.56 ATOM 3571 CZ PHE B 616 46.553 -21.008 -33.478 1.00 39.43 ATOM 3572 C PHE B 616 43.061 -24.613 -32.564 1.00 42.87 ATOM 3573 O PHE B 616 42.725 -23.522 -32.107 1.00 42.65 ATOM 3574 N TYR B 617 43.358 -25.656 -31.805 1.00 44.75 ATOM 3575 CA TYR B 617 43.320 -25.556 -30.361 1.00 46.98 ATOM 3576 CB TYR B 617 42.603 -26.769 -29.777 1.00 45.80 ATOM 3577 CG TYR B 617 41.158 -26.835 -30.193 1.00 44.97 ATOM 3578 CD1 TYR B 617 40.163 -26.258 -29.410 1.00 45.23 ATOM 3579 CE1 TYR B 617 38.833 -26.278 -29.811 1.00 44.83 ATOM 3580 CD2 TYR B 617 40.786 -27.437 -31.392 1.00 45.14 ATOM 3581 CE2 TYR B 617 39.459 -27.463 -31.804 1.00 44.58 ATOM 3582 CZ TYR B 617 38.489 -26.880 -31.009 1.00 44.77 ATOM 3583 OH TYR B 617 37.175 -26.899 -31.408 1.00 44.78 ATOM 3584 C TYR B 617 44.734 -25.446 -29.810 1.00 49.55 ATOM 3585 O TYR B 617 45.685 -25.982 -30.384 1.00 49.41 ATOM 3586 N SER B 618 44.864 -24.717 -28.707 1.00 52.52 ATOM 3587 CA SER B 618 46.145 -24.519 -28.051 1.00 55.71 ATOM 3588 CB SER B 618 46.712 -23.135 -28.383 1.00 55.34 ATOM 3589 OG SER B 618 45.861 -22.105 -27.913 1.00 54.95 ATOM 3590 C SER B 618 45.922 -24.647 -26.553 1.00 58.46 ATOM 3591 O SER B 618 44.925 -24.153 -26.013 1.00 58.65 ATOM 3592 N SER B 619 46.853 -25.321 -25.887 1.00 61.75 ATOM 3593 CA SER B 619 46.760 -25.538 -24.450 1.00 65.02 ATOM 3594 CB SER B 619 47.642 -26.720 -24.048 1.00 65.13 ATOM 3595 OG SER B 619 48.481 -27.102 -25.127 1.00 65.77 ATOM 3596 C SER B 619 47.169 -24.301 -23.665 1.00 67.06 ATOM 3597 O SER B 619 48.311 -23.843 -23.756 1.00 67.36 ATOM 3598 N GLY B 620 46.225 -23.754 -22.905 1.00 69.47 ATOM 3599 CA GLY B 620 46.519 -22.584 -22.100 1.00 72.26 ATOM 3600 C GLY B 620 47.488 -22.988 -21.006 1.00 74.06 ATOM 3601 O GLY B 620 47.119 -23.725 -20.086 1.00 74.48 ATOM 3602 N GLU B 621 48.729 -22.518 -21.110 1.00 75.50 ATOM 3603 CA GLU B 621 49.768 -22.840 -20.134 1.00 76.86 ATOM 3604 CB GLU B 621 51.078 -22.127 -20.503 1.00 77.43 ATOM 3605 CG GLU B 621 51.741 -22.645 -21.780 1.00 78.56 ATOM 3606 CD GLU B 621 51.928 -24.160 -21.785 1.00 79.35 ATOM 3607 OE1 GLU B 621 52.215 -24.739 -20.711 1.00 79.79 ATOM 3608 OE2 GLU B 621 51.789 -24.774 -22.867 1.00 79.59 ATOM 3609 C GLU B 621 49.358 -22.457 -18.713 1.00 77.24 ATOM 3610 O GLU B 621 50.156 -22.562 -17.781 1.00 77.50 ATOM 3611 N LYS B 622 48.110 -22.024 -18.555 1.00 77.64 ATOM 3612 CA LYS B 622 47.584 -21.613 -17.257 1.00 77.74 ATOM 3613 CB LYS B 622 46.555 -20.495 -17.443 1.00 77.74 ATOM 3614 CG LYS B 622 47.142 -19.202 -17.981 1.00 77.70 ATOM 3615 CD LYS B 622 46.062 -18.292 -18.535 1.00 77.52 ATOM 3616 CE LYS B 622 46.669 -17.187 -19.381 1.00 77.48 ATOM 3617 NZ LYS B 622 45.828 -15.963 -19.376 1.00 77.20 ATOM 3618 C LYS B 622 46.951 -22.752 -16.462 1.00 77.80 ATOM 3619 O LYS B 622 46.809 -22.652 -15.243 1.00 78.06 ATOM 3620 N LYS B 623 46.567 -23.827 -17.144 1.00 77.64 ATOM 3621 CA LYS B 623 45.949 -24.968 -16.473 1.00 77.46 ATOM 3622 CB LYS B 623 44.736 -24.504 -15.658 1.00 78.05 ATOM 3623 CG LYS B 623 44.509 -25.287 -14.375 1.00 78.91 ATOM 3624 CD LYS B 623 43.183 -24.918 -13.719 1.00 79.62 ATOM 3625 CE LYS B 623 42.626 -26.083 -12.904 1.00 80.05 ATOM 3626 NZ LYS B 623 41.349 -25.742 -12.211 1.00 80.41 ATOM 3627 C LYS B 623 45.505 -26.009 -17.492 1.00 77.02 ATOM 3628 O LYS B 623 46.093 -26.126 -18.569 1.00 77.27 ATOM 3629 N ASP B 624 44.471 -26.770 -17.139 1.00 76.15 ATOM 3630 CA ASP B 624 43.916 -27.787 -18.029 1.00 75.08 ATOM 3631 CB ASP B 624 43.249 -28.904 -17.212 1.00 75.93 ATOM 3632 CG ASP B 624 42.171 -28.384 -16.266 1.00 76.81 ATOM 3633 OD1 ASP B 624 41.330 -29.200 -15.822 1.00 77.19 ATOM 3634 OD2 ASP B 624 42.165 -27.166 -15.965 1.00 77.02 ATOM 3635 C ASP B 624 42.886 -27.109 -18.941 1.00 73.86 ATOM 3636 O ASP B 624 41.948 -27.742 -19.441 1.00 73.85 ATOM 3637 N GLU B 625 43.080 -25.809 -19.144 1.00 72.04 ATOM 3638 CA GLU B 625 42.204 -24.994 -19.976 1.00 70.10 ATOM 3639 CB GLU B 625 42.253 -23.544 -19.493 1.00 70.96 ATOM 3640 CG GLU B 625 43.659 -22.946 -19.510 1.00 72.02 ATOM 3641 CD GLU B 625 43.792 -21.731 -18.614 1.00 73.00 ATOM 3642 OE1 GLU B 625 43.478 -21.839 -17.410 1.00 73.95 ATOM 3643 OE2 GLU B 625 44.213 -20.665 -19.114 1.00 73.51 ATOM 3644 C GLU B 625 42.617 -25.054 -21.452 1.00 68.17 ATOM 3645 O GLU B 625 43.795 -24.892 -21.786 1.00 68.04 ATOM 3646 N VAL B 626 41.645 -25.286 -22.331 1.00 65.45 ATOM 3647 CA VAL B 626 41.917 -25.351 -23.765 1.00 62.42 ATOM 3648 CB VAL B 626 41.257 -26.575 -24.427 1.00 62.72 ATOM 3649 CG1 VAL B 626 41.980 -26.908 -25.720 1.00 62.56 ATOM 3650 CG2 VAL B 626 41.277 -27.762 -23.478 1.00 62.92 ATOM 3651 C VAL B 626 41.383 -24.108 -24.458 1.00 59.95 ATOM 3652 O VAL B 626 40.288 -23.634 -24.148 1.00 59.56 ATOM 3653 N TYR B 627 42.155 -23.592 -25.407 1.00 57.06 ATOM 3654 CA TYR B 627 41.752 -22.400 -26.134 1.00 54.40 ATOM 3655 CB TYR B 627 42.835 -21.326 -26.026 1.00 55.19 ATOM 3656 CG TYR B 627 42.910 -20.668 -24.669 1.00 56.83 ATOM 3657 CD1 TYR B 627 43.647 -21.245 -23.628 1.00 57.46 ATOM 3658 CE1 TYR B 627 43.722 -20.636 -22.371 1.00 57.93 ATOM 3659 CD2 TYR B 627 42.247 -19.468 -24.421 1.00 57.13 ATOM 3660 CE2 TYR B 627 42.314 -18.853 -23.173 1.00 57.88 ATOM 3661 CZ TYR B 627 43.052 -19.440 -22.152 1.00 58.22 ATOM 3662 OH TYR B 627 43.111 -18.825 -20.918 1.00 58.51 ATOM 3663 C TYR B 627 41.481 -22.675 -27.602 1.00 51.81 ATOM 3664 O TYR B 627 42.260 -23.360 -28.266 1.00 51.96 ATOM 3665 N LEU B 628 40.369 -22.147 -28.100 1.00 48.16 ATOM 3666 CA LEU B 628 40.027 -22.291 -29.505 1.00 44.73 ATOM 3667 CB LEU B 628 38.509 -22.368 -29.692 1.00 44.29 ATOM 3668 CG LEU B 628 37.997 -22.086 -31.108 1.00 43.71 ATOM 3669 CD1 LEU B 628 38.351 -23.246 -32.033 1.00 43.22 ATOM 3670 CD2 LEU B 628 36.496 -21.861 -31.069 1.00 43.53 ATOM 3671 C LEU B 628 40.583 -21.046 -30.192 1.00 42.73 ATOM 3672 O LEU B 628 40.370 -19.925 -29.727 1.00 42.19 ATOM 3673 N ASN B 629 41.315 -21.244 -31.282 1.00 40.44 ATOM 3674 CA ASN B 629 41.907 -20.141 -32.022 1.00 38.41 ATOM 3675 CB ASN B 629 43.415 -20.335 -32.150 1.00 38.35 ATOM 3676 CG ASN B 629 44.108 -20.407 -30.810 1.00 38.59 ATOM 3677 OD1 ASN B 629 44.714 -19.436 -30.361 1.00 38.40 ATOM 3678 ND2 ASN B 629 44.024 -21.563 -30.161 1.00 38.38 ATOM 3679 C ASN B 629 41.316 -20.031 -33.414 1.00 37.50 ATOM 3680 O ASN B 629 41.475 -20.933 -34.231 1.00 36.89 ATOM 3681 N LEU B 630 40.636 -18.923 -33.680 1.00 36.26 ATOM 3682 CA LEU B 630 40.041 -18.696 -34.985 1.00 35.28 ATOM 3683 CB LEU B 630 38.657 -18.060 -34.838 1.00 35.17 ATOM 3684 CG LEU B 630 37.620 -18.776 -33.967 1.00 34.97 ATOM 3685 CD1 LEU B 630 36.350 -17.950 -33.906 1.00 34.88 ATOM 3686 CD2 LEU B 630 37.319 -20.148 -34.537 1.00 35.00 ATOM 3687 C LEU B 630 40.958 -17.767 -35.770 1.00 34.95 ATOM 3688 O LEU B 630 41.225 -16.645 -35.340 1.00 34.56 ATOM 3689 N VAL B 631 41.453 -18.247 -36.910 1.00 34.22 ATOM 3690 CA VAL B 631 42.335 -17.456 -37.759 1.00 34.38 ATOM 3691 CB VAL B 631 43.422 -18.335 -38.408 1.00 33.97 ATOM 3692 CG1 VAL B 631 44.359 -17.478 -39.234 1.00 32.87 ATOM 3693 CG2 VAL B 631 44.191 -19.080 -37.330 1.00 33.64 ATOM 3694 C VAL B 631 41.501 -16.790 -38.851 1.00 34.80 ATOM 3695 O VAL B 631 40.965 -17.460 -39.742 1.00 34.76 ATOM 3696 N LEU B 632 41.401 -15.465 -38.777 1.00 34.79 ATOM 3697 CA LEU B 632 40.604 -14.701 -39.726 1.00 34.96 ATOM 3698 CB LEU B 632 39.584 -13.850 -38.977 1.00 34.07 ATOM 3699 CG LEU B 632 39.027 -14.474 -37.709 1.00 34.25 ATOM 3700 CD1 LEU B 632 38.498 -13.386 -36.802 1.00 34.13 ATOM 3701 CD2 LEU B 632 37.930 -15.453 -38.076 1.00 33.87 ATOM 3702 C LEU B 632 41.400 -13.781 -40.620 1.00 35.56 ATOM 3703 O LEU B 632 42.555 -13.456 -40.329 1.00 35.01 ATOM 3704 N ASP B 633 40.766 -13.367 -41.717 1.00 36.31 ATOM 3705 CA ASP B 633 41.397 -12.428 -42.631 1.00 36.67 ATOM 3706 CB ASP B 633 40.485 -12.120 -43.817 1.00 37.32 ATOM 3707 CG ASP B 633 40.640 -13.114 -44.942 1.00 38.65 ATOM 3708 OD1 ASP B 633 39.778 -13.131 -45.843 1.00 39.24 ATOM 3709 OD2 ASP B 633 41.623 -13.883 -44.930 1.00 40.30 ATOM 3710 C ASP B 633 41.553 -11.176 -41.781 1.00 36.64 ATOM 3711 O ASP B 633 40.696 -10.872 -40.952 1.00 36.24 ATOM 3712 N TYR B 634 42.648 -10.456 -41.968 1.00 36.96 ATOM 3713 CA TYR B 634 42.867 -9.248 -41.196 1.00 37.01 ATOM 3714 CB TYR B 634 44.362 -9.059 -40.940 1.00 38.39 ATOM 3715 CG TYR B 634 44.698 -7.715 -40.352 1.00 39.93 ATOM 3716 CD1 TYR B 634 45.110 -6.667 -41.170 1.00 40.18 ATOM 3717 CE1 TYR B 634 45.365 -5.408 -40.646 1.00 40.97 ATOM 3718 CD2 TYR B 634 44.557 -7.474 -38.987 1.00 40.17 ATOM 3719 CE2 TYR B 634 44.810 -6.217 -38.451 1.00 40.45 ATOM 3720 CZ TYR B 634 45.211 -5.189 -39.289 1.00 40.87 ATOM 3721 OH TYR B 634 45.432 -3.929 -38.781 1.00 41.95 ATOM 3722 C TYR B 634 42.300 -8.042 -41.943 1.00 36.08 ATOM 3723 O TYR B 634 42.481 -7.914 -43.152 1.00 36.11 ATOM 3724 N VAL B 635 41.587 -7.181 -41.223 1.00 34.89 ATOM 3725 CA VAL B 635 41.003 -5.968 -41.800 1.00 33.00 ATOM 3726 CB VAL B 635 39.477 -6.031 -41.818 1.00 32.50 ATOM 3727 CG1 VAL B 635 38.932 -4.917 -42.691 1.00 31.79 ATOM 3728 CG2 VAL B 635 39.028 -7.377 -42.349 1.00 32.45 ATOM 3729 C VAL B 635 41.485 -4.839 -40.896 1.00 32.57 ATOM 3730 O VAL B 635 41.283 -4.875 -39.688 1.00 31.87 ATOM 3731 N PRO B 636 42.106 -3.806 -41.484 1.00 32.50 ATOM 3732 CD PRO B 636 42.231 -3.679 -42.947 1.00 32.21 ATOM 3733 CA PRO B 636 42.672 -2.636 -40.797 1.00 32.11 ATOM 3734 CB PRO B 636 43.362 -1.870 -41.926 1.00 32.55 ATOM 3735 CG PRO B 636 42.569 -2.223 -43.133 1.00 32.74 ATOM 3736 C PRO B 636 41.812 -1.705 -39.948 1.00 31.83 ATOM 3737 O PRO B 636 42.286 -1.171 -38.938 1.00 32.39 ATOM 3738 N GLU B 637 40.563 -1.495 -40.338 1.00 30.61 ATOM 3739 CA GLU B 637 39.734 -0.567 -39.591 1.00 29.50 ATOM 3740 CB GLU B 637 39.501 0.686 -40.437 1.00 31.14 ATOM 3741 CG GLU B 637 40.702 1.578 -40.540 1.00 34.11 ATOM 3742 CD GLU B 637 40.906 2.406 -39.291 1.00 36.37 ATOM 3743 OE1 GLU B 637 41.859 3.208 -39.267 1.00 39.67 ATOM 3744 OE2 GLU B 637 40.117 2.259 -38.332 1.00 37.11 ATOM 3745 C GLU B 637 38.390 -1.097 -39.141 1.00 28.01 ATOM 3746 O GLU B 637 38.011 -2.232 -39.429 1.00 26.98 ATOM 3747 N THR B 638 37.680 -0.249 -38.411 1.00 26.38 ATOM 3748 CA THR B 638 36.350 -0.571 -37.957 1.00 25.66 ATOM 3749 CB THR B 638 36.310 -0.992 -36.463 1.00 25.91 ATOM 3750 OG1 THR B 638 36.642 0.127 -35.637 1.00 26.49 ATOM 3751 CG2 THR B 638 37.281 -2.130 -36.197 1.00 25.63 ATOM 3752 C THR B 638 35.539 0.699 -38.158 1.00 25.54 ATOM 3753 O THR B 638 36.075 1.813 -38.119 1.00 24.70 ATOM 3754 N VAL B 639 34.254 0.526 -38.415 1.00 24.95 ATOM 3755 CA VAL B 639 33.374 1.657 -38.600 1.00 25.13 ATOM 3756 CB VAL B 639 31.908 1.183 -38.781 1.00 24.75 ATOM 3757 CG1 VAL B 639 30.947 2.355 -38.661 1.00 22.95 ATOM 3758 CG2 VAL B 639 31.752 0.500 -40.143 1.00 24.16 ATOM 3759 C VAL B 639 33.494 2.522 -37.348 1.00 25.88 ATOM 3760 O VAL B 639 33.450 3.749 -37.421 1.00 26.05 ATOM 3761 N TYR B 640 33.662 1.874 -36.199 1.00 26.53 ATOM 3762 CA TYR B 640 33.779 2.595 -34.940 1.00 27.96 ATOM 3763 CB TYR B 640 33.973 1.614 -33.791 1.00 29.15 ATOM 3764 CG TYR B 640 34.210 2.295 -32.467 1.00 31.88 ATOM 3765 CD1 TYR B 640 35.503 2.483 -31.986 1.00 33.30 ATOM 3766 CE1 TYR B 640 35.732 3.129 -30.779 1.00 34.75 ATOM 3767 CD2 TYR B 640 33.144 2.770 -31.703 1.00 33.03 ATOM 3768 CE2 TYR B 640 33.357 3.415 -30.497 1.00 34.57 ATOM 3769 CZ TYR B 640 34.654 3.591 -30.040 1.00 35.32 ATOM 3770 OH TYR B 640 34.877 4.224 -28.841 1.00 37.22 ATOM 3771 C TYR B 640 34.925 3.608 -34.935 1.00 28.47 ATOM 3772 O TYR B 640 34.734 4.766 -34.576 1.00 27.82 ATOM 3773 N ARG B 641 36.113 3.167 -35.335 1.00 29.26 ATOM 3774 CA ARG B 641 37.284 4.040 -35.357 1.00 30.48 ATOM 3775 CB ARG B 641 38.550 3.222 -35.611 1.00 32.70 ATOM 3776 CG ARG B 641 39.033 2.466 -34.382 1.00 36.90 ATOM 3777 CD ARG B 641 40.222 1.576 -34.714 1.00 41.54 ATOM 3778 NE ARG B 641 41.221 2.281 -35.515 1.00 45.66 ATOM 3779 CZ ARG B 641 42.266 1.698 -36.098 1.00 48.10 ATOM 3780 NH1 ARG B 641 42.456 0.387 -35.971 1.00 49.35 ATOM 3781 NH2 ARG B 641 43.129 2.429 -36.802 1.00 49.56 ATOM 3782 C ARG B 641 37.167 5.146 -36.394 1.00 29.59 ATOM 3783 O ARG B 641 37.447 6.306 -36.108 1.00 28.87 ATOM 3784 N VAL B 642 36.745 4.786 -37.598 1.00 28.95 ATOM 3785 CA VAL B 642 36.589 5.768 -38.655 1.00 28.79 ATOM 3786 CB VAL B 642 36.135 5.096 -39.968 1.00 29.03 ATOM 3787 CG1 VAL B 642 35.681 6.148 -40.981 1.00 28.71 ATOM 3788 CG2 VAL B 642 37.278 4.255 -40.528 1.00 28.72 ATOM 3789 C VAL B 642 35.578 6.841 -38.265 1.00 29.30 ATOM 3790 O VAL B 642 35.850 8.028 -38.416 1.00 28.90 ATOM 3791 N ALA B 643 34.419 6.435 -37.759 1.00 29.33 ATOM 3792 CA ALA B 643 33.400 7.402 -37.375 1.00 30.84 ATOM 3793 CB ALA B 643 32.125 6.683 -36.912 1.00 30.29 ATOM 3794 C ALA B 643 33.911 8.330 -36.275 1.00 32.28 ATOM 3795 O ALA B 643 33.598 9.517 -36.263 1.00 32.20 ATOM 3796 N ARG B 644 34.692 7.780 -35.352 1.00 33.89 ATOM 3797 CA ARG B 644 35.246 8.552 -34.253 1.00 36.41 ATOM 3798 CB ARG B 644 35.899 7.610 -33.235 1.00 38.07 ATOM 3799 CG ARG B 644 36.336 8.283 -31.947 1.00 41.78 ATOM 3800 CD ARG B 644 37.243 7.371 -31.107 1.00 45.29 ATOM 3801 NE ARG B 644 38.196 6.617 -31.926 1.00 48.84 ATOM 3802 CZ ARG B 644 38.968 5.630 -31.472 1.00 50.16 ATOM 3803 NH1 ARG B 644 38.907 5.268 -30.195 1.00 51.12 ATOM 3804 NH2 ARG B 644 39.804 5.002 -32.295 1.00 51.10 ATOM 3805 C ARG B 644 36.264 9.580 -34.772 1.00 37.12 ATOM 3806 O ARG B 644 36.355 10.677 -34.240 1.00 37.01 ATOM 3807 N HIS B 645 37.019 9.222 -35.808 1.00 38.00 ATOM 3808 CA HIS B 645 38.000 10.138 -36.393 1.00 39.14 ATOM 3809 CB HIS B 645 38.741 9.476 -37.559 1.00 40.81 ATOM 3810 CG HIS B 645 39.840 8.548 -37.138 1.00 43.55 ATOM 3811 CD2 HIS B 645 40.676 8.578 -36.072 1.00 44.72 ATOM 3812 ND1 HIS B 645 40.185 7.426 -37.864 1.00 45.22 ATOM 3813 CE1 HIS B 645 41.186 6.804 -37.263 1.00 45.35 ATOM 3814 NE2 HIS B 645 41.503 7.483 -36.174 1.00 45.35 ATOM 3815 C HIS B 645 37.277 11.376 -36.912 1.00 38.61 ATOM 3816 O HIS B 645 37.689 12.503 -36.652 1.00 38.67 ATOM 3817 N TYR B 646 36.195 11.159 -37.649 1.00 38.12 ATOM 3818 CA TYR B 646 35.414 12.259 -38.198 1.00 37.86 ATOM 3819 CB TYR B 646 34.375 11.735 -39.184 1.00 35.43 ATOM 3820 CG TYR B 646 34.945 11.423 -40.538 1.00 32.88 ATOM 3821 CD1 TYR B 646 35.616 10.224 -40.766 1.00 31.61 ATOM 3822 CE1 TYR B 646 36.166 9.939 -42.003 1.00 30.17 ATOM 3823 CD2 TYR B 646 34.835 12.334 -41.590 1.00 31.50 ATOM 3824 CE2 TYR B 646 35.380 12.057 -42.832 1.00 30.20 ATOM 3825 CZ TYR B 646 36.044 10.858 -43.030 1.00 29.96 ATOM 3826 OH TYR B 646 36.590 10.573 -44.253 1.00 29.53 ATOM 3827 C TYR B 646 34.700 13.025 -37.103 1.00 39.17 ATOM 3828 O TYR B 646 34.538 14.234 -37.180 1.00 39.10 ATOM 3829 N SER B 647 34.265 12.311 -36.081 1.00 41.15 ATOM 3830 CA SER B 647 33.555 12.941 -34.989 1.00 43.87 ATOM 3831 CB SER B 647 33.015 11.873 -34.043 1.00 44.83 ATOM 3832 OG SER B 647 31.710 12.208 -33.613 1.00 47.61 ATOM 3833 C SER B 647 34.450 13.905 -34.223 1.00 45.54 ATOM 3834 O SER B 647 34.030 15.006 -33.859 1.00 45.56 ATOM 3835 N ARG B 648 35.685 13.486 -33.969 1.00 47.40 ATOM 3836 CA ARG B 648 36.630 14.327 -33.249 1.00 49.21 ATOM 3837 CB ARG B 648 37.953 13.588 -33.048 1.00 50.81 ATOM 3838 CG ARG B 648 37.903 12.482 -32.003 1.00 53.48 ATOM 3839 CD ARG B 648 39.287 11.874 -31.796 1.00 56.39 ATOM 3840 NE ARG B 648 39.247 10.647 -31.003 1.00 59.40 ATOM 3841 CZ ARG B 648 40.326 10.027 -30.525 1.00 61.03 ATOM 3842 NH1 ARG B 648 41.537 10.523 -30.763 1.00 61.83 ATOM 3843 NH2 ARG B 648 40.200 8.909 -29.811 1.00 61.21 ATOM 3844 C ARG B 648 36.860 15.603 -34.049 1.00 49.49 ATOM 3845 O ARG B 648 36.732 16.701 -33.522 1.00 50.09 ATOM 3846 N ALA B 649 37.183 15.450 -35.329 1.00 49.71 ATOM 3847 CA ALA B 649 37.421 16.589 -36.211 1.00 49.86 ATOM 3848 CB ALA B 649 38.036 16.111 -37.526 1.00 49.95 ATOM 3849 C ALA B 649 36.128 17.350 -36.486 1.00 49.96 ATOM 3850 O ALA B 649 36.082 18.221 -37.348 1.00 49.94 ATOM 3851 N LYS B 650 35.081 17.016 -35.744 1.00 50.53 ATOM 3852 CA LYS B 650 33.785 17.659 -35.910 1.00 51.05 ATOM 3853 CB LYS B 650 33.836 19.081 -35.355 1.00 52.99 ATOM 3854 CG LYS B 650 33.506 19.159 -33.875 1.00 54.80 ATOM 3855 CD LYS B 650 33.141 20.578 -33.470 1.00 56.96 ATOM 3856 CE LYS B 650 33.162 20.742 -31.951 1.00 58.61 ATOM 3857 NZ LYS B 650 32.588 22.056 -31.508 1.00 59.24 ATOM 3858 C LYS B 650 33.322 17.678 -37.369 1.00 50.48 ATOM 3859 O LYS B 650 32.653 18.613 -37.812 1.00 50.41 ATOM 3860 N GLN B 651 33.687 16.636 -38.107 1.00 49.63 ATOM 3861 CA GLN B 651 33.298 16.496 -39.505 1.00 48.28 ATOM 3862 CB GLN B 651 34.516 16.238 -40.388 1.00 49.29 ATOM 3863 CG GLN B 651 35.749 17.014 -39.997 1.00 51.57 ATOM 3864 CD GLN B 651 36.884 16.820 -40.980 1.00 53.21 ATOM 3865 OE1 GLN B 651 36.739 16.119 -41.986 1.00 54.33 ATOM 3866 NE2 GLN B 651 38.024 17.441 -40.696 1.00 54.13 ATOM 3867 C GLN B 651 32.365 15.300 -39.605 1.00 46.85 ATOM 3868 O GLN B 651 32.130 14.597 -38.622 1.00 46.61 ATOM 3869 N THR B 652 31.840 15.069 -40.801 1.00 45.14 ATOM 3870 CA THR B 652 30.950 13.941 -41.030 1.00 42.53 ATOM 3871 CB THR B 652 29.496 14.429 -41.281 1.00 42.93 ATOM 3872 OG1 THR B 652 28.630 13.819 -40.316 1.00 44.06 ATOM 3873 CG2 THR B 652 29.022 14.085 -42.696 1.00 43.44 ATOM 3874 C THR B 652 31.464 13.112 -42.211 1.00 39.82 ATOM 3875 O THR B 652 32.039 13.643 -43.163 1.00 38.88 ATOM 3876 N LEU B 653 31.277 11.801 -42.124 1.00 37.42 ATOM 3877 CA LEU B 653 31.714 10.898 -43.181 1.00 34.68 ATOM 3878 CB LEU B 653 31.466 9.453 -42.736 1.00 34.26 ATOM 3879 CG LEU B 653 31.956 8.283 -43.585 1.00 33.49 ATOM 3880 CD1 LEU B 653 33.476 8.236 -43.605 1.00 32.96 ATOM 3881 CD2 LEU B 653 31.377 6.990 -43.005 1.00 33.56 ATOM 3882 C LEU B 653 30.917 11.204 -44.449 1.00 32.83 ATOM 3883 O LEU B 653 29.697 11.330 -44.390 1.00 32.85 ATOM 3884 N PRO B 654 31.595 11.365 -45.601 1.00 31.41 ATOM 3885 CD PRO B 654 33.054 11.300 -45.812 1.00 31.10 ATOM 3886 CA PRO B 654 30.867 11.651 -46.845 1.00 30.55 ATOM 3887 CB PRO B 654 31.943 11.572 -47.936 1.00 29.92 ATOM 3888 CG PRO B 654 33.228 11.777 -47.230 1.00 29.89 ATOM 3889 C PRO B 654 29.781 10.592 -47.040 1.00 30.50 ATOM 3890 O PRO B 654 30.020 9.399 -46.839 1.00 30.17 ATOM 3891 N VAL B 655 28.593 11.032 -47.431 1.00 29.75 ATOM 3892 CA VAL B 655 27.470 10.134 -47.621 1.00 29.32 ATOM 3893 CB VAL B 655 26.238 10.918 -48.129 1.00 29.75 ATOM 3894 CG1 VAL B 655 25.032 9.994 -48.246 1.00 30.60 ATOM 3895 CG2 VAL B 655 25.933 12.064 -47.160 1.00 29.98 ATOM 3896 C VAL B 655 27.742 8.946 -48.542 1.00 28.83 ATOM 3897 O VAL B 655 27.149 7.892 -48.362 1.00 28.92 ATOM 3898 N ILE B 656 28.636 9.097 -49.516 1.00 28.07 ATOM 3899 CA ILE B 656 28.925 7.993 -50.424 1.00 27.08 ATOM 3900 CB ILE B 656 29.944 8.404 -51.520 1.00 27.70 ATOM 3901 CG2 ILE B 656 31.242 8.855 -50.889 1.00 28.19 ATOM 3902 CG1 ILE B 656 30.194 7.236 -52.477 1.00 27.25 ATOM 3903 CD1 ILE B 656 28.944 6.752 -53.205 1.00 28.28 ATOM 3904 C ILE B 656 29.454 6.797 -49.645 1.00 26.08 ATOM 3905 O ILE B 656 29.129 5.655 -49.962 1.00 25.77 ATOM 3906 N TYR B 657 30.258 7.062 -48.617 1.00 24.97 ATOM 3907 CA TYR B 657 30.804 6.004 -47.779 1.00 24.88 ATOM 3908 CB TYR B 657 31.949 6.544 -46.918 1.00 26.15 ATOM 3909 CG TYR B 657 33.203 6.765 -47.725 1.00 29.36 ATOM 3910 CD1 TYR B 657 33.743 8.048 -47.887 1.00 30.81 ATOM 3911 CE1 TYR B 657 34.878 8.259 -48.690 1.00 32.30 ATOM 3912 CD2 TYR B 657 33.821 5.699 -48.378 1.00 30.28 ATOM 3913 CE2 TYR B 657 34.942 5.894 -49.174 1.00 32.16 ATOM 3914 CZ TYR B 657 35.467 7.173 -49.326 1.00 33.07 ATOM 3915 OH TYR B 657 36.598 7.341 -50.098 1.00 36.17 ATOM 3916 C TYR B 657 29.693 5.437 -46.900 1.00 24.02 ATOM 3917 O TYR B 657 29.618 4.232 -46.686 1.00 22.70 ATOM 3918 N VAL B 658 28.829 6.314 -46.394 1.00 22.66 ATOM 3919 CA VAL B 658 27.721 5.870 -45.567 1.00 22.05 ATOM 3920 CB VAL B 658 26.840 7.071 -45.129 1.00 22.45 ATOM 3921 CG1 VAL B 658 25.568 6.576 -44.413 1.00 21.16 ATOM 3922 CG2 VAL B 658 27.647 8.000 -44.215 1.00 21.34 ATOM 3923 C VAL B 658 26.885 4.874 -46.396 1.00 22.05 ATOM 3924 O VAL B 658 26.469 3.822 -45.899 1.00 20.20 ATOM 3925 N LYS B 659 26.658 5.210 -47.665 1.00 20.95 ATOM 3926 CA LYS B 659 25.889 4.356 -48.565 1.00 21.27 ATOM 3927 CB LYS B 659 25.716 5.036 -49.930 1.00 20.82 ATOM 3928 CG LYS B 659 24.526 5.968 -50.012 1.00 22.16 ATOM 3929 CD LYS B 659 24.475 6.674 -51.352 1.00 22.30 ATOM 3930 CE LYS B 659 23.720 7.982 -51.236 1.00 23.46 ATOM 3931 NZ LYS B 659 23.523 8.603 -52.571 1.00 24.08 ATOM 3932 C LYS B 659 26.591 3.015 -48.770 1.00 21.59 ATOM 3933 O LYS B 659 25.988 1.955 -48.620 1.00 21.28 ATOM 3934 N LEU B 660 27.870 3.074 -49.117 1.00 21.64 ATOM 3935 CA LEU B 660 28.643 1.867 -49.359 1.00 21.72 ATOM 3936 CB LEU B 660 30.072 2.223 -49.799 1.00 21.61 ATOM 3937 CG LEU B 660 30.267 2.551 -51.282 1.00 22.33 ATOM 3938 CD1 LEU B 660 31.593 3.299 -51.460 1.00 23.25 ATOM 3939 CD2 LEU B 660 30.239 1.283 -52.116 1.00 20.97 ATOM 3940 C LEU B 660 28.710 0.954 -48.145 1.00 21.17 ATOM 3941 O LEU B 660 28.524 -0.252 -48.270 1.00 20.59 ATOM 3942 N TYR B 661 28.992 1.524 -46.976 1.00 20.96 ATOM 3943 CA TYR B 661 29.102 0.725 -45.764 1.00 20.34 ATOM 3944 CB TYR B 661 29.658 1.571 -44.615 1.00 22.36 ATOM 3945 CG TYR B 661 31.055 2.112 -44.850 1.00 24.29 ATOM 3946 CD1 TYR B 661 31.889 1.559 -45.818 1.00 25.89 ATOM 3947 CE1 TYR B 661 33.175 2.058 -46.031 1.00 27.67 ATOM 3948 CD2 TYR B 661 31.541 3.182 -44.099 1.00 25.89 ATOM 3949 CE2 TYR B 661 32.824 3.688 -44.303 1.00 26.33 ATOM 3950 CZ TYR B 661 33.632 3.122 -45.266 1.00 27.43 ATOM 3951 OH TYR B 661 34.911 3.596 -45.454 1.00 30.03 ATOM 3952 C TYR B 661 27.781 0.101 -45.337 1.00 19.76 ATOM 3953 O TYR B 661 27.720 -1.094 -45.052 1.00 19.09 ATOM 3954 N MET B 662 26.727 0.906 -45.287 1.00 18.55 ATOM 3955 CA MET B 662 25.425 0.405 -44.866 1.00 18.98 ATOM 3956 CB MET B 662 24.423 1.562 -44.737 1.00 19.22 ATOM 3957 CG MET B 662 24.700 2.500 -43.550 1.00 20.79 ATOM 3958 SD MET B 662 24.886 1.624 -41.972 1.00 22.93 ATOM 3959 CE MET B 662 23.245 0.871 -41.841 1.00 23.41 ATOM 3960 C MET B 662 24.898 -0.648 -45.834 1.00 18.51 ATOM 3961 O MET B 662 24.333 -1.658 -45.412 1.00 18.24 ATOM 3962 N TYR B 663 25.087 -0.413 -47.127 1.00 18.53 ATOM 3963 CA TYR B 663 24.628 -1.359 -48.143 1.00 18.65 ATOM 3964 CB TYR B 663 24.997 -0.865 -49.547 1.00 18.87 ATOM 3965 CG TYR B 663 24.633 -1.836 -50.659 1.00 18.92 ATOM 3966 CD1 TYR B 663 25.552 -2.793 -51.112 1.00 18.74 ATOM 3967 CE1 TYR B 663 25.228 -3.678 -52.135 1.00 18.50 ATOM 3968 CD2 TYR B 663 23.376 -1.793 -51.259 1.00 18.37 ATOM 3969 CE2 TYR B 663 23.037 -2.674 -52.287 1.00 19.71 ATOM 3970 CZ TYR B 663 23.966 -3.612 -52.720 1.00 20.14 ATOM 3971 OH TYR B 663 23.629 -4.469 -53.751 1.00 19.74 ATOM 3972 C TYR B 663 25.291 -2.710 -47.908 1.00 18.75 ATOM 3973 O TYR B 663 24.632 -3.747 -47.889 1.00 18.45 ATOM 3974 N GLN B 664 26.607 -2.688 -47.743 1.00 18.73 ATOM 3975 CA GLN B 664 27.351 -3.911 -47.508 1.00 18.63 ATOM 3976 CB GLN B 664 28.849 -3.602 -47.478 1.00 19.22 ATOM 3977 CG GLN B 664 29.433 -3.391 -48.877 1.00 19.50 ATOM 3978 CD GLN B 664 30.825 -2.793 -48.849 1.00 19.80 ATOM 3979 OE1 GLN B 664 30.994 -1.576 -48.737 1.00 20.21 ATOM 3980 NE2 GLN B 664 31.826 -3.641 -48.946 1.00 18.84 ATOM 3981 C GLN B 664 26.903 -4.575 -46.205 1.00 19.15 ATOM 3982 O GLN B 664 26.849 -5.813 -46.113 1.00 18.36 ATOM 3983 N LEU B 665 26.573 -3.771 -45.196 1.00 17.50 ATOM 3984 CA LEU B 665 26.117 -4.350 -43.931 1.00 18.21 ATOM 3985 CB LEU B 665 25.950 -3.264 -42.859 1.00 16.71 ATOM 3986 CG LEU B 665 25.138 -3.638 -41.609 1.00 17.59 ATOM 3987 CD1 LEU B 665 25.685 -4.903 -40.956 1.00 15.85 ATOM 3988 CD2 LEU B 665 25.172 -2.474 -40.634 1.00 16.75 ATOM 3989 C LEU B 665 24.782 -5.085 -44.155 1.00 18.02 ATOM 3990 O LEU B 665 24.573 -6.217 -43.678 1.00 18.20 ATOM 3991 N PHE B 666 23.881 -4.454 -44.890 1.00 17.93 ATOM 3992 CA PHE B 666 22.601 -5.083 -45.157 1.00 19.63 ATOM 3993 CB PHE B 666 21.668 -4.092 -45.832 1.00 19.47 ATOM 3994 CG PHE B 666 21.055 -3.121 -44.868 1.00 20.77 ATOM 3995 CD1 PHE B 666 21.160 -1.750 -45.073 1.00 20.36 ATOM 3996 CD2 PHE B 666 20.394 -3.581 -43.730 1.00 19.89 ATOM 3997 CE1 PHE B 666 20.615 -0.852 -44.162 1.00 20.15 ATOM 3998 CE2 PHE B 666 19.848 -2.690 -42.816 1.00 20.51 ATOM 3999 CZ PHE B 666 19.960 -1.321 -43.035 1.00 20.36 ATOM 4000 C PHE B 666 22.735 -6.362 -45.979 1.00 20.03 ATOM 4001 O PHE B 666 21.944 -7.294 -45.814 1.00 20.63 ATOM 4002 N ARG B 667 23.740 -6.419 -46.849 1.00 19.86 ATOM 4003 CA ARG B 667 23.958 -7.621 -47.645 1.00 20.48 ATOM 4004 CB ARG B 667 25.033 -7.390 -48.702 1.00 20.87 ATOM 4005 CG ARG B 667 24.514 -6.863 -50.031 1.00 22.70 ATOM 4006 CD ARG B 667 25.534 -7.092 -51.142 1.00 24.19 ATOM 4007 NE ARG B 667 25.595 -8.493 -51.560 1.00 24.57 ATOM 4008 CZ ARG B 667 26.468 -8.968 -52.442 1.00 25.72 ATOM 4009 NH1 ARG B 667 27.357 -8.157 -53.003 1.00 25.01 ATOM 4010 NH2 ARG B 667 26.444 -10.252 -52.779 1.00 25.24 ATOM 4011 C ARG B 667 24.394 -8.762 -46.730 1.00 20.50 ATOM 4012 O ARG B 667 23.906 -9.887 -46.857 1.00 21.25 ATOM 4013 N SER B 668 25.322 -8.484 -45.818 1.00 19.37 ATOM 4014 CA SER B 668 25.786 -9.512 -44.899 1.00 18.89 ATOM 4015 CB SER B 668 26.926 -8.970 -44.028 1.00 18.99 ATOM 4016 OG SER B 668 26.454 -8.038 -43.073 1.00 19.56 ATOM 4017 C SER B 668 24.615 -9.999 -44.034 1.00 18.67 ATOM 4018 O SER B 668 24.485 -11.196 -43.764 1.00 18.88 ATOM 4019 N LEU B 669 23.748 -9.079 -43.625 1.00 17.80 ATOM 4020 CA LEU B 669 22.594 -9.444 -42.816 1.00 18.75 ATOM 4021 CB LEU B 669 21.902 -8.199 -42.268 1.00 17.10 ATOM 4022 CG LEU B 669 22.652 -7.433 -41.162 1.00 17.98 ATOM 4023 CD1 LEU B 669 21.727 -6.319 -40.620 1.00 16.12 ATOM 4024 CD2 LEU B 669 23.118 -8.389 -40.053 1.00 15.57 ATOM 4025 C LEU B 669 21.592 -10.281 -43.620 1.00 19.98 ATOM 4026 O LEU B 669 21.040 -11.246 -43.107 1.00 19.99 ATOM 4027 N ALA B 670 21.348 -9.910 -44.871 1.00 20.70 ATOM 4028 CA ALA B 670 20.425 -10.674 -45.695 1.00 21.14 ATOM 4029 CB ALA B 670 20.312 -10.040 -47.078 1.00 20.47 ATOM 4030 C ALA B 670 20.946 -12.114 -45.805 1.00 21.74 ATOM 4031 O ALA B 670 20.171 -13.076 -45.806 1.00 22.14 ATOM 4032 N TYR B 671 22.265 -12.254 -45.866 1.00 21.88 ATOM 4033 CA TYR B 671 22.892 -13.563 -45.985 1.00 23.18 ATOM 4034 CB TYR B 671 24.364 -13.412 -46.360 1.00 23.97 ATOM 4035 CG TYR B 671 25.121 -14.721 -46.447 1.00 25.51 ATOM 4036 CD1 TYR B 671 26.073 -15.058 -45.483 1.00 25.63 ATOM 4037 CE1 TYR B 671 26.815 -16.237 -45.577 1.00 26.37 ATOM 4038 CD2 TYR B 671 24.922 -15.608 -47.517 1.00 25.92 ATOM 4039 CE2 TYR B 671 25.664 -16.796 -47.617 1.00 25.76 ATOM 4040 CZ TYR B 671 26.607 -17.097 -46.644 1.00 26.85 ATOM 4041 OH TYR B 671 27.363 -18.246 -46.726 1.00 28.07 ATOM 4042 C TYR B 671 22.781 -14.439 -44.743 1.00 24.16 ATOM 4043 O TYR B 671 22.319 -15.576 -44.843 1.00 24.12 ATOM 4044 N ILE B 672 23.210 -13.944 -43.579 1.00 23.43 ATOM 4045 CA ILE B 672 23.115 -14.775 -42.380 1.00 23.07 ATOM 4046 CB ILE B 672 23.875 -14.159 -41.156 1.00 23.05 ATOM 4047 CG2 ILE B 672 25.372 -14.114 -41.448 1.00 22.02 ATOM 4048 CG1 ILE B 672 23.336 -12.763 -40.815 1.00 21.63 ATOM 4049 CD1 ILE B 672 23.866 -12.221 -39.471 1.00 22.05 ATOM 4050 C ILE B 672 21.654 -15.041 -42.012 1.00 23.27 ATOM 4051 O ILE B 672 21.305 -16.134 -41.575 1.00 24.27 ATOM 4052 N HIS B 673 20.787 -14.061 -42.225 1.00 23.08 ATOM 4053 CA HIS B 673 19.386 -14.246 -41.901 1.00 23.68 ATOM 4054 CB HIS B 673 18.627 -12.935 -42.083 1.00 23.23 ATOM 4055 CG HIS B 673 18.902 -11.925 -41.010 1.00 23.12 ATOM 4056 CD2 HIS B 673 19.787 -11.932 -39.984 1.00 22.04 ATOM 4057 ND1 HIS B 673 18.224 -10.728 -40.920 1.00 23.23 ATOM 4058 CE1 HIS B 673 18.679 -10.043 -39.886 1.00 21.81 ATOM 4059 NE2 HIS B 673 19.627 -10.750 -39.302 1.00 21.40 ATOM 4060 C HIS B 673 18.741 -15.342 -42.754 1.00 25.54 ATOM 4061 O HIS B 673 17.823 -16.028 -42.297 1.00 25.72 ATOM 4062 N SER B 674 19.220 -15.500 -43.989 1.00 26.39 ATOM 4063 CA SER B 674 18.686 -16.508 -44.903 1.00 27.11 ATOM 4064 CB SER B 674 19.347 -16.386 -46.281 1.00 25.23 ATOM 4065 OG SER B 674 20.612 -17.017 -46.289 1.00 24.45 ATOM 4066 C SER B 674 18.917 -17.905 -44.337 1.00 28.30 ATOM 4067 O SER B 674 18.322 -18.873 -44.802 1.00 28.64 ATOM 4068 N PHE B 675 19.788 -17.996 -43.336 1.00 29.23 ATOM 4069 CA PHE B 675 20.089 -19.257 -42.665 1.00 29.36 ATOM 4070 CB PHE B 675 21.589 -19.386 -42.410 1.00 30.68 ATOM 4071 CG PHE B 675 22.386 -19.662 -43.638 1.00 32.37 ATOM 4072 CD1 PHE B 675 22.300 -20.899 -44.271 1.00 33.08 ATOM 4073 CD2 PHE B 675 23.216 -18.684 -44.177 1.00 33.25 ATOM 4074 CE1 PHE B 675 23.025 -21.160 -45.425 1.00 33.66 ATOM 4075 CE2 PHE B 675 23.950 -18.931 -45.332 1.00 33.95 ATOM 4076 CZ PHE B 675 23.854 -20.175 -45.959 1.00 34.19 ATOM 4077 C PHE B 675 19.381 -19.285 -41.317 1.00 28.94 ATOM 4078 O PHE B 675 19.542 -20.230 -40.548 1.00 29.39 ATOM 4079 N GLY B 676 18.616 -18.236 -41.028 1.00 28.42 ATOM 4080 CA GLY B 676 17.921 -18.150 -39.751 1.00 27.91 ATOM 4081 C GLY B 676 18.822 -17.652 -38.622 1.00 27.29 ATOM 4082 O GLY B 676 18.396 -17.558 -37.468 1.00 27.28 ATOM 4083 N ILE B 677 20.066 -17.320 -38.954 1.00 25.81 ATOM 4084 CA ILE B 677 21.033 -16.843 -37.969 1.00 25.03 ATOM 4085 CB ILE B 677 22.480 -17.184 -38.421 1.00 25.49 ATOM 4086 CG2 ILE B 677 23.508 -16.547 -37.491 1.00 24.89 ATOM 4087 CG1 ILE B 677 22.666 -18.703 -38.428 1.00 25.30 ATOM 4088 CD1 ILE B 677 23.835 -19.173 -39.250 1.00 25.77 ATOM 4089 C ILE B 677 20.923 -15.333 -37.711 1.00 24.66 ATOM 4090 O ILE B 677 20.904 -14.526 -38.646 1.00 23.33 ATOM 4091 N CYS B 678 20.824 -14.973 -36.431 1.00 23.26 ATOM 4092 CA CYS B 678 20.742 -13.576 -36.007 1.00 22.45 ATOM 4093 CB CYS B 678 19.600 -13.385 -34.998 1.00 21.46 ATOM 4094 SG CYS B 678 19.283 -11.653 -34.508 1.00 22.46 ATOM 4095 C CYS B 678 22.091 -13.257 -35.351 1.00 21.82 ATOM 4096 O CYS B 678 22.575 -14.026 -34.513 1.00 21.76 ATOM 4097 N HIS B 679 22.709 -12.143 -35.747 1.00 20.73 ATOM 4098 CA HIS B 679 24.008 -11.762 -35.190 1.00 19.20 ATOM 4099 CB HIS B 679 24.598 -10.597 -35.994 1.00 18.33 ATOM 4100 CG HIS B 679 25.937 -10.141 -35.503 1.00 18.72 ATOM 4101 CD2 HIS B 679 26.283 -9.349 -34.461 1.00 18.05 ATOM 4102 ND1 HIS B 679 27.117 -10.493 -36.123 1.00 19.00 ATOM 4103 CE1 HIS B 679 28.130 -9.937 -35.487 1.00 17.93 ATOM 4104 NE2 HIS B 679 27.652 -9.237 -34.475 1.00 19.43 ATOM 4105 C HIS B 679 23.860 -11.381 -33.707 1.00 19.14 ATOM 4106 O HIS B 679 24.670 -11.788 -32.870 1.00 19.02 ATOM 4107 N ARG B 680 22.811 -10.616 -33.403 1.00 19.08 ATOM 4108 CA ARG B 680 22.500 -10.166 -32.041 1.00 20.24 ATOM 4109 CB ARG B 680 22.318 -11.375 -31.103 1.00 18.60 ATOM 4110 CG ARG B 680 21.280 -12.385 -31.623 1.00 18.99 ATOM 4111 CD ARG B 680 20.675 -13.212 -30.508 1.00 17.55 ATOM 4112 NE ARG B 680 21.682 -14.028 -29.837 1.00 18.19 ATOM 4113 CZ ARG B 680 21.430 -14.836 -28.812 1.00 17.96 ATOM 4114 NH1 ARG B 680 20.199 -14.942 -28.331 1.00 18.65 ATOM 4115 NH2 ARG B 680 22.410 -15.529 -28.263 1.00 18.55 ATOM 4116 C ARG B 680 23.473 -9.170 -31.396 1.00 20.70 ATOM 4117 O ARG B 680 23.323 -8.832 -30.218 1.00 21.75 ATOM 4118 N ASP B 681 24.457 -8.693 -32.148 1.00 21.28 ATOM 4119 CA ASP B 681 25.406 -7.719 -31.602 1.00 21.34 ATOM 4120 CB ASP B 681 26.578 -8.439 -30.925 1.00 23.18 ATOM 4121 CG ASP B 681 27.403 -7.511 -30.022 1.00 25.68 ATOM 4122 OD1 ASP B 681 26.896 -6.436 -29.603 1.00 25.67 ATOM 4123 OD2 ASP B 681 28.567 -7.866 -29.732 1.00 26.38 ATOM 4124 C ASP B 681 25.932 -6.761 -32.677 1.00 20.75 ATOM 4125 O ASP B 681 27.129 -6.480 -32.742 1.00 20.48 ATOM 4126 N ILE B 682 25.034 -6.266 -33.524 1.00 19.54 ATOM 4127 CA ILE B 682 25.437 -5.337 -34.567 1.00 19.34 ATOM 4128 CB ILE B 682 24.314 -5.129 -35.616 1.00 18.66 ATOM 4129 CG2 ILE B 682 24.714 -4.041 -36.604 1.00 16.33 ATOM 4130 CG1 ILE B 682 24.010 -6.450 -36.340 1.00 16.92 ATOM 4131 CD1 ILE B 682 25.217 -7.098 -36.986 1.00 16.55 ATOM 4132 C ILE B 682 25.752 -3.989 -33.913 1.00 19.87 ATOM 4133 O ILE B 682 24.918 -3.423 -33.208 1.00 19.92 ATOM 4134 N LYS B 683 26.968 -3.502 -34.135 1.00 19.99 ATOM 4135 CA LYS B 683 27.424 -2.217 -33.606 1.00 20.50 ATOM 4136 CB LYS B 683 27.754 -2.328 -32.115 1.00 20.51 ATOM 4137 CG LYS B 683 28.887 -3.281 -31.797 1.00 21.36 ATOM 4138 CD LYS B 683 29.100 -3.357 -30.306 1.00 23.46 ATOM 4139 CE LYS B 683 30.202 -4.323 -29.962 1.00 24.36 ATOM 4140 NZ LYS B 683 30.166 -4.603 -28.493 1.00 27.47 ATOM 4141 C LYS B 683 28.668 -1.834 -34.397 1.00 20.51 ATOM 4142 O LYS B 683 29.306 -2.698 -35.007 1.00 20.44 ATOM 4143 N PRO B 684 29.035 -0.541 -34.397 1.00 20.30 ATOM 4144 CD PRO B 684 28.339 0.552 -33.689 1.00 19.81 ATOM 4145 CA PRO B 684 30.209 -0.047 -35.131 1.00 21.13 ATOM 4146 CB PRO B 684 30.303 1.429 -34.715 1.00 20.17 ATOM 4147 CG PRO B 684 28.926 1.783 -34.313 1.00 19.69 ATOM 4148 C PRO B 684 31.520 -0.798 -34.909 1.00 20.97 ATOM 4149 O PRO B 684 32.321 -0.925 -35.823 1.00 20.31 ATOM 4150 N GLN B 685 31.743 -1.306 -33.706 1.00 22.29 ATOM 4151 CA GLN B 685 32.979 -2.033 -33.427 1.00 24.11 ATOM 4152 CB GLN B 685 33.178 -2.149 -31.915 1.00 27.57 ATOM 4153 CG GLN B 685 33.824 -0.922 -31.297 1.00 32.85 ATOM 4154 CD GLN B 685 33.165 -0.537 -29.995 1.00 36.90 ATOM 4155 OE1 GLN B 685 31.929 -0.535 -29.885 1.00 39.58 ATOM 4156 NE2 GLN B 685 33.982 -0.211 -28.991 1.00 38.40 ATOM 4157 C GLN B 685 33.053 -3.431 -34.052 1.00 23.08 ATOM 4158 O GLN B 685 34.129 -4.028 -34.124 1.00 22.16 ATOM 4159 N ASN B 686 31.909 -3.953 -34.487 1.00 22.31 ATOM 4160 CA ASN B 686 31.854 -5.283 -35.094 1.00 21.91 ATOM 4161 CB ASN B 686 30.660 -6.067 -34.531 1.00 21.40 ATOM 4162 CG ASN B 686 30.934 -6.609 -33.145 1.00 22.18 ATOM 4163 OD1 ASN B 686 32.091 -6.805 -32.774 1.00 24.43 ATOM 4164 ND2 ASN B 686 29.882 -6.848 -32.369 1.00 20.88 ATOM 4165 C ASN B 686 31.750 -5.183 -36.616 1.00 21.32 ATOM 4166 O ASN B 686 31.408 -6.151 -37.288 1.00 21.56 ATOM 4167 N LEU B 687 32.046 -4.000 -37.144 1.00 20.51 ATOM 4168 CA LEU B 687 32.001 -3.756 -38.575 1.00 20.21 ATOM 4169 CB LEU B 687 30.990 -2.641 -38.887 1.00 18.52 ATOM 4170 CG LEU B 687 29.580 -2.853 -38.312 1.00 18.87 ATOM 4171 CD1 LEU B 687 28.683 -1.646 -38.593 1.00 17.90 ATOM 4172 CD2 LEU B 687 28.974 -4.108 -38.924 1.00 18.16 ATOM 4173 C LEU B 687 33.403 -3.356 -39.038 1.00 21.43 ATOM 4174 O LEU B 687 33.817 -2.207 -38.869 1.00 20.68 ATOM 4175 N LEU B 688 34.134 -4.320 -39.600 1.00 21.80 ATOM 4176 CA LEU B 688 35.487 -4.083 -40.087 1.00 23.41 ATOM 4177 CB LEU B 688 36.242 -5.407 -40.207 1.00 22.90 ATOM 4178 CG LEU B 688 36.134 -6.295 -38.969 1.00 23.78 ATOM 4179 CD1 LEU B 688 36.785 -7.650 -39.224 1.00 22.67 ATOM 4180 CD2 LEU B 688 36.783 -5.577 -37.796 1.00 22.86 ATOM 4181 C LEU B 688 35.471 -3.379 -41.435 1.00 24.49 ATOM 4182 O LEU B 688 34.578 -3.598 -42.246 1.00 24.34 ATOM 4183 N LEU B 689 36.475 -2.542 -41.674 1.00 25.80 ATOM 4184 CA LEU B 689 36.558 -1.785 -42.917 1.00 27.87 ATOM 4185 CB LEU B 689 36.156 -0.325 -42.679 1.00 28.15 ATOM 4186 CG LEU B 689 34.728 0.090 -42.366 1.00 28.86 ATOM 4187 CD1 LEU B 689 34.719 1.567 -41.948 1.00 27.99 ATOM 4188 CD2 LEU B 689 33.860 -0.141 -43.589 1.00 29.70 ATOM 4189 C LEU B 689 37.946 -1.744 -43.522 1.00 29.20 ATOM 4190 O LEU B 689 38.944 -1.671 -42.811 1.00 28.51 ATOM 4191 N ASP B 690 37.997 -1.783 -44.845 1.00 32.01 ATOM 4192 CA ASP B 690 39.255 -1.628 -45.556 1.00 35.53 ATOM 4193 CB ASP B 690 39.446 -2.695 -46.622 1.00 37.27 ATOM 4194 CG ASP B 690 40.846 -2.680 -47.192 1.00 39.50 ATOM 4195 OD1 ASP B 690 41.216 -1.670 -47.827 1.00 41.07 ATOM 4196 OD2 ASP B 690 41.579 -3.670 -46.997 1.00 41.36 ATOM 4197 C ASP B 690 39.024 -0.268 -46.206 1.00 36.78 ATOM 4198 O ASP B 690 38.263 -0.146 -47.161 1.00 36.55 ATOM 4199 N PRO B 691 39.680 0.777 -45.686 1.00 39.13 ATOM 4200 CD PRO B 691 40.666 0.692 -44.595 1.00 39.95 ATOM 4201 CA PRO B 691 39.542 2.149 -46.198 1.00 40.17 ATOM 4202 CB PRO B 691 40.575 2.940 -45.393 1.00 40.50 ATOM 4203 CG PRO B 691 40.818 2.118 -44.168 1.00 40.56 ATOM 4204 C PRO B 691 39.746 2.328 -47.702 1.00 40.84 ATOM 4205 O PRO B 691 38.934 2.967 -48.371 1.00 41.50 ATOM 4206 N ASP B 692 40.826 1.761 -48.225 1.00 41.07 ATOM 4207 CA ASP B 692 41.145 1.884 -49.640 1.00 41.41 ATOM 4208 CB ASP B 692 42.527 1.286 -49.912 1.00 43.78 ATOM 4209 CG ASP B 692 43.634 2.008 -49.149 1.00 45.89 ATOM 4210 OD1 ASP B 692 44.691 1.385 -48.901 1.00 47.02 ATOM 4211 OD2 ASP B 692 43.444 3.198 -48.797 1.00 46.96 ATOM 4212 C ASP B 692 40.121 1.266 -50.583 1.00 40.36 ATOM 4213 O ASP B 692 39.774 1.869 -51.600 1.00 41.25 ATOM 4214 N THR B 693 39.638 0.070 -50.256 1.00 38.24 ATOM 4215 CA THR B 693 38.662 -0.596 -51.109 1.00 35.18 ATOM 4216 CB THR B 693 38.824 -2.133 -51.068 1.00 35.46 ATOM 4217 OG1 THR B 693 38.739 -2.593 -49.715 1.00 34.67 ATOM 4218 CG2 THR B 693 40.168 -2.537 -51.647 1.00 35.94 ATOM 4219 C THR B 693 37.236 -0.262 -50.708 1.00 33.49 ATOM 4220 O THR B 693 36.306 -0.507 -51.469 1.00 33.40 ATOM 4221 N ALA B 694 37.071 0.303 -49.516 1.00 31.20 ATOM 4222 CA ALA B 694 35.749 0.651 -48.998 1.00 29.59 ATOM 4223 CB ALA B 694 35.012 1.576 -49.974 1.00 29.39 ATOM 4224 C ALA B 694 34.918 -0.605 -48.741 1.00 28.04 ATOM 4225 O ALA B 694 33.694 -0.554 -48.738 1.00 28.53 ATOM 4226 N VAL B 695 35.590 -1.733 -48.541 1.00 26.98 ATOM 4227 CA VAL B 695 34.907 -2.997 -48.272 1.00 25.46 ATOM 4228 CB VAL B 695 35.784 -4.219 -48.642 1.00 25.39 ATOM 4229 CG1 VAL B 695 35.156 -5.496 -48.092 1.00 26.18 ATOM 4230 CG2 VAL B 695 35.919 -4.329 -50.149 1.00 25.98 ATOM 4231 C VAL B 695 34.595 -3.087 -46.785 1.00 24.56 ATOM 4232 O VAL B 695 35.420 -2.731 -45.939 1.00 25.09 ATOM 4233 N LEU B 696 33.395 -3.548 -46.467 1.00 23.60 ATOM 4234 CA LEU B 696 33.017 -3.703 -45.075 1.00 22.26 ATOM 4235 CB LEU B 696 31.741 -2.909 -44.772 1.00 20.79 ATOM 4236 CG LEU B 696 31.115 -3.138 -43.394 1.00 21.00 ATOM 4237 CD1 LEU B 696 30.386 -1.880 -42.946 1.00 19.46 ATOM 4238 CD2 LEU B 696 30.157 -4.333 -43.458 1.00 19.25 ATOM 4239 C LEU B 696 32.795 -5.194 -44.833 1.00 22.46 ATOM 4240 O LEU B 696 32.230 -5.894 -45.675 1.00 23.07 ATOM 4241 N LYS B 697 33.256 -5.683 -43.692 1.00 22.20 ATOM 4242 CA LYS B 697 33.079 -7.089 -43.352 1.00 22.14 ATOM 4243 CB LYS B 697 34.406 -7.851 -43.468 1.00 23.21 ATOM 4244 CG LYS B 697 34.804 -8.187 -44.899 1.00 24.94 ATOM 4245 CD LYS B 697 36.221 -8.730 -44.942 1.00 27.27 ATOM 4246 CE LYS B 697 36.767 -8.766 -46.367 1.00 27.84 ATOM 4247 NZ LYS B 697 35.780 -9.344 -47.327 1.00 30.38 ATOM 4248 C LYS B 697 32.551 -7.209 -41.929 1.00 21.50 ATOM 4249 O LYS B 697 33.154 -6.709 -40.979 1.00 21.02 ATOM 4250 N LEU B 698 31.408 -7.870 -41.797 1.00 21.42 ATOM 4251 CA LEU B 698 30.785 -8.103 -40.502 1.00 20.48 ATOM 4252 CB LEU B 698 29.377 -8.676 -40.709 1.00 19.29 ATOM 4253 CG LEU B 698 28.553 -9.046 -39.475 1.00 19.12 ATOM 4254 CD1 LEU B 698 28.343 -7.815 -38.600 1.00 19.11 ATOM 4255 CD2 LEU B 698 27.221 -9.625 -39.922 1.00 18.46 ATOM 4256 C LEU B 698 31.666 -9.107 -39.754 1.00 20.95 ATOM 4257 O LEU B 698 32.191 -10.044 -40.363 1.00 20.38 ATOM 4258 N CYS B 699 31.852 -8.896 -38.453 1.00 20.61 ATOM 4259 CA CYS B 699 32.660 -9.802 -37.651 1.00 21.89 ATOM 4260 CB CYS B 699 34.078 -9.250 -37.458 1.00 22.16 ATOM 4261 SG CYS B 699 34.293 -7.985 -36.173 1.00 25.30 ATOM 4262 C CYS B 699 32.008 -10.058 -36.301 1.00 22.19 ATOM 4263 O CYS B 699 30.931 -9.549 -36.022 1.00 22.21 ATOM 4264 N ASP B 700 32.662 -10.874 -35.484 1.00 23.27 ATOM 4265 CA ASP B 700 32.189 -11.217 -34.144 1.00 23.82 ATOM 4266 CB ASP B 700 32.073 -9.967 -33.281 1.00 25.55 ATOM 4267 CG ASP B 700 31.905 -10.297 -31.815 1.00 28.71 ATOM 4268 OD1 ASP B 700 31.814 -11.500 -31.487 1.00 30.06 ATOM 4269 OD2 ASP B 700 31.863 -9.359 -30.991 1.00 29.98 ATOM 4270 C ASP B 700 30.868 -11.968 -34.079 1.00 24.12 ATOM 4271 O ASP B 700 29.816 -11.372 -33.840 1.00 24.33 ATOM 4272 N PHE B 701 30.919 -13.283 -34.262 1.00 23.43 ATOM 4273 CA PHE B 701 29.700 -14.068 -34.198 1.00 23.27 ATOM 4274 CB PHE B 701 29.670 -15.065 -35.353 1.00 22.84 ATOM 4275 CG PHE B 701 29.470 -14.406 -36.682 1.00 23.31 ATOM 4276 CD1 PHE B 701 30.540 -13.807 -37.340 1.00 24.07 ATOM 4277 CD2 PHE B 701 28.202 -14.293 -37.232 1.00 22.70 ATOM 4278 CE1 PHE B 701 30.343 -13.095 -38.527 1.00 23.53 ATOM 4279 CE2 PHE B 701 27.999 -13.587 -38.414 1.00 22.44 ATOM 4280 CZ PHE B 701 29.071 -12.986 -39.058 1.00 22.57 ATOM 4281 C PHE B 701 29.575 -14.755 -32.852 1.00 23.44 ATOM 4282 O PHE B 701 28.944 -15.803 -32.738 1.00 24.17 ATOM 4283 N GLY B 702 30.166 -14.134 -31.833 1.00 23.15 ATOM 4284 CA GLY B 702 30.132 -14.675 -30.487 1.00 22.61 ATOM 4285 C GLY B 702 28.782 -14.622 -29.800 1.00 23.28 ATOM 4286 O GLY B 702 28.606 -15.268 -28.773 1.00 23.33 ATOM 4287 N SER B 703 27.837 -13.852 -30.343 1.00 23.13 ATOM 4288 CA SER B 703 26.483 -13.737 -29.775 1.00 23.29 ATOM 4289 CB SER B 703 26.127 -12.269 -29.522 1.00 23.44 ATOM 4290 OG SER B 703 26.896 -11.705 -28.481 1.00 25.75 ATOM 4291 C SER B 703 25.453 -14.293 -30.752 1.00 23.42 ATOM 4292 O SER B 703 24.261 -14.387 -30.435 1.00 22.97 ATOM 4293 N ALA B 704 25.919 -14.640 -31.945 1.00 23.88 ATOM 4294 CA ALA B 704 25.046 -15.134 -32.995 1.00 25.70 ATOM 4295 CB ALA B 704 25.846 -15.328 -34.283 1.00 24.78 ATOM 4296 C ALA B 704 24.346 -16.425 -32.604 1.00 26.70 ATOM 4297 O ALA B 704 24.900 -17.254 -31.887 1.00 26.34 ATOM 4298 N LYS B 705 23.118 -16.581 -33.078 1.00 28.20 ATOM 4299 CA LYS B 705 22.347 -17.772 -32.781 1.00 29.70 ATOM 4300 CB LYS B 705 21.769 -17.675 -31.373 1.00 30.38 ATOM 4301 CG LYS B 705 21.114 -18.948 -30.874 1.00 31.98 ATOM 4302 CD LYS B 705 20.650 -18.755 -29.445 1.00 33.93 ATOM 4303 CE LYS B 705 20.001 -20.005 -28.883 1.00 34.90 ATOM 4304 NZ LYS B 705 18.590 -20.082 -29.329 1.00 36.87 ATOM 4305 C LYS B 705 21.217 -17.945 -33.775 1.00 30.63 ATOM 4306 O LYS B 705 20.615 -16.971 -34.226 1.00 29.60 ATOM 4307 N GLN B 706 20.934 -19.196 -34.120 1.00 32.46 ATOM 4308 CA GLN B 706 19.849 -19.490 -35.035 1.00 34.41 ATOM 4309 CB GLN B 706 19.981 -20.909 -35.570 1.00 36.36 ATOM 4310 CG GLN B 706 18.668 -21.478 -36.068 1.00 39.84 ATOM 4311 CD GLN B 706 18.866 -22.496 -37.160 1.00 41.13 ATOM 4312 OE1 GLN B 706 19.761 -23.334 -37.080 1.00 42.09 ATOM 4313 NE2 GLN B 706 18.032 -22.428 -38.194 1.00 42.17 ATOM 4314 C GLN B 706 18.549 -19.351 -34.247 1.00 34.71 ATOM 4315 O GLN B 706 18.320 -20.071 -33.278 1.00 35.89 ATOM 4316 N LEU B 707 17.699 -18.423 -34.657 1.00 34.62 ATOM 4317 CA LEU B 707 16.449 -18.201 -33.960 1.00 35.43 ATOM 4318 CB LEU B 707 16.034 -16.736 -34.082 1.00 34.22 ATOM 4319 CG LEU B 707 17.033 -15.661 -33.622 1.00 33.44 ATOM 4320 CD1 LEU B 707 16.308 -14.326 -33.583 1.00 32.88 ATOM 4321 CD2 LEU B 707 17.626 -15.994 -32.257 1.00 32.21 ATOM 4322 C LEU B 707 15.344 -19.089 -34.502 1.00 36.96 ATOM 4323 O LEU B 707 14.965 -18.974 -35.672 1.00 37.65 ATOM 4324 N VAL B 708 14.831 -19.971 -33.648 1.00 37.94 ATOM 4325 CA VAL B 708 13.750 -20.877 -34.028 1.00 38.63 ATOM 4326 CB VAL B 708 14.027 -22.319 -33.562 1.00 38.59 ATOM 4327 CG1 VAL B 708 12.943 -23.247 -34.088 1.00 37.98 ATOM 4328 CG2 VAL B 708 15.391 -22.769 -34.036 1.00 37.52 ATOM 4329 C VAL B 708 12.444 -20.428 -33.392 1.00 39.67 ATOM 4330 O VAL B 708 12.338 -20.363 -32.172 1.00 39.51 ATOM 4331 N ARG B 709 11.452 -20.119 -34.219 1.00 41.28 ATOM 4332 CA ARG B 709 10.151 -19.686 -33.721 1.00 43.17 ATOM 4333 CB ARG B 709 9.140 -19.662 -34.874 1.00 45.23 ATOM 4334 CG ARG B 709 7.823 -18.968 -34.558 1.00 48.95 ATOM 4335 CD ARG B 709 6.891 -18.963 -35.771 1.00 52.69 ATOM 4336 NE ARG B 709 6.673 -20.307 -36.314 1.00 56.43 ATOM 4337 CZ ARG B 709 5.803 -20.601 -37.281 1.00 57.76 ATOM 4338 NH1 ARG B 709 5.059 -19.642 -37.822 1.00 58.09 ATOM 4339 NH2 ARG B 709 5.673 -21.855 -37.704 1.00 58.72 ATOM 4340 C ARG B 709 9.693 -20.650 -32.624 1.00 43.23 ATOM 4341 O ARG B 709 9.908 -21.862 -32.717 1.00 43.35 ATOM 4342 N GLY B 710 9.081 -20.115 -31.575 1.00 43.12 ATOM 4343 CA GLY B 710 8.625 -20.962 -30.489 1.00 42.81 ATOM 4344 C GLY B 710 9.698 -21.216 -29.445 1.00 42.83 ATOM 4345 O GLY B 710 9.412 -21.690 -28.343 1.00 43.38 ATOM 4346 N GLU B 711 10.944 -20.920 -29.785 1.00 42.16 ATOM 4347 CA GLU B 711 12.031 -21.114 -28.837 1.00 41.32 ATOM 4348 CB GLU B 711 13.264 -21.642 -29.544 1.00 43.00 ATOM 4349 CG GLU B 711 13.283 -23.123 -29.766 1.00 46.10 ATOM 4350 CD GLU B 711 14.494 -23.531 -30.579 1.00 47.99 ATOM 4351 OE1 GLU B 711 15.544 -22.854 -30.452 1.00 48.75 ATOM 4352 OE2 GLU B 711 14.394 -24.516 -31.346 1.00 49.38 ATOM 4353 C GLU B 711 12.372 -19.775 -28.195 1.00 39.79 ATOM 4354 O GLU B 711 12.510 -18.763 -28.885 1.00 39.42 ATOM 4355 N PRO B 712 12.507 -19.752 -26.862 1.00 38.04 ATOM 4356 CD PRO B 712 12.339 -20.882 -25.931 1.00 37.34 ATOM 4357 CA PRO B 712 12.837 -18.506 -26.165 1.00 36.35 ATOM 4358 CB PRO B 712 12.403 -18.782 -24.730 1.00 36.71 ATOM 4359 CG PRO B 712 12.593 -20.266 -24.575 1.00 37.36 ATOM 4360 C PRO B 712 14.323 -18.172 -26.260 1.00 34.47 ATOM 4361 O PRO B 712 15.167 -19.063 -26.320 1.00 33.78 ATOM 4362 N ASN B 713 14.642 -16.884 -26.279 1.00 32.77 ATOM 4363 CA ASN B 713 16.034 -16.468 -26.349 1.00 31.28 ATOM 4364 CB ASN B 713 16.377 -16.043 -27.773 1.00 31.10 ATOM 4365 CG ASN B 713 16.451 -17.220 -28.717 1.00 30.93 ATOM 4366 OD1 ASN B 713 17.344 -18.062 -28.611 1.00 31.18 ATOM 4367 ND2 ASN B 713 15.506 -17.292 -29.643 1.00 30.98 ATOM 4368 C ASN B 713 16.280 -15.330 -25.366 1.00 30.18 ATOM 4369 O ASN B 713 15.383 -14.537 -25.089 1.00 29.71 ATOM 4370 N VAL B 714 17.498 -15.254 -24.840 1.00 29.27 ATOM 4371 CA VAL B 714 17.826 -14.223 -23.864 1.00 28.90 ATOM 4372 CB VAL B 714 19.216 -14.455 -23.266 1.00 27.90 ATOM 4373 CG1 VAL B 714 19.237 -15.818 -22.625 1.00 27.11 ATOM 4374 CG2 VAL B 714 20.292 -14.345 -24.329 1.00 27.61 ATOM 4375 C VAL B 714 17.723 -12.816 -24.419 1.00 28.58 ATOM 4376 O VAL B 714 17.983 -12.574 -25.598 1.00 27.76 ATOM 4377 N SER B 715 17.321 -11.884 -23.568 1.00 28.21 ATOM 4378 CA SER B 715 17.181 -10.525 -24.030 1.00 28.44 ATOM 4379 CB SER B 715 15.809 -9.981 -23.647 1.00 29.46 ATOM 4380 OG SER B 715 15.668 -9.954 -22.247 1.00 31.25 ATOM 4381 C SER B 715 18.279 -9.608 -23.528 1.00 27.61 ATOM 4382 O SER B 715 18.198 -8.399 -23.713 1.00 28.48 ATOM 4383 N TYR B 716 19.315 -10.168 -22.908 1.00 27.07 ATOM 4384 CA TYR B 716 20.411 -9.330 -22.430 1.00 26.67 ATOM 4385 CB TYR B 716 20.876 -9.748 -21.030 1.00 27.44 ATOM 4386 CG TYR B 716 21.178 -11.219 -20.861 1.00 28.96 ATOM 4387 CD1 TYR B 716 22.407 -11.757 -21.246 1.00 29.23 ATOM 4388 CE1 TYR B 716 22.689 -13.105 -21.052 1.00 29.47 ATOM 4389 CD2 TYR B 716 20.247 -12.067 -20.284 1.00 29.81 ATOM 4390 CE2 TYR B 716 20.518 -13.410 -20.086 1.00 30.20 ATOM 4391 CZ TYR B 716 21.734 -13.925 -20.467 1.00 30.79 ATOM 4392 OH TYR B 716 21.975 -15.263 -20.235 1.00 33.04 ATOM 4393 C TYR B 716 21.604 -9.305 -23.387 1.00 26.50 ATOM 4394 O TYR B 716 22.723 -8.970 -22.986 1.00 26.61 ATOM 4395 N ILE B 717 21.365 -9.672 -24.648 1.00 25.62 ATOM 4396 CA ILE B 717 22.406 -9.633 -25.673 1.00 24.54 ATOM 4397 CB ILE B 717 22.209 -10.731 -26.775 1.00 24.09 ATOM 4398 CG2 ILE B 717 22.895 -12.038 -26.346 1.00 23.25 ATOM 4399 CG1 ILE B 717 20.722 -10.976 -27.037 1.00 23.51 ATOM 4400 CD1 ILE B 717 20.026 -9.863 -27.797 1.00 21.34 ATOM 4401 C ILE B 717 22.307 -8.254 -26.336 1.00 24.42 ATOM 4402 O ILE B 717 21.351 -7.518 -26.095 1.00 23.24 ATOM 4403 N CYS B 718 23.289 -7.917 -27.168 1.00 25.08 ATOM 4404 CA CYS B 718 23.317 -6.637 -27.879 1.00 26.02 ATOM 4405 CB CYS B 718 21.951 -6.311 -28.472 1.00 26.04 ATOM 4406 SG CYS B 718 22.079 -5.189 -29.869 1.00 26.97 ATOM 4407 C CYS B 718 23.780 -5.460 -27.026 1.00 26.85 ATOM 4408 O CYS B 718 23.403 -5.326 -25.864 1.00 27.81 ATOM 4409 N SER B 719 24.578 -4.586 -27.622 1.00 27.30 ATOM 4410 CA SER B 719 25.118 -3.449 -26.899 1.00 27.74 ATOM 4411 CB SER B 719 26.428 -3.034 -27.543 1.00 27.84 ATOM 4412 OG SER B 719 27.302 -4.148 -27.528 1.00 31.61 ATOM 4413 C SER B 719 24.217 -2.241 -26.746 1.00 27.69 ATOM 4414 O SER B 719 23.501 -1.867 -27.667 1.00 26.12 ATOM 4415 N ARG B 720 24.266 -1.640 -25.561 1.00 29.07 ATOM 4416 CA ARG B 720 23.483 -0.450 -25.252 1.00 31.87 ATOM 4417 CB ARG B 720 23.907 0.121 -23.890 1.00 35.54 ATOM 4418 CG ARG B 720 25.331 0.681 -23.844 1.00 40.12 ATOM 4419 CD ARG B 720 25.521 1.622 -22.651 1.00 45.48 ATOM 4420 NE ARG B 720 26.611 2.572 -22.882 1.00 49.66 ATOM 4421 CZ ARG B 720 26.758 3.723 -22.226 1.00 51.69 ATOM 4422 NH1 ARG B 720 27.784 4.522 -22.509 1.00 52.13 ATOM 4423 NH2 ARG B 720 25.888 4.070 -21.277 1.00 52.53 ATOM 4424 C ARG B 720 23.689 0.595 -26.350 1.00 30.61 ATOM 4425 O ARG B 720 24.809 0.810 -26.815 1.00 31.86 ATOM 4426 N TYR B 721 22.592 1.227 -26.745 1.00 29.68 ATOM 4427 CA TYR B 721 22.520 2.237 -27.807 1.00 28.59 ATOM 4428 CB TYR B 721 23.884 2.840 -28.179 1.00 30.92 ATOM 4429 CG TYR B 721 24.532 3.740 -27.159 1.00 33.52 ATOM 4430 CD1 TYR B 721 24.142 3.718 -25.818 1.00 35.01 ATOM 4431 CE1 TYR B 721 24.820 4.476 -24.863 1.00 37.00 ATOM 4432 CD2 TYR B 721 25.610 4.550 -27.521 1.00 34.75 ATOM 4433 CE2 TYR B 721 26.292 5.309 -26.578 1.00 35.90 ATOM 4434 CZ TYR B 721 25.895 5.263 -25.255 1.00 37.14 ATOM 4435 OH TYR B 721 26.592 5.982 -24.314 1.00 39.86 ATOM 4436 C TYR B 721 21.967 1.591 -29.072 1.00 26.54 ATOM 4437 O TYR B 721 21.227 2.226 -29.814 1.00 25.45 ATOM 4438 N TYR B 722 22.340 0.330 -29.313 1.00 24.35 ATOM 4439 CA TYR B 722 21.914 -0.387 -30.519 1.00 23.47 ATOM 4440 CB TYR B 722 23.144 -1.022 -31.198 1.00 22.11 ATOM 4441 CG TYR B 722 24.270 -0.020 -31.387 1.00 21.84 ATOM 4442 CD1 TYR B 722 24.247 0.897 -32.448 1.00 21.02 ATOM 4443 CE1 TYR B 722 25.203 1.908 -32.558 1.00 20.73 ATOM 4444 CD2 TYR B 722 25.294 0.092 -30.441 1.00 21.14 ATOM 4445 CE2 TYR B 722 26.262 1.104 -30.539 1.00 22.17 ATOM 4446 CZ TYR B 722 26.206 2.012 -31.598 1.00 21.85 ATOM 4447 OH TYR B 722 27.139 3.030 -31.675 1.00 21.51 ATOM 4448 C TYR B 722 20.828 -1.441 -30.285 1.00 23.06 ATOM 4449 O TYR B 722 20.448 -2.157 -31.200 1.00 22.37 ATOM 4450 N ARG B 723 20.317 -1.508 -29.061 1.00 23.05 ATOM 4451 CA ARG B 723 19.280 -2.463 -28.689 1.00 23.55 ATOM 4452 CB ARG B 723 19.231 -2.595 -27.166 1.00 25.64 ATOM 4453 CG ARG B 723 20.246 -3.553 -26.610 1.00 28.77 ATOM 4454 CD ARG B 723 20.557 -3.252 -25.158 1.00 31.52 ATOM 4455 NE ARG B 723 19.506 -3.687 -24.242 1.00 34.84 ATOM 4456 CZ ARG B 723 19.161 -4.955 -24.025 1.00 35.97 ATOM 4457 NH1 ARG B 723 19.781 -5.941 -24.660 1.00 36.16 ATOM 4458 NH2 ARG B 723 18.205 -5.238 -23.148 1.00 35.88 ATOM 4459 C ARG B 723 17.883 -2.108 -29.183 1.00 22.52 ATOM 4460 O ARG B 723 17.410 -0.988 -28.988 1.00 22.23 ATOM 4461 N ALA B 724 17.225 -3.071 -29.821 1.00 22.58 ATOM 4462 CA ALA B 724 15.856 -2.881 -30.295 1.00 22.09 ATOM 4463 CB ALA B 724 15.392 -4.112 -31.095 1.00 21.85 ATOM 4464 C ALA B 724 14.979 -2.702 -29.049 1.00 22.22 ATOM 4465 O ALA B 724 15.280 -3.250 -27.991 1.00 21.60 ATOM 4466 N PRO B 725 13.882 -1.934 -29.165 1.00 23.21 ATOM 4467 CD PRO B 725 13.461 -1.238 -30.392 1.00 23.61 ATOM 4468 CA PRO B 725 12.975 -1.694 -28.034 1.00 23.54 ATOM 4469 CB PRO B 725 11.893 -0.777 -28.610 1.00 23.86 ATOM 4470 CG PRO B 725 12.059 -0.828 -30.100 1.00 24.17 ATOM 4471 C PRO B 725 12.389 -2.952 -27.406 1.00 24.63 ATOM 4472 O PRO B 725 12.155 -2.985 -26.198 1.00 25.35 ATOM 4473 N GLU B 726 12.150 -3.988 -28.208 1.00 24.59 ATOM 4474 CA GLU B 726 11.603 -5.235 -27.668 1.00 24.44 ATOM 4475 CB GLU B 726 11.171 -6.188 -28.798 1.00 23.26 ATOM 4476 CG GLU B 726 12.296 -6.625 -29.736 1.00 23.97 ATOM 4477 CD GLU B 726 12.367 -5.789 -31.003 1.00 23.61 ATOM 4478 OE1 GLU B 726 12.056 -4.580 -30.948 1.00 23.51 ATOM 4479 OE2 GLU B 726 12.737 -6.342 -32.062 1.00 24.65 ATOM 4480 C GLU B 726 12.642 -5.907 -26.765 1.00 24.63 ATOM 4481 O GLU B 726 12.293 -6.655 -25.848 1.00 25.27 ATOM 4482 N LEU B 727 13.923 -5.640 -27.011 1.00 23.86 ATOM 4483 CA LEU B 727 14.977 -6.211 -26.164 1.00 23.45 ATOM 4484 CB LEU B 727 16.349 -6.082 -26.845 1.00 22.29 ATOM 4485 CG LEU B 727 16.632 -7.019 -28.026 1.00 21.33 ATOM 4486 CD1 LEU B 727 18.094 -6.908 -28.417 1.00 19.79 ATOM 4487 CD2 LEU B 727 16.287 -8.461 -27.638 1.00 19.95 ATOM 4488 C LEU B 727 14.986 -5.442 -24.831 1.00 23.63 ATOM 4489 O LEU B 727 15.097 -6.028 -23.749 1.00 23.10 ATOM 4490 N ILE B 728 14.858 -4.120 -24.928 1.00 23.54 ATOM 4491 CA ILE B 728 14.837 -3.250 -23.754 1.00 23.81 ATOM 4492 CB ILE B 728 14.732 -1.756 -24.176 1.00 22.62 ATOM 4493 CG2 ILE B 728 14.616 -0.852 -22.942 1.00 22.23 ATOM 4494 CG1 ILE B 728 15.963 -1.363 -25.000 1.00 21.67 ATOM 4495 CD1 ILE B 728 15.907 0.067 -25.561 1.00 21.57 ATOM 4496 C ILE B 728 13.643 -3.641 -22.886 1.00 24.97 ATOM 4497 O ILE B 728 13.732 -3.654 -21.664 1.00 24.51 ATOM 4498 N PHE B 729 12.530 -3.977 -23.531 1.00 26.73 ATOM 4499 CA PHE B 729 11.322 -4.380 -22.825 1.00 28.25 ATOM 4500 CB PHE B 729 10.096 -4.236 -23.728 1.00 28.78 ATOM 4501 CG PHE B 729 9.600 -2.824 -23.862 1.00 29.84 ATOM 4502 CD1 PHE B 729 9.364 -2.272 -25.116 1.00 30.45 ATOM 4503 CD2 PHE B 729 9.349 -2.049 -22.736 1.00 30.67 ATOM 4504 CE1 PHE B 729 8.882 -0.963 -25.252 1.00 30.62 ATOM 4505 CE2 PHE B 729 8.866 -0.741 -22.861 1.00 31.03 ATOM 4506 CZ PHE B 729 8.633 -0.201 -24.125 1.00 30.76 ATOM 4507 C PHE B 729 11.417 -5.821 -22.340 1.00 29.35 ATOM 4508 O PHE B 729 10.465 -6.342 -21.780 1.00 30.82 ATOM 4509 N GLY B 730 12.554 -6.468 -22.575 1.00 30.08 ATOM 4510 CA GLY B 730 12.742 -7.839 -22.118 1.00 30.35 ATOM 4511 C GLY B 730 12.063 -8.980 -22.869 1.00 31.21 ATOM 4512 O GLY B 730 11.788 -10.023 -22.276 1.00 31.29 ATOM 4513 N ALA B 731 11.792 -8.814 -24.162 1.00 30.99 ATOM 4514 CA ALA B 731 11.156 -9.886 -24.928 1.00 30.51 ATOM 4515 CB ALA B 731 10.666 -9.360 -26.288 1.00 30.56 ATOM 4516 C ALA B 731 12.141 -11.027 -25.140 1.00 30.32 ATOM 4517 O ALA B 731 13.347 -10.797 -25.283 1.00 30.39 ATOM 4518 N THR B 732 11.628 -12.256 -25.143 1.00 29.89 ATOM 4519 CA THR B 732 12.457 -13.439 -25.375 1.00 30.50 ATOM 4520 CB THR B 732 12.401 -14.426 -24.189 1.00 30.90 ATOM 4521 OG1 THR B 732 11.054 -14.876 -24.004 1.00 30.97 ATOM 4522 CG2 THR B 732 12.894 -13.745 -22.910 1.00 30.77 ATOM 4523 C THR B 732 11.982 -14.161 -26.641 1.00 30.06 ATOM 4524 O THR B 732 12.501 -15.216 -27.001 1.00 30.00 ATOM 4525 N ASP B 733 10.997 -13.570 -27.309 1.00 30.06 ATOM 4526 CA ASP B 733 10.438 -14.123 -28.539 1.00 30.53 ATOM 4527 CB ASP B 733 8.919 -14.235 -28.412 1.00 32.31 ATOM 4528 CG ASP B 733 8.248 -12.877 -28.347 1.00 34.54 ATOM 4529 OD1 ASP B 733 8.889 -11.920 -27.857 1.00 36.22 ATOM 4530 OD2 ASP B 733 7.085 -12.757 -28.784 1.00 36.13 ATOM 4531 C ASP B 733 10.769 -13.211 -29.730 1.00 29.28 ATOM 4532 O ASP B 733 10.016 -13.141 -30.697 1.00 29.26 ATOM 4533 N TYR B 734 11.888 -12.504 -29.652 1.00 27.50 ATOM 4534 CA TYR B 734 12.268 -11.606 -30.731 1.00 25.65 ATOM 4535 CB TYR B 734 13.357 -10.633 -30.251 1.00 23.36 ATOM 4536 CG TYR B 734 14.573 -11.309 -29.643 1.00 21.83 ATOM 4537 CD1 TYR B 734 15.642 -11.717 -30.438 1.00 20.47 ATOM 4538 CE1 TYR B 734 16.777 -12.319 -29.869 1.00 21.05 ATOM 4539 CD2 TYR B 734 14.661 -11.521 -28.266 1.00 21.58 ATOM 4540 CE2 TYR B 734 15.786 -12.119 -27.694 1.00 20.26 ATOM 4541 CZ TYR B 734 16.839 -12.513 -28.494 1.00 20.19 ATOM 4542 OH TYR B 734 17.962 -13.082 -27.924 1.00 21.04 ATOM 4543 C TYR B 734 12.762 -12.385 -31.951 1.00 25.35 ATOM 4544 O TYR B 734 13.073 -13.572 -31.860 1.00 24.73 ATOM 4545 N THR B 735 12.841 -11.686 -33.082 1.00 26.01 ATOM 4546 CA THR B 735 13.288 -12.248 -34.352 1.00 25.56 ATOM 4547 CB THR B 735 12.221 -12.045 -35.434 1.00 26.26 ATOM 4548 OG1 THR B 735 12.160 -10.655 -35.786 1.00 27.58 ATOM 4549 CG2 THR B 735 10.854 -12.476 -34.917 1.00 25.84 ATOM 4550 C THR B 735 14.583 -11.581 -34.835 1.00 25.49 ATOM 4551 O THR B 735 15.196 -10.783 -34.124 1.00 25.35 ATOM 4552 N SER B 736 14.984 -11.908 -36.058 1.00 24.79 ATOM 4553 CA SER B 736 16.196 -11.360 -36.653 1.00 24.05 ATOM 4554 CB SER B 736 16.516 -12.110 -37.939 1.00 24.47 ATOM 4555 OG SER B 736 17.029 -13.396 -37.634 1.00 27.46 ATOM 4556 C SER B 736 16.063 -9.872 -36.943 1.00 22.85 ATOM 4557 O SER B 736 17.050 -9.193 -37.227 1.00 23.19 ATOM 4558 N SER B 737 14.842 -9.364 -36.860 1.00 21.29 ATOM 4559 CA SER B 737 14.611 -7.965 -37.119 1.00 20.73 ATOM 4560 CB SER B 737 13.119 -7.673 -37.173 1.00 21.34 ATOM 4561 OG SER B 737 12.513 -7.926 -35.919 1.00 23.12 ATOM 4562 C SER B 737 15.278 -7.082 -36.073 1.00 20.70 ATOM 4563 O SER B 737 15.278 -5.865 -36.222 1.00 20.98 ATOM 4564 N ILE B 738 15.825 -7.671 -35.007 1.00 19.87 ATOM 4565 CA ILE B 738 16.514 -6.846 -34.013 1.00 19.72 ATOM 4566 CB ILE B 738 16.821 -7.598 -32.682 1.00 19.08 ATOM 4567 CG2 ILE B 738 15.504 -8.018 -31.999 1.00 19.39 ATOM 4568 CG1 ILE B 738 17.747 -8.786 -32.937 1.00 18.69 ATOM 4569 CD1 ILE B 738 18.393 -9.341 -31.671 1.00 18.69 ATOM 4570 C ILE B 738 17.833 -6.371 -34.629 1.00 20.06 ATOM 4571 O ILE B 738 18.355 -5.322 -34.254 1.00 20.12 ATOM 4572 N ASP B 739 18.355 -7.133 -35.593 1.00 20.31 ATOM 4573 CA ASP B 739 19.603 -6.759 -36.263 1.00 19.41 ATOM 4574 CB ASP B 739 20.140 -7.904 -37.115 1.00 19.59 ATOM 4575 CG ASP B 739 20.869 -8.946 -36.307 1.00 19.79 ATOM 4576 OD1 ASP B 739 21.084 -10.042 -36.857 1.00 21.34 ATOM 4577 OD2 ASP B 739 21.231 -8.695 -35.136 1.00 19.30 ATOM 4578 C ASP B 739 19.326 -5.583 -37.177 1.00 19.63 ATOM 4579 O ASP B 739 20.195 -4.741 -37.413 1.00 18.87 ATOM 4580 N VAL B 740 18.109 -5.531 -37.705 1.00 19.54 ATOM 4581 CA VAL B 740 17.747 -4.447 -38.594 1.00 18.52 ATOM 4582 CB VAL B 740 16.429 -4.731 -39.330 1.00 19.03 ATOM 4583 CG1 VAL B 740 16.004 -3.518 -40.148 1.00 17.37 ATOM 4584 CG2 VAL B 740 16.620 -5.940 -40.241 1.00 18.96 ATOM 4585 C VAL B 740 17.643 -3.162 -37.801 1.00 18.72 ATOM 4586 O VAL B 740 18.068 -2.117 -38.286 1.00 18.49 ATOM 4587 N TRP B 741 17.091 -3.234 -36.588 1.00 18.63 ATOM 4588 CA TRP B 741 16.983 -2.036 -35.740 1.00 19.15 ATOM 4589 CB TRP B 741 16.282 -2.352 -34.408 1.00 19.03 ATOM 4590 CG TRP B 741 16.325 -1.193 -33.418 1.00 19.81 ATOM 4591 CD2 TRP B 741 15.312 -0.199 -33.212 1.00 20.16 ATOM 4592 CE2 TRP B 741 15.796 0.701 -32.231 1.00 20.63 ATOM 4593 CE3 TRP B 741 14.039 0.023 -33.764 1.00 20.74 ATOM 4594 CD1 TRP B 741 17.358 -0.865 -32.569 1.00 19.59 ATOM 4595 NE1 TRP B 741 17.044 0.272 -31.856 1.00 20.21 ATOM 4596 CZ2 TRP B 741 15.049 1.807 -31.790 1.00 20.41 ATOM 4597 CZ3 TRP B 741 13.300 1.126 -33.326 1.00 21.31 ATOM 4598 CH2 TRP B 741 13.811 2.002 -32.348 1.00 20.48 ATOM 4599 C TRP B 741 18.404 -1.527 -35.454 1.00 18.40 ATOM 4600 O TRP B 741 18.684 -0.336 -35.585 1.00 19.23 ATOM 4601 N SER B 742 19.292 -2.448 -35.080 1.00 17.71 ATOM 4602 CA SER B 742 20.679 -2.128 -34.780 1.00 17.35 ATOM 4603 CB SER B 742 21.443 -3.397 -34.388 1.00 17.55 ATOM 4604 OG SER B 742 20.868 -4.006 -33.248 1.00 20.56 ATOM 4605 C SER B 742 21.373 -1.466 -35.963 1.00 17.25 ATOM 4606 O SER B 742 22.127 -0.514 -35.786 1.00 16.94 ATOM 4607 N ALA B 743 21.139 -1.979 -37.170 1.00 16.99 ATOM 4608 CA ALA B 743 21.754 -1.388 -38.357 1.00 16.75 ATOM 4609 CB ALA B 743 21.488 -2.260 -39.592 1.00 16.38 ATOM 4610 C ALA B 743 21.193 0.022 -38.569 1.00 17.17 ATOM 4611 O ALA B 743 21.908 0.909 -39.035 1.00 17.97 ATOM 4612 N GLY B 744 19.913 0.221 -38.248 1.00 17.25 ATOM 4613 CA GLY B 744 19.312 1.539 -38.380 1.00 17.67 ATOM 4614 C GLY B 744 20.005 2.527 -37.447 1.00 18.71 ATOM 4615 O GLY B 744 20.203 3.690 -37.789 1.00 19.51 ATOM 4616 N CYS B 745 20.371 2.069 -36.253 1.00 19.13 ATOM 4617 CA CYS B 745 21.061 2.928 -35.291 1.00 19.57 ATOM 4618 CB CYS B 745 21.194 2.208 -33.947 1.00 19.12 ATOM 4619 SG CYS B 745 19.622 1.961 -33.086 1.00 21.01 ATOM 4620 C CYS B 745 22.455 3.305 -35.818 1.00 19.53 ATOM 4621 O CYS B 745 22.947 4.410 -35.585 1.00 19.38 ATOM 4622 N VAL B 746 23.095 2.377 -36.519 1.00 19.02 ATOM 4623 CA VAL B 746 24.414 2.636 -37.072 1.00 19.03 ATOM 4624 CB VAL B 746 25.052 1.361 -37.658 1.00 18.55 ATOM 4625 CG1 VAL B 746 26.337 1.717 -38.407 1.00 16.60 ATOM 4626 CG2 VAL B 746 25.343 0.372 -36.529 1.00 16.97 ATOM 4627 C VAL B 746 24.300 3.681 -38.169 1.00 20.07 ATOM 4628 O VAL B 746 25.096 4.619 -38.215 1.00 20.08 ATOM 4629 N LEU B 747 23.313 3.518 -39.048 1.00 19.87 ATOM 4630 CA LEU B 747 23.097 4.466 -40.135 1.00 20.73 ATOM 4631 CB LEU B 747 21.887 4.043 -40.973 1.00 21.37 ATOM 4632 CG LEU B 747 21.345 5.079 -41.965 1.00 21.93 ATOM 4633 CD1 LEU B 747 22.451 5.493 -42.943 1.00 22.06 ATOM 4634 CD2 LEU B 747 20.155 4.493 -42.724 1.00 22.99 ATOM 4635 C LEU B 747 22.849 5.865 -39.570 1.00 21.07 ATOM 4636 O LEU B 747 23.512 6.827 -39.956 1.00 21.84 ATOM 4637 N ALA B 748 21.888 5.971 -38.662 1.00 20.93 ATOM 4638 CA ALA B 748 21.556 7.247 -38.041 1.00 21.26 ATOM 4639 CB ALA B 748 20.467 7.057 -37.006 1.00 20.61 ATOM 4640 C ALA B 748 22.782 7.867 -37.387 1.00 21.82 ATOM 4641 O ALA B 748 22.984 9.071 -37.466 1.00 22.48 ATOM 4642 N GLU B 749 23.591 7.041 -36.734 1.00 22.16 ATOM 4643 CA GLU B 749 24.795 7.518 -36.068 1.00 22.27 ATOM 4644 CB GLU B 749 25.388 6.401 -35.214 1.00 23.21 ATOM 4645 CG GLU B 749 26.650 6.789 -34.460 1.00 24.42 ATOM 4646 CD GLU B 749 27.037 5.753 -33.420 1.00 25.51 ATOM 4647 OE1 GLU B 749 26.198 4.893 -33.076 1.00 24.67 ATOM 4648 OE2 GLU B 749 28.184 5.801 -32.942 1.00 25.97 ATOM 4649 C GLU B 749 25.838 8.024 -37.068 1.00 22.26 ATOM 4650 O GLU B 749 26.503 9.025 -36.822 1.00 21.01 ATOM 4651 N LEU B 750 25.995 7.332 -38.189 1.00 21.99 ATOM 4652 CA LEU B 750 26.957 7.780 -39.191 1.00 23.35 ATOM 4653 CB LEU B 750 27.111 6.738 -40.302 1.00 23.07 ATOM 4654 CG LEU B 750 27.804 5.434 -39.879 1.00 23.88 ATOM 4655 CD1 LEU B 750 27.902 4.472 -41.069 1.00 23.39 ATOM 4656 CD2 LEU B 750 29.177 5.744 -39.306 1.00 23.04 ATOM 4657 C LEU B 750 26.503 9.117 -39.784 1.00 24.36 ATOM 4658 O LEU B 750 27.328 9.949 -40.148 1.00 25.36 ATOM 4659 N LEU B 751 25.191 9.328 -39.871 1.00 24.92 ATOM 4660 CA LEU B 751 24.657 10.580 -40.400 1.00 26.04 ATOM 4661 CB LEU B 751 23.201 10.389 -40.835 1.00 25.32 ATOM 4662 CG LEU B 751 22.936 9.498 -42.054 1.00 25.33 ATOM 4663 CD1 LEU B 751 21.446 9.273 -42.180 1.00 25.36 ATOM 4664 CD2 LEU B 751 23.490 10.133 -43.317 1.00 24.82 ATOM 4665 C LEU B 751 24.734 11.714 -39.366 1.00 27.19 ATOM 4666 O LEU B 751 25.065 12.843 -39.705 1.00 28.29 ATOM 4667 N LEU B 752 24.448 11.402 -38.107 1.00 28.06 ATOM 4668 CA LEU B 752 24.459 12.393 -37.032 1.00 29.67 ATOM 4669 CB LEU B 752 23.591 11.920 -35.874 1.00 30.46 ATOM 4670 CG LEU B 752 22.079 11.980 -36.040 1.00 32.96 ATOM 4671 CD1 LEU B 752 21.440 11.162 -34.919 1.00 32.49 ATOM 4672 CD2 LEU B 752 21.596 13.444 -35.995 1.00 32.63 ATOM 4673 C LEU B 752 25.819 12.745 -36.452 1.00 29.96 ATOM 4674 O LEU B 752 26.026 13.867 -36.015 1.00 30.62 ATOM 4675 N GLY B 753 26.733 11.783 -36.415 1.00 30.05 ATOM 4676 CA GLY B 753 28.043 12.040 -35.843 1.00 29.10 ATOM 4677 C GLY B 753 28.077 11.595 -34.390 1.00 29.56 ATOM 4678 O GLY B 753 29.108 11.697 -33.727 1.00 29.72 ATOM 4679 N GLN B 754 26.942 11.112 -33.891 1.00 28.97 ATOM 4680 CA GLN B 754 26.839 10.627 -32.517 1.00 29.06 ATOM 4681 CB GLN B 754 26.585 11.788 -31.545 1.00 30.43 ATOM 4682 CG GLN B 754 25.258 12.504 -31.755 1.00 34.53 ATOM 4683 CD GLN B 754 24.983 13.584 -30.704 1.00 37.46 ATOM 4684 OE1 GLN B 754 25.785 13.809 -29.798 1.00 39.54 ATOM 4685 NE2 GLN B 754 23.841 14.254 -30.828 1.00 38.69 ATOM 4686 C GLN B 754 25.680 9.637 -32.444 1.00 27.66 ATOM 4687 O GLN B 754 24.768 9.684 -33.272 1.00 27.02 ATOM 4688 N PRO B 755 25.707 8.722 -31.460 1.00 27.09 ATOM 4689 CD PRO B 755 26.757 8.547 -30.441 1.00 27.12 ATOM 4690 CA PRO B 755 24.625 7.735 -31.320 1.00 26.87 ATOM 4691 CB PRO B 755 24.949 7.008 -30.016 1.00 26.78 ATOM 4692 CG PRO B 755 26.408 7.227 -29.802 1.00 28.01 ATOM 4693 C PRO B 755 23.264 8.414 -31.261 1.00 26.26 ATOM 4694 O PRO B 755 23.109 9.443 -30.617 1.00 26.11 ATOM 4695 N ILE B 756 22.273 7.842 -31.933 1.00 25.82 ATOM 4696 CA ILE B 756 20.947 8.441 -31.923 1.00 25.63 ATOM 4697 CB ILE B 756 20.130 8.008 -33.164 1.00 25.97 ATOM 4698 CG2 ILE B 756 19.948 6.484 -33.187 1.00 25.15 ATOM 4699 CG1 ILE B 756 18.778 8.725 -33.155 1.00 26.52 ATOM 4700 CD1 ILE B 756 18.132 8.853 -34.526 1.00 27.34 ATOM 4701 C ILE B 756 20.134 8.154 -30.655 1.00 25.74 ATOM 4702 O ILE B 756 19.349 8.995 -30.235 1.00 25.34 ATOM 4703 N PHE B 757 20.317 6.989 -30.032 1.00 25.15 ATOM 4704 CA PHE B 757 19.548 6.671 -28.827 1.00 25.78 ATOM 4705 CB PHE B 757 18.598 5.497 -29.089 1.00 24.46 ATOM 4706 CG PHE B 757 17.645 5.723 -30.236 1.00 24.55 ATOM 4707 CD1 PHE B 757 17.538 4.788 -31.264 1.00 23.57 ATOM 4708 CD2 PHE B 757 16.848 6.866 -30.283 1.00 24.15 ATOM 4709 CE1 PHE B 757 16.651 4.988 -32.326 1.00 23.95 ATOM 4710 CE2 PHE B 757 15.956 7.078 -31.339 1.00 24.83 ATOM 4711 CZ PHE B 757 15.858 6.133 -32.366 1.00 24.39 ATOM 4712 C PHE B 757 20.411 6.351 -27.607 1.00 26.70 ATOM 4713 O PHE B 757 20.347 5.248 -27.061 1.00 27.14 ATOM 4714 N PRO B 758 21.208 7.322 -27.142 1.00 27.28 ATOM 4715 CD PRO B 758 21.359 8.707 -27.634 1.00 27.79 ATOM 4716 CA PRO B 758 22.052 7.052 -25.976 1.00 27.53 ATOM 4717 CB PRO B 758 23.037 8.217 -25.964 1.00 27.50 ATOM 4718 CG PRO B 758 22.286 9.348 -26.612 1.00 27.39 ATOM 4719 C PRO B 758 21.232 6.985 -24.692 1.00 27.86 ATOM 4720 O PRO B 758 20.058 7.339 -24.676 1.00 27.84 ATOM 4721 N GLY B 759 21.867 6.532 -23.619 1.00 28.89 ATOM 4722 CA GLY B 759 21.195 6.428 -22.337 1.00 29.55 ATOM 4723 C GLY B 759 21.956 5.463 -21.451 1.00 31.07 ATOM 4724 O GLY B 759 22.456 4.435 -21.919 1.00 31.15 ATOM 4725 N ASP B 760 22.059 5.782 -20.169 1.00 31.68 ATOM 4726 CA ASP B 760 22.775 4.910 -19.249 1.00 32.17 ATOM 4727 CB ASP B 760 23.349 5.723 -18.099 1.00 34.84 ATOM 4728 CG ASP B 760 24.634 6.426 -18.481 1.00 37.26 ATOM 4729 OD1 ASP B 760 25.106 6.225 -19.632 1.00 38.26 ATOM 4730 OD2 ASP B 760 25.167 7.175 -17.632 1.00 39.48 ATOM 4731 C ASP B 760 21.881 3.807 -18.711 1.00 31.42 ATOM 4732 O ASP B 760 22.368 2.794 -18.213 1.00 30.99 ATOM 4733 N SER B 761 20.572 4.014 -18.818 1.00 30.36 ATOM 4734 CA SER B 761 19.597 3.035 -18.362 1.00 29.65 ATOM 4735 CB SER B 761 18.880 3.542 -17.116 1.00 29.77 ATOM 4736 OG SER B 761 17.774 4.344 -17.476 1.00 29.76 ATOM 4737 C SER B 761 18.577 2.813 -19.469 1.00 29.23 ATOM 4738 O SER B 761 18.443 3.639 -20.370 1.00 29.27 ATOM 4739 N GLY B 762 17.861 1.696 -19.401 1.00 28.80 ATOM 4740 CA GLY B 762 16.855 1.406 -20.406 1.00 28.00 ATOM 4741 C GLY B 762 15.803 2.499 -20.525 1.00 28.20 ATOM 4742 O GLY B 762 15.377 2.813 -21.630 1.00 27.74 ATOM 4743 N VAL B 763 15.380 3.083 -19.403 1.00 28.38 ATOM 4744 CA VAL B 763 14.364 4.141 -19.429 1.00 28.58 ATOM 4745 CB VAL B 763 13.918 4.566 -17.990 1.00 29.21 ATOM 4746 CG1 VAL B 763 13.475 3.351 -17.195 1.00 29.80 ATOM 4747 CG2 VAL B 763 15.054 5.256 -17.261 1.00 29.81 ATOM 4748 C VAL B 763 14.876 5.369 -20.168 1.00 28.17 ATOM 4749 O VAL B 763 14.131 6.020 -20.893 1.00 28.80 ATOM 4750 N ASP B 764 16.151 5.690 -19.987 1.00 28.00 ATOM 4751 CA ASP B 764 16.722 6.847 -20.658 1.00 28.00 ATOM 4752 CB ASP B 764 18.140 7.111 -20.152 1.00 29.61 ATOM 4753 CG ASP B 764 18.160 7.757 -18.772 1.00 31.60 ATOM 4754 OD1 ASP B 764 19.245 7.814 -18.164 1.00 33.22 ATOM 4755 OD2 ASP B 764 17.096 8.206 -18.291 1.00 32.03 ATOM 4756 C ASP B 764 16.748 6.589 -22.153 1.00 27.94 ATOM 4757 O ASP B 764 16.461 7.478 -22.952 1.00 27.81 ATOM 4758 N GLN B 765 17.086 5.361 -22.528 1.00 27.47 ATOM 4759 CA GLN B 765 17.142 4.992 -23.933 1.00 27.40 ATOM 4760 CB GLN B 765 17.713 3.572 -24.091 1.00 28.73 ATOM 4761 CG GLN B 765 19.220 3.499 -23.870 1.00 31.03 ATOM 4762 CD GLN B 765 19.737 2.090 -23.571 1.00 33.64 ATOM 4763 OE1 GLN B 765 20.715 1.918 -22.836 1.00 35.20 ATOM 4764 NE2 GLN B 765 19.088 1.084 -24.138 1.00 34.18 ATOM 4765 C GLN B 765 15.746 5.081 -24.535 1.00 27.06 ATOM 4766 O GLN B 765 15.570 5.629 -25.625 1.00 27.08 ATOM 4767 N LEU B 766 14.752 4.550 -23.827 1.00 26.55 ATOM 4768 CA LEU B 766 13.376 4.595 -24.317 1.00 27.27 ATOM 4769 CB LEU B 766 12.446 3.848 -23.365 1.00 27.94 ATOM 4770 CG LEU B 766 12.498 2.326 -23.453 1.00 28.82 ATOM 4771 CD1 LEU B 766 11.615 1.738 -22.367 1.00 29.29 ATOM 4772 CD2 LEU B 766 12.039 1.862 -24.831 1.00 29.49 ATOM 4773 C LEU B 766 12.901 6.039 -24.477 1.00 27.37 ATOM 4774 O LEU B 766 12.131 6.349 -25.381 1.00 26.94 ATOM 4775 N VAL B 767 13.355 6.922 -23.594 1.00 28.04 ATOM 4776 CA VAL B 767 12.978 8.330 -23.679 1.00 28.98 ATOM 4777 CB VAL B 767 13.555 9.145 -22.490 1.00 29.36 ATOM 4778 CG1 VAL B 767 13.492 10.641 -22.801 1.00 29.32 ATOM 4779 CG2 VAL B 767 12.787 8.824 -21.219 1.00 28.85 ATOM 4780 C VAL B 767 13.497 8.933 -24.989 1.00 29.09 ATOM 4781 O VAL B 767 12.758 9.620 -25.706 1.00 29.98 ATOM 4782 N GLU B 768 14.768 8.675 -25.295 1.00 29.03 ATOM 4783 CA GLU B 768 15.387 9.176 -26.523 1.00 28.68 ATOM 4784 CB GLU B 768 16.864 8.772 -26.580 1.00 30.17 ATOM 4785 CG GLU B 768 17.745 9.461 -25.569 1.00 32.49 ATOM 4786 CD GLU B 768 17.575 10.969 -25.590 1.00 35.59 ATOM 4787 OE1 GLU B 768 17.709 11.568 -26.679 1.00 36.19 ATOM 4788 OE2 GLU B 768 17.300 11.559 -24.517 1.00 37.62 ATOM 4789 C GLU B 768 14.671 8.630 -27.757 1.00 28.13 ATOM 4790 O GLU B 768 14.519 9.333 -28.751 1.00 28.45 ATOM 4791 N ILE B 769 14.248 7.369 -27.692 1.00 26.99 ATOM 4792 CA ILE B 769 13.548 6.723 -28.795 1.00 26.68 ATOM 4793 CB ILE B 769 13.351 5.216 -28.515 1.00 25.31 ATOM 4794 CG2 ILE B 769 12.384 4.618 -29.518 1.00 24.64 ATOM 4795 CG1 ILE B 769 14.699 4.497 -28.555 1.00 24.36 ATOM 4796 CD1 ILE B 769 14.621 3.034 -28.174 1.00 23.04 ATOM 4797 C ILE B 769 12.174 7.364 -28.990 1.00 28.17 ATOM 4798 O ILE B 769 11.769 7.684 -30.113 1.00 27.49 ATOM 4799 N ILE B 770 11.464 7.541 -27.879 1.00 29.61 ATOM 4800 CA ILE B 770 10.138 8.139 -27.891 1.00 31.38 ATOM 4801 CB ILE B 770 9.497 8.088 -26.476 1.00 31.69 ATOM 4802 CG2 ILE B 770 8.266 8.986 -26.411 1.00 30.63 ATOM 4803 CG1 ILE B 770 9.111 6.641 -26.151 1.00 31.28 ATOM 4804 CD1 ILE B 770 8.773 6.402 -24.711 1.00 31.51 ATOM 4805 C ILE B 770 10.213 9.576 -28.398 1.00 32.78 ATOM 4806 O ILE B 770 9.337 10.015 -29.136 1.00 33.94 ATOM 4807 N LYS B 771 11.262 10.300 -28.018 1.00 34.20 ATOM 4808 CA LYS B 771 11.437 11.676 -28.476 1.00 35.24 ATOM 4809 CB LYS B 771 12.784 12.227 -28.008 1.00 36.29 ATOM 4810 CG LYS B 771 12.787 12.821 -26.607 1.00 38.38 ATOM 4811 CD LYS B 771 14.028 13.676 -26.388 1.00 40.14 ATOM 4812 CE LYS B 771 14.405 13.741 -24.914 1.00 41.78 ATOM 4813 NZ LYS B 771 15.806 14.243 -24.721 1.00 44.00 ATOM 4814 C LYS B 771 11.388 11.732 -30.004 1.00 35.82 ATOM 4815 O LYS B 771 10.805 12.642 -30.578 1.00 36.32 ATOM 4816 N VAL B 772 12.001 10.746 -30.654 1.00 36.45 ATOM 4817 CA VAL B 772 12.050 10.688 -32.111 1.00 36.17 ATOM 4818 CB VAL B 772 13.348 10.014 -32.614 1.00 35.46 ATOM 4819 CG1 VAL B 772 13.383 10.043 -34.129 1.00 34.95 ATOM 4820 CG2 VAL B 772 14.569 10.718 -32.046 1.00 34.69 ATOM 4821 C VAL B 772 10.892 9.950 -32.766 1.00 37.02 ATOM 4822 O VAL B 772 10.332 10.426 -33.754 1.00 37.26 ATOM 4823 N LEU B 773 10.544 8.783 -32.232 1.00 37.38 ATOM 4824 CA LEU B 773 9.468 7.986 -32.814 1.00 37.63 ATOM 4825 CB LEU B 773 9.718 6.489 -32.584 1.00 36.40 ATOM 4826 CG LEU B 773 10.978 5.770 -33.084 1.00 34.99 ATOM 4827 CD1 LEU B 773 10.644 4.299 -33.295 1.00 33.53 ATOM 4828 CD2 LEU B 773 11.483 6.398 -34.360 1.00 35.48 ATOM 4829 C LEU B 773 8.098 8.322 -32.260 1.00 38.80 ATOM 4830 O LEU B 773 7.087 7.963 -32.850 1.00 39.27 ATOM 4831 N GLY B 774 8.058 8.997 -31.122 1.00 40.27 ATOM 4832 CA GLY B 774 6.780 9.314 -30.517 1.00 41.98 ATOM 4833 C GLY B 774 6.418 8.188 -29.568 1.00 43.55 ATOM 4834 O GLY B 774 7.044 7.126 -29.595 1.00 42.93 ATOM 4835 N THR B 775 5.419 8.416 -28.722 1.00 45.29 ATOM 4836 CA THR B 775 4.987 7.409 -27.761 1.00 46.73 ATOM 4837 CB THR B 775 3.926 7.984 -26.787 1.00 47.42 ATOM 4838 OG1 THR B 775 4.537 8.976 -25.950 1.00 48.18 ATOM 4839 CG2 THR B 775 3.346 6.878 -25.904 1.00 47.54 ATOM 4840 C THR B 775 4.398 6.215 -28.501 1.00 47.38 ATOM 4841 O THR B 775 3.585 6.376 -29.411 1.00 47.50 ATOM 4842 N PRO B 776 4.820 4.998 -28.131 1.00 47.78 ATOM 4843 CD PRO B 776 5.808 4.671 -27.089 1.00 47.77 ATOM 4844 CA PRO B 776 4.305 3.797 -28.790 1.00 48.89 ATOM 4845 CB PRO B 776 5.245 2.695 -28.312 1.00 48.32 ATOM 4846 CG PRO B 776 5.717 3.168 -26.988 1.00 47.96 ATOM 4847 C PRO B 776 2.858 3.502 -28.418 1.00 50.14 ATOM 4848 O PRO B 776 2.481 3.537 -27.241 1.00 50.32 ATOM 4849 N THR B 777 2.048 3.210 -29.427 1.00 51.38 ATOM 4850 CA THR B 777 0.655 2.889 -29.185 1.00 52.43 ATOM 4851 CB THR B 777 -0.109 2.660 -30.496 1.00 52.28 ATOM 4852 OG1 THR B 777 0.287 1.408 -31.071 1.00 51.87 ATOM 4853 CG2 THR B 777 0.176 3.782 -31.471 1.00 51.81 ATOM 4854 C THR B 777 0.608 1.608 -28.371 1.00 53.62 ATOM 4855 O THR B 777 1.566 0.831 -28.361 1.00 53.83 ATOM 4856 N ARG B 778 -0.508 1.397 -27.685 1.00 54.82 ATOM 4857 CA ARG B 778 -0.699 0.210 -26.863 1.00 55.86 ATOM 4858 CB ARG B 778 -2.113 0.222 -26.272 1.00 58.19 ATOM 4859 CG ARG B 778 -2.451 -0.998 -25.436 1.00 61.48 ATOM 4860 CD ARG B 778 -3.769 -0.823 -24.695 1.00 64.01 ATOM 4861 NE ARG B 778 -4.141 -2.042 -23.979 1.00 66.49 ATOM 4862 CZ ARG B 778 -5.293 -2.216 -23.337 1.00 67.83 ATOM 4863 NH1 ARG B 778 -6.202 -1.245 -23.314 1.00 68.64 ATOM 4864 NH2 ARG B 778 -5.539 -3.367 -22.717 1.00 68.52 ATOM 4865 C ARG B 778 -0.492 -1.048 -27.708 1.00 55.26 ATOM 4866 O ARG B 778 -0.025 -2.076 -27.212 1.00 54.80 ATOM 4867 N GLU B 779 -0.833 -0.947 -28.989 1.00 54.82 ATOM 4868 CA GLU B 779 -0.699 -2.062 -29.917 1.00 54.78 ATOM 4869 CB GLU B 779 -1.522 -1.793 -31.176 1.00 56.20 ATOM 4870 CG GLU B 779 -1.576 -2.969 -32.136 1.00 58.83 ATOM 4871 CD GLU B 779 -1.926 -2.544 -33.554 1.00 60.86 ATOM 4872 OE1 GLU B 779 -2.533 -1.457 -33.718 1.00 61.94 ATOM 4873 OE2 GLU B 779 -1.594 -3.295 -34.501 1.00 61.46 ATOM 4874 C GLU B 779 0.761 -2.315 -30.296 1.00 53.74 ATOM 4875 O GLU B 779 1.199 -3.463 -30.386 1.00 52.99 ATOM 4876 N GLN B 780 1.505 -1.238 -30.530 1.00 52.59 ATOM 4877 CA GLN B 780 2.916 -1.355 -30.877 1.00 51.58 ATOM 4878 CB GLN B 780 3.509 0.025 -31.152 1.00 49.77 ATOM 4879 CG GLN B 780 3.479 0.419 -32.607 1.00 48.08 ATOM 4880 CD GLN B 780 3.593 1.911 -32.797 1.00 47.50 ATOM 4881 OE1 GLN B 780 3.274 2.688 -31.896 1.00 47.52 ATOM 4882 NE2 GLN B 780 4.053 2.325 -33.972 1.00 47.16 ATOM 4883 C GLN B 780 3.647 -2.003 -29.706 1.00 51.93 ATOM 4884 O GLN B 780 4.558 -2.811 -29.895 1.00 51.46 ATOM 4885 N ILE B 781 3.233 -1.642 -28.494 1.00 52.55 ATOM 4886 CA ILE B 781 3.836 -2.179 -27.283 1.00 53.56 ATOM 4887 CB ILE B 781 3.215 -1.531 -26.023 1.00 53.42 ATOM 4888 CG2 ILE B 781 3.640 -2.296 -24.777 1.00 53.24 ATOM 4889 CG1 ILE B 781 3.658 -0.070 -25.920 1.00 53.50 ATOM 4890 CD1 ILE B 781 3.105 0.663 -24.718 1.00 53.18 ATOM 4891 C ILE B 781 3.608 -3.684 -27.240 1.00 54.47 ATOM 4892 O ILE B 781 4.499 -4.459 -26.882 1.00 54.05 ATOM 4893 N ARG B 782 2.402 -4.085 -27.617 1.00 55.97 ATOM 4894 CA ARG B 782 2.021 -5.488 -27.633 1.00 57.60 ATOM 4895 CB ARG B 782 0.544 -5.597 -28.007 1.00 59.36 ATOM 4896 CG ARG B 782 -0.007 -7.001 -28.040 1.00 61.76 ATOM 4897 CD ARG B 782 -1.439 -6.971 -28.537 1.00 64.13 ATOM 4898 NE ARG B 782 -2.014 -8.309 -28.628 1.00 66.91 ATOM 4899 CZ ARG B 782 -3.197 -8.578 -29.175 1.00 67.92 ATOM 4900 NH1 ARG B 782 -3.928 -7.591 -29.683 1.00 68.45 ATOM 4901 NH2 ARG B 782 -3.649 -9.829 -29.216 1.00 68.13 ATOM 4902 C ARG B 782 2.876 -6.268 -28.626 1.00 57.91 ATOM 4903 O ARG B 782 3.148 -7.453 -28.428 1.00 57.44 ATOM 4904 N GLU B 783 3.295 -5.587 -29.691 1.00 58.48 ATOM 4905 CA GLU B 783 4.121 -6.183 -30.740 1.00 59.25 ATOM 4906 CB GLU B 783 4.200 -5.243 -31.940 1.00 59.56 ATOM 4907 CG GLU B 783 2.859 -4.788 -32.458 1.00 60.38 ATOM 4908 CD GLU B 783 2.386 -5.625 -33.624 1.00 61.08 ATOM 4909 OE1 GLU B 783 1.431 -5.198 -34.312 1.00 61.43 ATOM 4910 OE2 GLU B 783 2.973 -6.708 -33.852 1.00 61.16 ATOM 4911 C GLU B 783 5.541 -6.507 -30.282 1.00 59.81 ATOM 4912 O GLU B 783 6.102 -7.537 -30.655 1.00 59.55 ATOM 4913 N MET B 784 6.125 -5.618 -29.488 1.00 60.61 ATOM 4914 CA MET B 784 7.479 -5.819 -28.994 1.00 62.08 ATOM 4915 CB MET B 784 8.041 -4.503 -28.482 1.00 60.53 ATOM 4916 CG MET B 784 8.066 -3.449 -29.548 1.00 59.21 ATOM 4917 SD MET B 784 8.112 -1.814 -28.870 1.00 57.92 ATOM 4918 CE MET B 784 9.042 -1.092 -30.036 1.00 58.83 ATOM 4919 C MET B 784 7.506 -6.860 -27.894 1.00 63.90 ATOM 4920 O MET B 784 8.215 -7.858 -27.987 1.00 64.03 ATOM 4921 N ASN B 785 6.742 -6.618 -26.839 1.00 66.67 ATOM 4922 CA ASN B 785 6.679 -7.572 -25.748 1.00 69.70 ATOM 4923 CB ASN B 785 7.785 -7.341 -24.727 1.00 69.24 ATOM 4924 CG ASN B 785 7.672 -8.284 -23.547 1.00 69.08 ATOM 4925 OD1 ASN B 785 7.709 -7.864 -22.392 1.00 68.86 ATOM 4926 ND2 ASN B 785 7.519 -9.573 -23.837 1.00 68.89 ATOM 4927 C ASN B 785 5.350 -7.513 -25.032 1.00 72.26 ATOM 4928 O ASN B 785 5.027 -6.520 -24.374 1.00 72.21 ATOM 4929 N PRO B 786 4.552 -8.585 -25.159 1.00 74.88 ATOM 4930 CD PRO B 786 4.840 -9.801 -25.944 1.00 75.21 ATOM 4931 CA PRO B 786 3.244 -8.650 -24.507 1.00 77.02 ATOM 4932 CB PRO B 786 2.447 -9.595 -25.404 1.00 76.58 ATOM 4933 CG PRO B 786 3.491 -10.482 -26.053 1.00 75.85 ATOM 4934 C PRO B 786 3.388 -9.187 -23.084 1.00 79.05 ATOM 4935 O PRO B 786 2.812 -10.222 -22.749 1.00 79.56 ATOM 4936 N ASN B 787 4.160 -8.488 -22.254 1.00 81.27 ATOM 4937 CA ASN B 787 4.363 -8.925 -20.879 1.00 83.62 ATOM 4938 CB ASN B 787 5.441 -10.019 -20.823 1.00 83.74 ATOM 4939 CG ASN B 787 5.037 -11.285 -21.556 1.00 83.90 ATOM 4940 OD1 ASN B 787 4.032 -11.919 -21.228 1.00 83.82 ATOM 4941 ND2 ASN B 787 5.826 -11.661 -22.554 1.00 84.25 ATOM 4942 C ASN B 787 4.741 -7.814 -19.897 1.00 85.07 ATOM 4943 O ASN B 787 4.234 -7.784 -18.776 1.00 85.61 ATOM 4944 N TYR B 788 5.622 -6.902 -20.303 1.00 86.70 ATOM 4945 CA TYR B 788 6.065 -5.849 -19.390 1.00 88.23 ATOM 4946 CB TYR B 788 7.272 -5.105 -19.977 1.00 88.00 ATOM 4947 CG TYR B 788 8.551 -5.794 -19.572 1.00 87.92 ATOM 4948 CD1 TYR B 788 8.710 -7.163 -19.802 1.00 87.98 ATOM 4949 CE1 TYR B 788 9.833 -7.847 -19.362 1.00 87.78 ATOM 4950 CD2 TYR B 788 9.563 -5.117 -18.888 1.00 87.51 ATOM 4951 CE2 TYR B 788 10.701 -5.798 -18.438 1.00 87.53 ATOM 4952 CZ TYR B 788 10.823 -7.166 -18.679 1.00 87.67 ATOM 4953 OH TYR B 788 11.918 -7.869 -18.231 1.00 87.23 ATOM 4954 C TYR B 788 5.009 -4.872 -18.893 1.00 89.26 ATOM 4955 O TYR B 788 4.126 -4.438 -19.638 1.00 89.59 ATOM 4956 N THR B 789 5.131 -4.540 -17.609 1.00 90.18 ATOM 4957 CA THR B 789 4.204 -3.668 -16.897 1.00 91.03 ATOM 4958 CB THR B 789 4.421 -3.813 -15.375 1.00 90.95 ATOM 4959 OG1 THR B 789 5.393 -4.837 -15.131 1.00 90.57 ATOM 4960 CG2 THR B 789 3.117 -4.189 -14.678 1.00 90.97 ATOM 4961 C THR B 789 4.168 -2.174 -17.235 1.00 91.61 ATOM 4962 O THR B 789 3.237 -1.715 -17.899 1.00 91.66 ATOM 4963 N GLU B 790 5.161 -1.417 -16.769 1.00 92.24 ATOM 4964 CA GLU B 790 5.193 0.028 -17.002 1.00 92.62 ATOM 4965 CB GLU B 790 6.610 0.594 -16.836 1.00 93.34 ATOM 4966 CG GLU B 790 6.669 2.091 -16.512 1.00 94.32 ATOM 4967 CD GLU B 790 7.895 2.787 -17.099 1.00 94.84 ATOM 4968 OE1 GLU B 790 8.890 2.098 -17.409 1.00 95.42 ATOM 4969 OE2 GLU B 790 7.866 4.027 -17.249 1.00 95.05 ATOM 4970 C GLU B 790 4.653 0.455 -18.356 1.00 92.46 ATOM 4971 O GLU B 790 5.163 0.061 -19.407 1.00 92.65 ATOM 4972 N PHE B 791 3.599 1.258 -18.301 1.00 92.07 ATOM 4973 CA PHE B 791 2.953 1.813 -19.481 1.00 91.46 ATOM 4974 CB PHE B 791 1.506 1.315 -19.588 1.00 91.81 ATOM 4975 CG PHE B 791 1.358 -0.017 -20.286 1.00 91.98 ATOM 4976 CD1 PHE B 791 0.092 -0.520 -20.575 1.00 92.03 ATOM 4977 CD2 PHE B 791 2.474 -0.769 -20.648 1.00 92.00 ATOM 4978 CE1 PHE B 791 -0.065 -1.750 -21.213 1.00 92.07 ATOM 4979 CE2 PHE B 791 2.326 -2.004 -21.287 1.00 92.14 ATOM 4980 CZ PHE B 791 1.055 -2.493 -21.570 1.00 91.97 ATOM 4981 C PHE B 791 2.975 3.316 -19.220 1.00 90.74 ATOM 4982 O PHE B 791 2.497 4.119 -20.024 1.00 90.64 ATOM 4983 N LYS B 792 3.546 3.671 -18.072 1.00 89.82 ATOM 4984 CA LYS B 792 3.665 5.055 -17.636 1.00 88.91 ATOM 4985 CB LYS B 792 3.830 5.108 -16.110 1.00 89.08 ATOM 4986 CG LYS B 792 4.339 6.441 -15.562 1.00 89.33 ATOM 4987 CD LYS B 792 4.984 6.275 -14.188 1.00 89.17 ATOM 4988 CE LYS B 792 4.893 7.555 -13.366 1.00 88.90 ATOM 4989 NZ LYS B 792 3.614 7.643 -12.605 1.00 88.43 ATOM 4990 C LYS B 792 4.856 5.725 -18.312 1.00 88.11 ATOM 4991 O LYS B 792 5.985 5.636 -17.837 1.00 88.00 ATOM 4992 N PHE B 793 4.595 6.395 -19.428 1.00 87.34 ATOM 4993 CA PHE B 793 5.645 7.084 -20.160 1.00 86.63 ATOM 4994 CB PHE B 793 6.292 6.140 -21.172 1.00 86.24 ATOM 4995 CG PHE B 793 7.745 5.888 -20.914 1.00 85.87 ATOM 4996 CD1 PHE B 793 8.210 4.599 -20.682 1.00 85.65 ATOM 4997 CD2 PHE B 793 8.654 6.941 -20.895 1.00 85.71 ATOM 4998 CE1 PHE B 793 9.558 4.361 -20.434 1.00 85.51 ATOM 4999 CE2 PHE B 793 10.004 6.714 -20.648 1.00 85.46 ATOM 5000 CZ PHE B 793 10.457 5.421 -20.418 1.00 85.31 ATOM 5001 C PHE B 793 5.092 8.307 -20.880 1.00 86.40 ATOM 5002 O PHE B 793 4.154 8.199 -21.673 1.00 86.42 ATOM 5003 N PRO B 794 5.662 9.492 -20.597 1.00 85.98 ATOM 5004 CD PRO B 794 6.757 9.687 -19.630 1.00 85.72 ATOM 5005 CA PRO B 794 5.245 10.759 -21.207 1.00 85.56 ATOM 5006 CB PRO B 794 6.502 11.619 -21.131 1.00 85.64 ATOM 5007 CG PRO B 794 7.257 11.078 -19.938 1.00 85.79 ATOM 5008 C PRO B 794 4.747 10.593 -22.644 1.00 85.11 ATOM 5009 O PRO B 794 5.418 9.979 -23.474 1.00 84.86 ATOM 5010 N GLN B 795 3.565 11.141 -22.922 1.00 84.67 ATOM 5011 CA GLN B 795 2.966 11.055 -24.252 1.00 84.13 ATOM 5012 CB GLN B 795 1.439 11.187 -24.165 1.00 84.61 ATOM 5013 CG GLN B 795 0.863 11.042 -22.764 1.00 85.14 ATOM 5014 CD GLN B 795 0.699 9.595 -22.345 1.00 85.54 ATOM 5015 OE1 GLN B 795 0.488 9.300 -21.167 1.00 85.96 ATOM 5016 NE2 GLN B 795 0.796 8.681 -23.309 1.00 85.57 ATOM 5017 C GLN B 795 3.513 12.128 -25.191 1.00 83.41 ATOM 5018 O GLN B 795 2.907 13.186 -25.368 1.00 83.23 ATOM 5019 N ILE B 796 4.661 11.840 -25.794 1.00 82.55 ATOM 5020 CA ILE B 796 5.301 12.766 -26.718 1.00 81.45 ATOM 5021 CB ILE B 796 6.848 12.642 -26.628 1.00 81.07 ATOM 5022 CG2 ILE B 796 7.490 12.877 -27.989 1.00 80.73 ATOM 5023 CG1 ILE B 796 7.386 13.643 -25.602 1.00 80.73 ATOM 5024 CD1 ILE B 796 7.492 13.085 -24.196 1.00 80.25 ATOM 5025 C ILE B 796 4.833 12.481 -28.147 1.00 81.02 ATOM 5026 O ILE B 796 4.558 11.334 -28.503 1.00 80.72 ATOM 5027 N LYS B 797 4.732 13.534 -28.954 1.00 80.52 ATOM 5028 CA LYS B 797 4.307 13.398 -30.345 1.00 79.97 ATOM 5029 CB LYS B 797 3.706 14.719 -30.849 1.00 79.77 ATOM 5030 CG LYS B 797 4.620 15.932 -30.710 1.00 79.70 ATOM 5031 CD LYS B 797 4.557 16.531 -29.310 1.00 79.45 ATOM 5032 CE LYS B 797 5.909 17.094 -28.893 1.00 79.42 ATOM 5033 NZ LYS B 797 6.177 16.912 -27.437 1.00 79.26 ATOM 5034 C LYS B 797 5.499 12.995 -31.216 1.00 79.53 ATOM 5035 O LYS B 797 6.654 13.200 -30.834 1.00 79.59 ATOM 5036 N ALA B 798 5.215 12.415 -32.380 1.00 78.86 ATOM 5037 CA ALA B 798 6.265 11.977 -33.299 1.00 78.21 ATOM 5038 CB ALA B 798 5.640 11.329 -34.537 1.00 78.22 ATOM 5039 C ALA B 798 7.172 13.137 -33.713 1.00 77.53 ATOM 5040 O ALA B 798 6.695 14.181 -34.165 1.00 77.52 ATOM 5041 N HIS B 799 8.480 12.942 -33.553 1.00 76.64 ATOM 5042 CA HIS B 799 9.475 13.960 -33.899 1.00 75.55 ATOM 5043 CB HIS B 799 10.745 13.759 -33.072 1.00 76.62 ATOM 5044 CG HIS B 799 11.726 14.882 -33.185 1.00 77.53 ATOM 5045 CD2 HIS B 799 13.009 14.992 -32.762 1.00 78.03 ATOM 5046 ND1 HIS B 799 11.416 16.085 -33.783 1.00 78.03 ATOM 5047 CE1 HIS B 799 12.465 16.886 -33.724 1.00 78.38 ATOM 5048 NE2 HIS B 799 13.444 16.247 -33.109 1.00 78.59 ATOM 5049 C HIS B 799 9.838 13.918 -35.379 1.00 74.00 ATOM 5050 O HIS B 799 10.370 12.918 -35.872 1.00 73.85 ATOM 5051 N PRO B 800 9.568 15.018 -36.106 1.00 72.45 ATOM 5052 CD PRO B 800 8.986 16.285 -35.635 1.00 72.26 ATOM 5053 CA PRO B 800 9.885 15.060 -37.538 1.00 70.66 ATOM 5054 CB PRO B 800 9.674 16.530 -37.924 1.00 71.24 ATOM 5055 CG PRO B 800 9.537 17.279 -36.609 1.00 71.83 ATOM 5056 C PRO B 800 11.319 14.602 -37.762 1.00 68.58 ATOM 5057 O PRO B 800 12.268 15.275 -37.361 1.00 68.66 ATOM 5058 N TRP B 801 11.461 13.439 -38.383 1.00 65.81 ATOM 5059 CA TRP B 801 12.768 12.876 -38.657 1.00 62.82 ATOM 5060 CB TRP B 801 12.612 11.635 -39.523 1.00 60.51 ATOM 5061 CG TRP B 801 12.409 10.370 -38.756 1.00 57.71 ATOM 5062 CD2 TRP B 801 13.417 9.600 -38.091 1.00 56.24 ATOM 5063 CE2 TRP B 801 12.792 8.432 -37.597 1.00 55.42 ATOM 5064 CE3 TRP B 801 14.789 9.779 -37.868 1.00 55.38 ATOM 5065 CD1 TRP B 801 11.246 9.665 -38.632 1.00 57.03 ATOM 5066 NE1 TRP B 801 11.469 8.498 -37.940 1.00 55.82 ATOM 5067 CZ2 TRP B 801 13.490 7.451 -36.895 1.00 54.43 ATOM 5068 CZ3 TRP B 801 15.485 8.800 -37.170 1.00 54.55 ATOM 5069 CH2 TRP B 801 14.832 7.651 -36.692 1.00 54.39 ATOM 5070 C TRP B 801 13.678 13.884 -39.359 1.00 62.24 ATOM 5071 O TRP B 801 14.899 13.861 -39.174 1.00 62.19 ATOM 5072 N THR B 802 13.089 14.767 -40.162 1.00 61.28 ATOM 5073 CA THR B 802 13.875 15.769 -40.880 1.00 60.37 ATOM 5074 CB THR B 802 13.017 16.529 -41.913 1.00 60.86 ATOM 5075 OG1 THR B 802 12.679 15.643 -42.989 1.00 61.26 ATOM 5076 CG2 THR B 802 13.783 17.721 -42.477 1.00 60.74 ATOM 5077 C THR B 802 14.507 16.760 -39.911 1.00 59.12 ATOM 5078 O THR B 802 15.566 17.328 -40.191 1.00 59.65 ATOM 5079 N LYS B 803 13.858 16.957 -38.769 1.00 57.30 ATOM 5080 CA LYS B 803 14.373 17.859 -37.748 1.00 55.14 ATOM 5081 CB LYS B 803 13.241 18.320 -36.826 1.00 56.84 ATOM 5082 CG LYS B 803 13.716 19.249 -35.713 1.00 59.07 ATOM 5083 CD LYS B 803 12.569 19.955 -35.004 1.00 60.46 ATOM 5084 CE LYS B 803 12.975 20.319 -33.584 1.00 61.50 ATOM 5085 NZ LYS B 803 11.812 20.723 -32.738 1.00 63.06 ATOM 5086 C LYS B 803 15.448 17.155 -36.919 1.00 52.81 ATOM 5087 O LYS B 803 16.159 17.785 -36.138 1.00 52.35 ATOM 5088 N VAL B 804 15.563 15.843 -37.098 1.00 50.20 ATOM 5089 CA VAL B 804 16.539 15.044 -36.363 1.00 47.22 ATOM 5090 CB VAL B 804 16.156 13.536 -36.398 1.00 47.22 ATOM 5091 CG1 VAL B 804 17.309 12.684 -35.882 1.00 46.23 ATOM 5092 CG2 VAL B 804 14.900 13.298 -35.572 1.00 46.37 ATOM 5093 C VAL B 804 17.960 15.200 -36.901 1.00 45.63 ATOM 5094 O VAL B 804 18.915 15.284 -36.129 1.00 44.61 ATOM 5095 N PHE B 805 18.092 15.246 -38.224 1.00 44.25 ATOM 5096 CA PHE B 805 19.398 15.359 -38.865 1.00 43.22 ATOM 5097 CB PHE B 805 19.458 14.406 -40.061 1.00 42.02 ATOM 5098 CG PHE B 805 19.177 12.973 -39.702 1.00 40.44 ATOM 5099 CD1 PHE B 805 17.945 12.395 -39.994 1.00 39.31 ATOM 5100 CD2 PHE B 805 20.138 12.208 -39.049 1.00 39.62 ATOM 5101 CE1 PHE B 805 17.675 11.077 -39.638 1.00 38.98 ATOM 5102 CE2 PHE B 805 19.877 10.892 -38.688 1.00 39.04 ATOM 5103 CZ PHE B 805 18.641 10.325 -38.983 1.00 39.00 ATOM 5104 C PHE B 805 19.774 16.771 -39.315 1.00 43.92 ATOM 5105 O PHE B 805 18.920 17.654 -39.428 1.00 43.57 ATOM 5106 N ARG B 806 21.066 16.968 -39.571 1.00 44.20 ATOM 5107 CA ARG B 806 21.578 18.256 -40.010 1.00 44.87 ATOM 5108 CB ARG B 806 23.103 18.198 -40.127 1.00 46.92 ATOM 5109 CG ARG B 806 23.598 17.452 -41.355 1.00 49.88 ATOM 5110 CD ARG B 806 25.106 17.551 -41.517 1.00 52.96 ATOM 5111 NE ARG B 806 25.536 17.046 -42.820 1.00 56.34 ATOM 5112 CZ ARG B 806 25.521 15.761 -43.173 1.00 58.47 ATOM 5113 NH1 ARG B 806 25.096 14.829 -42.321 1.00 59.58 ATOM 5114 NH2 ARG B 806 25.926 15.400 -44.387 1.00 59.23 ATOM 5115 C ARG B 806 20.962 18.642 -41.353 1.00 44.42 ATOM 5116 O ARG B 806 20.540 17.782 -42.126 1.00 44.00 ATOM 5117 N PRO B 807 20.894 19.953 -41.646 1.00 44.09 ATOM 5118 CD PRO B 807 21.352 21.089 -40.829 1.00 44.07 ATOM 5119 CA PRO B 807 20.313 20.386 -42.922 1.00 43.11 ATOM 5120 CB PRO B 807 20.334 21.913 -42.832 1.00 43.93 ATOM 5121 CG PRO B 807 21.405 22.217 -41.817 1.00 44.03 ATOM 5122 C PRO B 807 21.126 19.872 -44.099 1.00 41.99 ATOM 5123 O PRO B 807 22.352 19.812 -44.035 1.00 41.70 ATOM 5124 N ARG B 808 20.429 19.503 -45.166 1.00 41.25 ATOM 5125 CA ARG B 808 21.044 18.986 -46.385 1.00 41.25 ATOM 5126 CB ARG B 808 22.366 19.707 -46.677 1.00 42.20 ATOM 5127 CG ARG B 808 22.191 21.038 -47.396 1.00 44.49 ATOM 5128 CD ARG B 808 23.532 21.644 -47.799 1.00 46.32 ATOM 5129 NE ARG B 808 24.356 21.953 -46.634 1.00 48.15 ATOM 5130 CZ ARG B 808 24.126 22.969 -45.806 1.00 50.02 ATOM 5131 NH1 ARG B 808 23.095 23.784 -46.007 1.00 50.34 ATOM 5132 NH2 ARG B 808 24.921 23.167 -44.764 1.00 51.20 ATOM 5133 C ARG B 808 21.261 17.470 -46.340 1.00 40.06 ATOM 5134 O ARG B 808 21.830 16.887 -47.265 1.00 39.46 ATOM 5135 N THR B 809 20.813 16.838 -45.257 1.00 38.81 ATOM 5136 CA THR B 809 20.926 15.392 -45.141 1.00 37.82 ATOM 5137 CB THR B 809 20.425 14.889 -43.779 1.00 37.81 ATOM 5138 OG1 THR B 809 21.315 15.331 -42.750 1.00 37.53 ATOM 5139 CG2 THR B 809 20.363 13.366 -43.762 1.00 37.11 ATOM 5140 C THR B 809 20.006 14.843 -46.223 1.00 37.56 ATOM 5141 O THR B 809 18.856 15.269 -46.338 1.00 37.76 ATOM 5142 N PRO B 810 20.498 13.894 -47.038 1.00 37.13 ATOM 5143 CD PRO B 810 21.843 13.295 -47.015 1.00 36.72 ATOM 5144 CA PRO B 810 19.658 13.330 -48.101 1.00 36.39 ATOM 5145 CB PRO B 810 20.539 12.249 -48.720 1.00 36.40 ATOM 5146 CG PRO B 810 21.942 12.649 -48.360 1.00 36.68 ATOM 5147 C PRO B 810 18.333 12.777 -47.579 1.00 36.22 ATOM 5148 O PRO B 810 18.313 11.929 -46.685 1.00 36.06 ATOM 5149 N PRO B 811 17.207 13.263 -48.127 1.00 35.45 ATOM 5150 CD PRO B 811 17.159 14.286 -49.188 1.00 35.22 ATOM 5151 CA PRO B 811 15.863 12.829 -47.725 1.00 34.71 ATOM 5152 CB PRO B 811 14.938 13.545 -48.711 1.00 34.81 ATOM 5153 CG PRO B 811 15.727 14.733 -49.168 1.00 35.17 ATOM 5154 C PRO B 811 15.681 11.312 -47.767 1.00 34.01 ATOM 5155 O PRO B 811 14.956 10.748 -46.949 1.00 33.30 ATOM 5156 N GLU B 812 16.338 10.665 -48.727 1.00 33.34 ATOM 5157 CA GLU B 812 16.255 9.213 -48.872 1.00 32.95 ATOM 5158 CB GLU B 812 16.972 8.755 -50.148 1.00 33.78 ATOM 5159 CG GLU B 812 16.378 9.306 -51.428 1.00 36.17 ATOM 5160 CD GLU B 812 16.718 10.781 -51.654 1.00 38.68 ATOM 5161 OE1 GLU B 812 16.056 11.414 -52.513 1.00 40.87 ATOM 5162 OE2 GLU B 812 17.640 11.311 -50.983 1.00 38.18 ATOM 5163 C GLU B 812 16.887 8.533 -47.662 1.00 31.74 ATOM 5164 O GLU B 812 16.443 7.470 -47.240 1.00 31.06 ATOM 5165 N ALA B 813 17.931 9.153 -47.118 1.00 31.28 ATOM 5166 CA ALA B 813 18.620 8.614 -45.951 1.00 30.94 ATOM 5167 CB ALA B 813 19.878 9.419 -45.662 1.00 30.40 ATOM 5168 C ALA B 813 17.688 8.651 -44.748 1.00 30.56 ATOM 5169 O ALA B 813 17.636 7.705 -43.966 1.00 29.99 ATOM 5170 N ILE B 814 16.949 9.749 -44.620 1.00 31.01 ATOM 5171 CA ILE B 814 16.003 9.938 -43.524 1.00 31.35 ATOM 5172 CB ILE B 814 15.457 11.380 -43.514 1.00 32.61 ATOM 5173 CG2 ILE B 814 14.441 11.554 -42.397 1.00 32.87 ATOM 5174 CG1 ILE B 814 16.606 12.372 -43.341 1.00 33.44 ATOM 5175 CD1 ILE B 814 16.223 13.790 -43.709 1.00 34.52 ATOM 5176 C ILE B 814 14.826 8.975 -43.663 1.00 30.51 ATOM 5177 O ILE B 814 14.306 8.466 -42.670 1.00 30.78 ATOM 5178 N ALA B 815 14.404 8.737 -44.900 1.00 29.57 ATOM 5179 CA ALA B 815 13.295 7.829 -45.171 1.00 28.45 ATOM 5180 CB ALA B 815 12.905 7.897 -46.650 1.00 28.26 ATOM 5181 C ALA B 815 13.699 6.409 -44.802 1.00 27.62 ATOM 5182 O ALA B 815 12.911 5.668 -44.213 1.00 27.54 ATOM 5183 N LEU B 816 14.926 6.029 -45.160 1.00 26.42 ATOM 5184 CA LEU B 816 15.430 4.692 -44.847 1.00 25.72 ATOM 5185 CB LEU B 816 16.826 4.477 -45.444 1.00 23.90 ATOM 5186 CG LEU B 816 17.538 3.156 -45.106 1.00 24.53 ATOM 5187 CD1 LEU B 816 16.624 1.951 -45.405 1.00 23.08 ATOM 5188 CD2 LEU B 816 18.826 3.054 -45.915 1.00 21.78 ATOM 5189 C LEU B 816 15.478 4.516 -43.330 1.00 26.03 ATOM 5190 O LEU B 816 15.014 3.508 -42.807 1.00 25.69 ATOM 5191 N CYS B 817 16.033 5.496 -42.621 1.00 26.25 ATOM 5192 CA CYS B 817 16.102 5.403 -41.170 1.00 27.68 ATOM 5193 CB CYS B 817 16.618 6.700 -40.558 1.00 29.12 ATOM 5194 SG CYS B 817 18.387 6.877 -40.609 1.00 33.21 ATOM 5195 C CYS B 817 14.728 5.124 -40.584 1.00 27.70 ATOM 5196 O CYS B 817 14.563 4.189 -39.812 1.00 27.33 ATOM 5197 N SER B 818 13.742 5.936 -40.959 1.00 27.90 ATOM 5198 CA SER B 818 12.389 5.776 -40.436 1.00 28.34 ATOM 5199 CB SER B 818 11.485 6.891 -40.968 1.00 28.00 ATOM 5200 OG SER B 818 11.041 6.610 -42.276 1.00 30.15 ATOM 5201 C SER B 818 11.753 4.417 -40.715 1.00 28.09 ATOM 5202 O SER B 818 10.855 3.993 -39.991 1.00 28.99 ATOM 5203 N ARG B 819 12.215 3.728 -41.753 1.00 27.79 ATOM 5204 CA ARG B 819 11.666 2.418 -42.094 1.00 27.31 ATOM 5205 CB ARG B 819 11.672 2.227 -43.616 1.00 28.14 ATOM 5206 CG ARG B 819 10.719 3.164 -44.357 1.00 30.19 ATOM 5207 CD ARG B 819 9.257 2.887 -44.008 1.00 32.24 ATOM 5208 NE ARG B 819 8.739 1.716 -44.718 1.00 34.91 ATOM 5209 CZ ARG B 819 8.488 0.541 -44.144 1.00 35.94 ATOM 5210 NH1 ARG B 819 8.706 0.368 -42.843 1.00 36.19 ATOM 5211 NH2 ARG B 819 8.031 -0.469 -44.873 1.00 36.53 ATOM 5212 C ARG B 819 12.430 1.285 -41.416 1.00 26.23 ATOM 5213 O ARG B 819 11.994 0.129 -41.426 1.00 25.41 ATOM 5214 N LEU B 820 13.571 1.620 -40.823 1.00 25.03 ATOM 5215 CA LEU B 820 14.387 0.629 -40.128 1.00 24.48 ATOM 5216 CB LEU B 820 15.877 0.917 -40.346 1.00 23.29 ATOM 5217 CG LEU B 820 16.441 0.829 -41.767 1.00 22.75 ATOM 5218 CD1 LEU B 820 17.887 1.321 -41.772 1.00 21.03 ATOM 5219 CD2 LEU B 820 16.366 -0.606 -42.258 1.00 22.02 ATOM 5220 C LEU B 820 14.075 0.705 -38.636 1.00 24.85 ATOM 5221 O LEU B 820 13.921 -0.314 -37.946 1.00 24.49 ATOM 5222 N LEU B 821 13.977 1.938 -38.153 1.00 24.86 ATOM 5223 CA LEU B 821 13.711 2.204 -36.752 1.00 25.29 ATOM 5224 CB LEU B 821 14.439 3.489 -36.329 1.00 23.72 ATOM 5225 CG LEU B 821 15.957 3.410 -36.566 1.00 23.97 ATOM 5226 CD1 LEU B 821 16.656 4.681 -36.124 1.00 22.89 ATOM 5227 CD2 LEU B 821 16.523 2.205 -35.811 1.00 23.67 ATOM 5228 C LEU B 821 12.217 2.306 -36.482 1.00 26.34 ATOM 5229 O LEU B 821 11.689 3.396 -36.268 1.00 26.46 ATOM 5230 N GLU B 822 11.545 1.155 -36.508 1.00 27.17 ATOM 5231 CA GLU B 822 10.103 1.064 -36.255 1.00 28.81 ATOM 5232 CB GLU B 822 9.375 0.345 -37.400 1.00 29.49 ATOM 5233 CG GLU B 822 9.590 0.929 -38.775 1.00 32.78 ATOM 5234 CD GLU B 822 8.480 1.882 -39.182 1.00 35.66 ATOM 5235 OE1 GLU B 822 7.706 2.311 -38.291 1.00 37.30 ATOM 5236 OE2 GLU B 822 8.381 2.204 -40.392 1.00 36.70 ATOM 5237 C GLU B 822 9.869 0.255 -34.984 1.00 28.74 ATOM 5238 O GLU B 822 10.552 -0.745 -34.748 1.00 28.81 ATOM 5239 N TYR B 823 8.896 0.677 -34.180 1.00 28.42 ATOM 5240 CA TYR B 823 8.556 -0.035 -32.955 1.00 28.42 ATOM 5241 CB TYR B 823 7.397 0.658 -32.229 1.00 29.14 ATOM 5242 CG TYR B 823 7.762 1.902 -31.441 1.00 29.38 ATOM 5243 CD1 TYR B 823 8.737 1.865 -30.438 1.00 28.42 ATOM 5244 CE1 TYR B 823 9.044 2.992 -29.690 1.00 28.65 ATOM 5245 CD2 TYR B 823 7.105 3.112 -31.676 1.00 28.91 ATOM 5246 CE2 TYR B 823 7.409 4.249 -30.930 1.00 29.20 ATOM 5247 CZ TYR B 823 8.377 4.178 -29.940 1.00 29.37 ATOM 5248 OH TYR B 823 8.673 5.291 -29.195 1.00 30.92 ATOM 5249 C TYR B 823 8.125 -1.467 -33.288 1.00 28.18 ATOM 5250 O TYR B 823 8.647 -2.434 -32.735 1.00 28.26 ATOM 5251 N THR B 824 7.164 -1.597 -34.195 1.00 28.08 ATOM 5252 CA THR B 824 6.652 -2.911 -34.577 1.00 28.46 ATOM 5253 CB THR B 824 5.366 -2.760 -35.422 1.00 29.08 ATOM 5254 OG1 THR B 824 4.373 -2.059 -34.655 1.00 29.31 ATOM 5255 CG2 THR B 824 4.826 -4.124 -35.823 1.00 28.06 ATOM 5256 C THR B 824 7.714 -3.676 -35.358 1.00 28.55 ATOM 5257 O THR B 824 8.027 -3.337 -36.493 1.00 28.75 ATOM 5258 N PRO B 825 8.274 -4.737 -34.754 1.00 29.07 ATOM 5259 CD PRO B 825 7.930 -5.244 -33.412 1.00 28.65 ATOM 5260 CA PRO B 825 9.317 -5.546 -35.400 1.00 28.89 ATOM 5261 CB PRO B 825 9.477 -6.744 -34.460 1.00 28.81 ATOM 5262 CG PRO B 825 9.021 -6.238 -33.124 1.00 28.72 ATOM 5263 C PRO B 825 9.039 -5.966 -36.848 1.00 29.17 ATOM 5264 O PRO B 825 9.872 -5.757 -37.734 1.00 28.62 ATOM 5265 N THR B 826 7.872 -6.553 -37.090 1.00 29.04 ATOM 5266 CA THR B 826 7.515 -6.999 -38.434 1.00 28.54 ATOM 5267 CB THR B 826 6.208 -7.828 -38.417 1.00 28.38 ATOM 5268 OG1 THR B 826 5.162 -7.068 -37.803 1.00 28.93 ATOM 5269 CG2 THR B 826 6.409 -9.112 -37.641 1.00 28.04 ATOM 5270 C THR B 826 7.352 -5.848 -39.429 1.00 28.35 ATOM 5271 O THR B 826 7.318 -6.075 -40.638 1.00 28.71 ATOM 5272 N ALA B 827 7.257 -4.619 -38.929 1.00 27.95 ATOM 5273 CA ALA B 827 7.095 -3.451 -39.799 1.00 28.03 ATOM 5274 CB ALA B 827 6.413 -2.321 -39.031 1.00 27.27 ATOM 5275 C ALA B 827 8.416 -2.940 -40.403 1.00 27.99 ATOM 5276 O ALA B 827 8.413 -2.216 -41.395 1.00 28.70 ATOM 5277 N ARG B 828 9.541 -3.311 -39.804 1.00 27.26 ATOM 5278 CA ARG B 828 10.840 -2.873 -40.305 1.00 25.47 ATOM 5279 CB ARG B 828 11.933 -3.189 -39.279 1.00 24.25 ATOM 5280 CG ARG B 828 11.651 -2.646 -37.903 1.00 23.10 ATOM 5281 CD ARG B 828 12.580 -3.210 -36.853 1.00 22.27 ATOM 5282 NE ARG B 828 12.101 -2.791 -35.545 1.00 22.66 ATOM 5283 CZ ARG B 828 12.307 -3.450 -34.409 1.00 23.33 ATOM 5284 NH1 ARG B 828 13.001 -4.579 -34.403 1.00 21.64 ATOM 5285 NH2 ARG B 828 11.770 -2.996 -33.280 1.00 23.01 ATOM 5286 C ARG B 828 11.178 -3.574 -41.615 1.00 25.43 ATOM 5287 O ARG B 828 10.807 -4.729 -41.818 1.00 25.28 ATOM 5288 N LEU B 829 11.882 -2.878 -42.500 1.00 24.92 ATOM 5289 CA LEU B 829 12.303 -3.469 -43.770 1.00 24.45 ATOM 5290 CB LEU B 829 13.106 -2.461 -44.591 1.00 24.25 ATOM 5291 CG LEU B 829 12.475 -1.159 -45.064 1.00 25.35 ATOM 5292 CD1 LEU B 829 13.582 -0.195 -45.491 1.00 26.00 ATOM 5293 CD2 LEU B 829 11.540 -1.439 -46.228 1.00 25.44 ATOM 5294 C LEU B 829 13.225 -4.644 -43.461 1.00 24.19 ATOM 5295 O LEU B 829 13.856 -4.678 -42.392 1.00 24.27 ATOM 5296 N THR B 830 13.301 -5.608 -44.376 1.00 23.48 ATOM 5297 CA THR B 830 14.215 -6.737 -44.210 1.00 23.27 ATOM 5298 CB THR B 830 13.757 -7.980 -45.004 1.00 23.77 ATOM 5299 OG1 THR B 830 13.833 -7.700 -46.407 1.00 24.67 ATOM 5300 CG2 THR B 830 12.315 -8.344 -44.653 1.00 24.80 ATOM 5301 C THR B 830 15.548 -6.256 -44.810 1.00 22.86 ATOM 5302 O THR B 830 15.585 -5.256 -45.523 1.00 22.72 ATOM 5303 N PRO B 831 16.661 -6.933 -44.496 1.00 22.44 ATOM 5304 CD PRO B 831 16.810 -8.070 -43.569 1.00 22.07 ATOM 5305 CA PRO B 831 17.944 -6.503 -45.060 1.00 22.46 ATOM 5306 CB PRO B 831 18.928 -7.562 -44.568 1.00 22.52 ATOM 5307 CG PRO B 831 18.285 -8.130 -43.329 1.00 22.63 ATOM 5308 C PRO B 831 17.947 -6.390 -46.590 1.00 23.32 ATOM 5309 O PRO B 831 18.530 -5.458 -47.140 1.00 23.36 ATOM 5310 N LEU B 832 17.307 -7.338 -47.275 1.00 23.06 ATOM 5311 CA LEU B 832 17.266 -7.326 -48.742 1.00 23.17 ATOM 5312 CB LEU B 832 16.672 -8.647 -49.257 1.00 24.03 ATOM 5313 CG LEU B 832 17.073 -9.157 -50.645 1.00 25.34 ATOM 5314 CD1 LEU B 832 18.586 -9.362 -50.726 1.00 24.76 ATOM 5315 CD2 LEU B 832 16.313 -10.470 -50.929 1.00 24.99 ATOM 5316 C LEU B 832 16.454 -6.131 -49.236 1.00 22.83 ATOM 5317 O LEU B 832 16.818 -5.484 -50.217 1.00 23.30 ATOM 5318 N GLU B 833 15.364 -5.822 -48.542 1.00 22.69 ATOM 5319 CA GLU B 833 14.538 -4.675 -48.910 1.00 23.21 ATOM 5320 CB GLU B 833 13.246 -4.664 -48.093 1.00 24.22 ATOM 5321 CG GLU B 833 12.212 -5.681 -48.563 1.00 26.52 ATOM 5322 CD GLU B 833 11.051 -5.854 -47.592 1.00 28.03 ATOM 5323 OE1 GLU B 833 11.039 -5.198 -46.525 1.00 27.50 ATOM 5324 OE2 GLU B 833 10.146 -6.658 -47.901 1.00 28.70 ATOM 5325 C GLU B 833 15.314 -3.379 -48.657 1.00 23.00 ATOM 5326 O GLU B 833 15.179 -2.414 -49.405 1.00 23.01 ATOM 5327 N ALA B 834 16.107 -3.353 -47.587 1.00 22.13 ATOM 5328 CA ALA B 834 16.911 -2.175 -47.259 1.00 21.77 ATOM 5329 CB ALA B 834 17.667 -2.396 -45.928 1.00 20.40 ATOM 5330 C ALA B 834 17.901 -1.954 -48.412 1.00 21.07 ATOM 5331 O ALA B 834 18.079 -0.834 -48.874 1.00 21.17 ATOM 5332 N CYS B 835 18.526 -3.034 -48.874 1.00 20.64 ATOM 5333 CA CYS B 835 19.483 -2.964 -49.981 1.00 22.25 ATOM 5334 CB CYS B 835 19.995 -4.357 -50.341 1.00 22.35 ATOM 5335 SG CYS B 835 21.320 -4.944 -49.301 1.00 24.84 ATOM 5336 C CYS B 835 18.872 -2.355 -51.233 1.00 23.18 ATOM 5337 O CYS B 835 19.551 -1.645 -51.981 1.00 23.78 ATOM 5338 N ALA B 836 17.592 -2.642 -51.460 1.00 23.64 ATOM 5339 CA ALA B 836 16.882 -2.145 -52.633 1.00 24.09 ATOM 5340 CB ALA B 836 15.752 -3.107 -52.994 1.00 24.15 ATOM 5341 C ALA B 836 16.323 -0.743 -52.443 1.00 24.38 ATOM 5342 O ALA B 836 15.734 -0.180 -53.364 1.00 24.40 ATOM 5343 N HIS B 837 16.505 -0.173 -51.257 1.00 24.47 ATOM 5344 CA HIS B 837 15.995 1.167 -50.989 1.00 24.97 ATOM 5345 CB HIS B 837 16.242 1.543 -49.527 1.00 24.81 ATOM 5346 CG HIS B 837 15.464 2.741 -49.075 1.00 24.73 ATOM 5347 CD2 HIS B 837 14.253 2.845 -48.477 1.00 24.32 ATOM 5348 ND1 HIS B 837 15.927 4.031 -49.228 1.00 25.28 ATOM 5349 CE1 HIS B 837 15.037 4.878 -48.743 1.00 24.09 ATOM 5350 NE2 HIS B 837 14.012 4.185 -48.282 1.00 24.87 ATOM 5351 C HIS B 837 16.637 2.206 -51.912 1.00 25.55 ATOM 5352 O HIS B 837 17.775 2.035 -52.361 1.00 25.49 ATOM 5353 N SER B 838 15.903 3.288 -52.177 1.00 26.23 ATOM 5354 CA SER B 838 16.379 4.350 -53.058 1.00 27.32 ATOM 5355 CB SER B 838 15.240 5.334 -53.359 1.00 28.79 ATOM 5356 OG SER B 838 14.842 6.019 -52.182 1.00 32.63 ATOM 5357 C SER B 838 17.601 5.103 -52.527 1.00 26.74 ATOM 5358 O SER B 838 18.318 5.739 -53.303 1.00 26.84 ATOM 5359 N PHE B 839 17.841 5.045 -51.219 1.00 25.75 ATOM 5360 CA PHE B 839 19.020 5.704 -50.646 1.00 25.21 ATOM 5361 CB PHE B 839 19.074 5.488 -49.120 1.00 25.20 ATOM 5362 CG PHE B 839 20.346 5.995 -48.458 1.00 25.80 ATOM 5363 CD1 PHE B 839 20.708 7.341 -48.531 1.00 25.16 ATOM 5364 CD2 PHE B 839 21.172 5.122 -47.744 1.00 25.17 ATOM 5365 CE1 PHE B 839 21.873 7.812 -47.904 1.00 25.77 ATOM 5366 CE2 PHE B 839 22.340 5.584 -47.115 1.00 25.50 ATOM 5367 CZ PHE B 839 22.691 6.930 -47.195 1.00 24.64 ATOM 5368 C PHE B 839 20.268 5.108 -51.308 1.00 24.48 ATOM 5369 O PHE B 839 21.281 5.782 -51.452 1.00 25.28 ATOM 5370 N PHE B 840 20.189 3.851 -51.737 1.00 24.15 ATOM 5371 CA PHE B 840 21.337 3.207 -52.370 1.00 23.60 ATOM 5372 CB PHE B 840 21.445 1.747 -51.923 1.00 22.25 ATOM 5373 CG PHE B 840 21.579 1.576 -50.435 1.00 22.14 ATOM 5374 CD1 PHE B 840 22.718 2.021 -49.768 1.00 20.78 ATOM 5375 CD2 PHE B 840 20.568 0.969 -49.699 1.00 21.77 ATOM 5376 CE1 PHE B 840 22.850 1.863 -48.382 1.00 21.51 ATOM 5377 CE2 PHE B 840 20.690 0.807 -48.308 1.00 22.16 ATOM 5378 CZ PHE B 840 21.834 1.255 -47.653 1.00 21.03 ATOM 5379 C PHE B 840 21.339 3.255 -53.896 1.00 24.24 ATOM 5380 O PHE B 840 22.157 2.598 -54.538 1.00 23.67 ATOM 5381 N ASP B 841 20.436 4.029 -54.483 1.00 25.16 ATOM 5382 CA ASP B 841 20.372 4.116 -55.941 1.00 27.15 ATOM 5383 CB ASP B 841 19.293 5.108 -56.370 1.00 27.74 ATOM 5384 CG ASP B 841 17.912 4.497 -56.357 1.00 29.81 ATOM 5385 OD1 ASP B 841 17.808 3.259 -56.170 1.00 30.11 ATOM 5386 OD2 ASP B 841 16.935 5.262 -56.530 1.00 30.26 ATOM 5387 C ASP B 841 21.695 4.517 -56.575 1.00 27.00 ATOM 5388 O ASP B 841 22.071 3.990 -57.622 1.00 26.83 ATOM 5389 N GLU B 842 22.402 5.446 -55.939 1.00 27.02 ATOM 5390 CA GLU B 842 23.677 5.907 -56.469 1.00 27.11 ATOM 5391 CB GLU B 842 24.286 6.981 -55.558 1.00 28.18 ATOM 5392 CG GLU B 842 25.676 7.404 -56.005 1.00 29.65 ATOM 5393 CD GLU B 842 26.218 8.587 -55.239 1.00 30.87 ATOM 5394 OE1 GLU B 842 25.621 8.957 -54.208 1.00 31.73 ATOM 5395 OE2 GLU B 842 27.250 9.143 -55.668 1.00 31.92 ATOM 5396 C GLU B 842 24.677 4.764 -56.649 1.00 26.49 ATOM 5397 O GLU B 842 25.492 4.780 -57.581 1.00 25.89 ATOM 5398 N LEU B 843 24.624 3.772 -55.763 1.00 25.51 ATOM 5399 CA LEU B 843 25.547 2.639 -55.862 1.00 24.20 ATOM 5400 CB LEU B 843 25.453 1.768 -54.601 1.00 22.66 ATOM 5401 CG LEU B 843 25.768 2.445 -53.252 1.00 22.07 ATOM 5402 CD1 LEU B 843 25.841 1.385 -52.141 1.00 19.64 ATOM 5403 CD2 LEU B 843 27.095 3.220 -53.351 1.00 20.41 ATOM 5404 C LEU B 843 25.271 1.790 -57.107 1.00 23.91 ATOM 5405 O LEU B 843 26.151 1.074 -57.589 1.00 23.84 ATOM 5406 N ARG B 844 24.052 1.883 -57.629 1.00 24.98 ATOM 5407 CA ARG B 844 23.665 1.119 -58.812 1.00 26.62 ATOM 5408 CB ARG B 844 22.190 0.718 -58.711 1.00 25.34 ATOM 5409 CG ARG B 844 21.916 -0.443 -57.741 1.00 23.92 ATOM 5410 CD ARG B 844 20.424 -0.770 -57.664 1.00 22.36 ATOM 5411 NE ARG B 844 19.678 0.190 -56.848 1.00 22.33 ATOM 5412 CZ ARG B 844 19.519 0.097 -55.528 1.00 22.22 ATOM 5413 NH1 ARG B 844 20.055 -0.920 -54.863 1.00 21.18 ATOM 5414 NH2 ARG B 844 18.829 1.022 -54.872 1.00 22.00 ATOM 5415 C ARG B 844 23.928 1.874 -60.125 1.00 28.89 ATOM 5416 O ARG B 844 23.714 1.340 -61.218 1.00 29.61 ATOM 5417 N ASP B 845 24.396 3.115 -60.011 1.00 30.93 ATOM 5418 CA ASP B 845 24.720 3.931 -61.180 1.00 32.20 ATOM 5419 CB ASP B 845 24.996 5.370 -60.757 1.00 33.75 ATOM 5420 CG ASP B 845 25.276 6.279 -61.936 1.00 35.57 ATOM 5421 OD1 ASP B 845 26.125 5.930 -62.785 1.00 36.09 ATOM 5422 OD2 ASP B 845 24.644 7.351 -62.009 1.00 37.44 ATOM 5423 C ASP B 845 25.968 3.339 -61.825 1.00 32.84 ATOM 5424 O ASP B 845 26.976 3.116 -61.156 1.00 32.08 ATOM 5425 N PRO B 846 25.933 3.116 -63.149 1.00 33.75 ATOM 5426 CD PRO B 846 24.841 3.438 -64.083 1.00 34.39 ATOM 5427 CA PRO B 846 27.086 2.535 -63.844 1.00 34.68 ATOM 5428 CB PRO B 846 26.609 2.418 -65.292 1.00 34.28 ATOM 5429 CG PRO B 846 25.543 3.455 -65.415 1.00 35.12 ATOM 5430 C PRO B 846 28.395 3.311 -63.732 1.00 35.47 ATOM 5431 O PRO B 846 29.475 2.725 -63.842 1.00 36.08 ATOM 5432 N ASN B 847 28.316 4.615 -63.502 1.00 35.82 ATOM 5433 CA ASN B 847 29.540 5.402 -63.420 1.00 37.82 ATOM 5434 CB ASN B 847 29.392 6.705 -64.206 1.00 38.82 ATOM 5435 CG ASN B 847 29.040 6.470 -65.660 1.00 39.73 ATOM 5436 OD1 ASN B 847 28.136 7.113 -66.195 1.00 41.48 ATOM 5437 ND2 ASN B 847 29.747 5.542 -66.307 1.00 38.75 ATOM 5438 C ASN B 847 30.015 5.729 -62.023 1.00 38.17 ATOM 5439 O ASN B 847 30.989 6.463 -61.867 1.00 38.33 ATOM 5440 N VAL B 848 29.341 5.196 -61.007 1.00 38.04 ATOM 5441 CA VAL B 848 29.741 5.462 -59.628 1.00 37.84 ATOM 5442 CB VAL B 848 28.768 4.781 -58.621 1.00 37.31 ATOM 5443 CG1 VAL B 848 29.008 3.276 -58.588 1.00 36.21 ATOM 5444 CG2 VAL B 848 28.946 5.388 -57.228 1.00 36.36 ATOM 5445 C VAL B 848 31.173 4.978 -59.368 1.00 38.75 ATOM 5446 O VAL B 848 31.563 3.890 -59.796 1.00 38.76 ATOM 5447 N LYS B 849 31.963 5.799 -58.682 1.00 39.89 ATOM 5448 CA LYS B 849 33.342 5.438 -58.353 1.00 41.18 ATOM 5449 CB LYS B 849 34.320 6.098 -59.338 1.00 41.91 ATOM 5450 CG LYS B 849 34.188 5.621 -60.783 1.00 43.29 ATOM 5451 CD LYS B 849 34.864 4.275 -60.994 1.00 45.14 ATOM 5452 CE LYS B 849 34.542 3.697 -62.372 1.00 46.63 ATOM 5453 NZ LYS B 849 33.068 3.557 -62.605 1.00 47.54 ATOM 5454 C LYS B 849 33.659 5.902 -56.932 1.00 41.23 ATOM 5455 O LYS B 849 32.946 6.736 -56.381 1.00 41.53 ATOM 5456 N LEU B 850 34.709 5.352 -56.332 1.00 41.33 ATOM 5457 CA LEU B 850 35.102 5.771 -54.991 1.00 42.22 ATOM 5458 CB LEU B 850 36.153 4.823 -54.413 1.00 41.39 ATOM 5459 CG LEU B 850 35.723 3.403 -54.046 1.00 41.14 ATOM 5460 CD1 LEU B 850 36.820 2.746 -53.213 1.00 40.60 ATOM 5461 CD2 LEU B 850 34.409 3.440 -53.285 1.00 40.47 ATOM 5462 C LEU B 850 35.716 7.162 -55.134 1.00 43.20 ATOM 5463 O LEU B 850 36.226 7.505 -56.198 1.00 43.40 ATOM 5464 N PRO B 851 35.665 7.986 -54.079 1.00 44.31 ATOM 5465 CD PRO B 851 35.048 7.760 -52.760 1.00 44.48 ATOM 5466 CA PRO B 851 36.255 9.327 -54.189 1.00 45.50 ATOM 5467 CB PRO B 851 36.106 9.906 -52.782 1.00 45.62 ATOM 5468 CG PRO B 851 34.941 9.154 -52.194 1.00 45.19 ATOM 5469 C PRO B 851 37.717 9.287 -54.655 1.00 46.40 ATOM 5470 O PRO B 851 38.160 10.156 -55.401 1.00 46.33 ATOM 5471 N ASN B 852 38.459 8.271 -54.222 1.00 47.45 ATOM 5472 CA ASN B 852 39.857 8.128 -54.620 1.00 48.24 ATOM 5473 CB ASN B 852 40.585 7.149 -53.686 1.00 48.96 ATOM 5474 CG ASN B 852 39.991 5.742 -53.720 1.00 50.25 ATOM 5475 OD1 ASN B 852 40.275 4.915 -52.845 1.00 50.94 ATOM 5476 ND2 ASN B 852 39.167 5.465 -54.728 1.00 50.41 ATOM 5477 C ASN B 852 39.972 7.640 -56.068 1.00 48.53 ATOM 5478 O ASN B 852 40.990 7.065 -56.450 1.00 48.94 ATOM 5479 N GLY B 853 38.920 7.862 -56.857 1.00 48.27 ATOM 5480 CA GLY B 853 38.916 7.447 -58.252 1.00 47.53 ATOM 5481 C GLY B 853 38.813 5.948 -58.494 1.00 47.18 ATOM 5482 O GLY B 853 38.545 5.508 -59.614 1.00 46.93 ATOM 5483 N ARG B 854 39.023 5.157 -57.447 1.00 46.99 ATOM 5484 CA ARG B 854 38.959 3.702 -57.565 1.00 46.46 ATOM 5485 CB ARG B 854 39.572 3.060 -56.319 1.00 48.07 ATOM 5486 CG ARG B 854 39.768 1.564 -56.423 1.00 50.40 ATOM 5487 CD ARG B 854 40.506 1.025 -55.206 1.00 52.40 ATOM 5488 NE ARG B 854 41.609 1.895 -54.795 1.00 53.89 ATOM 5489 CZ ARG B 854 42.588 1.515 -53.976 1.00 54.90 ATOM 5490 NH1 ARG B 854 42.599 0.283 -53.479 1.00 55.18 ATOM 5491 NH2 ARG B 854 43.553 2.366 -53.646 1.00 55.12 ATOM 5492 C ARG B 854 37.540 3.161 -57.779 1.00 45.02 ATOM 5493 O ARG B 854 36.545 3.857 -57.563 1.00 44.56 ATOM 5494 N ASP B 855 37.460 1.910 -58.214 1.00 43.95 ATOM 5495 CA ASP B 855 36.179 1.250 -58.458 1.00 42.60 ATOM 5496 CB ASP B 855 36.395 -0.034 -59.254 1.00 43.82 ATOM 5497 CG ASP B 855 35.994 0.097 -60.707 1.00 45.45 ATOM 5498 OD1 ASP B 855 36.145 -0.906 -61.441 1.00 46.64 ATOM 5499 OD2 ASP B 855 35.533 1.187 -61.115 1.00 46.28 ATOM 5500 C ASP B 855 35.545 0.874 -57.130 1.00 40.88 ATOM 5501 O ASP B 855 36.253 0.628 -56.153 1.00 40.52 ATOM 5502 N THR B 856 34.218 0.824 -57.086 1.00 38.99 ATOM 5503 CA THR B 856 33.538 0.423 -55.859 1.00 37.41 ATOM 5504 CB THR B 856 31.998 0.685 -55.919 1.00 38.21 ATOM 5505 OG1 THR B 856 31.421 -0.023 -57.024 1.00 39.10 ATOM 5506 CG2 THR B 856 31.703 2.167 -56.066 1.00 38.12 ATOM 5507 C THR B 856 33.763 -1.084 -55.725 1.00 35.85 ATOM 5508 O THR B 856 34.182 -1.745 -56.679 1.00 34.92 ATOM 5509 N PRO B 857 33.536 -1.641 -54.530 1.00 34.36 ATOM 5510 CD PRO B 857 33.139 -0.997 -53.269 1.00 33.51 ATOM 5511 CA PRO B 857 33.731 -3.088 -54.381 1.00 33.21 ATOM 5512 CB PRO B 857 33.743 -3.308 -52.866 1.00 33.31 ATOM 5513 CG PRO B 857 33.690 -1.924 -52.244 1.00 34.01 ATOM 5514 C PRO B 857 32.575 -3.837 -55.048 1.00 32.39 ATOM 5515 O PRO B 857 31.655 -3.213 -55.582 1.00 31.42 ATOM 5516 N ALA B 858 32.631 -5.168 -55.020 1.00 31.90 ATOM 5517 CA ALA B 858 31.573 -6.007 -55.595 1.00 31.29 ATOM 5518 CB ALA B 858 31.947 -7.476 -55.451 1.00 31.90 ATOM 5519 C ALA B 858 30.270 -5.724 -54.844 1.00 30.37 ATOM 5520 O ALA B 858 30.219 -5.837 -53.620 1.00 31.23 ATOM 5521 N LEU B 859 29.219 -5.360 -55.569 1.00 29.12 ATOM 5522 CA LEU B 859 27.954 -5.033 -54.927 1.00 28.43 ATOM 5523 CB LEU B 859 27.672 -3.539 -55.085 1.00 27.83 ATOM 5524 CG LEU B 859 28.718 -2.554 -54.560 1.00 28.40 ATOM 5525 CD1 LEU B 859 28.387 -1.159 -55.064 1.00 28.54 ATOM 5526 CD2 LEU B 859 28.737 -2.583 -53.036 1.00 27.90 ATOM 5527 C LEU B 859 26.746 -5.795 -55.444 1.00 27.82 ATOM 5528 O LEU B 859 25.695 -5.807 -54.801 1.00 27.14 ATOM 5529 N PHE B 860 26.890 -6.434 -56.598 1.00 27.68 ATOM 5530 CA PHE B 860 25.760 -7.120 -57.199 1.00 28.19 ATOM 5531 CB PHE B 860 25.391 -6.400 -58.505 1.00 28.86 ATOM 5532 CG PHE B 860 25.543 -4.900 -58.431 1.00 28.80 ATOM 5533 CD1 PHE B 860 26.608 -4.261 -59.063 1.00 28.70 ATOM 5534 CD2 PHE B 860 24.637 -4.130 -57.715 1.00 28.77 ATOM 5535 CE1 PHE B 860 26.769 -2.883 -58.983 1.00 27.86 ATOM 5536 CE2 PHE B 860 24.786 -2.744 -57.628 1.00 29.02 ATOM 5537 CZ PHE B 860 25.857 -2.120 -58.265 1.00 28.27 ATOM 5538 C PHE B 860 25.890 -8.618 -57.447 1.00 28.15 ATOM 5539 O PHE B 860 25.018 -9.205 -58.067 1.00 28.13 ATOM 5540 N ASN B 861 26.952 -9.238 -56.946 1.00 28.63 ATOM 5541 CA ASN B 861 27.143 -10.670 -57.131 1.00 29.54 ATOM 5542 CB ASN B 861 28.632 -11.024 -57.019 1.00 30.79 ATOM 5543 CG ASN B 861 29.281 -10.476 -55.760 1.00 33.30 ATOM 5544 OD1 ASN B 861 30.395 -10.872 -55.404 1.00 34.86 ATOM 5545 ND2 ASN B 861 28.596 -9.563 -55.080 1.00 33.43 ATOM 5546 C ASN B 861 26.317 -11.480 -56.124 1.00 29.84 ATOM 5547 O ASN B 861 26.846 -12.312 -55.379 1.00 29.41 ATOM 5548 N PHE B 862 25.010 -11.228 -56.127 1.00 30.23 ATOM 5549 CA PHE B 862 24.069 -11.899 -55.231 1.00 31.18 ATOM 5550 CB PHE B 862 22.685 -11.242 -55.325 1.00 30.58 ATOM 5551 CG PHE B 862 22.578 -9.913 -54.626 1.00 30.75 ATOM 5552 CD1 PHE B 862 22.251 -9.845 -53.274 1.00 30.05 ATOM 5553 CD2 PHE B 862 22.793 -8.726 -55.323 1.00 30.57 ATOM 5554 CE1 PHE B 862 22.140 -8.612 -52.618 1.00 30.07 ATOM 5555 CE2 PHE B 862 22.686 -7.487 -54.682 1.00 30.60 ATOM 5556 CZ PHE B 862 22.359 -7.430 -53.324 1.00 30.45 ATOM 5557 C PHE B 862 23.921 -13.380 -55.585 1.00 32.31 ATOM 5558 O PHE B 862 23.970 -13.751 -56.761 1.00 33.22 ATOM 5559 N THR B 863 23.748 -14.231 -54.577 1.00 32.44 ATOM 5560 CA THR B 863 23.542 -15.652 -54.840 1.00 32.85 ATOM 5561 CB THR B 863 24.312 -16.571 -53.891 1.00 32.79 ATOM 5562 OG1 THR B 863 23.802 -16.409 -52.560 1.00 33.10 ATOM 5563 CG2 THR B 863 25.802 -16.282 -53.945 1.00 31.97 ATOM 5564 C THR B 863 22.075 -15.965 -54.645 1.00 33.40 ATOM 5565 O THR B 863 21.290 -15.096 -54.239 1.00 33.79 ATOM 5566 N THR B 864 21.702 -17.208 -54.944 1.00 33.03 ATOM 5567 CA THR B 864 20.321 -17.649 -54.794 1.00 32.03 ATOM 5568 CB THR B 864 20.123 -19.082 -55.355 1.00 32.84 ATOM 5569 OG1 THR B 864 20.395 -19.084 -56.765 1.00 32.03 ATOM 5570 CG2 THR B 864 18.678 -19.548 -55.118 1.00 32.15 ATOM 5571 C THR B 864 19.969 -17.631 -53.313 1.00 31.43 ATOM 5572 O THR B 864 18.883 -17.203 -52.917 1.00 31.15 ATOM 5573 N GLN B 865 20.910 -18.092 -52.501 1.00 31.38 ATOM 5574 CA GLN B 865 20.738 -18.132 -51.054 1.00 32.47 ATOM 5575 CB GLN B 865 22.020 -18.646 -50.392 1.00 33.50 ATOM 5576 CG GLN B 865 21.964 -18.704 -48.866 1.00 35.89 ATOM 5577 CD GLN B 865 20.931 -19.699 -48.359 1.00 38.12 ATOM 5578 OE1 GLN B 865 20.617 -20.687 -49.036 1.00 39.66 ATOM 5579 NE2 GLN B 865 20.394 -19.447 -47.166 1.00 37.73 ATOM 5580 C GLN B 865 20.430 -16.721 -50.555 1.00 32.12 ATOM 5581 O GLN B 865 19.418 -16.478 -49.894 1.00 32.08 ATOM 5582 N GLU B 866 21.313 -15.796 -50.903 1.00 31.68 ATOM 5583 CA GLU B 866 21.183 -14.404 -50.509 1.00 31.58 ATOM 5584 CB GLU B 866 22.319 -13.602 -51.136 1.00 32.01 ATOM 5585 CG GLU B 866 22.688 -12.357 -50.379 1.00 33.34 ATOM 5586 CD GLU B 866 23.997 -11.760 -50.858 1.00 33.68 ATOM 5587 OE1 GLU B 866 24.338 -10.668 -50.376 1.00 34.93 ATOM 5588 OE2 GLU B 866 24.683 -12.378 -51.707 1.00 33.96 ATOM 5589 C GLU B 866 19.842 -13.785 -50.891 1.00 30.80 ATOM 5590 O GLU B 866 19.300 -12.961 -50.157 1.00 30.12 ATOM 5591 N LEU B 867 19.305 -14.183 -52.039 1.00 30.74 ATOM 5592 CA LEU B 867 18.033 -13.637 -52.511 1.00 30.59 ATOM 5593 CB LEU B 867 18.051 -13.543 -54.037 1.00 30.14 ATOM 5594 CG LEU B 867 19.123 -12.620 -54.609 1.00 29.78 ATOM 5595 CD1 LEU B 867 19.597 -13.148 -55.947 1.00 30.26 ATOM 5596 CD2 LEU B 867 18.556 -11.223 -54.737 1.00 29.07 ATOM 5597 C LEU B 867 16.803 -14.432 -52.076 1.00 30.65 ATOM 5598 O LEU B 867 15.679 -13.951 -52.191 1.00 30.43 ATOM 5599 N SER B 868 17.020 -15.636 -51.561 1.00 31.25 ATOM 5600 CA SER B 868 15.913 -16.502 -51.156 1.00 31.96 ATOM 5601 CB SER B 868 16.446 -17.656 -50.302 1.00 31.85 ATOM 5602 OG SER B 868 17.138 -17.183 -49.168 1.00 32.92 ATOM 5603 C SER B 868 14.721 -15.845 -50.454 1.00 31.96 ATOM 5604 O SER B 868 13.587 -16.256 -50.664 1.00 31.92 ATOM 5605 N SER B 869 14.957 -14.819 -49.642 1.00 32.38 ATOM 5606 CA SER B 869 13.856 -14.175 -48.926 1.00 32.39 ATOM 5607 CB SER B 869 14.406 -13.202 -47.866 1.00 32.71 ATOM 5608 OG SER B 869 14.502 -11.870 -48.356 1.00 32.24 ATOM 5609 C SER B 869 12.851 -13.449 -49.823 1.00 32.64 ATOM 5610 O SER B 869 11.697 -13.255 -49.440 1.00 32.47 ATOM 5611 N ASN B 870 13.284 -13.048 -51.015 1.00 32.03 ATOM 5612 CA ASN B 870 12.414 -12.330 -51.946 1.00 31.35 ATOM 5613 CB ASN B 870 12.135 -10.923 -51.399 1.00 31.82 ATOM 5614 CG ASN B 870 10.924 -10.266 -52.037 1.00 32.37 ATOM 5615 OD1 ASN B 870 10.513 -10.621 -53.145 1.00 33.32 ATOM 5616 ND2 ASN B 870 10.347 -9.297 -51.340 1.00 31.90 ATOM 5617 C ASN B 870 13.133 -12.256 -53.303 1.00 31.19 ATOM 5618 O ASN B 870 13.648 -11.210 -53.693 1.00 29.79 ATOM 5619 N PRO B 871 13.178 -13.384 -54.036 1.00 31.00 ATOM 5620 CD PRO B 871 12.593 -14.690 -53.672 1.00 30.39 ATOM 5621 CA PRO B 871 13.842 -13.438 -55.344 1.00 30.93 ATOM 5622 CB PRO B 871 13.435 -14.807 -55.889 1.00 31.03 ATOM 5623 CG PRO B 871 13.236 -15.636 -54.650 1.00 30.93 ATOM 5624 C PRO B 871 13.546 -12.297 -56.324 1.00 30.82 ATOM 5625 O PRO B 871 14.456 -11.811 -56.990 1.00 30.23 ATOM 5626 N PRO B 872 12.276 -11.866 -56.435 1.00 30.99 ATOM 5627 CD PRO B 872 11.107 -12.401 -55.716 1.00 31.90 ATOM 5628 CA PRO B 872 11.894 -10.779 -57.346 1.00 31.75 ATOM 5629 CB PRO B 872 10.385 -10.627 -57.134 1.00 31.57 ATOM 5630 CG PRO B 872 9.947 -11.883 -56.512 1.00 31.53 ATOM 5631 C PRO B 872 12.623 -9.453 -57.105 1.00 32.01 ATOM 5632 O PRO B 872 12.688 -8.600 -58.000 1.00 32.39 ATOM 5633 N LEU B 873 13.160 -9.276 -55.900 1.00 31.61 ATOM 5634 CA LEU B 873 13.874 -8.049 -55.563 1.00 31.00 ATOM 5635 CB LEU B 873 14.284 -8.047 -54.084 1.00 30.18 ATOM 5636 CG LEU B 873 13.208 -7.520 -53.129 1.00 30.57 ATOM 5637 CD1 LEU B 873 13.793 -7.301 -51.736 1.00 30.40 ATOM 5638 CD2 LEU B 873 12.637 -6.220 -53.674 1.00 29.94 ATOM 5639 C LEU B 873 15.104 -7.890 -56.435 1.00 30.48 ATOM 5640 O LEU B 873 15.604 -6.785 -56.610 1.00 30.65 ATOM 5641 N ALA B 874 15.582 -8.998 -56.991 1.00 30.88 ATOM 5642 CA ALA B 874 16.762 -8.978 -57.848 1.00 31.43 ATOM 5643 CB ALA B 874 17.087 -10.381 -58.328 1.00 31.11 ATOM 5644 C ALA B 874 16.570 -8.051 -59.038 1.00 31.85 ATOM 5645 O ALA B 874 17.537 -7.518 -59.571 1.00 32.53 ATOM 5646 N THR B 875 15.322 -7.848 -59.452 1.00 32.28 ATOM 5647 CA THR B 875 15.053 -6.969 -60.585 1.00 32.14 ATOM 5648 CB THR B 875 13.568 -6.992 -60.957 1.00 31.98 ATOM 5649 OG1 THR B 875 12.801 -6.379 -59.917 1.00 32.42 ATOM 5650 CG2 THR B 875 13.107 -8.426 -61.143 1.00 30.74 ATOM 5651 C THR B 875 15.488 -5.537 -60.272 1.00 32.52 ATOM 5652 O THR B 875 15.649 -4.714 -61.173 1.00 31.61 ATOM 5653 N ILE B 876 15.681 -5.249 -58.988 1.00 32.45 ATOM 5654 CA ILE B 876 16.123 -3.925 -58.557 1.00 32.31 ATOM 5655 CB ILE B 876 15.312 -3.401 -57.350 1.00 33.00 ATOM 5656 CG2 ILE B 876 15.948 -2.109 -56.808 1.00 33.75 ATOM 5657 CG1 ILE B 876 13.871 -3.127 -57.759 1.00 33.04 ATOM 5658 CD1 ILE B 876 12.999 -2.734 -56.596 1.00 32.93 ATOM 5659 C ILE B 876 17.578 -4.006 -58.112 1.00 31.53 ATOM 5660 O ILE B 876 18.399 -3.179 -58.484 1.00 32.05 ATOM 5661 N LEU B 877 17.882 -5.020 -57.314 1.00 30.22 ATOM 5662 CA LEU B 877 19.219 -5.210 -56.774 1.00 29.46 ATOM 5663 CB LEU B 877 19.223 -6.422 -55.840 1.00 28.63 ATOM 5664 CG LEU B 877 18.338 -6.212 -54.606 1.00 28.01 ATOM 5665 CD1 LEU B 877 18.271 -7.494 -53.805 1.00 27.22 ATOM 5666 CD2 LEU B 877 18.886 -5.062 -53.767 1.00 27.74 ATOM 5667 C LEU B 877 20.325 -5.345 -57.807 1.00 28.97 ATOM 5668 O LEU B 877 21.428 -4.841 -57.604 1.00 28.81 ATOM 5669 N ILE B 878 20.041 -6.036 -58.903 1.00 28.53 ATOM 5670 CA ILE B 878 21.029 -6.213 -59.953 1.00 28.56 ATOM 5671 CB ILE B 878 21.016 -7.655 -60.483 1.00 29.07 ATOM 5672 CG2 ILE B 878 22.194 -7.878 -61.414 1.00 27.72 ATOM 5673 CG1 ILE B 878 21.098 -8.632 -59.304 1.00 28.52 ATOM 5674 CD1 ILE B 878 20.893 -10.071 -59.687 1.00 29.14 ATOM 5675 C ILE B 878 20.693 -5.240 -61.076 1.00 28.91 ATOM 5676 O ILE B 878 19.753 -5.462 -61.832 1.00 29.07 ATOM 5677 N PRO B 879 21.469 -4.146 -61.196 1.00 28.32 ATOM 5678 CD PRO B 879 22.653 -3.817 -60.378 1.00 28.39 ATOM 5679 CA PRO B 879 21.235 -3.137 -62.230 1.00 28.15 ATOM 5680 CB PRO B 879 22.155 -1.986 -61.814 1.00 27.96 ATOM 5681 CG PRO B 879 23.298 -2.673 -61.138 1.00 27.19 ATOM 5682 C PRO B 879 21.531 -3.648 -63.643 1.00 28.34 ATOM 5683 O PRO B 879 22.355 -4.555 -63.833 1.00 27.65 ATOM 5684 N PRO B 880 20.867 -3.060 -64.653 1.00 28.97 ATOM 5685 CD PRO B 880 19.890 -1.961 -64.536 1.00 28.13 ATOM 5686 CA PRO B 880 21.067 -3.469 -66.047 1.00 29.48 ATOM 5687 CB PRO B 880 20.415 -2.348 -66.848 1.00 29.79 ATOM 5688 CG PRO B 880 19.348 -1.822 -65.939 1.00 29.42 ATOM 5689 C PRO B 880 22.521 -3.672 -66.434 1.00 30.41 ATOM 5690 O PRO B 880 22.878 -4.739 -66.925 1.00 31.65 ATOM 5691 N HIS B 881 23.368 -2.670 -66.196 1.00 30.69 ATOM 5692 CA HIS B 881 24.776 -2.781 -66.572 1.00 31.07 ATOM 5693 CB HIS B 881 25.544 -1.484 -66.239 1.00 30.64 ATOM 5694 CG HIS B 881 25.830 -1.285 -64.777 1.00 31.15 ATOM 5695 CD2 HIS B 881 25.130 -0.639 -63.811 1.00 30.39 ATOM 5696 ND1 HIS B 881 26.993 -1.719 -64.179 1.00 30.99 ATOM 5697 CE1 HIS B 881 26.999 -1.354 -62.909 1.00 31.68 ATOM 5698 NE2 HIS B 881 25.879 -0.696 -62.659 1.00 31.44 ATOM 5699 C HIS B 881 25.483 -3.980 -65.969 1.00 31.77 ATOM 5700 O HIS B 881 26.467 -4.456 -66.519 1.00 32.12 ATOM 5701 N ALA B 882 24.985 -4.477 -64.843 1.00 32.87 ATOM 5702 CA ALA B 882 25.595 -5.633 -64.199 1.00 33.72 ATOM 5703 CB ALA B 882 25.211 -5.674 -62.716 1.00 33.99 ATOM 5704 C ALA B 882 25.151 -6.919 -64.898 1.00 34.73 ATOM 5705 O ALA B 882 25.718 -7.987 -64.678 1.00 34.29 ATOM 5706 N ARG B 883 24.139 -6.803 -65.753 1.00 36.29 ATOM 5707 CA ARG B 883 23.618 -7.953 -66.487 1.00 38.13 ATOM 5708 CB ARG B 883 22.097 -7.885 -66.543 1.00 37.15 ATOM 5709 CG ARG B 883 21.445 -7.729 -65.201 1.00 36.39 ATOM 5710 CD ARG B 883 19.949 -7.793 -65.354 1.00 35.76 ATOM 5711 NE ARG B 883 19.273 -7.102 -64.272 1.00 35.07 ATOM 5712 CZ ARG B 883 18.032 -6.650 -64.347 1.00 35.75 ATOM 5713 NH1 ARG B 883 17.330 -6.823 -65.462 1.00 36.15 ATOM 5714 NH2 ARG B 883 17.494 -6.031 -63.308 1.00 35.69 ATOM 5715 C ARG B 883 24.154 -8.045 -67.917 1.00 40.04 ATOM 5716 O ARG B 883 23.766 -8.938 -68.675 1.00 40.32 ATOM 5717 N ILE B 884 25.030 -7.119 -68.288 1.00 42.07 ATOM 5718 CA ILE B 884 25.596 -7.111 -69.632 1.00 44.27 ATOM 5719 CB ILE B 884 26.403 -5.826 -69.875 1.00 42.87 ATOM 5720 CG2 ILE B 884 27.295 -5.989 -71.097 1.00 42.70 ATOM 5721 CG1 ILE B 884 25.440 -4.650 -70.048 1.00 41.80 ATOM 5722 CD1 ILE B 884 26.103 -3.289 -69.996 1.00 41.38 ATOM 5723 C ILE B 884 26.489 -8.327 -69.879 1.00 47.06 ATOM 5724 O ILE B 884 27.400 -8.610 -69.097 1.00 47.20 ATOM 5725 N GLN B 885 26.215 -9.036 -70.978 1.00 50.10 ATOM 5726 CA GLN B 885 26.970 -10.229 -71.364 1.00 52.93 ATOM 5727 CB GLN B 885 26.421 -10.798 -72.677 1.00 53.84 ATOM 5728 CG GLN B 885 25.846 -12.200 -72.569 1.00 55.89 ATOM 5729 CD GLN B 885 25.857 -12.944 -73.895 1.00 57.31 ATOM 5730 OE1 GLN B 885 25.472 -12.401 -74.933 1.00 58.16 ATOM 5731 NE2 GLN B 885 26.301 -14.196 -73.866 1.00 58.61 ATOM 5732 C GLN B 885 28.458 -9.922 -71.525 1.00 54.42 ATOM 5733 O GLN B 885 29.291 -10.433 -70.772 1.00 55.12 ATOM 5734 N ALA B 886 28.780 -9.089 -72.512 1.00 55.96 ATOM 5735 CA ALA B 886 30.160 -8.691 -72.795 1.00 57.60 ATOM 5736 CB ALA B 886 30.801 -8.086 -71.538 1.00 57.79 ATOM 5737 C ALA B 886 31.025 -9.843 -73.328 1.00 58.64 ATOM 5738 O ALA B 886 31.871 -9.573 -74.212 1.00 59.46 ATOM 5739 OT ALA B 886 30.857 -10.998 -72.865 1.00 59.18 HETATM 5740 PB ADP E 430 17.408 13.100 -13.929 1.00 61.10 HETATM 5741 O1B ADP E 430 18.442 12.036 -13.518 1.00 60.04 HETATM 5742 O2B ADP E 430 17.782 13.646 -15.317 1.00 61.69 HETATM 5743 O3B ADP E 430 16.023 12.459 -13.980 1.00 60.74 HETATM 5744 PA ADP E 430 18.343 14.498 -11.509 1.00 57.05 HETATM 5745 O1A ADP E 430 17.481 14.741 -10.281 1.00 55.97 HETATM 5746 O2A ADP E 430 19.253 13.281 -11.326 1.00 57.21 HETATM 5747 O3A ADP E 430 17.417 14.323 -12.864 1.00 58.76 HETATM 5748 O5' ADP E 430 19.249 15.799 -11.769 1.00 55.88 HETATM 5749 C5' ADP E 430 20.196 15.860 -12.880 1.00 52.84 HETATM 5750 C4' ADP E 430 21.540 16.362 -12.355 1.00 50.42 HETATM 5751 O4' ADP E 430 21.286 17.709 -11.859 1.00 48.67 HETATM 5752 C3' ADP E 430 22.098 15.589 -11.120 1.00 49.82 HETATM 5753 O3' ADP E 430 22.752 14.339 -11.346 1.00 50.29 HETATM 5754 C2' ADP E 430 22.924 16.677 -10.450 1.00 48.63 HETATM 5755 O2' ADP E 430 24.265 16.769 -10.921 1.00 48.85 HETATM 5756 C1' ADP E 430 22.086 17.960 -10.680 1.00 47.33 HETATM 5757 N9 ADP E 430 21.247 18.122 -9.460 1.00 44.44 HETATM 5758 C8 ADP E 430 20.008 17.568 -9.073 1.00 43.75 HETATM 5759 N7 ADP E 430 19.423 17.850 -7.869 1.00 42.95 HETATM 5760 C5 ADP E 430 20.402 18.701 -7.411 1.00 41.77 HETATM 5761 C6 ADP E 430 20.533 19.434 -6.151 1.00 41.28 HETATM 5762 N6 ADP E 430 19.599 19.361 -5.198 1.00 41.53 HETATM 5763 N1 ADP E 430 21.617 20.228 -5.929 1.00 40.42 HETATM 5764 C2 ADP E 430 22.592 20.345 -6.841 1.00 39.97 HETATM 5765 N3 ADP E 430 22.655 19.762 -8.022 1.00 40.47 HETATM 5766 C4 ADP E 430 21.523 18.869 -8.371 1.00 42.58 HETATM 5767 PB ADP F 930 34.808 -9.885 -28.875 1.00 52.52 HETATM 5768 O1B ADP F 930 33.741 -8.827 -29.209 1.00 51.07 HETATM 5769 O2B ADP F 930 35.737 -9.332 -27.776 1.00 52.67 HETATM 5770 O3B ADP F 930 34.111 -11.155 -28.381 1.00 52.86 HETATM 5771 PA ADP F 930 35.610 -9.569 -31.686 1.00 48.16 HETATM 5772 O1A ADP F 930 35.534 -10.644 -32.752 1.00 47.98 HETATM 5773 O2A ADP F 930 34.441 -8.586 -31.776 1.00 47.88 HETATM 5774 O3A ADP F 930 35.715 -10.206 -30.172 1.00 49.72 HETATM 5775 O5' ADP F 930 36.980 -8.752 -31.857 1.00 47.03 HETATM 5776 C5' ADP F 930 37.301 -7.658 -30.949 1.00 43.63 HETATM 5777 C4' ADP F 930 37.974 -6.547 -31.727 1.00 41.86 HETATM 5778 O4' ADP F 930 39.147 -7.156 -32.331 1.00 41.39 HETATM 5779 C3' ADP F 930 37.161 -5.992 -32.927 1.00 41.19 HETATM 5780 O3' ADP F 930 36.130 -5.045 -32.640 1.00 41.63 HETATM 5781 C2' ADP F 930 38.288 -5.517 -33.838 1.00 40.66 HETATM 5782 O2' ADP F 930 38.726 -4.178 -33.581 1.00 40.22 HETATM 5783 C1' ADP F 930 39.390 -6.582 -33.631 1.00 39.63 HETATM 5784 N9 ADP F 930 39.234 -7.595 -34.711 1.00 37.78 HETATM 5785 C8 ADP F 930 38.441 -8.762 -34.820 1.00 36.73 HETATM 5786 N7 ADP F 930 38.451 -9.551 -35.943 1.00 36.49 HETATM 5787 C5 ADP F 930 39.372 -8.804 -36.659 1.00 35.73 HETATM 5788 C6 ADP F 930 39.933 -8.985 -38.001 1.00 35.01 HETATM 5789 N6 ADP F 930 39.577 -10.010 -38.772 1.00 34.88 HETATM 5790 N1 ADP F 930 40.842 -8.097 -38.490 1.00 35.52 HETATM 5791 C2 ADP F 930 41.245 -7.036 -37.764 1.00 34.83 HETATM 5792 N3 ADP F 930 40.854 -6.704 -36.547 1.00 34.88 HETATM 5793 C4 ADP F 930 39.856 -7.609 -35.914 1.00 36.26 HETATM 5794 MG MG C 431 20.340 11.243 -12.258 1.00 55.89 HETATM 5795 MG MG D 931 33.081 -6.981 -30.644 1.00 47.98 HETATM 5796 O HOH G 1 26.029 -4.586 -11.822 1.00 21.54 SOLV O HETATM 5797 O HOH G 2 20.160 -2.817 -9.247 1.00 20.26 SOLV O HETATM 5798 O HOH G 3 24.313 12.102 15.276 1.00 17.67 SOLV O HETATM 5799 O HOH G 4 7.670 -0.677 -12.732 1.00 23.0 SOLV O HETATM 5800 O HOH G 5 13.945 -14.664 -36.899 1.00 25.3 SOLV O HETATM 5801 O HOH G 6 17.526 -1.865 -19.900 1.00 2175 SOLV O HETATM 5802 O HOH G 7 21.950 4.595 -30.543 1.00 15.68 SOLV O HETATM 5803 O HOH G 8 22.133 -6.663 -33.403 1.00 18.58 SOLV O HETATM 5804 O HOH G 9 14.719 6.965 -8.553 1.00 20.29 SOLV O HETATM 5805 O HOH G 10 17.278 -13.182 -48.440 1.00 34.32 SOLV O HETATM 5806 O HOH G 11 22.328 -5.624 -23.356 1.00 21.75 SOLV O HETATM 5807 O HOH G 12 21.101 -6.047 -20.773 1.00 27.16 SOLV O HETATM 5808 O HOH G 13 18.550 18.625 1.730 1.00 28.03 SOLV O HETATM 5809 O HOH G 14 19.310 0.840 -7.707 1.00 15.80 SOLV O HETATM 5810 O HOH G 15 23.319 5.058 -32.954 1.00 22.72 SOLV O HETATM 5811 O HOH G 16 29.972 -1.761 -11.748 1.00 19.26 SOLV O HETATM 5812 O HOH G 17 26.274 3.723 13.628 1.00 16.59 SOLV O HETATM 5813 O HOH G 18 17.716 -12.878 -45.909 1.00 27.92 SOLV O HETATM 5814 O HOH G 19 38.055 7.167 -7.511 1.00 25.83 SOLV O HETATM 5815 O HOH G 20 9.981 -9.233 -36.856 1.00 26.75 SOLV O HETATM 5816 O HOH G 21 30.875 -0.098 -9.910 1.00 19.53 SOLV O HETATM 5817 O HOH G 22 15.729 -3.400 2.394 1.00 21.49 SOLV O HETATM 5818 O HOH G 23 14.584 -0.373 6.289 1.00 21.00 SOLV O HETATM 5819 O HOH G 24 24.862 13.153 7.666 1.00 17.17 SOLV O HETATM 5820 O HOH G 25 29.747 2.674 -30.762 1.00 28.38 SOLV O HETATM 5821 O HOH G 26 17.114 -2.050 6.301 1.00 20.24 SOLV O HETATM 5822 O HOH G 27 35.077 -8.874 -13.496 1.00 32.54 SOLV O HETATM 5823 O HOH G 28 23.878 9.842 8.559 1.00 21.02 SOLV O HETATM 5824 O HOH G 29 16.257 3.915 -13.968 1.00 20.35 SOLV O HETATM 5825 O HOH G 30 8.827 -6.170 -8.493 1.00 36.58 SOLV O HETATM 5826 O HOH G 31 24.592 -2.805 -15.147 1.00 36.23 SOLV O HETATM 5827 O HOH G 32 18.543 -9.231 0.898 1.00 27.58 SOLV O HETATM 5828 O HOH G 33 13.401 -6.658 -40.467 1.00 23.94 SOLV O HETATM 5829 O HOH G 34 35.332 -12.459 -46.672 1.00 30.89 SOLV O HETATM 5830 O HOH G 35 15.376 -9.645 -2.040 1.00 25.02 SOLV O HETATM 5831 O HOH G 36 25.961 20.222 4.491 1.00 40.06 SOLV O HETATM 5832 O HOH G 37 9.849 -9.577 -32.406 1.00 24.25 SOLV O HETATM 5833 O HOH G 38 36.383 -11.308 -35.094 1.00 35.84 SOLV O HETATM 5834 O HOH G 39 13.330 -9.648 -48.175 1.00 24.31 SOLV O HETATM 5835 O HOH G 40 29.174 -10.576 -29.893 1.00 25.01 SOLV O HETATM 5836 O HOH G 41 23.610 -18.525 -16.802 1.00 50.22 SOLV O HETATM 5837 O HOH G 42 5.104 4.245 -6.075 1.00 27.04 SOLV O HETATM 5838 O HOH G 43 14.790 14.700 3.183 1.00 18.65 SOLV O HETATM 5839 O HOH G 44 31.474 8.960 16.537 1.00 26.81 SOLV O HETATM 5840 O HOH G 45 15.244 -3.764 5.208 1.00 36.35 SOLV O HETATM 5841 O HOH G 46 25.957 -6.207 10.016 1.00 36.37 SOLV O HETATM 5842 O HOH G 47 12.383 -8.902 -33.180 1.00 24.66 SOLV O HETATM 5843 O HOH G 48 37.092 14.925 -0.710 1.00 39.32 SOLV O HETATM 5844 O HOH G 49 43.655 16.120 9.307 1.00 34.77 SOLV O HETATM 5845 O HOH G 50 18.692 -0.182 -17.551 1.00 24.94 SOLV O HETATM 5846 O HOH G 51 37.414 16.641 5.043 1.00 25.93 SOLV O HETATM 5847 O HOH G 52 7.407 3.128 -35.149 1.00 28.32 SOLV O HETATM 5848 O HOH G 53 10.387 20.287 3.298 1.00 45.78 SOLV O HETATM 5849 O HOH G 54 14.726 -0.442 8.833 1.00 28.22 SOLV O HETATM 5850 O HOH G 55 34.730 -12.669 -36.067 1.00 27.95 SOLV O HETATM 5851 O HOH G 56 11.983 0.530 -50.032 1.00 43.51 SOLV O HETATM 5852 O HOH G 57 19.057 -6.390 0.727 1.00 26.57 SOLV O HETATM 5853 O HOH G 58 39.147 -3.899 8.108 1.00 33.96 SOLV O HETATM 5854 O HOH G 59 22.156 -4.659 -18.205 1.00 34.46 SOLV O HETATM 5855 O HOH G 60 23.197 15.509 7.738 1.00 35.00 SOLV O HETATM 5856 O HOH G 61 19.325 8.569 -53.891 1.00 40.27 SOLV O HETATM 5857 O HOH G 62 39.206 4.002 -1.608 1.00 25.56 SOLV O HETATM 5858 O HOH G 63 33.426 -14.605 -34.930 1.00 28.49 SOLV O HETATM 5859 O HOH G 64 22.041 -3.223 -55.559 1.00 27.55 SOLV O HETATM 5860 O HOH G 65 29.369 -6.839 -58.546 1.00 31.64 SOLV O HETATM 5861 O HOH G 66 40.556 -3.336 -35.634 1.00 47.33 SOLV O HETATM 5862 O HOH G 67 25.005 16.954 9.911 1.00 30.21 SOLV O HETATM 5863 O HOH G 68 7.575 10.773 -11.817 1.00 37.15 SOLV O HETATM 5864 O HOH G 69 15.660 -8.227 -5.793 1.00 23.76 SOLV O HETATM 5865 O HOH G 70 16.368 -10.108 -46.118 1.00 27.05 SOLV O HETATM 5866 O HOH G 71 37.140 -1.060 -54.358 1.00 38.75 SOLV O HETATM 5867 O HOH G 72 27.440 -17.757 -31.505 1.00 24.56 SOLV O HETATM 5868 O HOH G 73 27.388 -12.133 -32.605 1.00 22.49 SOLV O HETATM 5869 O HOH G 74 31.134 10.394 -37.281 1.00 27.31 SOLV O HETATM 5870 O HOH G 75 31.606 -11.789 -28.423 1.00 50.15 SOLV O HETATM 5871 O HOH G 76 32.926 -15.130 -45.266 1.00 32.85 SOLV O HETATM 5872 O HOH G 77 13.665 -15.617 -29.678 1.00 32.36 SOLV O HETATM 5873 O HOH G 78 25.177 -4.424 -30.336 1.00 36.55 SOLV O HETATM 5874 O HOH G 79 13.781 13.694 -7.070 1.00 26.97 SOLV O HETATM 5875 O HOH G 80 29.301 6.144 -12.926 1.00 30.12 SOLV O HETATM 5876 O HOH G 81 18.842 -5.058 -31.409 1.00 20.55 SOLV O HETATM 5877 O HOH G 82 36.209 5.315 -8.128 1.00 25.73 SOLV O HETATM 5878 O HOH G 83 18.103 16.933 3.745 1.00 25.08 SOLV O HETATM 5879 O HOH G 84 18.537 1.414 -29.702 1.00 19.46 SOLV O HETATM 5880 O HOH G 85 22.274 11.066 -51.522 1.00 40.54 SOLV O HETATM 5881 O HOH G 86 18.816 -1.416 -22.488 1.00 30.89 SOLV O HETATM 5882 O HOH G 87 35.807 -6.717 -11.997 1.00 40.42 SOLV O HETATM 5883 O HOH G 88 30.240 17.780 9.308 1.00 27.51 SOLV O HETATM 5884 O HOH G 89 19.474 -10.305 5.139 1.00 45.75 SOLV O HETATM 5885 O HOH G 90 18.531 1.795 -58.737 1.00 39.97 SOLV O HETATM 5886 O HOH G 91 9.274 24.412 3.011 1.00 39.79 SOLV O HETATM 5887 O HOH G 92 21.111 4.170 -60.155 1.00 48.79 SOLV O HETATM 5888 O HOH G 93 37.247 -11.867 -45.056 1.00 33.27 SOLV O HETATM 5889 O HOH G 94 17.796 -4.697 8.835 1.00 34.76 SOLV O HETATM 5890 O HOH G 95 15.668 -10.887 -41.879 1.00 28.26 SOLV O HETATM 5891 O HOH G 96 39.637 0.550 7.887 1.00 34.09 SOLV O HETATM 5892 O HOH G 97 29.662 8.225 -33.362 1.00 36.73 SOLV O HETATM 5893 O HOH G 98 41.181 7.482 5.605 1.00 31.20 SOLV O HETATM 5894 O HOH G 99 39.601 6.825 -34.221 1.00 51.44 SOLV O HETATM 5895 O HOH G 100 26.856 -14.894 -4.426 1.00 29.93 SOLV O HETATM 5896 O HOH G 101 21.755 3.036 -11.313 1.00 39.15 SOLV O HETATM 5897 O HOH G 102 14.047 -11.431 -8.553 1.00 31.77 SOLV O HETATM 5898 O HOH G 103 9.008 8.034 -9.044 1.00 25.33 SOLV O HETATM 5899 O HOH G 104 -2.770 20.309 4.313 1.00 60.38 SOLV O HETATM 5900 O HOH G 105 10.861 -5.106 -1.700 1.00 24.36 SOLV O HETATM 5901 O HOH G 106 28.587 -6.059 -51.271 1.00 25.59 SOLV O HETATM 5902 O HOH G 107 6.377 -8.852 -8.163 1.00 48.75 SOLV O HETATM 5903 O HOH G 108 16.088 14.736 -6.430 1.00 31.75 SOLV O HETATM 5904 O HOH G 109 35.215 5.473 -10.879 1.00 36.94 SOLV O HETATM 5905 O HOH G 110 13.049 3.265 -51.822 1.00 41.27 SOLV O HETATM 5906 O HOH G 111 38.298 18.608 3.073 1.00 34.08 SOLV O HETATM 5907 O HOH G 112 17.375 12.129 9.583 1.00 35.22 SOLV O HETATM 5908 O HOH G 113 35.956 1.100 10.587 1.00 24.95 SOLV O HETATM 5909 O HOH G 114 30.509 -6.614 10.653 1.00 35.30 SOLV O HETATM 5910 O HOH G 115 32.882 6.065 -33.338 1.00 44.15 SOLV O HETATM 5911 O HOH G 116 33.393 14.157 15.002 1.00 37.52 SOLV O HETATM 5912 O HOH G 117 16.220 8.039 -11.724 1.00 29.65 SOLV O HETATM 5913 O HOH G 118 25.680 -9.395 -27.213 1.00 23.28 SOLV O HETATM 5914 O HOH G 119 30.551 -19.329 -28.963 1.00 38.48 SOLV O HETATM 5915 O HOH G 120 14.449 -10.669 -6.040 1.00 26.21 SOLV O HETATM 5916 O HOH G 121 16.747 -5.334 1.216 1.00 32.85 SOLV O HETATM 5917 O HOH G 122 31.061 -7.191 -29.387 1.00 40.82 SOLV O HETATM 5918 O HOH G 123 13.362 14.509 0.831 1.00 32.89 SOLV O HETATM 5919 O HOH G 124 37.787 -1.444 8.235 1.00 38.71 SOLV O HETATM 5920 O HOH G 125 31.970 -5.576 -51.130 1.00 26.21 SOLV O HETATM 5921 O HOH G 126 15.678 -1.299 20.173 1.00 35.45 SOLV O HETATM 5922 O HOH G 127 23.969 -15.673 -3.418 1.00 45.66 SOLV O HETATM 5923 O HOH G 128 29.240 8.892 -35.934 1.00 32.01 SOLV O HETATM 5924 O HOH G 129 40.138 7.018 -41.053 1.00 53.26 SOLV O HETATM 5925 O HOH G 130 28.008 -8.457 -26.318 1.00 32.30 SOLV O HETATM 5926 O HOH G 131 10.925 -6.887 -40.144 1.00 31.05 SOLV O HETATM 5927 O HOH G 132 24.938 21.587 0.871 1.00 46.89 SOLV O HETATM 5928 O HOH G 133 22.553 -21.482 -33.235 1.00 35.15 SOLV O HETATM 5929 O HOH G 134 5.036 -3.147 -7.043 1.00 33.75 SOLV O HETATM 5930 O HOH G 135 21.719 1.607 -62.840 1.00 36.47 SOLV O HETATM 5931 O HOH G 136 37.283 -0.292 -33.202 1.00 33.08 SOLV O HETATM 5932 O HOH G 137 16.874 -16.815 -54.355 1.00 35.18 SOLV O HETATM 5933 O HOH G 138 36.730 20.819 3.190 1.00 49.30 SOLV O HETATM 5934 O HOH G 139 8.851 12.752 -12.579 1.00 38.63 SOLV O HETATM 5935 O HOH G 140 27.908 14.050 -11.329 1.00 37.47 SOLV O HETATM 5936 O HOH G 141 29.849 -3.439 14.151 1.00 35.84 SOLV O HETATM 5937 O HOH G 142 12.287 -16.395 -35.636 1.00 43.09 SOLV O HETATM 5938 O HOH G 143 30.093 -3.366 -58.089 1.00 48.47 SOLV O HETATM 5939 O HOH G 144 22.785 0.072 -65.107 1.00 33.54 SOLV O HETATM 5940 O HOH G 145 27.390 11.240 -42.698 1.00 34.86 SOLV O HETATM 5941 O HOH G 146 11.394 16.062 1.043 1.00 29.50 SOLV O HETATM 5942 O HOH G 147 7.000 -6.086 -6.325 1.00 29.17 SOLV O HETATM 5943 O HOH G 148 14.250 -11.949 -3.432 1.00 39.75 SOLV O HETATM 5944 O HOH G 149 31.146 8.604 -58.499 1.00 35.07 SOLV O HETATM 5945 O HOH G 150 15.908 -20.087 -31.105 1.00 32.86 SOLV O HETATM 5946 O HOH G 151 20.158 -4.263 25.152 1.00 51.08 SOLV O HETATM 5947 O HOH G 152 15.083 -9.683 0.410 1.00 35.64 SOLV O HETATM 5948 O HOH G 153 29.408 11.569 -50.814 1.00 37.81 SOLV O HETATM 5949 O HOH G 154 8.929 -6.776 -2.462 1.00 37.77 SOLV O HETATM 5950 O HOH G 155 13.937 -5.839 5.645 1.00 41.71 SOLV O HETATM 5951 O HOH G 156 16.296 11.346 -29.152 1.00 40.31 SOLV O HETATM 5952 O HOH G 157 27.293 -4.612 -14.504 1.00 39.47 SOLV O HETATM 5953 O HOH G 158 21.481 7.242 -53.851 1.00 32.11 SOLV O HETATM 5954 O HOH G 159 25.124 6.194 -15.118 1.00 44.86 SOLV O HETATM 5955 O HOH G 160 43.821 -28.201 -33.390 1.00 36.20 SOLV O HETATM 5956 O HOH G 161 16.410 -14.993 -40.058 1.00 24.09 SOLV O HETATM 5957 O HOH G 162 27.160 0.621 -60.166 1.00 31.74 SOLV O HETATM 5958 O HOH G 163 12.385 -13.488 -39.187 1.00 35.51 SOLV O HETATM 5959 O HOH G 164 17.954 -1.328 21.611 1.00 34.21 SOLV O HETATM 5960 O HOH G 165 30.999 0.023 16.735 1.00 33.88 SOLV O HETATM 5961 O HOH G 166 11.028 -9.105 -48.737 1.00 39.64 SOLV O HETATM 5962 O HOH G 167 28.178 18.293 12.827 1.00 53.86 SOLV O HETATM 5963 O HOH G 168 11.983 -16.268 -33.089 1.00 47.54 SOLV O HETATM 5964 O HOH G 169 36.802 -1.483 10.958 1.00 43.87 SOLV O HETATM 5965 O HOH G 170 29.487 -12.631 -51.507 1.00 40.29 SOLV O HETATM 5966 O HOH G 171 27.224 -13.520 -52.255 1.00 38.50 SOLV O HETATM 5967 O HOH G 172 27.406 0.864 -26.709 1.00 47.26 SOLV O HETATM 5968 O HOH G 173 11.341 -2.092 0.804 1.00 27.47 SOLV O HETATM 5969 O HOH G 174 12.878 -3.801 2.055 1.00 36.57 SOLV O HETATM 5970 O HOH G 175 8.524 8.294 -11.512 1.00 40.76 SOLV O HETATM 5971 O HOH G 176 39.792 8.110 13.386 1.00 41.53 SOLV O HETATM 5972 O HOH G 177 8.710 -6.268 -44.028 1.00 46.10 SOLV O HETATM 5973 O HOH G 178 9.608 10.446 8.075 1.00 37.18 SOLV O HETATM 5974 O HOH G 179 14.752 -13.557 -41.320 1.00 34.86 SOLV O HETATM 5975 O HOH G 180 41.329 15.892 11.468 1.00 34.41 SOLV O HETATM 5976 O HOH G 181 28.737 -22.463 -46.681 1.00 60.45 SOLV O HETATM 5977 O HOH G 182 23.791 -22.704 -36.496 1.00 49.58 SOLV O HETATM 5978 O HOH G 183 5.783 0.875 -35.872 1.00 38.48 SOLV O HETATM 5979 O HOH G 184 11.404 3.193 18.984 1.00 37.63 SOLV O HETATM 5980 O HOH G 185 7.813 -13.487 -12.492 1.00 46.26 SOLV O HETATM 5981 O HOH G 186 14.823 -11.915 -44.434 1.00 42.72 SOLV O HETATM 5982 O HOH G 187 26.398 3.706 -15.896 1.00 46.07 SOLV O HETATM 5983 O HOH G 188 25.695 1.508 21.739 1.00 44.76 SOLV O HETATM 5984 O HOH G 189 19.865 9.676 -51.421 1.00 42.76 SOLV O HETATM 5985 O HOH G 190 17.678 -7.271 9.499 1.00 44.68 SOLV O HETATM 5986 O HOH G 191 7.941 -9.696 -34.518 1.00 39.03 SOLV O HETATM 5987 O HOH G 192 13.107 -18.480 -51.957 1.00 39.19 SOLV O HETATM 5988 O HOH G 193 29.899 10.402 -39.502 1.00 35.70 SOLV O HETATM 5989 O HOH G 194 39.893 -27.804 -47.049 1.00 58.74 SOLV O HETATM 5990 O HOH G 195 9.624 7.252 13.582 1.00 36.73 SOLV O HETATM 5991 O HOH G 196 18.251 -22.038 -46.291 1.00 52.89 SOLV O HETATM 5992 O HOH G 197 4.886 10.368 -12.537 1.00 40.97 SOLV O HETATM 5993 O HOH G 198 32.854 -16.066 -42.712 1.00 35.54 SOLV O HETATM 5994 O HOH G 199 38.618 14.613 -42.856 1.00 51.57 SOLV O HETATM 5995 O HOH G 200 29.786 -12.075 -2.995 1.00 39.60 SOLV O HETATM 5996 O HOH G 201 14.822 -3.926 20.187 1.00 45.67 SOLV O HETATM 5997 O HOH G 202 10.454 5.229 -37.706 1.00 35.02 SOLV O HETATM 5998 O HOH G 203 35.277 -14.388 -48.350 1.00 44.75 SOLV O HETATM 5999 O HOH G 204 25.473 14.283 -11.597 1.00 51.11 SOLV O HETATM 6000 O HOH G 205 5.874 10.176 5.774 1.00 48.65 SOLV O HETATM 6001 O HOH G 206 4.456 29.607 -11.365 1.00 50.33 SOLV O HETATM 6002 O HOH G 207 24.822 10.661 -28.525 1.00 46.59 SOLV O HETATM 6003 O HOH G 208 27.994 12.537 14.358 1.00 42.97 SOLV O HETATM 6004 O HOH G 209 17.259 16.204 -7.998 1.00 44.30 SOLV O HETATM 6005 O HOH G 210 9.433 -3.171 -0.861 1.00 37.98 SOLV O HETATM 6006 O HOH G 211 28.334 -7.890 9.961 1.00 35.48 SOLV O HETATM 6007 O HOH G 212 43.475 -6.797 1.298 1.00 58.14 SOLV O HETATM 6008 O HOH G 213 33.158 -18.354 -28.761 1.00 36.90 SOLV O HETATM 6009 O HOH G 214 27.557 19.085 9.585 1.00 43.98 SOLV O HETATM 6010 O HOH G 215 9.859 4.537 -14.797 1.00 52.70 SOLV O HETATM 6011 O HOH G 216 8.733 5.398 -11.271 1.00 51.52 SOLV O HETATM 6012 O HOH G 217 29.175 15.442 -13.650 1.00 42.00 SOLV O HETATM 6013 O HOH G 218 31.718 -4.738 -23.028 1.00 45.11 SOLV O HETATM 6014 O HOH G 219 13.171 -1.410 -50.567 1.00 32.69 SOLV O HETATM 6015 O HOH G 220 39.887 10.858 12.927 1.00 47.73 SOLV O HETATM 6016 O HOH G 221 13.270 -17.635 -31.529 1.00 40.88 SOLV O HETATM 6017 O HOH G 222 20.906 16.272 -50.556 1.00 51.48 SOLV O HETATM 6018 O HOH G 223 33.880 -7.502 -51.356 1.00 34.20 SOLV O HETATM 6019 O HOH G 224 31.732 3.276 19.976 1.00 39.49 SOLV O HETATM 6020 O HOH G 225 24.706 16.267 -37.998 1.00 54.82 SOLV O HETATM 6021 O HOH G 226 31.318 5.595 22.437 1.00 40.83 SOLV O HETATM 6022 O HOH G 227 32.563 -8.727 -20.111 1.00 60.87 SOLV O HETATM 6023 O HOH G 228 20.619 13.211 -15.345 1.00 54.18 SOLV O HETATM 6024 O HOH G 229 20.817 -0.087 -26.115 1.00 40.05 SOLV O HETATM 6025 O HOH G 230 24.841 -17.415 -28.900 1.00 45.40 SOLV O HETATM 6026 O HOH G 231 33.868 -18.246 -42.815 1.00 36.65 SOLV O HETATM 6027 O HOH G 232 34.338 -16.523 -47.111 1.00 35.29 SOLV O HETATM 6028 O HOH G 233 36.506 -2.373 -32.127 1.00 38.95 SOLV O HETATM 6029 O HOH G 234 10.375 -17.334 -28.998 1.00 43.24 SOLV O HETATM 6030 O HOH G 235 14.388 10.719 -13.092 1.00 55.51 SOLV O HETATM 6031 O HOH G 236 3.032 30.179 -9.393 1.00 40.59 SOLV O HETATM 6032 O HOH G 237 36.747 16.725 1.181 1.00 39.63 SOLV O HETATM 6033 O HOH G 238 4.047 6.388 -4.224 1.00 48.71 SOLV O HETATM 6034 O HOH G 239 2.763 12.040 -1.090 1.00 38.86 SOLV O HETATM 6035 O HOH G 240 12.886 -2.176 5.435 1.00 38.92 SOLV O HETATM 6036 O HOH G 241 11.908 0.563 15.094 1.00 33.17 SOLV O HETATM 6037 O HOH G 242 9.368 -0.734 15.031 1.00 32.40 SOLV O HETATM 6038 O HOH G 243 8.621 -7.146 -4.995 1.00 40.44 SOLV O HETATM 6039 O HOH G 244 6.842 -11.117 -12.054 1.00 45.13 SOLV O HETATM 6040 O HOH G 245 10.567 -12.593 -12.924 1.00 45.30 SOLV O HETATM 6041 O HOH G 246 20.903 19.753 5.355 1.00 50.63 SOLV O HETATM 6042 O HOH G 247 7.984 22.126 3.438 1.00 47.92 SOLV O HETATM 6043 O HOH G 248 29.802 -13.684 0.952 1.00 55.29 SOLV O HETATM 6044 O HOH G 249 41.761 -35.744 -40.022 1.00 59.66 SOLV O HETATM 6045 O HOH G 250 44.802 0.485 -39.044 1.00 54.56 SOLV O HETATM 6046 O HOH G 251 24.622 7.331 -64.792 1.00 59.18 SOLV O HETATM 6047 O HOH G 252 22.296 10.118 -55.442 1.00 47.44 SOLV O HETATM 6048 O HOH G 253 29.908 -19.263 -23.525 1.00 64.78 SOLV O HETATM 6049 O HOH G 254 28.339 26.296 -3.818 1.00 44.40 SOLV O HETATM 6050 O HOH G 255 4.646 5.336 -1.633 1.00 55.60 SOLV O HETATM 6051 O HOH G 256 41.037 -10.178 -47.896 1.00 57.38 SOLV O HETATM 6052 O HOH G 257 11.285 -11.440 -42.537 1.00 57.08 SOLV O HETATM 6053 O HOH G 258 13.281 -18.584 -38.002 1.00 59.44 SOLV O HETATM 6054 O HOH G 259 33.683 6.613 -29.496 1.00 54.25 SOLV O HETATM 6055 O HOH G 260 6.876 -8.809 -18.740 1.00 56.48 SOLV O HETATM 6056 O HOH G 261 29.950 -3.042 16.937 1.00 48.71 SOLV O HETATM 6057 O HOH G 262 5.811 2.020 7.387 1.00 50.20 SOLV O HETATM 6058 O HOH G 263 12.224 -6.188 0.235 1.00 39.10 SOLV O HETATM 6059 O HOH G 264 16.430 9.881 10.565 1.00 52.30 SOLV O HETATM 6060 O HOH G 265 32.873 1.610 -59.534 1.00 48.93 SOLV O HETATM 6061 O HOH G 266 22.797 -2.235 -21.289 1.00 49.64 SOLV O HETATM 6062 O HOH G 267 17.045 -16.295 -56.955 1.00 53.84 SOLV O END
【0055】
【表2】表2 ADPと相互作用しているTPK I のアミノ酸残基の各原子とその相互作用の 距離、および相互作用の様式 TPK I ADP 距離(Å) 様式 I62 O O4' 4.38 ESI G65 N O1B 4.83 ESI G65 N O2B 4.44 ESI G65 O O1B 4.80 ESI G65 O O2B 4.91 ESI S66 N O1B 3.05 ESI S66 N O2B 4.21 ESI S66 OG O1B 4.75 ESI P67 N O2B 4.50 ESI G68 N O2B 4.75 ESI V70 CB O4' 4.00 VDW V70 CG2 O4' 3.84 VDW V70 CG2 C5 3.85 VDW V70 CG2 O5 3.76 VDW A83 CB N1 3.72 VDW A83 CB C5 3.86 VDW A83 CB C6 3.52 VDW A83 CB N6 3.75 VDW K85 NZ O1A 2.67 ESI K85 NZ O2A 4.89 ESI K85 NZ O3A 4.44 ESI K85 NZ O2B 3.56 ESI K85 NZ O3B 3.20 HYD E97 OE1 O1A 4.85 ESI V110 CG2 N6 3.39 VDW L132 CB N6 3.73 VDW L132 CD1 N6 3.98 VDW L132 CD1 N7 3.92 VDW L132 O N6 4.69 ESI D133 N N6 4.47 ESI D133 O N1 3.42 ESI D133 O N6 2.53 HYD Y134 N N1 4.42 ESI Y134 N N6 4.49 ESI Y134 CA N1 3.49 VDW Y134 CD2 N1 3.88 VDW Y134 CD2 C2 3.55 VDW Y134 CE2 C2 3.76 VDW Y134 C N1 3.66 VDW Y134 O N1 4.84 ESI V135 N N1 2.91 HYD V135 N C2 3.28 VDW V135 N N3 4.54 ESI V135 N N6 4.36 ESI V135 CA N1 3.88 VDW V135 C C2 3.78 VDW V135 O N1 3.61 ESI V135 O C2 2.92 VDW V135 O N3 3.55 VDW V135 O N3 2.57 3.50 WMH 291 E137 O N3 2.89 3.50 WMH 291 T138 OG1 O2' 2.78 2.44 2.88 WMH 189 371 T138 OG1 O3' 2.78 2.44 2.75 WMH 189 371 R141 NH2 N3 2.51 3.21 WMH 331 R141 NH2 O2' 3.31 ESI R141 NH2 O2' 2.51 3.33 WMH 331 D181 OD2 O2A 2.50 2.57 2.81 MWMB 357 431 K183 NZ O2A 3.17 2.57 2.81 MWMB 357 431 Q185 O O2' 3.45 2.88 WMH 371 Q185 O O3' 3.40 ESI Q185 O O3' 3.45 2.75 WMH 371 N186 OD1 O2' 2.41 2.81 MMB 431 N186 OD1 O3' 4.56 ESI N186 OD1 O2A 3.44 ESI L188 CD1 C5 3.83 VDW L188 CD1 C6 3.66 VDW L188 CD1 N6 3.79 VDW C199 SG N7 4.70 ESI C199 SG O2A 4.03 ESI D200 N O1A 4.74 ESI D200 N O2A 4.45 ESI D200 OD1 O1A 3.78 ESI D200 OD1 O2A 4.16 ESI D200 OD1 O3A 4.35 ESI D200 OD1 O2B 4.97 ESI D200 OD1 O3B 2.72 HYD D200 OD2 O1A 4.12 ESI D200 OD2 O2A 3.25 ESI D200 OD2 O2A 2.59 2.81 MMB 431 D200 OD2 O2A 2.88 2.57 2.81 MWMB 357 431 D200 OD2 O3A 3.55 ESI D200 OD2 O1B 4.42 ESID200 OD2 O3B 2.99 ESI
【0056】
【表3】 表3 TPK IとAMPPNPの複合体結晶から得られた3次元構造座標 CRYST 82.790 86.260 178.370 90.00 90.00 90.00 P212121 ATOM 1 CB SER A 35 19.645 42.301 -9.939 1.00 61.79 ATOM 2 OG SER A 35 20.308 43.405 -10.536 1.00 62.82 ATOM 3 C SER A 35 18.051 40.849 -11.201 1.00 60.50 ATOM 4 O SER A 35 17.169 41.383 -10.525 1.00 61.03 ATOM 5 N SER A 35 20.264 41.408 -12.172 1.00 61.63 ATOM 6 CA SER A 35 19.523 41.119 -10.910 1.00 61.18 ATOM 7 N LYS A 36 17.790 40.022 -12.211 1.00 59.21 ATOM 8 CA LYS A 36 16.420 39.681 -12.581 1.00 57.74 ATOM 9 CB LYS A 36 16.389 38.982 -13.942 1.00 58.45 ATOM 10 CG LYS A 36 14.996 38.572 -14.395 1.00 59.38 ATOM 11 CD LYS A 36 14.925 37.078 -14.669 1.00 60.25 ATOM 12 CE LYS A 36 14.108 36.777 -15.914 1.00 60.96 ATOM 13 NZ LYS A 36 14.627 35.586 -16.650 1.00 61.69 ATOM 14 C LYS A 36 15.801 38.771 -11.528 1.00 56.36 ATOM 15 O LYS A 36 16.261 37.647 -11.312 1.00 56.38 ATOM 16 N VAL A 37 14.759 39.263 -10.869 1.00 54.17 ATOM 17 CA VAL A 37 14.087 38.486 -9.840 1.00 51.58 ATOM 18 CB VAL A 37 13.643 39.386 -8.675 1.00 51.42 ATOM 19 CG1 VAL A 37 12.979 38.548 -7.590 1.00 51.14 ATOM 20 CG2 VAL A 37 14.843 40.133 -8.118 1.00 51.25 ATOM 21 C VAL A 37 12.867 37.764 -10.402 1.00 49.89 ATOM 22 O VAL A 37 12.142 38.308 -11.238 1.00 49.77 ATOM 23 N THR A 38 12.664 36.528 -9.953 1.00 47.17 ATOM 24 CA THR A 38 11.524 35.725 -10.374 1.00 44.31 ATOM 25 CB THR A 38 11.964 34.411 -11.049 1.00 44.50 ATOM 26 OG1 THR A 38 12.733 34.704 -12.222 1.00 44.43 ATOM 27 CG2 THR A 38 10.746 33.584 -11.444 1.00 44.24 ATOM 28 C THR A 38 10.720 35.390 -9.121 1.00 42.36 ATOM 29 O THR A 38 11.266 34.887 -8.135 1.00 41.65 ATOM 30 N THR A 39 9.426 35.694 -9.155 1.00 40.03 ATOM 31 CA THR A 39 8.549 35.424 -8.022 1.00 37.78 ATOM 32 CB THR A 39 7.870 36.709 -7.508 1.00 37.96 ATOM 33 OG1 THR A 39 8.872 37.655 -7.126 1.00 38.34 ATOM 34 CG2 THR A 39 6.989 36.404 -6.299 1.00 37.62 ATOM 35 C THR A 39 7.471 34.438 -8.432 1.00 36.05 ATOM 36 O THR A 39 6.818 34.611 -9.458 1.00 36.02 ATOM 37 N VAL A 40 7.299 33.399 -7.624 1.00 33.87 ATOM 38 CA VAL A 40 6.305 32.376 -7.896 1.00 31.64 ATOM 39 CB VAL A 40 6.969 31.032 -8.363 1.00 31.35 ATOM 40 CG1 VAL A 40 7.819 31.262 -9.609 1.00 30.18 ATOM 41 CG2 VAL A 40 7.821 30.444 -7.239 1.00 29.68 ATOM 42 C VAL A 40 5.532 32.112 -6.611 1.00 30.51 ATOM 43 O VAL A 40 5.933 32.555 -5.535 1.00 30.58 ATOM 44 N VAL A 41 4.409 31.414 -6.731 1.00 29.32 ATOM 45 CA VAL A 41 3.624 31.053 -5.565 1.00 28.29 ATOM 46 CB VAL A 41 2.119 31.361 -5.742 1.00 28.03 ATOM 47 CG1 VAL A 41 1.359 30.907 -4.515 1.00 26.90 ATOM 48 CG2 VAL A 41 1.908 32.857 -5.961 1.00 28.25 ATOM 49 C VAL A 41 3.844 29.555 -5.499 1.00 27.78 ATOM 50 O VAL A 41 3.275 28.802 -6.288 1.00 27.29 ATOM 51 N ALA A 42 4.692 29.132 -4.565 1.00 27.27 ATOM 52 CA ALA A 42 5.040 27.726 -4.425 1.00 26.99 ATOM 53 CB ALA A 42 6.562 27.566 -4.505 1.00 26.37 ATOM 54 C ALA A 42 4.516 27.075 -3.159 1.00 26.60 ATOM 55 O ALA A 42 4.343 27.722 -2.133 1.00 26.76 ATOM 56 N THR A 43 4.289 25.772 -3.250 1.00 26.73 ATOM 57 CA THR A 43 3.769 24.981 -2.148 1.00 27.89 ATOM 58 CB THR A 43 2.857 23.861 -2.682 1.00 27.64 ATOM 59 OG1 THR A 43 1.881 24.420 -3.569 1.00 29.09 ATOM 60 CG2 THR A 43 2.163 23.146 -1.551 1.00 27.70 ATOM 61 C THR A 43 4.884 24.320 -1.342 1.00 29.20 ATOM 62 O THR A 43 5.732 23.623 -1.903 1.00 28.45 ATOM 63 N PRO A 44 4.906 24.539 -0.015 1.00 30.27 ATOM 64 CD PRO A 44 3.989 25.393 0.766 1.00 31.14 ATOM 65 CA PRO A 44 5.939 23.928 0.828 1.00 31.42 ATOM 66 CB PRO A 44 5.447 24.199 2.250 1.00 31.10 ATOM 67 CG PRO A 44 4.644 25.453 2.126 1.00 31.02 ATOM 68 C PRO A 44 6.027 22.430 0.527 1.00 32.59 ATOM 69 O PRO A 44 5.006 21.751 0.390 1.00 31.42 ATOM 70 N GLY A 45 7.249 21.924 0.421 1.00 34.02 ATOM 71 CA GLY A 45 7.449 20.523 0.112 1.00 37.27 ATOM 72 C GLY A 45 6.797 19.598 1.111 1.00 40.10 ATOM 73 O GLY A 45 6.297 18.532 0.751 1.00 40.55 ATOM 74 N GLN A 46 6.802 20.002 2.374 1.00 42.60 ATOM 75 CA GLN A 46 6.204 19.190 3.418 1.00 45.68 ATOM 76 CB GLN A 46 7.301 18.580 4.295 1.00 47.28 ATOM 77 CG GLN A 46 8.541 18.171 3.509 1.00 49.67 ATOM 78 CD GLN A 46 9.138 16.863 3.984 1.00 51.44 ATOM 79 OE1 GLN A 46 8.415 15.900 4.273 1.00 51.97 ATOM 80 NE2 GLN A 46 10.471 16.817 4.068 1.00 51.94 ATOM 81 C GLN A 46 5.259 20.035 4.258 1.00 46.67 ATOM 82 O GLN A 46 5.401 21.255 4.343 1.00 47.36 ATOM 83 N GLY A 47 4.283 19.384 4.873 1.00 47.48 ATOM 84 CA GLY A 47 3.340 20.112 5.694 1.00 48.14 ATOM 85 C GLY A 47 2.005 20.299 5.006 1.00 48.62 ATOM 86 O GLY A 47 1.564 19.435 4.246 1.00 49.19 ATOM 87 N PRO A 48 1.336 21.436 5.244 1.00 48.67 ATOM 88 CD PRO A 48 1.775 22.556 6.098 1.00 48.81 ATOM 89 CA PRO A 48 0.034 21.705 4.632 1.00 47.95 ATOM 90 CB PRO A 48 -0.653 22.599 5.657 1.00 48.50 ATOM 91 CG PRO A 48 0.499 23.365 6.300 1.00 48.83 ATOM 92 C PRO A 48 0.152 22.389 3.276 1.00 46.70 ATOM 93 O PRO A 48 1.090 23.155 3.040 1.00 46.78 ATOM 94 N ASP A 49 -0.800 22.109 2.390 1.00 45.18 ATOM 95 CA ASP A 49 -0.798 22.716 1.066 1.00 43.75 ATOM 96 CB ASP A 49 -1.763 21.974 0.141 1.00 45.30 ATOM 97 CG ASP A 49 -1.121 20.775 -0.526 1.00 46.68 ATOM 98 OD1 ASP A 49 -0.414 20.021 0.171 1.00 47.90 ATOM 99 OD2 ASP A 49 -1.320 20.582 -1.745 1.00 48.02 ATOM 100 C ASP A 49 -1.197 24.188 1.163 1.00 41.77 ATOM 101 O ASP A 49 -2.307 24.568 0.788 1.00 41.88 ATOM 102 N ARG A 50 -0.284 25.004 1.682 1.00 39.23 ATOM 103 CA ARG A 50 -0.506 26.436 1.841 1.00 36.73 ATOM 104 CB ARG A 50 -0.491 26.818 3.324 1.00 37.21 ATOM 105 CG ARG A 50 -1.612 26.194 4.139 1.00 38.57 ATOM 106 CD ARG A 50 -2.985 26.685 3.688 1.00 39.50 ATOM 107 NE ARG A 50 -4.052 25.922 4.330 1.00 41.40 ATOM 108 CZ ARG A 50 -4.769 24.975 3.728 1.00 41.83 ATOM 109 NH1 ARG A 50 -4.543 24.665 2.456 1.00 42.04 ATOM 110 NH2 ARG A 50 -5.699 24.318 4.407 1.00 42.59 ATOM 111 C ARG A 50 0.598 27.183 1.105 1.00 34.66 ATOM 112 O ARG A 50 1.596 27.601 1.698 1.00 33.92 ATOM 113 N PRO A 51 0.435 27.346 -0.211 1.00 33.21 ATOM 114 CD PRO A 51 -0.706 26.839 -0.996 1.00 32.31 ATOM 115 CA PRO A 51 1.412 28.039 -1.054 1.00 32.34 ATOM 116 CB PRO A 51 0.751 28.058 -2.432 1.00 31.86 ATOM 117 CG PRO A 51 -0.189 26.881 -2.409 1.00 31.70 ATOM 118 C PRO A 51 1.767 29.436 -0.574 1.00 32.63 ATOM 119 O PRO A 51 0.934 30.137 0.004 1.00 32.31 ATOM 120 N GLN A 52 3.010 29.838 -0.812 1.00 32.52 ATOM 121 CA GLN A 52 3.466 31.167 -0.427 1.00 33.23 ATOM 122 CB GLN A 52 4.312 31.103 0.841 1.00 34.83 ATOM 123 CG GLN A 52 5.430 30.097 0.788 1.00 37.63 ATOM 124 CD GLN A 52 6.080 29.901 2.144 1.00 39.72 ATOM 125 OE1 GLN A 52 5.460 29.370 3.073 1.00 40.64 ATOM 126 NE2 GLN A 52 7.332 30.336 2.269 1.00 39.44 ATOM 127 C GLN A 52 4.280 31.778 -1.549 1.00 33.31 ATOM 128 O GLN A 52 4.777 31.073 -2.426 1.00 32.29 ATOM 129 N GLU A 53 4.406 33.097 -1.529 1.00 33.92 ATOM 130 CA GLU A 53 5.171 33.788 -2.552 1.00 35.11 ATOM 131 CB GLU A 53 4.867 35.290 -2.520 1.00 36.98 ATOM 132 CG GLU A 53 3.761 35.724 -3.484 1.00 39.95 ATOM 133 CD GLU A 53 2.737 36.665 -2.846 1.00 42.17 ATOM 134 OE1 GLU A 53 2.884 36.995 -1.642 1.00 43.11 ATOM 135 OE2 GLU A 53 1.780 37.073 -3.552 1.00 42.04 ATOM 136 C GLU A 53 6.651 33.542 -2.283 1.00 34.32 ATOM 137 O GLU A 53 7.124 33.726 -1.163 1.00 34.30 ATOM 138 N VAL A 54 7.370 33.093 -3.306 1.00 33.56 ATOM 139 CA VAL A 54 8.799 32.838 -3.174 1.00 32.52 ATOM 140 CB VAL A 54 9.129 31.328 -3.242 1.00 31.58 ATOM 141 CG1 VAL A 54 10.637 31.123 -3.126 1.00 30.56 ATOM 142 CG2 VAL A 54 8.411 30.586 -2.132 1.00 30.25 ATOM 143 C VAL A 54 9.508 33.542 -4.312 1.00 32.82 ATOM 144 O VAL A 54 9.125 33.400 -5.473 1.00 32.55 ATOM 145 N SER A 55 10.534 34.314 -3.975 1.00 33.60 ATOM 146 CA SER A 55 11.292 35.041 -4.978 1.00 34.64 ATOM 147 CB SER A 55 11.253 36.540 -4.680 1.00 35.66 ATOM 148 OG SER A 55 9.961 37.072 -4.944 1.00 37.33 ATOM 149 C SER A 55 12.734 34.564 -5.015 1.00 34.67 ATOM 150 O SER A 55 13.333 34.287 -3.977 1.00 34.38 ATOM 151 N TYR A 56 13.285 34.465 -6.219 1.00 35.48 ATOM 152 CA TYR A 56 14.663 34.031 -6.383 1.00 36.72 ATOM 153 CB TYR A 56 14.729 32.509 -6.526 1.00 35.35 ATOM 154 CG TYR A 56 13.984 31.952 -7.717 1.00 34.88 ATOM 155 CD1 TYR A 56 12.720 31.371 -7.566 1.00 34.70 ATOM 156 CE1 TYR A 56 12.051 30.811 -8.652 1.00 33.87 ATOM 157 CD2 TYR A 56 14.557 31.961 -8.992 1.00 34.23 ATOM 158 CE2 TYR A 56 13.896 31.404 -10.083 1.00 33.91 ATOM 159 CZ TYR A 56 12.644 30.830 -9.902 1.00 34.19 ATOM 160 OH TYR A 56 11.991 30.270 -10.972 1.00 35.29 ATOM 161 C TYR A 56 15.346 34.700 -7.573 1.00 37.96 ATOM 162 O TYR A 56 14.691 35.243 -8.465 1.00 37.76 ATOM 163 N THR A 57 16.674 34.642 -7.581 1.00 39.76 ATOM 164 CA THR A 57 17.464 35.257 -8.640 1.00 41.45 ATOM 165 CB THR A 57 17.844 36.707 -8.244 1.00 42.14 ATOM 166 OG1 THR A 57 18.424 37.381 -9.371 1.00 43.41 ATOM 167 CG2 THR A 57 18.826 36.703 -7.070 1.00 41.27 ATOM 168 C THR A 57 18.740 34.459 -8.917 1.00 42.23 ATOM 169 O THR A 57 18.948 33.387 -8.347 1.00 41.59 ATOM 170 N ASP A 58 19.582 34.991 -9.800 1.00 43.12 ATOM 171 CA ASP A 58 20.850 34.359 -10.154 1.00 44.22 ATOM 172 CB ASP A 58 21.793 34.377 -8.950 1.00 45.44 ATOM 173 CG ASP A 58 22.155 35.784 -8.520 1.00 46.63 ATOM 174 OD1 ASP A 58 22.247 36.669 -9.400 1.00 47.30 ATOM 175 OD2 ASP A 58 22.341 36.005 -7.303 1.00 47.80 ATOM 176 C ASP A 58 20.684 32.932 -10.655 1.00 44.53 ATOM 177 O ASP A 58 21.382 32.017 -10.218 1.00 44.28 ATOM 178 N THR A 59 19.758 32.756 -11.586 1.00 45.27 ATOM 179 CA THR A 59 19.483 31.449 -12.155 1.00 46.53 ATOM 180 CB THR A 59 18.100 31.447 -12.835 1.00 46.76 ATOM 181 OG1 THR A 59 17.080 31.493 -11.830 1.00 47.20 ATOM 182 CG2 THR A 59 17.914 30.199 -13.685 1.00 47.19 ATOM 183 C THR A 59 20.546 31.036 -13.172 1.00 47.37 ATOM 184 O THR A 59 21.052 31.864 -13.927 1.00 47.92 ATOM 185 N LYS A 60 20.884 29.752 -13.179 1.00 47.86 ATOM 186 CA LYS A 60 21.867 29.219 -14.112 1.00 48.87 ATOM 187 CB LYS A 60 23.285 29.643 -13.717 1.00 49.79 ATOM 188 CG LYS A 60 23.554 29.624 -12.228 1.00 51.37 ATOM 189 CD LYS A 60 25.041 29.749 -11.943 1.00 52.50 ATOM 190 CE LYS A 60 25.786 28.476 -12.327 1.00 53.48 ATOM 191 NZ LYS A 60 26.926 28.189 -11.398 1.00 54.33 ATOM 192 C LYS A 60 21.764 27.705 -14.132 1.00 48.85 ATOM 193 O LYS A 60 21.553 27.080 -13.092 1.00 48.66 ATOM 194 N VAL A 61 21.904 27.127 -15.321 1.00 48.98 ATOM 195 CA VAL A 61 21.814 25.683 -15.499 1.00 49.50 ATOM 196 CB VAL A 61 21.802 25.318 -16.993 1.00 49.06 ATOM 197 CG1 VAL A 61 21.894 23.813 -17.165 1.00 48.58 ATOM 198 CG2 VAL A 61 20.541 25.860 -17.641 1.00 48.42 ATOM 199 C VAL A 61 22.977 24.970 -14.827 1.00 50.24 ATOM 200 O VAL A 61 24.128 25.331 -15.035 1.00 50.82 ATOM 201 N ILE A 62 22.671 23.956 -14.022 1.00 50.92 ATOM 202 CA ILE A 62 23.703 23.199 -13.319 1.00 51.80 ATOM 203 CB ILE A 62 23.667 23.463 -11.791 1.00 51.28 ATOM 204 CG2 ILE A 62 23.832 24.948 -11.512 1.00 50.92 ATOM 205 CG1 ILE A 62 22.357 22.934 -11.198 1.00 50.53 ATOM 206 CD1 ILE A 62 22.350 22.884 -9.684 1.00 49.61 ATOM 207 C ILE A 62 23.557 21.698 -13.534 1.00 52.97 ATOM 208 O ILE A 62 24.294 20.903 -12.944 1.00 53.03 ATOM 209 N GLY A 63 22.605 21.312 -14.375 1.00 54.15 ATOM 210 CA GLY A 63 22.384 19.902 -14.623 1.00 55.81 ATOM 211 C GLY A 63 21.408 19.640 -15.750 1.00 57.06 ATOM 212 O GLY A 63 20.798 20.563 -16.294 1.00 56.85 ATOM 213 N ASN A 64 21.256 18.368 -16.096 1.00 58.39 ATOM 214 CA ASN A 64 20.363 17.972 -17.175 1.00 59.76 ATOM 215 CB ASN A 64 21.014 18.282 -18.530 1.00 60.17 ATOM 216 CG ASN A 64 20.102 19.068 -19.455 1.00 61.09 ATOM 217 OD1 ASN A 64 20.418 20.194 -19.849 1.00 61.57 ATOM 218 ND2 ASN A 64 18.964 18.477 -19.808 1.00 61.26 ATOM 219 C ASN A 64 20.049 16.483 -17.090 1.00 60.30 ATOM 220 O ASN A 64 20.672 15.739 -16.326 1.00 60.64 ATOM 221 N GLY A 65 19.074 16.060 -17.885 1.00 60.55 ATOM 222 CA GLY A 65 18.674 14.668 -17.921 1.00 60.57 ATOM 223 C GLY A 65 17.732 14.480 -19.091 1.00 60.83 ATOM 224 O GLY A 65 17.367 15.455 -19.752 1.00 61.38 ATOM 225 N SER A 66 17.340 13.241 -19.367 1.00 60.56 ATOM 226 CA SER A 66 16.422 12.996 -20.471 1.00 60.04 ATOM 227 CB SER A 66 16.333 11.492 -20.768 1.00 60.06 ATOM 228 OG SER A 66 15.766 10.778 -19.683 1.00 60.53 ATOM 229 C SER A 66 15.041 13.559 -20.117 1.00 59.37 ATOM 230 O SER A 66 14.241 13.863 -21.004 1.00 59.26 ATOM 231 N PHE A 67 14.790 13.723 -18.815 1.00 58.83 ATOM 232 CA PHE A 67 13.512 14.238 -18.306 1.00 57.64 ATOM 233 CB PHE A 67 13.175 13.591 -16.955 1.00 58.30 ATOM 234 CG PHE A 67 12.937 12.110 -17.037 1.00 58.98 ATOM 235 CD1 PHE A 67 13.565 11.241 -16.148 1.00 59.13 ATOM 236 CD2 PHE A 67 12.100 11.580 -18.017 1.00 59.22 ATOM 237 CE1 PHE A 67 13.369 9.866 -16.230 1.00 59.42 ATOM 238 CE2 PHE A 67 11.895 10.203 -18.110 1.00 59.65 ATOM 239 CZ PHE A 67 12.532 9.345 -17.214 1.00 59.85 ATOM 240 C PHE A 67 13.450 15.753 -18.150 1.00 56.12 ATOM 241 O PHE A 67 12.445 16.377 -18.489 1.00 56.04 ATOM 242 N GLY A 68 14.511 16.355 -17.631 1.00 54.42 ATOM 243 CA GLY A 68 14.480 17.794 -17.464 1.00 52.19 ATOM 244 C GLY A 68 15.808 18.470 -17.211 1.00 50.19 ATOM 245 O GLY A 68 16.880 17.887 -17.401 1.00 50.40 ATOM 246 N VAL A 69 15.719 19.723 -16.780 1.00 47.91 ATOM 247 CA VAL A 69 16.891 20.531 -16.486 1.00 45.17 ATOM 248 CB VAL A 69 16.901 21.829 -17.318 1.00 45.55 ATOM 249 CG1 VAL A 69 18.282 22.455 -17.283 1.00 45.46 ATOM 250 CG2 VAL A 69 16.482 21.531 -18.743 1.00 46.13 ATOM 251 C VAL A 69 16.901 20.924 -15.020 1.00 43.06 ATOM 252 O VAL A 69 15.850 21.051 -14.389 1.00 42.55 ATOM 253 N VAL A 70 18.099 21.115 -14.488 1.00 40.33 ATOM 254 CA VAL A 70 18.266 21.520 -13.108 1.00 38.29 ATOM 255 CB VAL A 70 19.061 20.470 -12.304 1.00 37.51 ATOM 256 CG1 VAL A 70 19.235 20.933 -10.870 1.00 36.72 ATOM 257 CG2 VAL A 70 18.337 19.136 -12.345 1.00 36.54 ATOM 258 C VAL A 70 19.019 22.846 -13.122 1.00 37.97 ATOM 259 O VAL A 70 20.072 22.972 -13.754 1.00 37.50 ATOM 260 N TYR A 71 18.452 23.844 -12.453 1.00 36.90 ATOM 261 CA TYR A 71 19.059 25.162 -12.378 1.00 36.62 ATOM 262 CB TYR A 71 18.084 26.264 -12.807 1.00 38.17 ATOM 263 CG TYR A 71 17.419 26.057 -14.142 1.00 40.50 ATOM 264 CD1 TYR A 71 17.760 26.847 -15.241 1.00 41.56 ATOM 265 CE1 TYR A 71 17.146 26.664 -16.477 1.00 42.12 ATOM 266 CD2 TYR A 71 16.442 25.075 -14.310 1.00 41.25 ATOM 267 CE2 TYR A 71 15.823 24.881 -15.541 1.00 42.36 ATOM 268 CZ TYR A 71 16.179 25.678 -16.619 1.00 43.04 ATOM 269 OH TYR A 71 15.568 25.480 -17.838 1.00 43.85 ATOM 270 C TYR A 71 19.426 25.434 -10.946 1.00 35.82 ATOM 271 O TYR A 71 18.956 24.764 -10.030 1.00 35.47 ATOM 272 N GLN A 72 20.274 26.429 -10.761 1.00 34.98 ATOM 273 CA GLN A 72 20.660 26.843 -9.434 1.00 34.69 ATOM 274 CB GLN A 72 22.177 26.884 -9.284 1.00 35.05 ATOM 275 CG GLN A 72 22.629 27.200 -7.870 1.00 35.66 ATOM 276 CD GLN A 72 24.032 27.756 -7.827 1.00 36.51 ATOM 277 OE1 GLN A 72 24.339 28.745 -8.490 1.00 36.73 ATOM 278 NE2 GLN A 72 24.897 27.120 -7.047 1.00 37.24 ATOM 279 C GLN A 72 20.089 28.245 -9.341 1.00 34.07 ATOM 280 O GLN A 72 19.994 28.944 -10.348 1.00 33.61 ATOM 281 N ALA A 73 19.683 28.642 -8.146 1.00 33.89 ATOM 282 CA ALA A 73 19.126 29.968 -7.941 1.00 33.95 ATOM 283 CB ALA A 73 17.636 29.979 -8.285 1.00 33.93 ATOM 284 C ALA A 73 19.335 30.345 -6.491 1.00 34.18 ATOM 285 O ALA A 73 19.630 29.492 -5.654 1.00 33.79 ATOM 286 N LYS A 74 19.195 31.630 -6.197 1.00 35.25 ATOM 287 CA LYS A 74 19.375 32.117 -4.842 1.00 36.39 ATOM 288 CB LYS A 74 20.474 33.178 -4.810 1.00 37.81 ATOM 289 CG LYS A 74 20.680 33.818 -3.454 1.00 40.22 ATOM 290 CD LYS A 74 21.254 35.215 -3.609 1.00 43.26 ATOM 291 CE LYS A 74 22.367 35.470 -2.604 1.00 45.31 ATOM 292 NZ LYS A 74 23.014 36.805 -2.817 1.00 47.13 ATOM 293 C LYS A 74 18.073 32.710 -4.348 1.00 36.44 ATOM 294 O LYS A 74 17.483 33.562 -5.010 1.00 36.40 ATOM 295 N LEU A 75 17.615 32.245 -3.193 1.00 36.95 ATOM 296 CA LEU A 75 16.382 32.751 -2.614 1.00 37.84 ATOM 297 CB LEU A 75 15.948 31.871 -1.445 1.00 36.84 ATOM 298 CG LEU A 75 15.616 30.420 -1.793 1.00 36.03 ATOM 299 CD1 LEU A 75 15.043 29.735 -0.573 1.00 35.52 ATOM 300 CD2 LEU A 75 14.624 30.373 -2.944 1.00 35.58 ATOM 301 C LEU A 75 16.664 34.163 -2.130 1.00 39.06 ATOM 302 O LEU A 75 17.597 34.379 -1.364 1.00 39.10 ATOM 303 N CYS A 76 15.864 35.120 -2.588 1.00 40.97 ATOM 304 CA CYS A 76 16.041 36.523 -2.216 1.00 42.81 ATOM 305 CB CYS A 76 14.996 37.387 -2.912 1.00 41.94 ATOM 306 SG CYS A 76 15.114 37.349 -4.690 1.00 43.44 ATOM 307 C CYS A 76 15.968 36.788 -0.724 1.00 44.18 ATOM 308 O CYS A 76 16.781 37.531 -0.177 1.00 44.94 ATOM 309 N ASP A 77 14.991 36.182 -0.065 1.00 45.94 ATOM 310 CA ASP A 77 14.813 36.387 1.363 1.00 47.52 ATOM 311 CB ASP A 77 13.497 35.747 1.817 1.00 49.38 ATOM 312 CG ASP A 77 12.302 36.676 1.621 1.00 51.45 ATOM 313 OD1 ASP A 77 12.086 37.146 0.478 1.00 52.02 ATOM 314 OD2 ASP A 77 11.581 36.940 2.612 1.00 52.70 ATOM 315 C ASP A 77 15.966 35.874 2.222 1.00 47.59 ATOM 316 O ASP A 77 16.476 36.598 3.077 1.00 48.39 ATOM 317 N SER A 78 16.391 34.638 1.988 1.00 46.78 ATOM 318 CA SER A 78 17.461 34.047 2.782 1.00 45.51 ATOM 319 CB SER A 78 17.081 32.614 3.160 1.00 45.36 ATOM 320 OG SER A 78 16.998 31.792 2.005 1.00 45.00 ATOM 321 C SER A 78 18.839 34.036 2.126 1.00 44.89 ATOM 322 O SER A 78 19.845 33.830 2.804 1.00 45.51 ATOM 323 N GLY A 79 18.894 34.247 0.817 1.00 43.74 ATOM 324 CA GLY A 79 20.176 34.220 0.134 1.00 41.98 ATOM 325 C GLY A 79 20.670 32.787 -0.013 1.00 41.13 ATOM 326 O GLY A 79 21.760 32.544 -0.533 1.00 41.11 ATOM 327 N GLU A 80 19.861 31.835 0.446 1.00 39.93 ATOM 328 CA GLU A 80 20.207 30.418 0.360 1.00 38.74 ATOM 329 CB GLU A 80 19.247 29.580 1.201 1.00 40.37 ATOM 330 CG GLU A 80 19.627 29.486 2.668 1.00 43.42 ATOM 331 CD GLU A 80 18.583 28.759 3.496 1.00 45.32 ATOM 332 OE1 GLU A 80 18.941 28.208 4.564 1.00 47.42 ATOM 333 OE2 GLU A 80 17.404 28.740 3.082 1.00 46.18 ATOM 334 C GLU A 80 20.160 29.930 -1.080 1.00 36.93 ATOM 335 O GLU A 80 19.308 30.351 -1.865 1.00 36.28 ATOM 336 N LEU A 81 21.081 29.038 -1.424 1.00 34.98 ATOM 337 CA LEU A 81 21.138 28.496 -2.770 1.00 32.90 ATOM 338 CB LEU A 81 22.575 28.128 -3.138 1.00 33.42 ATOM 339 CG LEU A 81 23.580 29.273 -3.267 1.00 34.05 ATOM 340 CD1 LEU A 81 24.945 28.687 -3.579 1.00 33.97 ATOM 341 CD2 LEU A 81 23.147 30.244 -4.364 1.00 33.47 ATOM 342 C LEU A 81 20.263 27.262 -2.864 1.00 31.01 ATOM 343 O LEU A 81 20.237 26.436 -1.957 1.00 31.13 ATOM 344 N VAL A 82 19.543 27.143 -3.970 1.00 29.13 ATOM 345 CA VAL A 82 18.679 26.000 -4.181 1.00 27.77 ATOM 346 CB VAL A 82 17.173 26.363 -3.992 1.00 28.04 ATOM 347 CG1 VAL A 82 16.907 26.806 -2.557 1.00 27.42 ATOM 348 CG2 VAL A 82 16.767 27.463 -4.980 1.00 27.47 ATOM 349 C VAL A 82 18.866 25.512 -5.604 1.00 27.03 ATOM 350 O VAL A 82 19.435 26.209 -6.449 1.00 26.68 ATOM 351 N ALA A 83 18.385 24.303 -5.856 1.00 25.58 ATOM 352 CA ALA A 83 18.440 23.718 -7.178 1.00 25.36 ATOM 353 CB ALA A 83 19.143 22.385 -7.134 1.00 25.09 ATOM 354 C ALA A 83 16.982 23.534 -7.583 1.00 25.89 ATOM 355 O ALA A 83 16.172 23.048 -6.795 1.00 25.58 ATOM 356 N ILE A 84 16.637 23.956 -8.791 1.00 25.16 ATOM 357 CA ILE A 84 15.274 23.803 -9.257 1.00 25.88 ATOM 358 CB ILE A 84 14.702 25.139 -9.779 1.00 25.89 ATOM 359 CG2 ILE A 84 13.271 24.929 -10.294 1.00 25.74 ATOM 360 CG1 ILE A 84 14.741 26.191 -8.665 1.00 25.94 ATOM 361 CD1 ILE A 84 14.260 27.567 -9.105 1.00 26.90 ATOM 362 C ILE A 84 15.270 22.781 -10.375 1.00 25.92 ATOM 363 O ILE A 84 15.844 23.016 -11.436 1.00 26.67 ATOM 364 N LYS A 85 14.644 21.636 -10.123 1.00 26.17 ATOM 365 CA LYS A 85 14.554 20.578 -11.119 1.00 27.08 ATOM 366 CB LYS A 85 14.573 19.206 -10.442 1.00 26.75 ATOM 367 CG LYS A 85 14.419 18.035 -11.409 1.00 26.66 ATOM 368 CD LYS A 85 14.577 16.701 -10.687 1.00 25.86 ATOM 369 CE LYS A 85 14.606 15.539 -11.666 1.00 26.65 ATOM 370 NZ LYS A 85 14.853 14.240 -10.974 1.00 25.51 ATOM 371 C LYS A 85 13.246 20.776 -11.876 1.00 28.95 ATOM 372 O LYS A 85 12.158 20.649 -11.305 1.00 27.78 ATOM 373 N LYS A 86 13.358 21.094 -13.160 1.00 30.23 ATOM 374 CA LYS A 86 12.194 21.335 -13.997 1.00 32.89 ATOM 375 CB LYS A 86 12.450 22.561 -14.867 1.00 33.71 ATOM 376 CG LYS A 86 11.214 23.163 -15.483 1.00 35.13 ATOM 377 CD LYS A 86 11.601 24.352 -16.324 1.00 36.77 ATOM 378 CE LYS A 86 10.398 24.962 -17.000 1.00 38.55 ATOM 379 NZ LYS A 86 10.787 26.241 -17.671 1.00 40.57 ATOM 380 C LYS A 86 11.863 20.131 -14.874 1.00 34.47 ATOM 381 O LYS A 86 12.715 19.638 -15.618 1.00 34.68 ATOM 382 N VAL A 87 10.622 19.665 -14.792 1.00 35.83 ATOM 383 CA VAL A 87 10.190 18.511 -15.568 1.00 37.77 ATOM 384 CB VAL A 87 10.162 17.247 -14.670 1.00 37.66 ATOM 385 CG1 VAL A 87 9.444 16.109 -15.369 1.00 38.38 ATOM 386 CG2 VAL A 87 11.585 16.836 -14.322 1.00 37.16 ATOM 387 C VAL A 87 8.810 18.724 -16.202 1.00 39.71 ATOM 388 O VAL A 87 7.938 19.363 -15.615 1.00 39.02 ATOM 389 N LEU A 88 8.629 18.200 -17.412 1.00 41.91 ATOM 390 CA LEU A 88 7.358 18.310 -18.118 1.00 44.42 ATOM 391 CB LEU A 88 7.507 17.800 -19.551 1.00 44.54 ATOM 392 CG LEU A 88 6.405 18.192 -20.530 1.00 44.72 ATOM 393 CD1 LEU A 88 6.600 19.634 -20.974 1.00 44.54 ATOM 394 CD2 LEU A 88 6.434 17.246 -21.720 1.00 44.91 ATOM 395 C LEU A 88 6.347 17.451 -17.371 1.00 46.27 ATOM 396 O LEU A 88 6.567 16.259 -17.177 1.00 46.39 ATOM 397 N GLN A 89 5.241 18.050 -16.947 1.00 48.79 ATOM 398 CA GLN A 89 4.238 17.297 -16.209 1.00 51.70 ATOM 399 CB GLN A 89 3.822 18.063 -14.948 1.00 52.32 ATOM 400 CG GLN A 89 3.073 17.220 -13.912 1.00 53.75 ATOM 401 CD GLN A 89 3.407 15.731 -13.994 1.00 54.85 ATOM 402 OE1 GLN A 89 2.516 14.889 -14.116 1.00 55.12 ATOM 403 NE2 GLN A 89 4.695 15.405 -13.925 1.00 54.81 ATOM 404 C GLN A 89 3.001 16.961 -17.024 1.00 53.45 ATOM 405 O GLN A 89 2.442 17.812 -17.714 1.00 53.42 ATOM 406 N ASP A 90 2.583 15.704 -16.947 1.00 55.78 ATOM 407 CA ASP A 90 1.391 15.273 -17.650 1.00 58.36 ATOM 408 CB ASP A 90 1.310 13.746 -17.701 1.00 59.84 ATOM 409 CG ASP A 90 0.254 13.253 -18.681 1.00 61.59 ATOM 410 OD1 ASP A 90 0.230 12.035 -18.969 1.00 62.48 ATOM 411 OD2 ASP A 90 -0.550 14.086 -19.164 1.00 62.23 ATOM 412 C ASP A 90 0.221 15.824 -16.848 1.00 59.35 ATOM 413 O ASP A 90 -0.003 15.421 -15.704 1.00 59.27 ATOM 414 N LYS A 91 -0.512 16.756 -17.448 1.00 60.51 ATOM 415 CA LYS A 91 -1.655 17.381 -16.790 1.00 61.49 ATOM 416 CB LYS A 91 -2.370 18.318 -17.769 1.00 62.41 ATOM 417 CG LYS A 91 -2.661 17.688 -19.124 1.00 63.40 ATOM 418 CD LYS A 91 -3.709 18.486 -19.883 1.00 64.50 ATOM 419 CE LYS A 91 -4.523 17.601 -20.818 1.00 64.77 ATOM 420 NZ LYS A 91 -5.008 18.365 -22.004 1.00 65.26 ATOM 421 C LYS A 91 -2.656 16.367 -16.241 1.00 61.34 ATOM 422 O LYS A 91 -3.161 16.521 -15.128 1.00 61.46 ATOM 423 N ARG A 92 -2.925 15.325 -17.022 1.00 61.12 ATOM 424 CA ARG A 92 -3.891 14.302 -16.635 1.00 60.92 ATOM 425 CB ARG A 92 -4.365 13.548 -17.883 1.00 62.67 ATOM 426 CG ARG A 92 -5.326 14.342 -18.764 1.00 64.65 ATOM 427 CD ARG A 92 -6.530 14.847 -17.967 1.00 66.50 ATOM 428 NE ARG A 92 -7.399 13.757 -17.525 1.00 67.94 ATOM 429 CZ ARG A 92 -8.506 13.928 -16.808 1.00 68.88 ATOM 430 NH1 ARG A 92 -8.883 15.149 -16.450 1.00 69.58 ATOM 431 NH2 ARG A 92 -9.243 12.881 -16.457 1.00 69.26 ATOM 432 C ARG A 92 -3.453 13.293 -15.574 1.00 59.60 ATOM 433 O ARG A 92 -4.228 12.408 -15.207 1.00 59.89 ATOM 434 N PHE A 93 -2.225 13.406 -15.078 1.00 57.75 ATOM 435 CA PHE A 93 -1.751 12.467 -14.060 1.00 55.49 ATOM 436 CB PHE A 93 -1.077 11.271 -14.736 1.00 56.72 ATOM 437 CG PHE A 93 -1.877 10.698 -15.872 1.00 58.15 ATOM 438 CD1 PHE A 93 -2.830 9.710 -15.641 1.00 58.80 ATOM 439 CD2 PHE A 93 -1.710 11.180 -17.168 1.00 58.67 ATOM 440 CE1 PHE A 93 -3.609 9.210 -16.686 1.00 59.02 ATOM 441 CE2 PHE A 93 -2.481 10.689 -18.221 1.00 58.89 ATOM 442 CZ PHE A 93 -3.433 9.704 -17.979 1.00 59.04 ATOM 443 C PHE A 93 -0.796 13.131 -13.075 1.00 52.97 ATOM 444 O PHE A 93 -0.183 14.154 -13.389 1.00 53.04 ATOM 445 N LYS A 94 -0.674 12.564 -11.878 1.00 49.47 ATOM 446 CA LYS A 94 0.218 13.164 -10.901 1.00 46.34 ATOM 447 CB LYS A 94 -0.339 13.046 -9.484 1.00 46.81 ATOM 448 CG LYS A 94 0.165 14.172 -8.561 1.00 47.68 ATOM 449 CD LYS A 94 0.401 15.495 -9.321 1.00 46.88 ATOM 450 CE LYS A 94 1.851 15.972 -9.229 1.00 46.37 ATOM 451 NZ LYS A 94 2.226 16.978 -10.282 1.00 44.20 ATOM 452 C LYS A 94 1.631 12.613 -10.943 1.00 43.22 ATOM 453 O LYS A 94 1.854 11.435 -11.226 1.00 43.06 ATOM 454 N ASN A 95 2.579 13.495 -10.656 1.00 39.55 ATOM 455 CA ASN A 95 3.994 13.166 -10.669 1.00 35.49 ATOM 456 CB ASN A 95 4.801 14.459 -10.632 1.00 34.96 ATOM 457 CG ASN A 95 6.233 14.253 -11.039 1.00 34.43 ATOM 458 OD1 ASN A 95 6.605 14.481 -12.194 1.00 34.43 ATOM 459 ND2 ASN A 95 7.051 13.813 -10.095 1.00 32.82 ATOM 460 C ASN A 95 4.400 12.258 -9.514 1.00 33.02 ATOM 461 O ASN A 95 4.295 12.635 -8.346 1.00 31.46 ATOM 462 N ARG A 96 4.864 11.058 -9.849 1.00 30.82 ATOM 463 CA ARG A 96 5.289 10.091 -8.843 1.00 29.39 ATOM 464 CB ARG A 96 5.624 8.748 -9.498 1.00 29.94 ATOM 465 CG ARG A 96 5.964 7.650 -8.507 1.00 32.00 ATOM 466 CD ARG A 96 6.301 6.342 -9.210 1.00 34.25 ATOM 467 NE ARG A 96 5.127 5.754 -9.853 1.00 36.93 ATOM 468 CZ ARG A 96 5.157 4.690 -10.651 1.00 38.08 ATOM 469 NH1 ARG A 96 6.304 4.081 -10.915 1.00 39.05 ATOM 470 NH2 ARG A 96 4.035 4.236 -11.191 1.00 39.31 ATOM 471 C ARG A 96 6.502 10.584 -8.049 1.00 27.57 ATOM 472 O ARG A 96 6.582 10.381 -6.835 1.00 26.70 ATOM 473 N GLU A 97 7.444 11.222 -8.736 1.00 25.99 ATOM 474 CA GLU A 97 8.642 11.729 -8.074 1.00 24.79 ATOM 475 CB GLU A 97 9.583 12.373 -9.106 1.00 24.53 ATOM 476 CG GLU A 97 10.971 12.732 -8.565 1.00 24.69 ATOM 477 CD GLU A 97 11.881 13.371 -9.615 1.00 25.38 ATOM 478 OE1 GLU A 97 12.966 13.865 -9.240 1.00 26.51 ATOM 479 OE2 GLU A 97 11.521 13.382 -10.814 1.00 25.91 ATOM 480 C GLU A 97 8.238 12.750 -7.003 1.00 24.37 ATOM 481 O GLU A 97 8.761 12.737 -5.885 1.00 22.97 ATOM 482 N LEU A 98 7.293 13.623 -7.343 1.00 23.64 ATOM 483 CA LEU A 98 6.829 14.634 -6.401 1.00 23.75 ATOM 484 CB LEU A 98 5.854 15.593 -7.097 1.00 23.38 ATOM 485 CG LEU A 98 5.135 16.580 -6.173 1.00 23.81 ATOM 486 CD1 LEU A 98 6.166 17.473 -5.487 1.00 23.56 ATOM 487 CD2 LEU A 98 4.150 17.421 -6.969 1.00 23.71 ATOM 488 C LEU A 98 6.138 13.984 -5.204 1.00 24.38 ATOM 489 O LEU A 98 6.398 14.331 -4.053 1.00 23.47 ATOM 490 N GLN A 99 5.252 13.035 -5.484 1.00 25.85 ATOM 491 CA GLN A 99 4.517 12.357 -4.426 1.00 26.99 ATOM 492 CB GLN A 99 3.551 11.333 -5.026 1.00 29.47 ATOM 493 CG GLN A 99 2.476 11.924 -5.937 1.00 33.61 ATOM 494 CD GLN A 99 2.178 13.397 -5.655 1.00 36.63 ATOM 495 OE1 GLN A 99 1.775 13.773 -4.543 1.00 38.60 ATOM 496 NE2 GLN A 99 2.368 14.239 -6.670 1.00 38.74 ATOM 497 C GLN A 99 5.454 11.666 -3.444 1.00 26.52 ATOM 498 O GLN A 99 5.229 11.702 -2.235 1.00 26.05 ATOM 499 N ILE A 100 6.504 11.037 -3.967 1.00 25.89 ATOM 500 CA ILE A 100 7.460 10.342 -3.116 1.00 25.21 ATOM 501 CB ILE A 100 8.403 9.433 -3.951 1.00 25.36 ATOM 502 CG2 ILE A 100 9.639 9.054 -3.131 1.00 24.69 ATOM 503 CG1 ILE A 100 7.656 8.160 -4.368 1.00 25.10 ATOM 504 CD1 ILE A 100 8.367 7.342 -5.444 1.00 24.77 ATOM 505 C ILE A 100 8.284 11.341 -2.308 1.00 25.13 ATOM 506 O ILE A 100 8.434 11.176 -1.102 1.00 24.42 ATOM 507 N MET A 101 8.796 12.381 -2.968 1.00 25.51 ATOM 508 CA MET A 101 9.605 13.408 -2.300 1.00 26.76 ATOM 509 CB MET A 101 10.026 14.504 -3.282 1.00 29.54 ATOM 510 CG MET A 101 11.010 14.105 -4.343 1.00 33.44 ATOM 511 SD MET A 101 12.543 13.608 -3.632 1.00 41.28 ATOM 512 CE MET A 101 13.354 15.192 -3.356 1.00 37.45 ATOM 513 C MET A 101 8.861 14.103 -1.162 1.00 26.96 ATOM 514 O MET A 101 9.441 14.404 -0.122 1.00 25.78 ATOM 515 N ARG A 102 7.581 14.391 -1.379 1.00 26.75 ATOM 516 CA ARG A 102 6.786 15.080 -0.378 1.00 27.51 ATOM 517 CB ARG A 102 5.368 15.301 -0.898 1.00 27.83 ATOM 518 CG ARG A 102 5.280 16.308 -2.015 1.00 29.77 ATOM 519 CD ARG A 102 3.869 16.862 -2.126 1.00 31.34 ATOM 520 NE ARG A 102 3.669 17.942 -1.165 1.00 33.72 ATOM 521 CZ ARG A 102 2.529 18.606 -1.008 1.00 35.16 ATOM 522 NH1 ARG A 102 1.475 18.299 -1.754 1.00 34.91 ATOM 523 NH2 ARG A 102 2.449 19.585 -0.110 1.00 35.66 ATOM 524 C ARG A 102 6.730 14.358 0.957 1.00 27.69 ATOM 525 O ARG A 102 6.557 14.986 1.999 1.00 28.47 ATOM 526 N LYS A 103 6.886 13.042 0.943 1.00 27.67 ATOM 527 CA LYS A 103 6.822 12.294 2.192 1.00 28.31 ATOM 528 CB LYS A 103 6.006 11.020 1.989 1.00 30.67 ATOM 529 CG LYS A 103 6.688 9.971 1.148 1.00 33.55 ATOM 530 CD LYS A 103 5.823 8.715 1.049 1.00 36.56 ATOM 531 CE LYS A 103 4.487 8.999 0.363 1.00 37.77 ATOM 532 NZ LYS A 103 3.717 7.752 0.039 1.00 38.91 ATOM 533 C LYS A 103 8.170 11.938 2.833 1.00 27.25 ATOM 534 O LYS A 103 8.209 11.366 3.919 1.00 27.49 ATOM 535 N LEU A 104 9.273 12.282 2.179 1.00 25.69 ATOM 536 CA LEU A 104 10.591 11.965 2.730 1.00 23.92 ATOM 537 CB LEU A 104 11.572 11.619 1.604 1.00 22.45 ATOM 538 CG LEU A 104 11.114 10.520 0.641 1.00 22.07 ATOM 539 CD1 LEU A 104 12.111 10.367 -0.500 1.00 21.66 ATOM 540 CD2 LEU A 104 10.954 9.220 1.404 1.00 22.46 ATOM 541 C LEU A 104 11.180 13.089 3.564 1.00 23.59 ATOM 542 O LEU A 104 11.125 14.259 3.190 1.00 23.50 ATOM 543 N ASP A 105 11.757 12.717 4.698 1.00 23.09 ATOM 544 CA ASP A 105 12.384 13.680 5.587 1.00 23.71 ATOM 545 CB ASP A 105 11.379 14.207 6.606 1.00 25.65 ATOM 546 CG ASP A 105 12.025 15.097 7.647 1.00 28.68 ATOM 547 OD1 ASP A 105 13.110 15.658 7.371 1.00 29.91 ATOM 548 OD2 ASP A 105 11.452 15.235 8.749 1.00 30.43 ATOM 549 C ASP A 105 13.516 12.958 6.301 1.00 23.01 ATOM 550 O ASP A 105 13.307 12.340 7.350 1.00 22.48 ATOM 551 N HIS A 106 14.712 13.031 5.717 1.00 21.20 ATOM 552 CA HIS A 106 15.891 12.370 6.272 1.00 19.57 ATOM 553 CB HIS A 106 16.013 10.976 5.660 1.00 18.78 ATOM 554 CG HIS A 106 17.030 10.105 6.324 1.00 18.65 ATOM 555 CD2 HIS A 106 16.899 9.131 7.256 1.00 18.72 ATOM 556 ND1 HIS A 106 18.367 10.139 5.992 1.00 19.25 ATOM 557 CE1 HIS A 106 19.017 9.222 6.689 1.00 18.24 ATOM 558 NE2 HIS A 106 18.149 8.596 7.464 1.00 17.99 ATOM 559 C HIS A 106 17.134 13.216 5.967 1.00 19.09 ATOM 560 O HIS A 106 17.225 13.822 4.898 1.00 18.69 ATOM 561 N CYS A 107 18.083 13.256 6.905 1.00 18.59 ATOM 562 CA CYS A 107 19.299 14.057 6.737 1.00 18.83 ATOM 563 CB CYS A 107 20.102 14.082 8.047 1.00 19.38 ATOM 564 SG CYS A 107 20.689 12.479 8.625 1.00 24.38 ATOM 565 C CYS A 107 20.196 13.621 5.579 1.00 17.88 ATOM 566 O CYS A 107 21.058 14.386 5.132 1.00 18.37 ATOM 567 N ASN A 108 19.984 12.409 5.076 1.00 16.29 ATOM 568 CA ASN A 108 20.776 11.907 3.961 1.00 15.53 ATOM 569 CB ASN A 108 21.402 10.569 4.350 1.00 15.33 ATOM 570 CG ASN A 108 22.453 10.734 5.429 1.00 15.93 ATOM 571 OD1 ASN A 108 23.326 11.601 5.319 1.00 18.33 ATOM 572 ND2 ASN A 108 22.372 9.930 6.477 1.00 14.24 ATOM 573 C ASN A 108 19.992 11.794 2.645 1.00 15.57 ATOM 574 O ASN A 108 20.342 11.008 1.762 1.00 14.72 ATOM 575 N ILE A 109 18.929 12.586 2.526 1.00 15.43 ATOM 576 CA ILE A 109 18.121 12.620 1.305 1.00 16.31 ATOM 577 CB ILE A 109 16.764 11.886 1.479 1.00 16.00 ATOM 578 CG2 ILE A 109 15.909 12.055 0.210 1.00 16.29 ATOM 579 CG1 ILE A 109 17.017 10.402 1.763 1.00 16.89 ATOM 580 CD1 ILE A 109 15.746 9.567 1.897 1.00 17.10 ATOM 581 C ILE A 109 17.884 14.090 1.025 1.00 16.85 ATOM 582 O ILE A 109 17.482 14.831 1.926 1.00 17.31 ATOM 583 N VAL A 110 18.148 14.524 -0.204 1.00 17.54 ATOM 584 CA VAL A 110 17.968 15.933 -0.554 1.00 19.50 ATOM 585 CB VAL A 110 18.338 16.201 -2.046 1.00 20.31 ATOM 586 CG1 VAL A 110 17.245 15.703 -2.976 1.00 20.04 ATOM 587 CG2 VAL A 110 18.591 17.690 -2.251 1.00 22.22 ATOM 588 C VAL A 110 16.540 16.387 -0.249 1.00 20.12 ATOM 589 O VAL A 110 15.565 15.732 -0.612 1.00 19.72 ATOM 590 N ARG A 111 16.428 17.521 0.427 1.00 20.98 ATOM 591 CA ARG A 111 15.129 18.037 0.836 1.00 22.15 ATOM 592 CB ARG A 111 15.311 18.925 2.076 1.00 24.43 ATOM 593 CG ARG A 111 14.050 19.637 2.534 1.00 28.08 ATOM 594 CD ARG A 111 14.339 20.578 3.687 1.00 31.44 ATOM 595 NE ARG A 111 15.334 21.582 3.318 1.00 36.77 ATOM 596 CZ ARG A 111 15.815 22.509 4.147 1.00 38.67 ATOM 597 NH1 ARG A 111 15.389 22.563 5.403 1.00 40.36 ATOM 598 NH2 ARG A 111 16.730 23.376 3.729 1.00 39.57 ATOM 599 C ARG A 111 14.345 18.803 -0.229 1.00 21.70 ATOM 600 O ARG A 111 14.899 19.639 -0.948 1.00 20.88 ATOM 601 N LEU A 112 13.053 18.497 -0.340 1.00 21.24 ATOM 602 CA LEU A 112 12.192 19.213 -1.278 1.00 21.82 ATOM 603 CB LEU A 112 11.014 18.336 -1.724 1.00 20.92 ATOM 604 CG LEU A 112 10.022 19.067 -2.643 1.00 21.42 ATOM 605 CD1 LEU A 112 10.663 19.284 -4.004 1.00 20.84 ATOM 606 CD2 LEU A 112 8.728 18.256 -2.779 1.00 21.11 ATOM 607 C LEU A 112 11.676 20.429 -0.500 1.00 22.24 ATOM 608 O LEU A 112 10.883 20.285 0.429 1.00 22.39 ATOM 609 N ARG A 113 12.147 21.617 -0.857 1.00 22.87 ATOM 610 CA ARG A 113 11.733 22.833 -0.169 1.00 24.46 ATOM 611 CB ARG A 113 12.745 23.942 -0.424 1.00 26.41 ATOM 612 CG ARG A 113 14.048 23.806 0.339 1.00 30.64 ATOM 613 CD ARG A 113 14.803 25.121 0.245 1.00 35.39 ATOM 614 NE ARG A 113 16.009 25.155 1.068 1.00 40.10 ATOM 615 CZ ARG A 113 16.744 26.246 1.260 1.00 41.14 ATOM 616 NH1 ARG A 113 16.393 27.390 0.690 1.00 43.00 ATOM 617 NH2 ARG A 113 17.837 26.192 2.009 1.00 42.71 ATOM 618 C ARG A 113 10.344 23.304 -0.603 1.00 24.46 ATOM 619 O ARG A 113 9.483 23.584 0.236 1.00 23.86 ATOM 620 N TYR A 114 10.140 23.392 -1.914 1.00 24.70 ATOM 621 CA TYR A 114 8.866 23.821 -2.495 1.00 25.11 ATOM 622 CB TYR A 114 8.837 25.333 -2.771 1.00 26.14 ATOM 623 CG TYR A 114 9.195 26.235 -1.626 1.00 29.01 ATOM 624 CD1 TYR A 114 8.239 26.605 -0.683 1.00 30.13 ATOM 625 CE1 TYR A 114 8.565 27.446 0.377 1.00 31.89 ATOM 626 CD2 TYR A 114 10.493 26.731 -1.486 1.00 30.06 ATOM 627 CE2 TYR A 114 10.831 27.570 -0.434 1.00 31.34 ATOM 628 CZ TYR A 114 9.864 27.922 0.495 1.00 32.58 ATOM 629 OH TYR A 114 10.195 28.738 1.553 1.00 35.02 ATOM 630 C TYR A 114 8.712 23.174 -3.853 1.00 25.40 ATOM 631 O TYR A 114 9.621 22.518 -4.357 1.00 24.21 ATOM 632 N PHE A 115 7.542 23.379 -4.445 1.00 24.51 ATOM 633 CA PHE A 115 7.292 22.931 -5.795 1.00 24.60 ATOM 634 CB PHE A 115 6.809 21.475 -5.856 1.00 24.60 ATOM 635 CG PHE A 115 5.447 21.237 -5.272 1.00 25.91 ATOM 636 CD1 PHE A 115 5.308 20.825 -3.949 1.00 25.87 ATOM 637 CD2 PHE A 115 4.302 21.350 -6.065 1.00 26.60 ATOM 638 CE1 PHE A 115 4.043 20.517 -3.417 1.00 26.55 ATOM 639 CE2 PHE A 115 3.035 21.048 -5.542 1.00 26.34 ATOM 640 CZ PHE A 115 2.909 20.630 -4.218 1.00 25.78 ATOM 641 C PHE A 115 6.267 23.902 -6.353 1.00 24.74 ATOM 642 O PHE A 115 5.468 24.470 -5.607 1.00 24.21 ATOM 643 N PHE A 116 6.336 24.141 -7.652 1.00 24.85 ATOM 644 CA PHE A 116 5.406 25.042 -8.303 1.00 25.99 ATOM 645 CB PHE A 116 5.846 26.501 -8.122 1.00 25.22 ATOM 646 CG PHE A 116 7.147 26.844 -8.793 1.00 25.73 ATOM 647 CD1 PHE A 116 8.352 26.761 -8.092 1.00 25.69 ATOM 648 CD2 PHE A 116 7.169 27.276 -10.117 1.00 25.25 ATOM 649 CE1 PHE A 116 9.562 27.105 -8.701 1.00 24.81 ATOM 650 CE2 PHE A 116 8.374 27.625 -10.737 1.00 26.05 ATOM 651 CZ PHE A 116 9.573 27.538 -10.026 1.00 25.01 ATOM 652 C PHE A 116 5.320 24.675 -9.774 1.00 27.44 ATOM 653 O PHE A 116 6.123 23.875 -10.271 1.00 27.14 ATOM 654 N TYR A 117 4.331 25.239 -10.460 1.00 28.42 ATOM 655 CA TYR A 117 4.136 24.967 -11.876 1.00 30.06 ATOM 656 CB TYR A 117 2.717 24.458 -12.116 1.00 28.26 ATOM 657 CG TYR A 117 2.416 23.196 -11.360 1.00 26.68 ATOM 658 CD1 TYR A 117 2.648 21.953 -11.937 1.00 25.86 ATOM 659 CE1 TYR A 117 2.434 20.786 -11.224 1.00 26.16 ATOM 660 CD2 TYR A 117 1.951 23.243 -10.045 1.00 25.77 ATOM 661 CE2 TYR A 117 1.733 22.081 -9.321 1.00 26.30 ATOM 662 CZ TYR A 117 1.979 20.856 -9.916 1.00 26.12 ATOM 663 OH TYR A 117 1.780 19.695 -9.212 1.00 27.47 ATOM 664 C TYR A 117 4.384 26.214 -12.701 1.00 32.32 ATOM 665 O TYR A 117 4.090 27.320 -12.263 1.00 32.65 ATOM 666 N SER A 118 4.949 26.029 -13.886 1.00 35.51 ATOM 667 CA SER A 118 5.229 27.132 -14.795 1.00 39.40 ATOM 668 CB SER A 118 6.706 27.537 -14.728 1.00 38.98 ATOM 669 OG SER A 118 7.567 26.434 -14.938 1.00 38.76 ATOM 670 C SER A 118 4.873 26.640 -16.189 1.00 42.93 ATOM 671 O SER A 118 4.934 25.441 -16.465 1.00 43.17 ATOM 672 N SER A 119 4.487 27.555 -17.067 1.00 47.35 ATOM 673 CA SER A 119 4.097 27.163 -18.414 1.00 51.99 ATOM 674 CB SER A 119 2.922 28.021 -18.897 1.00 52.50 ATOM 675 OG SER A 119 1.739 27.713 -18.175 1.00 53.25 ATOM 676 C SER A 119 5.237 27.246 -19.414 1.00 54.89 ATOM 677 O SER A 119 6.060 28.163 -19.363 1.00 55.28 ATOM 678 N GLY A 120 5.278 26.269 -20.316 1.00 58.17 ATOM 679 CA GLY A 120 6.303 26.241 -21.342 1.00 62.10 ATOM 680 C GLY A 120 5.719 26.892 -22.576 1.00 64.93 ATOM 681 O GLY A 120 4.925 26.276 -23.289 1.00 65.55 ATOM 682 N GLU A 121 6.104 28.142 -22.819 1.00 67.32 ATOM 683 CA GLU A 121 5.607 28.909 -23.960 1.00 69.77 ATOM 684 CB GLU A 121 6.443 30.181 -24.140 1.00 70.70 ATOM 685 CG GLU A 121 6.038 31.324 -23.212 1.00 72.36 ATOM 686 CD GLU A 121 5.294 30.843 -21.972 1.00 73.13 ATOM 687 OE1 GLU A 121 4.049 30.969 -21.933 1.00 73.53 ATOM 688 OE2 GLU A 121 5.957 30.341 -21.036 1.00 73.62 ATOM 689 C GLU A 121 5.568 28.132 -25.271 1.00 70.77 ATOM 690 O GLU A 121 4.772 28.447 -26.159 1.00 71.08 ATOM 691 N LYS A 122 6.422 27.118 -25.392 1.00 71.68 ATOM 692 CA LYS A 122 6.467 26.308 -26.605 1.00 72.57 ATOM 693 CB LYS A 122 7.449 25.144 -26.431 1.00 73.28 ATOM 694 CG LYS A 122 7.843 24.468 -27.737 1.00 74.02 ATOM 695 CD LYS A 122 8.395 23.073 -27.494 1.00 74.56 ATOM 696 CE LYS A 122 8.644 22.346 -28.806 1.00 75.00 ATOM 697 NZ LYS A 122 9.266 21.007 -28.593 1.00 75.26 ATOM 698 C LYS A 122 5.082 25.768 -26.963 1.00 72.52 ATOM 699 O LYS A 122 4.840 25.358 -28.100 1.00 72.93 ATOM 700 N LYS A 123 4.177 25.777 -25.988 1.00 71.92 ATOM 701 CA LYS A 123 2.815 25.296 -26.192 1.00 71.21 ATOM 702 CB LYS A 123 2.833 23.813 -26.569 1.00 71.90 ATOM 703 CG LYS A 123 1.643 23.371 -27.401 1.00 73.11 ATOM 704 CD LYS A 123 1.635 21.864 -27.599 1.00 74.20 ATOM 705 CE LYS A 123 0.244 21.365 -27.973 1.00 74.79 ATOM 706 NZ LYS A 123 0.286 20.038 -28.658 1.00 75.44 ATOM 707 C LYS A 123 2.016 25.487 -24.912 1.00 70.26 ATOM 708 O LYS A 123 2.309 26.377 -24.114 1.00 70.59 ATOM 709 N ASP A 124 0.996 24.658 -24.727 1.00 68.77 ATOM 710 CA ASP A 124 0.178 24.712 -23.524 1.00 67.11 ATOM 711 CB ASP A 124 -1.275 24.360 -23.845 1.00 68.50 ATOM 712 CG ASP A 124 -1.425 23.699 -25.199 1.00 69.77 ATOM 713 OD1 ASP A 124 -1.222 24.389 -26.224 1.00 70.55 ATOM 714 OD2 ASP A 124 -1.745 22.489 -25.239 1.00 70.78 ATOM 715 C ASP A 124 0.780 23.671 -22.587 1.00 65.13 ATOM 716 O ASP A 124 0.080 23.036 -21.793 1.00 65.22 ATOM 717 N GLU A 125 2.094 23.501 -22.710 1.00 62.21 ATOM 718 CA GLU A 125 2.851 22.553 -21.906 1.00 58.88 ATOM 719 CB GLU A 125 4.204 22.266 -22.571 1.00 60.34 ATOM 720 CG GLU A 125 4.567 23.244 -23.692 1.00 62.12 ATOM 721 CD GLU A 125 6.028 23.152 -24.121 1.00 63.22 ATOM 722 OE1 GLU A 125 6.417 22.115 -24.703 1.00 63.90 ATOM 723 OE2 GLU A 125 6.785 24.118 -23.881 1.00 63.76 ATOM 724 C GLU A 125 3.076 23.113 -20.506 1.00 55.55 ATOM 725 O GLU A 125 3.433 24.282 -20.345 1.00 54.77 ATOM 726 N VAL A 126 2.858 22.268 -19.500 1.00 51.70 ATOM 727 CA VAL A 126 3.041 22.662 -18.109 1.00 47.65 ATOM 728 CB VAL A 126 1.786 22.366 -17.275 1.00 47.49 ATOM 729 CG1 VAL A 126 2.024 22.748 -15.820 1.00 46.91 ATOM 730 CG2 VAL A 126 0.610 23.137 -17.836 1.00 47.79 ATOM 731 C VAL A 126 4.221 21.929 -17.481 1.00 44.86 ATOM 732 O VAL A 126 4.384 20.721 -17.655 1.00 43.95 ATOM 733 N TYR A 127 5.035 22.675 -16.745 1.00 41.67 ATOM 734 CA TYR A 127 6.200 22.110 -16.089 1.00 38.42 ATOM 735 CB TYR A 127 7.445 22.911 -16.456 1.00 39.92 ATOM 736 CG TYR A 127 7.866 22.729 -17.884 1.00 41.87 ATOM 737 CD1 TYR A 127 7.436 23.611 -18.876 1.00 42.86 ATOM 738 CE1 TYR A 127 7.798 23.424 -20.210 1.00 43.96 ATOM 739 CD2 TYR A 127 8.672 21.655 -18.255 1.00 42.87 ATOM 740 CE2 TYR A 127 9.040 21.458 -19.582 1.00 43.97 ATOM 741 CZ TYR A 127 8.601 22.343 -20.552 1.00 44.50 ATOM 742 OH TYR A 127 8.963 22.133 -21.862 1.00 45.92 ATOM 743 C TYR A 127 6.065 22.096 -14.579 1.00 35.42 ATOM 744 O TYR A 127 5.557 23.041 -13.983 1.00 34.33 ATOM 745 N LEU A 128 6.521 21.006 -13.974 1.00 32.37 ATOM 746 CA LEU A 128 6.526 20.866 -12.529 1.00 29.70 ATOM 747 CB LEU A 128 6.282 19.413 -12.120 1.00 28.45 ATOM 748 CG LEU A 128 6.661 19.061 -10.674 1.00 28.49 ATOM 749 CD1 LEU A 128 5.820 19.880 -9.695 1.00 26.67 ATOM 750 CD2 LEU A 128 6.460 17.566 -10.442 1.00 27.32 ATOM 751 C LEU A 128 7.943 21.283 -12.147 1.00 28.59 ATOM 752 O LEU A 128 8.913 20.817 -12.755 1.00 28.16 ATOM 753 N ASN A 129 8.062 22.170 -11.166 1.00 26.78 ATOM 754 CA ASN A 129 9.361 22.662 -10.714 1.00 25.23 ATOM 755 CB ASN A 129 9.414 24.188 -10.801 1.00 25.58 ATOM 756 CG ASN A 129 9.340 24.698 -12.226 1.00 26.46 ATOM 757 OD1 ASN A 129 10.355 25.064 -12.811 1.00 26.68 ATOM 758 ND2 ASN A 129 8.133 24.730 -12.792 1.00 26.29 ATOM 759 C ASN A 129 9.618 22.248 -9.278 1.00 24.38 ATOM 760 O ASN A 129 8.913 22.686 -8.365 1.00 23.41 ATOM 761 N LEU A 130 10.626 21.403 -9.076 1.00 23.30 ATOM 762 CA LEU A 130 10.985 20.939 -7.738 1.00 23.29 ATOM 763 CB LEU A 130 11.431 19.475 -7.783 1.00 22.29 ATOM 764 CG LEU A 130 10.473 18.486 -8.451 1.00 23.97 ATOM 765 CD1 LEU A 130 11.093 17.097 -8.448 1.00 23.75 ATOM 766 CD2 LEU A 130 9.141 18.486 -7.704 1.00 24.33 ATOM 767 C LEU A 130 12.116 21.798 -7.181 1.00 22.94 ATOM 768 O LEU A 130 13.222 21.808 -7.733 1.00 23.43 ATOM 769 N VAL A 131 11.840 22.528 -6.102 1.00 22.63 ATOM 770 CA VAL A 131 12.854 23.380 -5.487 1.00 22.33 ATOM 771 CB VAL A 131 12.254 24.686 -4.931 1.00 22.68 ATOM 772 CG1 VAL A 131 13.357 25.548 -4.337 1.00 22.89 ATOM 773 CG2 VAL A 131 11.552 25.453 -6.049 1.00 23.17 ATOM 774 C VAL A 131 13.508 22.597 -4.357 1.00 22.06 ATOM 775 O VAL A 131 12.891 22.332 -3.322 1.00 21.64 ATOM 776 N LEU A 132 14.769 22.232 -4.569 1.00 22.12 ATOM 777 CA LEU A 132 15.513 21.441 -3.604 1.00 21.23 ATOM 778 CB LEU A 132 16.032 20.163 -4.272 1.00 21.38 ATOM 779 CG LEU A 132 15.144 19.473 -5.304 1.00 20.94 ATOM 780 CD1 LEU A 132 15.991 18.672 -6.277 1.00 21.93 ATOM 781 CD2 LEU A 132 14.181 18.559 -4.583 1.00 21.73 ATOM 782 C LEU A 132 16.692 22.176 -3.005 1.00 21.66 ATOM 783 O LEU A 132 17.122 23.209 -3.511 1.00 21.74 ATOM 784 N ASP A 133 17.211 21.631 -1.912 1.00 22.28 ATOM 785 CA ASP A 133 18.395 22.202 -1.280 1.00 23.15 ATOM 786 CB ASP A 133 18.764 21.417 -0.027 1.00 24.36 ATOM 787 CG ASP A 133 18.020 21.883 1.186 1.00 25.74 ATOM 788 OD1 ASP A 133 18.005 21.138 2.176 1.00 28.30 ATOM 789 OD2 ASP A 133 17.451 22.991 1.158 1.00 27.40 ATOM 790 C ASP A 133 19.505 22.015 -2.307 1.00 22.82 ATOM 791 O ASP A 133 19.567 20.976 -2.977 1.00 21.97 ATOM 792 N TYR A 134 20.369 23.012 -2.444 1.00 22.80 ATOM 793 CA TYR A 134 21.470 22.895 -3.383 1.00 22.89 ATOM 794 CB TYR A 134 21.865 24.274 -3.914 1.00 24.91 ATOM 795 CG TYR A 134 23.153 24.276 -4.698 1.00 25.56 ATOM 796 CD1 TYR A 134 24.348 24.662 -4.095 1.00 26.87 ATOM 797 CE1 TYR A 134 25.548 24.646 -4.798 1.00 27.31 ATOM 798 CD2 TYR A 134 23.183 23.874 -6.030 1.00 26.17 ATOM 799 CE2 TYR A 134 24.379 23.853 -6.746 1.00 27.47 ATOM 800 CZ TYR A 134 25.558 24.243 -6.113 1.00 27.42 ATOM 801 OH TYR A 134 26.752 24.229 -6.791 1.00 28.82 ATOM 802 C TYR A 134 22.657 22.233 -2.675 1.00 22.28 ATOM 803 O TYR A 134 23.008 22.599 -1.548 1.00 21.22 ATOM 804 N VAL A 135 23.238 21.230 -3.329 1.00 21.42 ATOM 805 CA VAL A 135 24.395 20.511 -2.796 1.00 20.96 ATOM 806 CB VAL A 135 24.055 19.044 -2.529 1.00 19.97 ATOM 807 CG1 VAL A 135 25.167 18.393 -1.721 1.00 19.94 ATOM 808 CG2 VAL A 135 22.742 18.968 -1.746 1.00 19.59 ATOM 809 C VAL A 135 25.462 20.658 -3.884 1.00 21.11 ATOM 810 O VAL A 135 25.237 20.298 -5.034 1.00 20.82 ATOM 811 N PRO A 136 26.651 21.161 -3.515 1.00 21.90 ATOM 812 CD PRO A 136 27.027 21.492 -2.128 1.00 21.11 ATOM 813 CA PRO A 136 27.762 21.397 -4.447 1.00 21.92 ATOM 814 CB PRO A 136 28.759 22.190 -3.606 1.00 21.68 ATOM 815 CG PRO A 136 28.518 21.720 -2.223 1.00 21.71 ATOM 816 C PRO A 136 28.454 20.299 -5.248 1.00 22.49 ATOM 817 O PRO A 136 28.887 20.560 -6.372 1.00 22.96 ATOM 818 N GLU A 137 28.565 19.090 -4.709 1.00 21.94 ATOM 819 CA GLU A 137 29.265 18.023 -5.425 1.00 22.34 ATOM 820 CB GLU A 137 30.602 17.748 -4.729 1.00 24.10 ATOM 821 CG GLU A 137 31.637 18.826 -4.937 1.00 27.56 ATOM 822 CD GLU A 137 32.217 18.782 -6.338 1.00 30.63 ATOM 823 OE1 GLU A 137 32.890 19.759 -6.739 1.00 32.82 ATOM 824 OE2 GLU A 137 31.994 17.767 -7.039 1.00 32.01 ATOM 825 C GLU A 137 28.487 16.715 -5.515 1.00 21.88 ATOM 826 O GLU A 137 27.365 16.618 -5.047 1.00 21.12 ATOM 827 N THR A 138 29.110 15.716 -6.133 1.00 21.29 ATOM 828 CA THR A 138 28.529 14.384 -6.258 1.00 21.06 ATOM 829 CB THR A 138 27.943 14.114 -7.657 1.00 20.77 ATOM 830 OG1 THR A 138 29.001 14.122 -8.623 1.00 21.51 ATOM 831 CG2 THR A 138 26.906 15.156 -8.020 1.00 20.96 ATOM 832 C THR A 138 29.664 13.400 -6.035 1.00 20.80 ATOM 833 O THR A 138 30.840 13.742 -6.217 1.00 20.20 ATOM 834 N VAL A 139 29.320 12.185 -5.633 1.00 20.06 ATOM 835 CA VAL A 139 30.330 11.154 -5.402 1.00 20.98 ATOM 836 CB VAL A 139 29.675 9.852 -4.873 1.00 20.81 ATOM 837 CG1 VAL A 139 30.620 8.675 -5.038 1.00 20.94 ATOM 838 CG2 VAL A 139 29.291 10.031 -3.414 1.00 20.07 ATOM 839 C VAL A 139 31.026 10.877 -6.734 1.00 21.61 ATOM 840 O VAL A 139 32.207 10.524 -6.777 1.00 21.73 ATOM 841 N TYR A 140 30.284 11.046 -7.820 1.00 21.82 ATOM 842 CA TYR A 140 30.834 10.821 -9.148 1.00 23.36 ATOM 843 CB TYR A 140 29.753 11.056 -10.201 1.00 24.63 ATOM 844 CG TYR A 140 30.271 10.962 -11.612 1.00 27.88 ATOM 845 CD1 TYR A 140 30.634 12.109 -12.315 1.00 28.82 ATOM 846 CE1 TYR A 140 31.130 12.032 -13.612 1.00 31.07 ATOM 847 CD2 TYR A 140 30.416 9.726 -12.239 1.00 28.50 ATOM 848 CE2 TYR A 140 30.910 9.636 -13.540 1.00 31.03 ATOM 849 CZ TYR A 140 31.264 10.796 -14.217 1.00 31.62 ATOM 850 OH TYR A 140 31.736 10.726 -15.510 1.00 34.75 ATOM 851 C TYR A 140 32.026 11.748 -9.420 1.00 23.94 ATOM 852 O TYR A 140 33.112 11.291 -9.784 1.00 23.20 ATOM 853 N ARG A 141 31.818 13.049 -9.243 1.00 23.69 ATOM 854 CA ARG A 141 32.872 14.028 -9.497 1.00 25.22 ATOM 855 CB ARG A 141 32.326 15.444 -9.356 1.00 27.20 ATOM 856 CG ARG A 141 31.417 15.878 -10.482 1.00 31.12 ATOM 857 CD ARG A 141 30.689 17.158 -10.090 1.00 35.40 ATOM 858 NE ARG A 141 29.407 17.287 -10.779 1.00 39.94 ATOM 859 CZ ARG A 141 28.433 18.114 -10.403 1.00 41.91 ATOM 860 NH1 ARG A 141 28.594 18.890 -9.334 1.00 42.69 ATOM 861 NH2 ARG A 141 27.304 18.182 -11.106 1.00 43.21 ATOM 862 C ARG A 141 34.063 13.855 -8.564 1.00 24.60 ATOM 863 O ARG A 141 35.212 13.881 -9.001 1.00 24.36 ATOM 864 N VAL A 142 33.795 13.677 -7.278 1.00 24.15 ATOM 865 CA VAL A 142 34.873 13.502 -6.314 1.00 24.53 ATOM 866 CB VAL A 142 34.322 13.407 -4.871 1.00 24.07 ATOM 867 CG1 VAL A 142 35.397 12.892 -3.927 1.00 23.32 ATOM 868 CG2 VAL A 142 33.839 14.791 -4.418 1.00 23.41 ATOM 869 C VAL A 142 35.700 12.257 -6.638 1.00 25.52 ATOM 870 O VAL A 142 36.928 12.306 -6.613 1.00 25.40 ATOM 871 N ALA A 143 35.032 11.148 -6.947 1.00 25.74 ATOM 872 CA ALA A 143 35.738 9.909 -7.285 1.00 26.55 ATOM 873 CB ALA A 143 34.740 8.753 -7.455 1.00 25.28 ATOM 874 C ALA A 143 36.557 10.084 -8.568 1.00 27.56 ATOM 875 O ALA A 143 37.637 9.502 -8.715 1.00 27.86 ATOM 876 N ARG A 144 36.039 10.883 -9.496 1.00 28.39 ATOM 877 CA ARG A 144 36.728 11.123 -10.757 1.00 30.27 ATOM 878 CB ARG A 144 35.822 11.892 -11.714 1.00 31.15 ATOM 879 CG ARG A 144 36.287 11.851 -13.156 1.00 34.23 ATOM 880 CD ARG A 144 35.296 12.541 -14.092 1.00 37.20 ATOM 881 NE ARG A 144 34.832 13.822 -13.558 1.00 39.57 ATOM 882 CZ ARG A 144 33.984 14.631 -14.188 1.00 41.01 ATOM 883 NH1 ARG A 144 33.502 14.295 -15.381 1.00 41.87 ATOM 884 NH2 ARG A 144 33.611 15.774 -13.624 1.00 41.63 ATOM 885 C ARG A 144 38.019 11.902 -10.528 1.00 31.03 ATOM 886 O ARG A 144 39.014 11.695 -11.226 1.00 30.59 ATOM 887 N HIS A 145 38.002 12.800 -9.549 1.00 32.00 ATOM 888 CA HIS A 145 39.185 13.588 -9.236 1.00 32.93 ATOM 889 CB HIS A 145 38.885 14.612 -8.132 1.00 34.62 ATOM 890 CG HIS A 145 40.107 15.081 -7.398 1.00 37.08 ATOM 891 CD2 HIS A 145 40.772 14.549 -6.344 1.00 37.90 ATOM 892 ND1 HIS A 145 40.814 16.206 -7.768 1.00 37.93 ATOM 893 CE1 HIS A 145 41.861 16.347 -6.974 1.00 38.16 ATOM 894 NE2 HIS A 145 41.859 15.355 -6.102 1.00 38.42 ATOM 895 C HIS A 145 40.309 12.658 -8.783 1.00 32.84 ATOM 896 O HIS A 145 41.435 12.741 -9.281 1.00 32.94 ATOM 897 N TYR A 146 40.005 11.777 -7.835 1.00 31.94 ATOM 898 CA TYR A 146 41.000 10.848 -7.328 1.00 32.69 ATOM 899 CB TYR A 146 40.453 10.091 -6.118 1.00 30.56 ATOM 900 CG TYR A 146 40.386 10.942 -4.871 1.00 29.38 ATOM 901 CD1 TYR A 146 39.258 11.717 -4.593 1.00 28.59 ATOM 902 CE1 TYR A 146 39.206 12.540 -3.468 1.00 27.76 ATOM 903 CD2 TYR A 146 41.467 11.007 -3.984 1.00 28.51 ATOM 904 CE2 TYR A 146 41.424 11.827 -2.857 1.00 27.64 ATOM 905 CZ TYR A 146 40.293 12.591 -2.607 1.00 27.60 ATOM 906 OH TYR A 146 40.244 13.408 -1.504 1.00 27.28 ATOM 907 C TYR A 146 41.427 9.869 -8.415 1.00 34.32 ATOM 908 O TYR A 146 42.587 9.469 -8.484 1.00 34.37 ATOM 909 N SER A 147 40.485 9.485 -9.265 1.00 35.57 ATOM 910 CA SER A 147 40.786 8.565 -10.349 1.00 38.08 ATOM 911 CB SER A 147 39.516 8.260 -11.143 1.00 38.72 ATOM 912 OG SER A 147 39.265 6.869 -11.165 1.00 41.59 ATOM 913 C SER A 147 41.823 9.192 -11.269 1.00 38.83 ATOM 914 O SER A 147 42.846 8.585 -11.581 1.00 39.16 ATOM 915 N ARG A 148 41.550 10.420 -11.691 1.00 40.37 ATOM 916 CA ARG A 148 42.440 11.147 -12.583 1.00 42.13 ATOM 917 CB ARG A 148 41.790 12.475 -12.984 1.00 42.99 ATOM 918 CG ARG A 148 40.653 12.321 -13.987 1.00 44.60 ATOM 919 CD ARG A 148 39.757 13.556 -14.014 1.00 47.07 ATOM 920 NE ARG A 148 38.918 13.622 -15.213 1.00 48.76 ATOM 921 CZ ARG A 148 38.083 14.624 -15.495 1.00 49.47 ATOM 922 NH1 ARG A 148 37.968 15.656 -14.664 1.00 49.38 ATOM 923 NH2 ARG A 148 37.366 14.601 -16.612 1.00 49.63 ATOM 924 C ARG A 148 43.810 11.393 -11.951 1.00 42.81 ATOM 925 O ARG A 148 44.840 11.248 -12.612 1.00 43.23 ATOM 926 N ALA A 149 43.822 11.763 -10.674 1.00 43.05 ATOM 927 CA ALA A 149 45.070 12.022 -9.968 1.00 43.22 ATOM 928 CB ALA A 149 44.803 12.828 -8.700 1.00 42.78 ATOM 929 C ALA A 149 45.754 10.711 -9.610 1.00 43.67 ATOM 930 O ALA A 149 46.723 10.699 -8.850 1.00 44.06 ATOM 931 N LYS A 150 45.251 9.609 -10.160 1.00 43.86 ATOM 932 CA LYS A 150 45.815 8.293 -9.876 1.00 44.36 ATOM 933 CB LYS A 150 47.163 8.136 -10.590 1.00 45.75 ATOM 934 CG LYS A 150 47.249 8.904 -11.905 1.00 47.52 ATOM 935 CD LYS A 150 48.317 8.339 -12.832 1.00 49.38 ATOM 936 CE LYS A 150 48.352 9.089 -14.163 1.00 50.29 ATOM 937 NZ LYS A 150 49.672 8.953 -14.853 1.00 51.41 ATOM 938 C LYS A 150 45.988 8.144 -8.364 1.00 43.96 ATOM 939 O LYS A 150 47.002 7.644 -7.879 1.00 43.96 ATOM 940 N GLN A 151 44.979 8.597 -7.629 1.00 43.19 ATOM 941 CA GLN A 151 44.973 8.548 -6.174 1.00 42.93 ATOM 942 CB GLN A 151 44.879 9.967 -5.607 1.00 44.48 ATOM 943 CG GLN A 151 46.205 10.601 -5.253 1.00 47.33 ATOM 944 CD GLN A 151 46.989 9.774 -4.253 1.00 49.43 ATOM 945 OE1 GLN A 151 46.412 9.047 -3.434 1.00 51.06 ATOM 946 NE2 GLN A 151 48.313 9.875 -4.313 1.00 50.37 ATOM 947 C GLN A 151 43.761 7.753 -5.709 1.00 41.91 ATOM 948 O GLN A 151 42.768 7.639 -6.429 1.00 42.17 ATOM 949 N THR A 152 43.846 7.207 -4.504 1.00 40.53 ATOM 950 CA THR A 152 42.744 6.445 -3.927 1.00 39.29 ATOM 951 CB THR A 152 43.260 5.264 -3.081 1.00 40.71 ATOM 952 OG1 THR A 152 44.042 4.384 -3.899 1.00 43.49 ATOM 953 CG2 THR A 152 42.097 4.493 -2.475 1.00 41.95 ATOM 954 C THR A 152 41.960 7.365 -2.996 1.00 36.78 ATOM 955 O THR A 152 42.554 8.156 -2.261 1.00 36.56 ATOM 956 N LEU A 153 40.634 7.282 -3.025 1.00 33.62 ATOM 957 CA LEU A 153 39.844 8.107 -2.125 1.00 30.70 ATOM 958 CB LEU A 153 38.347 8.024 -2.466 1.00 30.13 ATOM 959 CG LEU A 153 37.378 8.603 -1.424 1.00 29.97 ATOM 960 CD1 LEU A 153 37.488 10.122 -1.398 1.00 30.14 ATOM 961 CD2 LEU A 153 35.952 8.191 -1.750 1.00 30.35 ATOM 962 C LEU A 153 40.100 7.542 -0.725 1.00 28.98 ATOM 963 O LEU A 153 39.935 6.337 -0.496 1.00 28.07 ATOM 964 N PRO A 154 40.552 8.394 0.218 1.00 27.59 ATOM 965 CD PRO A 154 40.860 9.828 0.061 1.00 27.32 ATOM 966 CA PRO A 154 40.819 7.926 1.582 1.00 26.73 ATOM 967 CB PRO A 154 41.067 9.217 2.361 1.00 26.95 ATOM 968 CG PRO A 154 41.594 10.162 1.335 1.00 26.50 ATOM 969 C PRO A 154 39.640 7.122 2.132 1.00 26.57 ATOM 970 O PRO A 154 38.481 7.524 1.995 1.00 25.64 ATOM 971 N VAL A 155 39.946 5.989 2.756 1.00 25.82 ATOM 972 CA VAL A 155 38.923 5.109 3.297 1.00 25.68 ATOM 973 CB VAL A 155 39.561 3.869 3.961 1.00 26.40 ATOM 974 CG1 VAL A 155 38.483 2.854 4.332 1.00 27.62 ATOM 975 CG2 VAL A 155 40.553 3.232 3.001 1.00 28.20 ATOM 976 C VAL A 155 37.970 5.771 4.288 1.00 24.69 ATOM 977 O VAL A 155 36.827 5.340 4.427 1.00 24.60 ATOM 978 N ILE A 156 38.423 6.811 4.979 1.00 23.35 ATOM 979 CA ILE A 156 37.550 7.469 5.937 1.00 22.39 ATOM 980 CB ILE A 156 38.292 8.605 6.687 1.00 21.78 ATOM 981 CG2 ILE A 156 38.799 9.639 5.708 1.00 20.64 ATOM 982 CG1 ILE A 156 37.352 9.277 7.690 1.00 22.58 ATOM 983 CD1 ILE A 156 36.625 8.316 8.622 1.00 23.23 ATOM 984 C ILE A 156 36.329 8.019 5.186 1.00 21.81 ATOM 985 O ILE A 156 35.209 7.968 5.694 1.00 21.64 ATOM 986 N TYR A 157 36.550 8.523 3.972 1.00 21.66 ATOM 987 CA TYR A 157 35.467 9.064 3.150 1.00 21.13 ATOM 988 CB TYR A 157 36.019 9.889 1.988 1.00 22.43 ATOM 989 CG TYR A 157 36.674 11.173 2.427 1.00 24.60 ATOM 990 CD1 TYR A 157 38.020 11.416 2.155 1.00 25.62 ATOM 991 CE1 TYR A 157 38.646 12.579 2.597 1.00 26.81 ATOM 992 CD2 TYR A 157 35.961 12.126 3.153 1.00 24.96 ATOM 993 CE2 TYR A 157 36.574 13.294 3.602 1.00 27.34 ATOM 994 CZ TYR A 157 37.921 13.512 3.317 1.00 27.77 ATOM 995 OH TYR A 157 38.534 14.667 3.740 1.00 29.58 ATOM 996 C TYR A 157 34.610 7.935 2.592 1.00 21.08 ATOM 997 O TYR A 157 33.397 8.071 2.485 1.00 21.08 ATOM 998 N VAL A 158 35.239 6.828 2.216 1.00 20.40 ATOM 999 CA VAL A 158 34.488 5.691 1.695 1.00 20.07 ATOM 1000 CB VAL A 158 35.440 4.530 1.290 1.00 20.30 ATOM 1001 CG1 VAL A 158 34.636 3.277 0.935 1.00 20.95 ATOM 1002 CG2 VAL A 158 36.291 4.957 0.095 1.00 20.29 ATOM 1003 C VAL A 158 33.520 5.219 2.798 1.00 19.96 ATOM 1004 O VAL A 158 32.373 4.850 2.524 1.00 18.77 ATOM 1005 N LYS A 159 33.991 5.238 4.045 1.00 18.59 ATOM 1006 CA LYS A 159 33.162 4.830 5.180 1.00 18.87 ATOM 1007 CB LYS A 159 33.993 4.776 6.472 1.00 19.47 ATOM 1008 CG LYS A 159 34.984 3.629 6.514 1.00 20.34 ATOM 1009 CD LYS A 159 35.814 3.634 7.786 1.00 20.89 ATOM 1010 CE LYS A 159 36.759 2.430 7.797 1.00 21.57 ATOM 1011 NZ LYS A 159 37.720 2.451 8.936 1.00 23.26 ATOM 1012 C LYS A 159 32.020 5.822 5.362 1.00 18.53 ATOM 1013 O LYS A 159 30.857 5.436 5.456 1.00 18.33 ATOM 1014 N LEU A 160 32.357 7.104 5.407 1.00 17.89 ATOM 1015 CA LEU A 160 31.355 8.143 5.597 1.00 18.57 ATOM 1016 CB LEU A 160 32.025 9.519 5.651 1.00 18.33 ATOM 1017 CG LEU A 160 32.679 9.906 6.983 1.00 18.68 ATOM 1018 CD1 LEU A 160 33.681 11.041 6.727 1.00 18.74 ATOM 1019 CD2 LEU A 160 31.606 10.331 8.002 1.00 19.29 ATOM 1020 C LEU A 160 30.274 8.166 4.520 1.00 18.90 ATOM 1021 O LEU A 160 29.081 8.229 4.826 1.00 19.19 ATOM 1022 N TYR A 161 30.691 8.118 3.259 1.00 18.53 ATOM 1023 CA TYR A 161 29.741 8.172 2.154 1.00 19.08 ATOM 1024 CB TYR A 161 30.480 8.355 0.825 1.00 20.47 ATOM 1025 CG TYR A 161 31.256 9.648 0.744 1.00 22.58 ATOM 1026 CD1 TYR A 161 31.013 10.682 1.646 1.00 23.90 ATOM 1027 CE1 TYR A 161 31.731 11.866 1.594 1.00 26.61 ATOM 1028 CD2 TYR A 161 32.245 9.836 -0.222 1.00 23.92 ATOM 1029 CE2 TYR A 161 32.973 11.027 -0.285 1.00 25.49 ATOM 1030 CZ TYR A 161 32.705 12.032 0.626 1.00 26.29 ATOM 1031 OH TYR A 161 33.382 13.230 0.568 1.00 30.94 ATOM 1032 C TYR A 161 28.846 6.949 2.075 1.00 18.45 ATOM 1033 O TYR A 161 27.629 7.077 1.935 1.00 18.20 ATOM 1034 N MET A 162 29.443 5.767 2.165 1.00 17.42 ATOM 1035 CA MET A 162 28.673 4.529 2.096 1.00 17.69 ATOM 1036 CB MET A 162 29.624 3.336 2.000 1.00 18.41 ATOM 1037 CG MET A 162 30.372 3.273 0.656 1.00 19.20 ATOM 1038 SD MET A 162 29.279 3.310 -0.800 1.00 20.62 ATOM 1039 CE MET A 162 28.198 1.875 -0.436 1.00 21.54 ATOM 1040 C MET A 162 27.711 4.365 3.284 1.00 17.21 ATOM 1041 O MET A 162 26.590 3.903 3.108 1.00 17.09 ATOM 1042 N TYR A 163 28.142 4.752 4.484 1.00 16.40 ATOM 1043 CA TYR A 163 27.298 4.656 5.676 1.00 16.00 ATOM 1044 CB TYR A 163 28.062 5.144 6.911 1.00 16.22 ATOM 1045 CG TYR A 163 27.210 5.193 8.166 1.00 16.21 ATOM 1046 CD1 TYR A 163 26.549 6.361 8.543 1.00 17.25 ATOM 1047 CE1 TYR A 163 25.774 6.410 9.713 1.00 16.51 ATOM 1048 CD2 TYR A 163 27.080 4.071 8.983 1.00 16.57 ATOM 1049 CE2 TYR A 163 26.318 4.109 10.142 1.00 16.17 ATOM 1050 CZ TYR A 163 25.672 5.278 10.504 1.00 16.63 ATOM 1051 OH TYR A 163 24.941 5.325 11.669 1.00 17.13 ATOM 1052 C TYR A 163 26.051 5.516 5.509 1.00 16.21 ATOM 1053 O TYR A 163 24.928 5.091 5.814 1.00 16.01 ATOM 1054 N GLN A 164 26.258 6.741 5.038 1.00 15.69 ATOM 1055 CA GLN A 164 25.155 7.664 4.833 1.00 15.63 ATOM 1056 CB GLN A 164 25.701 9.062 4.542 1.00 15.91 ATOM 1057 CG GLN A 164 26.371 9.682 5.767 1.00 15.22 ATOM 1058 CD GLN A 164 27.060 10.984 5.447 1.00 16.39 ATOM 1059 OE1 GLN A 164 28.232 10.998 5.047 1.00 18.24 ATOM 1060 NE2 GLN A 164 26.345 12.090 5.614 1.00 14.14 ATOM 1061 C GLN A 164 24.230 7.170 3.720 1.00 16.14 ATOM 1062 O GLN A 164 23.009 7.326 3.814 1.00 15.63 ATOM 1063 N LEU A 165 24.798 6.556 2.679 1.00 14.93 ATOM 1064 CA LEU A 165 23.976 6.013 1.599 1.00 14.80 ATOM 1065 CB LEU A 165 24.849 5.432 0.480 1.00 14.40 ATOM 1066 CG LEU A 165 24.103 4.553 -0.546 1.00 14.94 ATOM 1067 CD1 LEU A 165 22.926 5.337 -1.149 1.00 14.06 ATOM 1068 CD2 LEU A 165 25.063 4.120 -1.636 1.00 14.75 ATOM 1069 C LEU A 165 23.086 4.897 2.171 1.00 15.71 ATOM 1070 O LEU A 165 21.887 4.842 1.894 1.00 15.65 ATOM 1071 N PHE A 166 23.669 4.014 2.978 1.00 15.23 ATOM 1072 CA PHE A 166 22.887 2.929 3.550 1.00 15.73 ATOM 1073 CB PHE A 166 23.811 1.940 4.261 1.00 16.40 ATOM 1074 CG PHE A 166 24.556 1.043 3.317 1.00 16.67 ATOM 1075 CD1 PHE A 166 25.948 0.968 3.357 1.00 18.69 ATOM 1076 CD2 PHE A 166 23.865 0.282 2.372 1.00 18.23 ATOM 1077 CE1 PHE A 166 26.650 0.137 2.459 1.00 19.49 ATOM 1078 CE2 PHE A 166 24.547 -0.550 1.467 1.00 19.45 ATOM 1079 CZ PHE A 166 25.946 -0.622 1.512 1.00 18.61 ATOM 1080 C PHE A 166 21.783 3.448 4.475 1.00 16.26 ATOM 1081 O PHE A 166 20.694 2.875 4.527 1.00 16.41 ATOM 1082 N ARG A 167 22.042 4.543 5.190 1.00 16.25 ATOM 1083 CA ARG A 167 21.023 5.123 6.065 1.00 15.49 ATOM 1084 CB ARG A 167 21.600 6.290 6.862 1.00 15.45 ATOM 1085 CG ARG A 167 22.324 5.875 8.119 1.00 15.48 ATOM 1086 CD ARG A 167 22.469 7.063 9.069 1.00 17.50 ATOM 1087 NE ARG A 167 21.199 7.436 9.691 1.00 16.65 ATOM 1088 CZ ARG A 167 20.975 8.586 10.317 1.00 17.52 ATOM 1089 NH1 ARG A 167 21.937 9.500 10.411 1.00 16.44 ATOM 1090 NH2 ARG A 167 19.787 8.815 10.866 1.00 17.95 ATOM 1091 C ARG A 167 19.863 5.618 5.211 1.00 16.08 ATOM 1092 O ARG A 167 18.701 5.395 5.551 1.00 16.88 ATOM 1093 N SER A 168 20.164 6.293 4.099 1.00 15.10 ATOM 1094 CA SER A 168 19.100 6.791 3.232 1.00 15.10 ATOM 1095 CB SER A 168 19.666 7.677 2.099 1.00 14.28 ATOM 1096 OG SER A 168 20.280 6.928 1.068 1.00 13.30 ATOM 1097 C SER A 168 18.268 5.637 2.653 1.00 14.97 ATOM 1098 O SER A 168 17.046 5.765 2.520 1.00 15.45 ATOM 1099 N LEU A 169 18.922 4.519 2.322 1.00 14.72 ATOM 1100 CA LEU A 169 18.229 3.346 1.778 1.00 14.87 ATOM 1101 CB LEU A 169 19.240 2.343 1.202 1.00 12.90 ATOM 1102 CG LEU A 169 20.017 2.823 -0.033 1.00 13.64 ATOM 1103 CD1 LEU A 169 20.911 1.696 -0.560 1.00 13.79 ATOM 1104 CD2 LEU A 169 19.044 3.309 -1.112 1.00 13.80 ATOM 1105 C LEU A 169 17.383 2.665 2.868 1.00 16.00 ATOM 1106 O LEU A 169 16.260 2.226 2.602 1.00 16.34 ATOM 1107 N ALA A 170 17.925 2.563 4.082 1.00 16.54 ATOM 1108 CA ALA A 170 17.172 1.977 5.193 1.00 16.68 ATOM 1109 CB ALA A 170 17.992 2.036 6.488 1.00 15.70 ATOM 1110 C ALA A 170 15.882 2.789 5.350 1.00 17.35 ATOM 1111 O ALA A 170 14.789 2.238 5.498 1.00 17.37 ATOM 1112 N TYR A 171 16.011 4.107 5.296 1.00 16.49 ATOM 1113 CA TYR A 171 14.859 4.969 5.441 1.00 17.72 ATOM 1114 CB TYR A 171 15.312 6.433 5.515 1.00 17.51 ATOM 1115 CG TYR A 171 14.179 7.421 5.658 1.00 18.90 ATOM 1116 CD1 TYR A 171 13.727 8.149 4.562 1.00 19.12 ATOM 1117 CE1 TYR A 171 12.693 9.059 4.678 1.00 20.56 ATOM 1118 CD2 TYR A 171 13.557 7.629 6.892 1.00 19.48 ATOM 1119 CE2 TYR A 171 12.507 8.546 7.021 1.00 21.03 ATOM 1120 CZ TYR A 171 12.083 9.257 5.912 1.00 20.29 ATOM 1121 OH TYR A 171 11.066 10.192 6.022 1.00 22.06 ATOM 1122 C TYR A 171 13.813 4.783 4.320 1.00 18.25 ATOM 1123 O TYR A 171 12.643 4.536 4.605 1.00 18.87 ATOM 1124 N ILE A 172 14.204 4.890 3.052 1.00 16.85 ATOM 1125 CA ILE A 172 13.190 4.728 2.010 1.00 17.09 ATOM 1126 CB ILE A 172 13.693 5.151 0.601 1.00 16.71 ATOM 1127 CG2 ILE A 172 13.997 6.631 0.601 1.00 16.80 ATOM 1128 CG1 ILE A 172 14.902 4.321 0.167 1.00 16.41 ATOM 1129 CD1 ILE A 172 15.300 4.567 -1.307 1.00 16.65 ATOM 1130 C ILE A 172 12.623 3.314 1.931 1.00 16.51 ATOM 1131 O ILE A 172 11.437 3.144 1.666 1.00 16.94 ATOM 1132 N HIS A 173 13.451 2.305 2.175 1.00 17.07 ATOM 1133 CA HIS A 173 12.987 0.922 2.108 1.00 18.02 ATOM 1134 CB HIS A 173 14.161 -0.047 2.236 1.00 17.17 ATOM 1135 CG HIS A 173 15.026 -0.098 1.018 1.00 17.15 ATOM 1136 CD2 HIS A 173 14.966 0.595 -0.145 1.00 17.84 ATOM 1137 ND1 HIS A 173 16.119 -0.927 0.913 1.00 18.09 ATOM 1138 CE1 HIS A 173 16.697 -0.744 -0.263 1.00 18.88 ATOM 1139 NE2 HIS A 173 16.016 0.177 -0.924 1.00 18.01 ATOM 1140 C HIS A 173 11.953 0.606 3.189 1.00 19.53 ATOM 1141 O HIS A 173 11.100 -0.275 3.001 1.00 19.96 ATOM 1142 N SER A 174 12.023 1.318 4.312 1.00 19.07 ATOM 1143 CA SER A 174 11.084 1.084 5.402 1.00 20.01 ATOM 1144 CB SER A 174 11.533 1.823 6.677 1.00 18.49 ATOM 1145 OG SER A 174 11.275 3.213 6.595 1.00 17.80 ATOM 1146 C SER A 174 9.676 1.506 4.987 1.00 21.95 ATOM 1147 O SER A 174 8.695 1.131 5.630 1.00 23.74 ATOM 1148 N PHE A 175 9.573 2.298 3.922 1.00 22.58 ATOM 1149 CA PHE A 175 8.269 2.719 3.408 1.00 23.49 ATOM 1150 CB PHE A 175 8.280 4.188 2.980 1.00 24.97 ATOM 1151 CG PHE A 175 8.400 5.155 4.122 1.00 28.40 ATOM 1152 CD1 PHE A 175 7.315 5.389 4.973 1.00 29.22 ATOM 1153 CD2 PHE A 175 9.603 5.823 4.361 1.00 28.17 ATOM 1154 CE1 PHE A 175 7.430 6.271 6.047 1.00 30.69 ATOM 1155 CE2 PHE A 175 9.727 6.700 5.425 1.00 30.02 ATOM 1156 CZ PHE A 175 8.643 6.929 6.275 1.00 30.44 ATOM 1157 C PHE A 175 7.948 1.872 2.179 1.00 23.21 ATOM 1158 O PHE A 175 6.979 2.141 1.477 1.00 23.94 ATOM 1159 N GLY A 176 8.772 0.858 1.920 1.00 22.98 ATOM 1160 CA GLY A 176 8.566 0.001 0.764 1.00 22.64 ATOM 1161 C GLY A 176 8.995 0.655 -0.543 1.00 22.97 ATOM 1162 O GLY A 176 8.752 0.112 -1.624 1.00 23.29 ATOM 1163 N ILE A 177 9.643 1.820 -0.450 1.00 21.88 ATOM 1164 CA ILE A 177 10.092 2.552 -1.638 1.00 20.29 ATOM 1165 CB ILE A 177 10.061 4.087 -1.404 1.00 20.51 ATOM 1166 CG2 ILE A 177 10.714 4.824 -2.569 1.00 19.47 ATOM 1167 CG1 ILE A 177 8.611 4.558 -1.252 1.00 21.13 ATOM 1168 CD1 ILE A 177 8.487 5.936 -0.621 1.00 22.20 ATOM 1169 C ILE A 177 11.506 2.148 -2.052 1.00 20.12 ATOM 1170 O ILE A 177 12.435 2.147 -1.237 1.00 19.01 ATOM 1171 N CYS A 178 11.646 1.803 -3.328 1.00 19.64 ATOM 1172 CA CYS A 178 12.929 1.405 -3.912 1.00 19.22 ATOM 1173 CB CYS A 178 12.756 0.107 -4.717 1.00 19.13 ATOM 1174 SG CYS A 178 14.273 -0.615 -5.409 1.00 20.10 ATOM 1175 C CYS A 178 13.357 2.555 -4.830 1.00 18.68 ATOM 1176 O CYS A 178 12.552 3.065 -5.601 1.00 18.08 ATOM 1177 N HIS A 179 14.624 2.959 -4.743 1.00 17.54 ATOM 1178 CA HIS A 179 15.132 4.059 -5.555 1.00 16.53 ATOM 1179 CB HIS A 179 16.485 4.523 -5.001 1.00 15.47 ATOM 1180 CG HIS A 179 17.081 5.677 -5.743 1.00 15.98 ATOM 1181 CD2 HIS A 179 17.734 5.732 -6.928 1.00 14.32 ATOM 1182 ND1 HIS A 179 17.039 6.973 -5.267 1.00 16.20 ATOM 1183 CE1 HIS A 179 17.638 7.774 -6.130 1.00 14.72 ATOM 1184 NE2 HIS A 179 18.069 7.046 -7.145 1.00 17.10 ATOM 1185 C HIS A 179 15.257 3.656 -7.029 1.00 16.17 ATOM 1186 O HIS A 179 14.853 4.407 -7.911 1.00 15.54 ATOM 1187 N ARG A 180 15.826 2.474 -7.271 1.00 16.06 ATOM 1188 CA ARG A 180 15.990 1.909 -8.614 1.00 16.96 ATOM 1189 CB ARG A 180 14.624 1.825 -9.320 1.00 16.22 ATOM 1190 CG ARG A 180 13.562 1.049 -8.518 1.00 16.42 ATOM 1191 CD ARG A 180 12.513 0.433 -9.442 1.00 16.49 ATOM 1192 NE ARG A 180 11.716 1.457 -10.113 1.00 17.03 ATOM 1193 CZ ARG A 180 10.698 1.193 -10.927 1.00 17.60 ATOM 1194 NH1 ARG A 180 10.353 -0.067 -11.175 1.00 16.74 ATOM 1195 NH2 ARG A 180 10.008 2.189 -11.472 1.00 17.50 ATOM 1196 C ARG A 180 17.013 2.578 -9.543 1.00 17.37 ATOM 1197 O ARG A 180 17.134 2.176 -10.706 1.00 18.13 ATOM 1198 N ASP A 181 17.745 3.580 -9.046 1.00 17.23 ATOM 1199 CA ASP A 181 18.783 4.240 -9.852 1.00 17.37 ATOM 1200 CB ASP A 181 18.214 5.444 -10.610 1.00 17.87 ATOM 1201 CG ASP A 181 19.094 5.871 -11.776 1.00 19.99 ATOM 1202 OD1 ASP A 181 19.907 5.046 -12.261 1.00 20.78 ATOM 1203 OD2 ASP A 181 18.971 7.034 -12.208 1.00 21.11 ATOM 1204 C ASP A 181 19.949 4.701 -8.976 1.00 16.56 ATOM 1205 O ASP A 181 20.403 5.848 -9.076 1.00 16.89 ATOM 1206 N ILE A 182 20.425 3.810 -8.110 1.00 16.14 ATOM 1207 CA ILE A 182 21.543 4.138 -7.232 1.00 15.87 ATOM 1208 CB ILE A 182 21.658 3.132 -6.054 1.00 15.34 ATOM 1209 CG2 ILE A 182 22.975 3.369 -5.281 1.00 15.87 ATOM 1210 CG1 ILE A 182 20.428 3.242 -5.131 1.00 14.60 ATOM 1211 CD1 ILE A 182 20.216 4.611 -4.467 1.00 14.54 ATOM 1212 C ILE A 182 22.832 4.120 -8.058 1.00 16.14 ATOM 1213 O ILE A 182 23.188 3.100 -8.662 1.00 15.99 ATOM 1214 N LYS A 183 23.518 5.260 -8.084 1.00 16.34 ATOM 1215 CA LYS A 183 24.763 5.411 -8.836 1.00 16.91 ATOM 1216 CB LYS A 183 24.462 5.537 -10.336 1.00 16.32 ATOM 1217 CG LYS A 183 23.633 6.747 -10.696 1.00 18.06 ATOM 1218 CD LYS A 183 23.372 6.796 -12.193 1.00 19.29 ATOM 1219 CE LYS A 183 22.628 8.054 -12.573 1.00 22.44 ATOM 1220 NZ LYS A 183 22.262 8.026 -14.019 1.00 26.60 ATOM 1221 C LYS A 183 25.483 6.664 -8.328 1.00 17.49 ATOM 1222 O LYS A 183 24.857 7.554 -7.744 1.00 16.90 ATOM 1223 N PRO A 184 26.801 6.768 -8.572 1.00 18.65 ATOM 1224 CD PRO A 184 27.651 5.808 -9.301 1.00 18.87 ATOM 1225 CA PRO A 184 27.573 7.930 -8.106 1.00 18.72 ATOM 1226 CB PRO A 184 28.959 7.716 -8.724 1.00 19.35 ATOM 1227 CG PRO A 184 29.048 6.219 -8.893 1.00 19.38 ATOM 1228 C PRO A 184 27.009 9.304 -8.415 1.00 18.58 ATOM 1229 O PRO A 184 27.101 10.206 -7.585 1.00 18.74 ATOM 1230 N GLN A 185 26.427 9.465 -9.596 1.00 19.00 ATOM 1231 CA GLN A 185 25.866 10.748 -9.998 1.00 20.70 ATOM 1232 CB GLN A 185 25.532 10.731 -11.487 1.00 24.20 ATOM 1233 CG GLN A 185 26.753 10.651 -12.379 1.00 30.41 ATOM 1234 CD GLN A 185 26.414 10.161 -13.774 1.00 35.02 ATOM 1235 OE1 GLN A 185 25.746 10.861 -14.547 1.00 37.97 ATOM 1236 NE2 GLN A 185 26.865 8.948 -14.106 1.00 36.63 ATOM 1237 C GLN A 185 24.618 11.143 -9.213 1.00 19.85 ATOM 1238 O GLN A 185 24.219 12.310 -9.215 1.00 19.57 ATOM 1239 N ASN A 186 23.998 10.174 -8.548 1.00 18.81 ATOM 1240 CA ASN A 186 22.803 10.466 -7.765 1.00 18.38 ATOM 1241 CB ASN A 186 21.730 9.402 -8.027 1.00 17.74 ATOM 1242 CG ASN A 186 21.085 9.571 -9.385 1.00 18.36 ATOM 1243 OD1 ASN A 186 21.151 10.651 -9.973 1.00 18.43 ATOM 1244 ND2 ASN A 186 20.462 8.513 -9.895 1.00 16.98 ATOM 1245 C ASN A 186 23.103 10.572 -6.278 1.00 18.18 ATOM 1246 O ASN A 186 22.191 10.561 -5.449 1.00 17.88 ATOM 1247 N LEU A 187 24.384 10.688 -5.944 1.00 17.16 ATOM 1248 CA LEU A 187 24.810 10.819 -4.556 1.00 17.18 ATOM 1249 CB LEU A 187 25.802 9.712 -4.202 1.00 16.88 ATOM 1250 CG LEU A 187 25.303 8.284 -4.439 1.00 17.08 ATOM 1251 CD1 LEU A 187 26.398 7.298 -4.066 1.00 17.96 ATOM 1252 CD2 LEU A 187 24.032 8.033 -3.605 1.00 16.41 ATOM 1253 C LEU A 187 25.466 12.186 -4.393 1.00 17.84 ATOM 1254 O LEU A 187 26.655 12.356 -4.704 1.00 17.58 ATOM 1255 N LEU A 188 24.686 13.161 -3.931 1.00 17.62 ATOM 1256 CA LEU A 188 25.195 14.520 -3.745 1.00 17.83 ATOM 1257 CB LEU A 188 24.032 15.515 -3.635 1.00 17.84 ATOM 1258 CG LEU A 188 22.995 15.468 -4.764 1.00 17.71 ATOM 1259 CD1 LEU A 188 21.947 16.548 -4.530 1.00 18.68 ATOM 1260 CD2 LEU A 188 23.670 15.661 -6.115 1.00 18.05 ATOM 1261 C LEU A 188 26.084 14.599 -2.504 1.00 18.43 ATOM 1262 O LEU A 188 25.862 13.886 -1.524 1.00 17.26 ATOM 1263 N LEU A 189 27.087 15.471 -2.559 1.00 18.94 ATOM 1264 CA LEU A 189 28.036 15.631 -1.463 1.00 21.11 ATOM 1265 CB LEU A 189 29.366 14.954 -1.801 1.00 21.94 ATOM 1266 CG LEU A 189 29.565 13.455 -1.898 1.00 24.21 ATOM 1267 CD1 LEU A 189 30.993 13.177 -2.390 1.00 23.13 ATOM 1268 CD2 LEU A 189 29.322 12.831 -0.526 1.00 24.55 ATOM 1269 C LEU A 189 28.392 17.073 -1.161 1.00 22.19 ATOM 1270 O LEU A 189 28.506 17.896 -2.068 1.00 21.41 ATOM 1271 N ASP A 190 28.575 17.363 0.121 1.00 24.06 ATOM 1272 CA ASP A 190 29.046 18.673 0.540 1.00 26.82 ATOM 1273 CB ASP A 190 28.193 19.272 1.649 1.00 29.14 ATOM 1274 CG ASP A 190 28.704 20.633 2.087 1.00 31.91 ATOM 1275 OD1 ASP A 190 29.887 20.941 1.821 1.00 34.82 ATOM 1276 OD2 ASP A 190 27.931 21.396 2.694 1.00 34.09 ATOM 1277 C ASP A 190 30.417 18.299 1.106 1.00 27.64 ATOM 1278 O ASP A 190 30.517 17.841 2.241 1.00 27.08 ATOM 1279 N PRO A 191 31.487 18.474 0.309 1.00 29.12 ATOM 1280 CD PRO A 191 31.428 19.035 -1.051 1.00 30.27 ATOM 1281 CA PRO A 191 32.870 18.153 0.696 1.00 29.84 ATOM 1282 CB PRO A 191 33.715 18.693 -0.467 1.00 30.37 ATOM 1283 CG PRO A 191 32.803 19.610 -1.232 1.00 30.71 ATOM 1284 C PRO A 191 33.369 18.672 2.039 1.00 29.82 ATOM 1285 O PRO A 191 34.106 17.974 2.737 1.00 30.70 ATOM 1286 N ASP A 192 32.979 19.887 2.402 1.00 29.62 ATOM 1287 CA ASP A 192 33.431 20.464 3.658 1.00 29.78 ATOM 1288 CB ASP A 192 33.112 21.957 3.687 1.00 32.57 ATOM 1289 CG ASP A 192 33.903 22.741 2.645 1.00 35.15 ATOM 1290 OD1 ASP A 192 33.546 23.917 2.403 1.00 37.32 ATOM 1291 OD2 ASP A 192 34.872 22.184 2.068 1.00 35.97 ATOM 1292 C ASP A 192 32.856 19.787 4.897 1.00 28.64 ATOM 1293 O ASP A 192 33.561 19.612 5.896 1.00 28.92 ATOM 1294 N THR A 193 31.586 19.398 4.838 1.00 26.28 ATOM 1295 CA THR A 193 30.940 18.741 5.977 1.00 24.30 ATOM 1296 CB THR A 193 29.491 19.219 6.128 1.00 24.35 ATOM 1297 OG1 THR A 193 28.758 18.859 4.953 1.00 22.93 ATOM 1298 CG2 THR A 193 29.441 20.735 6.298 1.00 23.99 ATOM 1299 C THR A 193 30.929 17.214 5.858 1.00 23.06 ATOM 1300 O THR A 193 30.677 16.505 6.834 1.00 22.25 ATOM 1301 N ALA A 194 31.207 16.721 4.657 1.00 21.83 ATOM 1302 CA ALA A 194 31.220 15.289 4.380 1.00 21.37 ATOM 1303 CB ALA A 194 32.124 14.569 5.366 1.00 21.40 ATOM 1304 C ALA A 194 29.804 14.694 4.410 1.00 20.98 ATOM 1305 O ALA A 194 29.622 13.484 4.560 1.00 21.21 ATOM 1306 N VAL A 195 28.802 15.550 4.248 1.00 20.61 ATOM 1307 CA VAL A 195 27.421 15.096 4.233 1.00 19.54 ATOM 1308 CB VAL A 195 26.446 16.230 4.634 1.00 19.96 ATOM 1309 CG1 VAL A 195 24.999 15.805 4.348 1.00 20.22 ATOM 1310 CG2 VAL A 195 26.622 16.561 6.105 1.00 18.92 ATOM 1311 C VAL A 195 27.048 14.606 2.837 1.00 19.26 ATOM 1312 O VAL A 195 27.361 15.253 1.834 1.00 18.91 ATOM 1313 N LEU A 196 26.401 13.444 2.785 1.00 18.17 ATOM 1314 CA LEU A 196 25.948 12.860 1.525 1.00 17.36 ATOM 1315 CB LEU A 196 26.400 11.393 1.409 1.00 17.05 ATOM 1316 CG LEU A 196 25.885 10.601 0.190 1.00 17.81 ATOM 1317 CD1 LEU A 196 26.912 9.546 -0.207 1.00 18.37 ATOM 1318 CD2 LEU A 196 24.530 9.945 0.497 1.00 17.36 ATOM 1319 C LEU A 196 24.420 12.923 1.528 1.00 17.10 ATOM 1320 O LEU A 196 23.780 12.689 2.564 1.00 16.50 ATOM 1321 N LYS A 197 23.845 13.255 0.379 1.00 16.59 ATOM 1322 CA LYS A 197 22.397 13.326 0.231 1.00 16.75 ATOM 1323 CB LYS A 197 21.926 14.782 0.214 1.00 17.73 ATOM 1324 CG LYS A 197 21.916 15.416 1.606 1.00 20.93 ATOM 1325 CD LYS A 197 21.480 16.856 1.549 1.00 22.66 ATOM 1326 CE LYS A 197 21.746 17.541 2.873 1.00 22.69 ATOM 1327 NZ LYS A 197 21.280 16.717 4.013 1.00 25.66 ATOM 1328 C LYS A 197 21.974 12.636 -1.054 1.00 16.20 ATOM 1329 O LYS A 197 22.411 13.002 -2.147 1.00 15.79 ATOM 1330 N LEU A 198 21.130 11.623 -0.909 1.00 15.31 ATOM 1331 CA LEU A 198 20.608 10.871 -2.042 1.00 15.04 ATOM 1332 CB LEU A 198 19.886 9.616 -1.530 1.00 14.31 ATOM 1333 CG LEU A 198 19.180 8.718 -2.555 1.00 14.96 ATOM 1334 CD1 LEU A 198 20.179 8.073 -3.517 1.00 15.25 ATOM 1335 CD2 LEU A 198 18.408 7.648 -1.784 1.00 14.83 ATOM 1336 C LEU A 198 19.635 11.758 -2.823 1.00 14.91 ATOM 1337 O LEU A 198 18.832 12.480 -2.228 1.00 14.30 ATOM 1338 N CYS A 199 19.715 11.720 -4.147 1.00 14.78 ATOM 1339 CA CYS A 199 18.831 12.528 -4.973 1.00 17.27 ATOM 1340 CB CYS A 199 19.553 13.786 -5.472 1.00 17.23 ATOM 1341 SG CYS A 199 20.688 13.521 -6.867 1.00 20.31 ATOM 1342 C CYS A 199 18.285 11.753 -6.164 1.00 17.25 ATOM 1343 O CYS A 199 18.566 10.566 -6.332 1.00 18.09 ATOM 1344 N ASP A 200 17.488 12.445 -6.971 1.00 18.32 ATOM 1345 CA ASP A 200 16.865 11.892 -8.169 1.00 18.75 ATOM 1346 CB ASP A 200 17.922 11.443 -9.175 1.00 19.25 ATOM 1347 CG ASP A 200 17.308 11.004 -10.492 1.00 20.73 ATOM 1348 OD1 ASP A 200 16.068 11.141 -10.647 1.00 20.80 ATOM 1349 OD2 ASP A 200 18.057 10.520 -11.364 1.00 21.57 ATOM 1350 C ASP A 200 15.924 10.736 -7.897 1.00 18.92 ATOM 1351 O ASP A 200 16.297 9.565 -8.029 1.00 19.47 ATOM 1352 N PHE A 201 14.691 11.063 -7.536 1.00 19.27 ATOM 1353 CA PHE A 201 13.708 10.027 -7.267 1.00 19.43 ATOM 1354 CB PHE A 201 12.900 10.406 -6.027 1.00 19.36 ATOM 1355 CG PHE A 201 13.680 10.236 -4.759 1.00 19.69 ATOM 1356 CD1 PHE A 201 14.594 11.208 -4.354 1.00 19.13 ATOM 1357 CD2 PHE A 201 13.595 9.054 -4.037 1.00 18.92 ATOM 1358 CE1 PHE A 201 15.415 10.997 -3.256 1.00 19.25 ATOM 1359 CE2 PHE A 201 14.417 8.834 -2.935 1.00 19.21 ATOM 1360 CZ PHE A 201 15.328 9.806 -2.548 1.00 18.93 ATOM 1361 C PHE A 201 12.814 9.787 -8.483 1.00 19.74 ATOM 1362 O PHE A 201 11.692 9.290 -8.361 1.00 19.89 ATOM 1363 N GLY A 202 13.353 10.111 -9.655 1.00 19.05 ATOM 1364 CA GLY A 202 12.622 9.942 -10.900 1.00 19.94 ATOM 1365 C GLY A 202 12.367 8.504 -11.323 1.00 20.34 ATOM 1366 O GLY A 202 11.568 8.261 -12.221 1.00 21.95 ATOM 1367 N SER A 203 13.037 7.546 -10.698 1.00 19.56 ATOM 1368 CA SER A 203 12.837 6.142 -11.046 1.00 19.88 ATOM 1369 CB SER A 203 14.167 5.475 -11.421 1.00 20.18 ATOM 1370 OG SER A 203 14.681 5.998 -12.628 1.00 22.54 ATOM 1371 C SER A 203 12.257 5.397 -9.861 1.00 19.50 ATOM 1372 O SER A 203 11.930 4.220 -9.966 1.00 19.59 ATOM 1373 N ALA A 204 12.141 6.094 -8.733 1.00 19.37 ATOM 1374 CA ALA A 204 11.648 5.505 -7.496 1.00 19.97 ATOM 1375 CB ALA A 204 11.804 6.508 -6.351 1.00 19.59 ATOM 1376 C ALA A 204 10.208 5.000 -7.570 1.00 20.54 ATOM 1377 O ALA A 204 9.368 5.559 -8.269 1.00 20.42 ATOM 1378 N LYS A 205 9.935 3.933 -6.833 1.00 22.86 ATOM 1379 CA LYS A 205 8.606 3.337 -6.826 1.00 24.27 ATOM 1380 CB LYS A 205 8.395 2.545 -8.122 1.00 24.60 ATOM 1381 CG LYS A 205 7.029 1.882 -8.253 1.00 25.34 ATOM 1382 CD LYS A 205 6.815 1.391 -9.682 1.00 26.14 ATOM 1383 CE LYS A 205 5.352 1.025 -9.931 1.00 27.10 ATOM 1384 NZ LYS A 205 5.010 -0.260 -9.279 1.00 26.87 ATOM 1385 C LYS A 205 8.391 2.415 -5.637 1.00 25.17 ATOM 1386 O LYS A 205 9.299 1.693 -5.207 1.00 23.72 ATOM 1387 N GLN A 206 7.183 2.438 -5.096 1.00 26.44 ATOM 1388 CA GLN A 206 6.886 1.558 -3.988 1.00 28.38 ATOM 1389 CB GLN A 206 5.611 2.005 -3.278 1.00 31.11 ATOM 1390 CG GLN A 206 4.918 0.871 -2.547 1.00 35.55 ATOM 1391 CD GLN A 206 4.331 1.307 -1.233 1.00 38.10 ATOM 1392 OE1 GLN A 206 4.355 2.493 -0.894 1.00 40.54 ATOM 1393 NE2 GLN A 206 3.799 0.350 -0.475 1.00 38.77 ATOM 1394 C GLN A 206 6.695 0.168 -4.590 1.00 28.46 ATOM 1395 O GLN A 206 5.870 -0.018 -5.491 1.00 28.34 ATOM 1396 N LEU A 207 7.470 -0.800 -4.113 1.00 28.61 ATOM 1397 CA LEU A 207 7.376 -2.162 -4.621 1.00 30.02 ATOM 1398 CB LEU A 207 8.751 -2.824 -4.639 1.00 28.91 ATOM 1399 CG LEU A 207 9.812 -2.085 -5.460 1.00 28.08 ATOM 1400 CD1 LEU A 207 11.073 -2.921 -5.533 1.00 27.86 ATOM 1401 CD2 LEU A 207 9.273 -1.779 -6.850 1.00 27.16 ATOM 1402 C LEU A 207 6.431 -2.974 -3.760 1.00 31.68 ATOM 1403 O LEU A 207 6.610 -3.071 -2.546 1.00 32.11 ATOM 1404 N VAL A 208 5.424 -3.556 -4.401 1.00 33.22 ATOM 1405 CA VAL A 208 4.430 -4.360 -3.704 1.00 35.53 ATOM 1406 CB VAL A 208 3.003 -3.902 -4.060 1.00 35.36 ATOM 1407 CG1 VAL A 208 1.987 -4.669 -3.226 1.00 35.74 ATOM 1408 CG2 VAL A 208 2.869 -2.406 -3.830 1.00 35.13 ATOM 1409 C VAL A 208 4.592 -5.822 -4.088 1.00 37.14 ATOM 1410 O VAL A 208 4.523 -6.174 -5.266 1.00 37.42 ATOM 1411 N ARG A 209 4.821 -6.667 -3.091 1.00 39.36 ATOM 1412 CA ARG A 209 4.993 -8.091 -3.329 1.00 41.61 ATOM 1413 CB ARG A 209 4.941 -8.841 -1.996 1.00 44.20 ATOM 1414 CG ARG A 209 4.902 -10.350 -2.124 1.00 48.00 ATOM 1415 CD ARG A 209 6.198 -10.882 -2.699 1.00 51.23 ATOM 1416 NE ARG A 209 6.360 -12.315 -2.461 1.00 54.10 ATOM 1417 CZ ARG A 209 7.444 -13.007 -2.804 1.00 55.55 ATOM 1418 NH1 ARG A 209 8.461 -12.394 -3.402 1.00 56.47 ATOM 1419 NH2 ARG A 209 7.515 -14.309 -2.549 1.00 55.99 ATOM 1420 C ARG A 209 3.896 -8.592 -4.271 1.00 41.55 ATOM 1421 O ARG A 209 2.715 -8.312 -4.066 1.00 41.91 ATOM 1422 N GLY A 210 4.288 -9.302 -5.324 1.00 41.32 ATOM 1423 CA GLY A 210 3.303 -9.817 -6.261 1.00 40.52 ATOM 1424 C GLY A 210 2.967 -8.922 -7.442 1.00 40.22 ATOM 1425 O GLY A 210 2.395 -9.393 -8.421 1.00 40.50 ATOM 1426 N GLU A 211 3.296 -7.635 -7.354 1.00 39.50 ATOM 1427 CA GLU A 211 3.030 -6.700 -8.450 1.00 38.99 ATOM 1428 CB GLU A 211 2.702 -5.315 -7.907 1.00 40.48 ATOM 1429 CG GLU A 211 1.291 -5.174 -7.373 1.00 43.65 ATOM 1430 CD GLU A 211 1.083 -3.854 -6.647 1.00 45.70 ATOM 1431 OE1 GLU A 211 1.902 -2.927 -6.856 1.00 47.37 ATOM 1432 OE2 GLU A 211 0.106 -3.746 -5.870 1.00 46.69 ATOM 1433 C GLU A 211 4.276 -6.607 -9.331 1.00 37.48 ATOM 1434 O GLU A 211 5.365 -6.317 -8.840 1.00 37.85 ATOM 1435 N PRO A 212 4.130 -6.840 -10.645 1.00 35.99 ATOM 1436 CD PRO A 212 2.894 -7.172 -11.375 1.00 35.28 ATOM 1437 CA PRO A 212 5.292 -6.771 -11.541 1.00 34.39 ATOM 1438 CB PRO A 212 4.780 -7.395 -12.839 1.00 34.56 ATOM 1439 CG PRO A 212 3.320 -7.111 -12.819 1.00 35.16 ATOM 1440 C PRO A 212 5.830 -5.359 -11.760 1.00 32.64 ATOM 1441 O PRO A 212 5.084 -4.381 -11.718 1.00 32.41 ATOM 1442 N ASN A 213 7.133 -5.268 -12.001 1.00 30.54 ATOM 1443 CA ASN A 213 7.777 -3.987 -12.246 1.00 28.58 ATOM 1444 CB ASN A 213 8.471 -3.526 -10.971 1.00 28.23 ATOM 1445 CG ASN A 213 7.479 -3.057 -9.918 1.00 28.73 ATOM 1446 OD1 ASN A 213 6.863 -1.990 -10.052 1.00 28.14 ATOM 1447 ND2 ASN A 213 7.310 -3.856 -8.872 1.00 28.42 ATOM 1448 C ASN A 213 8.767 -4.100 -13.411 1.00 27.27 ATOM 1449 O ASN A 213 9.305 -5.178 -13.662 1.00 27.19 ATOM 1450 N VAL A 214 8.995 -2.996 -14.121 1.00 26.23 ATOM 1451 CA VAL A 214 9.900 -3.010 -15.270 1.00 26.34 ATOM 1452 CB VAL A 214 9.852 -1.693 -16.053 1.00 26.47 ATOM 1453 CG1 VAL A 214 8.456 -1.476 -16.561 1.00 27.19 ATOM 1454 CG2 VAL A 214 10.311 -0.533 -15.186 1.00 26.10 ATOM 1455 C VAL A 214 11.346 -3.303 -14.916 1.00 26.69 ATOM 1456 O VAL A 214 11.876 -2.811 -13.918 1.00 26.08 ATOM 1457 N SER A 215 11.990 -4.103 -15.757 1.00 26.38 ATOM 1458 CA SER A 215 13.365 -4.485 -15.514 1.00 26.27 ATOM 1459 CB SER A 215 13.577 -5.940 -15.939 1.00 26.15 ATOM 1460 OG SER A 215 13.360 -6.083 -17.331 1.00 28.59 ATOM 1461 C SER A 215 14.373 -3.582 -16.219 1.00 25.32 ATOM 1462 O SER A 215 15.573 -3.825 -16.131 1.00 26.31 ATOM 1463 N TYR A 216 13.903 -2.539 -16.899 1.00 23.98 ATOM 1464 CA TYR A 216 14.836 -1.659 -17.590 1.00 23.65 ATOM 1465 CB TYR A 216 14.325 -1.284 -18.987 1.00 25.29 ATOM 1466 CG TYR A 216 12.897 -0.825 -19.038 1.00 27.09 ATOM 1467 CD1 TYR A 216 12.554 0.496 -18.756 1.00 28.31 ATOM 1468 CE1 TYR A 216 11.227 0.926 -18.850 1.00 30.07 ATOM 1469 CD2 TYR A 216 11.887 -1.708 -19.409 1.00 28.28 ATOM 1470 CE2 TYR A 216 10.568 -1.294 -19.507 1.00 30.17 ATOM 1471 CZ TYR A 216 10.243 0.021 -19.229 1.00 30.49 ATOM 1472 OH TYR A 216 8.934 0.423 -19.356 1.00 32.88 ATOM 1473 C TYR A 216 15.225 -0.394 -16.843 1.00 23.10 ATOM 1474 O TYR A 216 15.728 0.555 -17.450 1.00 22.56 ATOM 1475 N ILE A 217 14.990 -0.360 -15.534 1.00 21.38 ATOM 1476 CA ILE A 217 15.405 0.802 -14.766 1.00 20.75 ATOM 1477 CB ILE A 217 14.505 1.052 -13.502 1.00 20.37 ATOM 1478 CG2 ILE A 217 13.362 2.001 -13.871 1.00 20.30 ATOM 1479 CG1 ILE A 217 13.950 -0.258 -12.941 1.00 19.60 ATOM 1480 CD1 ILE A 217 14.984 -1.143 -12.270 1.00 19.20 ATOM 1481 C ILE A 217 16.845 0.517 -14.327 1.00 20.88 ATOM 1482 O ILE A 217 17.373 -0.573 -14.585 1.00 20.46 ATOM 1483 N CYS A 218 17.473 1.497 -13.684 1.00 21.34 ATOM 1484 CA CYS A 218 18.845 1.387 -13.183 1.00 21.86 ATOM 1485 CB CYS A 218 19.031 0.101 -12.385 1.00 20.82 ATOM 1486 SG CYS A 218 20.400 0.200 -11.201 1.00 24.28 ATOM 1487 C CYS A 218 19.926 1.483 -14.259 1.00 23.03 ATOM 1488 O CYS A 218 19.852 0.842 -15.310 1.00 22.13 ATOM 1489 N SER A 219 20.945 2.287 -13.977 1.00 24.17 ATOM 1490 CA SER A 219 22.031 2.502 -14.928 1.00 25.31 ATOM 1491 CB SER A 219 22.772 3.788 -14.579 1.00 26.07 ATOM 1492 OG SER A 219 21.839 4.849 -14.491 1.00 29.89 ATOM 1493 C SER A 219 23.022 1.363 -15.039 1.00 25.86 ATOM 1494 O SER A 219 23.304 0.662 -14.068 1.00 24.07 ATOM 1495 N ARG A 220 23.552 1.201 -16.246 1.00 27.86 ATOM 1496 CA ARG A 220 24.539 0.171 -16.539 1.00 30.34 ATOM 1497 CB ARG A 220 24.990 0.289 -18.000 1.00 33.98 ATOM 1498 CG ARG A 220 25.729 1.591 -18.325 1.00 38.78 ATOM 1499 CD ARG A 220 26.655 1.406 -19.529 1.00 43.51 ATOM 1500 NE ARG A 220 27.693 2.435 -19.601 1.00 47.58 ATOM 1501 CZ ARG A 220 28.623 2.490 -20.551 1.00 49.23 ATOM 1502 NH1 ARG A 220 29.528 3.464 -20.538 1.00 49.82 ATOM 1503 NH2 ARG A 220 28.644 1.572 -21.515 1.00 49.85 ATOM 1504 C ARG A 220 25.742 0.314 -15.608 1.00 29.39 ATOM 1505 O ARG A 220 26.188 1.426 -15.308 1.00 30.16 ATOM 1506 N TYR A 221 26.264 -0.828 -15.183 1.00 28.03 ATOM 1507 CA TYR A 221 27.387 -0.943 -14.255 1.00 26.93 ATOM 1508 CB TYR A 221 28.258 0.323 -14.190 1.00 28.75 ATOM 1509 CG TYR A 221 29.073 0.623 -15.426 1.00 31.35 ATOM 1510 CD1 TYR A 221 28.968 -0.167 -16.574 1.00 32.69 ATOM 1511 CE1 TYR A 221 29.687 0.146 -17.730 1.00 34.45 ATOM 1512 CD2 TYR A 221 29.920 1.733 -15.462 1.00 32.51 ATOM 1513 CE2 TYR A 221 30.641 2.054 -16.608 1.00 33.34 ATOM 1514 CZ TYR A 221 30.520 1.259 -17.735 1.00 34.43 ATOM 1515 OH TYR A 221 31.236 1.577 -18.868 1.00 36.93 ATOM 1516 C TYR A 221 26.830 -1.191 -12.862 1.00 24.44 ATOM 1517 O TYR A 221 27.443 -1.915 -12.087 1.00 23.81 ATOM 1518 N TYR A 222 25.662 -0.608 -12.561 1.00 22.56 ATOM 1519 CA TYR A 222 25.046 -0.732 -11.227 1.00 21.05 ATOM 1520 CB TYR A 222 24.720 0.672 -10.680 1.00 20.73 ATOM 1521 CG TYR A 222 25.891 1.615 -10.812 1.00 19.56 ATOM 1522 CD1 TYR A 222 26.957 1.557 -9.914 1.00 19.82 ATOM 1523 CE1 TYR A 222 28.108 2.322 -10.109 1.00 20.32 ATOM 1524 CD2 TYR A 222 25.997 2.475 -11.909 1.00 21.14 ATOM 1525 CE2 TYR A 222 27.141 3.247 -12.117 1.00 20.19 ATOM 1526 CZ TYR A 222 28.195 3.161 -11.216 1.00 21.23 ATOM 1527 OH TYR A 222 29.341 3.892 -11.442 1.00 20.73 ATOM 1528 C TYR A 222 23.802 -1.618 -11.142 1.00 21.29 ATOM 1529 O TYR A 222 23.233 -1.787 -10.063 1.00 20.02 ATOM 1530 N ARG A 223 23.398 -2.192 -12.274 1.00 21.47 ATOM 1531 CA ARG A 223 22.216 -3.061 -12.341 1.00 22.16 ATOM 1532 CB ARG A 223 21.838 -3.301 -13.802 1.00 23.78 ATOM 1533 CG ARG A 223 21.136 -2.146 -14.467 1.00 26.69 ATOM 1534 CD ARG A 223 21.252 -2.235 -15.978 1.00 28.95 ATOM 1535 NE ARG A 223 20.514 -3.358 -16.555 1.00 32.16 ATOM 1536 CZ ARG A 223 19.190 -3.497 -16.522 1.00 32.05 ATOM 1537 NH1 ARG A 223 18.431 -2.587 -15.935 1.00 32.53 ATOM 1538 NH2 ARG A 223 18.621 -4.543 -17.100 1.00 33.88 ATOM 1539 C ARG A 223 22.404 -4.423 -11.673 1.00 21.59 ATOM 1540 O ARG A 223 23.375 -5.133 -11.964 1.00 21.52 ATOM 1541 N ALA A 224 21.469 -4.802 -10.799 1.00 20.66 ATOM 1542 CA ALA A 224 21.544 -6.106 -10.134 1.00 20.92 ATOM 1543 CB ALA A 224 20.434 -6.242 -9.092 1.00 20.50 ATOM 1544 C ALA A 224 21.393 -7.176 -11.214 1.00 20.91 ATOM 1545 O ALA A 224 20.741 -6.942 -12.235 1.00 20.20 ATOM 1546 N PRO A 225 22.013 -8.352 -11.018 1.00 21.79 ATOM 1547 CD PRO A 225 22.860 -8.730 -9.874 1.00 21.70 ATOM 1548 CA PRO A 225 21.917 -9.427 -12.014 1.00 22.54 ATOM 1549 CB PRO A 225 22.734 -10.571 -11.404 1.00 22.60 ATOM 1550 CG PRO A 225 22.876 -10.225 -9.943 1.00 21.81 ATOM 1551 C PRO A 225 20.494 -9.844 -12.370 1.00 23.24 ATOM 1552 O PRO A 225 20.205 -10.135 -13.531 1.00 23.99 ATOM 1553 N GLU A 226 19.595 -9.865 -11.389 1.00 23.24 ATOM 1554 CA GLU A 226 18.226 -10.251 -11.677 1.00 23.14 ATOM 1555 CB GLU A 226 17.381 -10.309 -10.392 1.00 23.00 ATOM 1556 CG GLU A 226 17.327 -9.033 -9.572 1.00 23.44 ATOM 1557 CD GLU A 226 18.328 -9.034 -8.428 1.00 24.29 ATOM 1558 OE1 GLU A 226 19.437 -9.591 -8.597 1.00 24.32 ATOM 1559 OE2 GLU A 226 18.008 -8.471 -7.358 1.00 23.95 ATOM 1560 C GLU A 226 17.604 -9.299 -12.695 1.00 22.91 ATOM 1561 O GLU A 226 16.727 -9.701 -13.466 1.00 22.52 ATOM 1562 N LEU A 227 18.064 -8.045 -12.707 1.00 22.14 ATOM 1563 CA LEU A 227 17.564 -7.051 -13.658 1.00 22.30 ATOM 1564 CB LEU A 227 17.999 -5.632 -13.254 1.00 21.85 ATOM 1565 CG LEU A 227 17.365 -4.989 -12.009 1.00 21.73 ATOM 1566 CD1 LEU A 227 17.962 -3.606 -11.826 1.00 20.70 ATOM 1567 CD2 LEU A 227 15.849 -4.904 -12.144 1.00 21.68 ATOM 1568 C LEU A 227 18.122 -7.371 -15.053 1.00 22.66 ATOM 1569 O LEU A 227 17.405 -7.297 -16.054 1.00 22.56 ATOM 1570 N ILE A 228 19.403 -7.720 -15.116 1.00 22.74 ATOM 1571 CA ILE A 228 20.013 -8.058 -16.394 1.00 23.58 ATOM 1572 CB ILE A 228 21.519 -8.346 -16.237 1.00 23.35 ATOM 1573 CG2 ILE A 228 22.116 -8.728 -17.586 1.00 23.72 ATOM 1574 CG1 ILE A 228 22.238 -7.087 -15.730 1.00 23.51 ATOM 1575 CD1 ILE A 228 23.639 -7.335 -15.208 1.00 22.46 ATOM 1576 C ILE A 228 19.288 -9.291 -16.948 1.00 24.53 ATOM 1577 O ILE A 228 19.051 -9.396 -18.151 1.00 25.21 ATOM 1578 N PHE A 229 18.925 -10.209 -16.059 1.00 25.17 ATOM 1579 CA PHE A 229 18.211 -11.423 -16.445 1.00 26.66 ATOM 1580 CB PHE A 229 18.314 -12.482 -15.343 1.00 26.43 ATOM 1581 CG PHE A 229 19.608 -13.238 -15.342 1.00 27.67 ATOM 1582 CD1 PHE A 229 20.405 -13.273 -14.204 1.00 28.72 ATOM 1583 CD2 PHE A 229 20.027 -13.927 -16.469 1.00 28.89 ATOM 1584 CE1 PHE A 229 21.603 -13.985 -14.187 1.00 29.55 ATOM 1585 CE2 PHE A 229 21.225 -14.644 -16.464 1.00 29.82 ATOM 1586 CZ PHE A 229 22.014 -14.673 -15.321 1.00 30.01 ATOM 1587 C PHE A 229 16.736 -11.149 -16.726 1.00 27.14 ATOM 1588 O PHE A 229 15.972 -12.080 -16.945 1.00 28.69 ATOM 1589 N GLY A 230 16.328 -9.884 -16.690 1.00 27.29 ATOM 1590 CA GLY A 230 14.946 -9.530 -16.976 1.00 27.25 ATOM 1591 C GLY A 230 13.847 -9.801 -15.950 1.00 28.08 ATOM 1592 O GLY A 230 12.667 -9.835 -16.310 1.00 27.16 ATOM 1593 N ALA A 231 14.200 -9.984 -14.681 1.00 28.10 ATOM 1594 CA ALA A 231 13.182 -10.235 -13.662 1.00 27.61 ATOM 1595 CB ALA A 231 13.841 -10.557 -12.332 1.00 27.81 ATOM 1596 C ALA A 231 12.242 -9.041 -13.502 1.00 27.90 ATOM 1597 O ALA A 231 12.640 -7.893 -13.698 1.00 27.71 ATOM 1598 N THR A 232 10.987 -9.320 -13.158 1.00 27.86 ATOM 1599 CA THR A 232 9.990 -8.267 -12.952 1.00 27.90 ATOM 1600 CB THR A 232 8.821 -8.389 -13.950 1.00 28.28 ATOM 1601 OG1 THR A 232 8.291 -9.720 -13.892 1.00 28.83 ATOM 1602 CG2 THR A 232 9.286 -8.080 -15.370 1.00 27.88 ATOM 1603 C THR A 232 9.436 -8.384 -11.530 1.00 27.72 ATOM 1604 O THR A 232 8.595 -7.592 -11.106 1.00 27.49 ATOM 1605 N ASP A 233 9.921 -9.385 -10.806 1.00 28.01 ATOM 1606 CA ASP A 233 9.501 -9.638 -9.434 1.00 28.94 ATOM 1607 CB ASP A 233 9.114 -11.111 -9.273 1.00 30.79 ATOM 1608 CG ASP A 233 10.298 -12.049 -9.444 1.00 33.35 ATOM 1609 OD1 ASP A 233 11.331 -11.629 -10.014 1.00 34.35 ATOM 1610 OD2 ASP A 233 10.199 -13.214 -9.003 1.00 35.14 ATOM 1611 C ASP A 233 10.620 -9.297 -8.443 1.00 27.93 ATOM 1612 O ASP A 233 10.674 -9.839 -7.335 1.00 27.39 ATOM 1613 N TYR A 234 11.517 -8.404 -8.847 1.00 26.37 ATOM 1614 CA TYR A 234 12.622 -8.013 -7.979 1.00 24.75 ATOM 1615 CB TYR A 234 13.661 -7.219 -8.780 1.00 23.32 ATOM 1616 CG TYR A 234 13.120 -5.979 -9.445 1.00 21.72 ATOM 1617 CD1 TYR A 234 13.053 -4.762 -8.755 1.00 21.02 ATOM 1618 CE1 TYR A 234 12.578 -3.610 -9.372 1.00 19.82 ATOM 1619 CD2 TYR A 234 12.695 -6.008 -10.771 1.00 20.85 ATOM 1620 CE2 TYR A 234 12.220 -4.862 -11.400 1.00 20.73 ATOM 1621 CZ TYR A 234 12.162 -3.666 -10.698 1.00 20.46 ATOM 1622 OH TYR A 234 11.686 -2.534 -11.324 1.00 20.23 ATOM 1623 C TYR A 234 12.144 -7.198 -6.772 1.00 24.28 ATOM 1624 O TYR A 234 11.022 -6.696 -6.742 1.00 24.07 ATOM 1625 N THR A 235 13.017 -7.068 -5.781 1.00 24.65 ATOM 1626 CA THR A 235 12.702 -6.336 -4.558 1.00 24.05 ATOM 1627 CB THR A 235 12.847 -7.243 -3.344 1.00 24.63 ATOM 1628 OG1 THR A 235 14.233 -7.565 -3.168 1.00 25.44 ATOM 1629 CG2 THR A 235 12.054 -8.533 -3.546 1.00 25.06 ATOM 1630 C THR A 235 13.648 -5.148 -4.359 1.00 24.28 ATOM 1631 O THR A 235 14.468 -4.834 -5.225 1.00 23.17 ATOM 1632 N SER A 236 13.536 -4.508 -3.200 1.00 23.65 ATOM 1633 CA SER A 236 14.365 -3.353 -2.867 1.00 23.21 ATOM 1634 CB SER A 236 13.894 -2.741 -1.544 1.00 23.60 ATOM 1635 OG SER A 236 12.630 -2.122 -1.714 1.00 27.21 ATOM 1636 C SER A 236 15.839 -3.722 -2.768 1.00 22.22 ATOM 1637 O SER A 236 16.705 -2.839 -2.746 1.00 21.41 ATOM 1638 N SER A 237 16.128 -5.019 -2.694 1.00 20.75 ATOM 1639 CA SER A 237 17.507 -5.471 -2.602 1.00 20.59 ATOM 1640 CB SER A 237 17.574 -6.971 -2.310 1.00 21.22 ATOM 1641 OG SER A 237 17.136 -7.730 -3.419 1.00 24.47 ATOM 1642 C SER A 237 18.304 -5.148 -3.871 1.00 19.50 ATOM 1643 O SER A 237 19.513 -5.360 -3.904 1.00 18.81 ATOM 1644 N ILE A 238 17.641 -4.657 -4.918 1.00 18.94 ATOM 1645 CA ILE A 238 18.393 -4.287 -6.118 1.00 18.51 ATOM 1646 CB ILE A 238 17.481 -4.013 -7.358 1.00 18.89 ATOM 1647 CG2 ILE A 238 16.671 -5.258 -7.704 1.00 18.53 ATOM 1648 CG1 ILE A 238 16.558 -2.816 -7.106 1.00 18.22 ATOM 1649 CD1 ILE A 238 15.963 -2.226 -8.386 1.00 18.53 ATOM 1650 C ILE A 238 19.191 -3.011 -5.782 1.00 18.30 ATOM 1651 O ILE A 238 20.240 -2.750 -6.373 1.00 18.27 ATOM 1652 N ASP A 239 18.698 -2.229 -4.821 1.00 17.90 ATOM 1653 CA ASP A 239 19.378 -0.988 -4.414 1.00 17.15 ATOM 1654 CB ASP A 239 18.496 -0.141 -3.485 1.00 16.86 ATOM 1655 CG ASP A 239 17.470 0.714 -4.233 1.00 16.61 ATOM 1656 OD1 ASP A 239 16.552 1.228 -3.553 1.00 16.56 ATOM 1657 OD2 ASP A 239 17.570 0.885 -5.471 1.00 16.52 ATOM 1658 C ASP A 239 20.646 -1.344 -3.648 1.00 17.15 ATOM 1659 O ASP A 239 21.638 -0.609 -3.675 1.00 16.70 ATOM 1660 N VAL A 240 20.601 -2.469 -2.944 1.00 17.30 ATOM 1661 CA VAL A 240 21.752 -2.913 -2.159 1.00 17.26 ATOM 1662 CB VAL A 240 21.338 -4.019 -1.166 1.00 17.80 ATOM 1663 CG1 VAL A 240 22.558 -4.653 -0.548 1.00 17.88 ATOM 1664 CG2 VAL A 240 20.453 -3.423 -0.076 1.00 17.18 ATOM 1665 C VAL A 240 22.867 -3.409 -3.093 1.00 17.52 ATOM 1666 O VAL A 240 24.057 -3.197 -2.832 1.00 16.51 ATOM 1667 N TRP A 241 22.489 -4.066 -4.186 1.00 16.75 ATOM 1668 CA TRP A 241 23.491 -4.527 -5.136 1.00 17.39 ATOM 1669 CB TRP A 241 22.845 -5.334 -6.276 1.00 17.62 ATOM 1670 CG TRP A 241 23.800 -5.636 -7.393 1.00 18.12 ATOM 1671 CD2 TRP A 241 24.557 -6.840 -7.576 1.00 19.40 ATOM 1672 CE2 TRP A 241 25.354 -6.661 -8.735 1.00 18.98 ATOM 1673 CE3 TRP A 241 24.642 -8.053 -6.875 1.00 19.12 ATOM 1674 CD1 TRP A 241 24.155 -4.802 -8.421 1.00 18.60 ATOM 1675 NE1 TRP A 241 25.088 -5.411 -9.228 1.00 18.63 ATOM 1676 CZ2 TRP A 241 26.226 -7.650 -9.208 1.00 20.50 ATOM 1677 CZ3 TRP A 241 25.512 -9.039 -7.347 1.00 19.19 ATOM 1678 CH2 TRP A 241 26.292 -8.828 -8.504 1.00 19.46 ATOM 1679 C TRP A 241 24.174 -3.276 -5.698 1.00 16.88 ATOM 1680 O TRP A 241 25.404 -3.200 -5.725 1.00 16.80 ATOM 1681 N SER A 242 23.368 -2.299 -6.127 1.00 16.77 ATOM 1682 CA SER A 242 23.882 -1.049 -6.686 1.00 17.01 ATOM 1683 CB SER A 242 22.739 -0.099 -7.046 1.00 16.10 ATOM 1684 OG SER A 242 21.908 -0.655 -8.052 1.00 16.64 ATOM 1685 C SER A 242 24.817 -0.360 -5.700 1.00 17.45 ATOM 1686 O SER A 242 25.881 0.131 -6.086 1.00 17.12 ATOM 1687 N ALA A 243 24.414 -0.314 -4.431 1.00 16.83 ATOM 1688 CA ALA A 243 25.255 0.293 -3.399 1.00 16.66 ATOM 1689 CB ALA A 243 24.531 0.269 -2.046 1.00 16.30 ATOM 1690 C ALA A 243 26.590 -0.470 -3.313 1.00 16.83 ATOM 1691 O ALA A 243 27.660 0.128 -3.168 1.00 16.33 ATOM 1692 N GLY A 244 26.525 -1.795 -3.407 1.00 17.52 ATOM 1693 CA GLY A 244 27.734 -2.600 -3.365 1.00 17.55 ATOM 1694 C GLY A 244 28.645 -2.289 -4.542 1.00 18.17 ATOM 1695 O GLY A 244 29.867 -2.357 -4.427 1.00 18.24 ATOM 1696 N CYS A 245 28.060 -1.947 -5.685 1.00 18.75 ATOM 1697 CA CYS A 245 28.848 -1.622 -6.873 1.00 18.28 ATOM 1698 CB CYS A 245 27.948 -1.533 -8.103 1.00 19.08 ATOM 1699 SG CYS A 245 27.376 -3.137 -8.714 1.00 20.26 ATOM 1700 C CYS A 245 29.543 -0.288 -6.651 1.00 18.29 ATOM 1701 O CYS A 245 30.663 -0.077 -7.115 1.00 18.06 ATOM 1702 N VAL A 246 28.875 0.621 -5.945 1.00 17.90 ATOM 1703 CA VAL A 246 29.463 1.925 -5.654 1.00 17.15 ATOM 1704 CB VAL A 246 28.423 2.906 -5.031 1.00 17.18 ATOM 1705 CG1 VAL A 246 29.116 4.194 -4.592 1.00 16.99 ATOM 1706 CG2 VAL A 246 27.350 3.246 -6.059 1.00 16.85 ATOM 1707 C VAL A 246 30.643 1.749 -4.691 1.00 17.78 ATOM 1708 O VAL A 246 31.707 2.336 -4.895 1.00 18.21 ATOM 1709 N LEU A 247 30.461 0.942 -3.647 1.00 17.68 ATOM 1710 CA LEU A 247 31.534 0.693 -2.685 1.00 18.89 ATOM 1711 CB LEU A 247 31.073 -0.295 -1.600 1.00 19.28 ATOM 1712 CG LEU A 247 32.163 -0.848 -0.660 1.00 20.45 ATOM 1713 CD1 LEU A 247 32.785 0.301 0.140 1.00 20.61 ATOM 1714 CD2 LEU A 247 31.568 -1.897 0.283 1.00 20.73 ATOM 1715 C LEU A 247 32.768 0.125 -3.396 1.00 19.64 ATOM 1716 O LEU A 247 33.873 0.630 -3.229 1.00 19.09 ATOM 1717 N ALA A 248 32.575 -0.923 -4.190 1.00 19.60 ATOM 1718 CA ALA A 248 33.688 -1.548 -4.909 1.00 20.28 ATOM 1719 CB ALA A 248 33.178 -2.734 -5.747 1.00 19.90 ATOM 1720 C ALA A 248 34.400 -0.541 -5.802 1.00 20.56 ATOM 1721 O ALA A 248 35.629 -0.524 -5.876 1.00 21.26 ATOM 1722 N GLU A 249 33.624 0.310 -6.468 1.00 20.35 ATOM 1723 CA GLU A 249 34.177 1.330 -7.358 1.00 20.36 ATOM 1724 CB GLU A 249 33.043 2.032 -8.103 1.00 19.88 ATOM 1725 CG GLU A 249 33.478 3.193 -8.979 1.00 21.12 ATOM 1726 CD GLU A 249 32.455 3.526 -10.052 1.00 21.83 ATOM 1727 OE1 GLU A 249 31.437 2.793 -10.173 1.00 22.86 ATOM 1728 OE2 GLU A 249 32.671 4.520 -10.775 1.00 21.44 ATOM 1729 C GLU A 249 35.027 2.363 -6.608 1.00 20.46 ATOM 1730 O GLU A 249 36.045 2.826 -7.119 1.00 20.00 ATOM 1731 N LEU A 250 34.602 2.738 -5.404 1.00 21.55 ATOM 1732 CA LEU A 250 35.364 3.709 -4.612 1.00 22.73 ATOM 1733 CB LEU A 250 34.541 4.191 -3.415 1.00 22.21 ATOM 1734 CG LEU A 250 33.324 5.052 -3.763 1.00 22.05 ATOM 1735 CD1 LEU A 250 32.571 5.424 -2.483 1.00 22.14 ATOM 1736 CD2 LEU A 250 33.776 6.299 -4.504 1.00 21.65 ATOM 1737 C LEU A 250 36.662 3.074 -4.120 1.00 23.58 ATOM 1738 O LEU A 250 37.673 3.756 -3.954 1.00 25.01 ATOM 1739 N LEU A 251 36.627 1.765 -3.883 1.00 23.62 ATOM 1740 CA LEU A 251 37.800 1.026 -3.421 1.00 24.65 ATOM 1741 CB LEU A 251 37.378 -0.307 -2.790 1.00 24.21 ATOM 1742 CG LEU A 251 36.574 -0.262 -1.488 1.00 24.27 ATOM 1743 CD1 LEU A 251 36.139 -1.666 -1.087 1.00 24.15 ATOM 1744 CD2 LEU A 251 37.427 0.370 -0.399 1.00 24.65 ATOM 1745 C LEU A 251 38.755 0.746 -4.582 1.00 25.37 ATOM 1746 O LEU A 251 39.975 0.845 -4.429 1.00 26.02 ATOM 1747 N LEU A 252 38.192 0.404 -5.738 1.00 25.36 ATOM 1748 CA LEU A 252 38.969 0.082 -6.935 1.00 26.35 ATOM 1749 CB LEU A 252 38.143 -0.785 -7.880 1.00 27.06 ATOM 1750 CG LEU A 252 38.018 -2.263 -7.542 1.00 28.09 ATOM 1751 CD1 LEU A 252 36.922 -2.877 -8.403 1.00 28.82 ATOM 1752 CD2 LEU A 252 39.360 -2.954 -7.779 1.00 29.19 ATOM 1753 C LEU A 252 39.458 1.280 -7.726 1.00 26.41 ATOM 1754 O LEU A 252 40.559 1.256 -8.276 1.00 27.37 ATOM 1755 N GLY A 253 38.634 2.317 -7.808 1.00 26.02 ATOM 1756 CA GLY A 253 39.017 3.490 -8.569 1.00 25.20 ATOM 1757 C GLY A 253 38.383 3.461 -9.944 1.00 25.65 ATOM 1758 O GLY A 253 38.647 4.326 -10.780 1.00 26.10 ATOM 1759 N GLN A 254 37.540 2.460 -10.179 1.00 25.64 ATOM 1760 CA GLN A 254 36.837 2.318 -11.454 1.00 26.35 ATOM 1761 CB GLN A 254 37.795 1.790 -12.525 1.00 28.07 ATOM 1762 CG GLN A 254 38.511 0.532 -12.095 1.00 30.94 ATOM 1763 CD GLN A 254 39.407 -0.024 -13.177 1.00 33.92 ATOM 1764 OE1 GLN A 254 40.372 0.618 -13.587 1.00 35.58 ATOM 1765 NE2 GLN A 254 39.097 -1.228 -13.644 1.00 35.30 ATOM 1766 C GLN A 254 35.677 1.338 -11.270 1.00 25.54 ATOM 1767 O GLN A 254 35.674 0.549 -10.326 1.00 24.24 ATOM 1768 N PRO A 255 34.679 1.368 -12.175 1.00 25.24 ATOM 1769 CD PRO A 255 34.547 2.251 -13.348 1.00 25.23 ATOM 1770 CA PRO A 255 33.539 0.443 -12.040 1.00 25.27 ATOM 1771 CB PRO A 255 32.699 0.706 -13.297 1.00 24.85 ATOM 1772 CG PRO A 255 33.097 2.095 -13.740 1.00 25.82 ATOM 1773 C PRO A 255 33.990 -1.016 -11.944 1.00 25.23 ATOM 1774 O PRO A 255 34.923 -1.431 -12.638 1.00 24.56 ATOM 1775 N ILE A 256 33.330 -1.797 -11.094 1.00 24.75 ATOM 1776 CA ILE A 256 33.710 -3.197 -10.933 1.00 24.93 ATOM 1777 CB ILE A 256 33.395 -3.705 -9.500 1.00 24.77 ATOM 1778 CG2 ILE A 256 31.899 -3.682 -9.247 1.00 24.04 ATOM 1779 CG1 ILE A 256 33.991 -5.105 -9.315 1.00 25.80 ATOM 1780 CD1 ILE A 256 34.116 -5.550 -7.863 1.00 27.04 ATOM 1781 C ILE A 256 33.090 -4.150 -11.962 1.00 24.78 ATOM 1782 O ILE A 256 33.675 -5.186 -12.269 1.00 25.38 ATOM 1783 N PHE A 257 31.930 -3.805 -12.507 1.00 24.03 ATOM 1784 CA PHE A 257 31.277 -4.663 -13.498 1.00 25.00 ATOM 1785 CB PHE A 257 29.988 -5.282 -12.932 1.00 23.87 ATOM 1786 CG PHE A 257 30.197 -6.099 -11.679 1.00 23.89 ATOM 1787 CD1 PHE A 257 29.366 -5.922 -10.573 1.00 22.58 ATOM 1788 CD2 PHE A 257 31.222 -7.044 -11.603 1.00 24.11 ATOM 1789 CE1 PHE A 257 29.549 -6.669 -9.409 1.00 22.39 ATOM 1790 CE2 PHE A 257 31.414 -7.800 -10.439 1.00 23.56 ATOM 1791 CZ PHE A 257 30.570 -7.607 -9.341 1.00 23.10 ATOM 1792 C PHE A 257 30.937 -3.883 -14.768 1.00 25.84 ATOM 1793 O PHE A 257 29.770 -3.686 -15.092 1.00 25.96 ATOM 1794 N PRO A 258 31.960 -3.433 -15.511 1.00 26.72 ATOM 1795 CD PRO A 258 33.402 -3.605 -15.264 1.00 26.71 ATOM 1796 CA PRO A 258 31.705 -2.680 -16.741 1.00 27.01 ATOM 1797 CB PRO A 258 33.054 -2.045 -17.047 1.00 27.43 ATOM 1798 CG PRO A 258 34.039 -3.049 -16.522 1.00 26.75 ATOM 1799 C PRO A 258 31.240 -3.600 -17.863 1.00 27.75 ATOM 1800 O PRO A 258 31.330 -4.819 -17.751 1.00 27.94 ATOM 1801 N GLY A 259 30.745 -3.009 -18.946 1.00 28.87 ATOM 1802 CA GLY A 259 30.272 -3.794 -20.072 1.00 30.22 ATOM 1803 C GLY A 259 29.275 -3.010 -20.902 1.00 31.52 ATOM 1804 O GLY A 259 28.410 -2.325 -20.353 1.00 31.99 ATOM 1805 N ASP A 260 29.388 -3.107 -22.224 1.00 31.83 ATOM 1806 CA ASP A 260 28.481 -2.383 -23.109 1.00 32.22 ATOM 1807 CB ASP A 260 29.172 -2.076 -24.441 1.00 34.69 ATOM 1808 CG ASP A 260 30.107 -0.873 -24.347 1.00 37.00 ATOM 1809 OD1 ASP A 260 29.879 0.004 -23.481 1.00 38.41 ATOM 1810 OD2 ASP A 260 31.075 -0.806 -25.139 1.00 39.25 ATOM 1811 C ASP A 260 27.170 -3.126 -23.350 1.00 30.95 ATOM 1812 O ASP A 260 26.191 -2.536 -23.805 1.00 31.14 ATOM 1813 N SER A 261 27.154 -4.417 -23.047 1.00 29.28 ATOM 1814 CA SER A 261 25.948 -5.220 -23.205 1.00 28.10 ATOM 1815 CB SER A 261 26.097 -6.201 -24.370 1.00 28.03 ATOM 1816 OG SER A 261 26.859 -7.337 -23.997 1.00 28.52 ATOM 1817 C SER A 261 25.707 -5.999 -21.918 1.00 27.14 ATOM 1818 O SER A 261 26.609 -6.125 -21.090 1.00 25.99 ATOM 1819 N GLY A 262 24.493 -6.519 -21.762 1.00 26.70 ATOM 1820 CA GLY A 262 24.166 -7.294 -20.581 1.00 26.50 ATOM 1821 C GLY A 262 25.054 -8.513 -20.455 1.00 26.46 ATOM 1822 O GLY A 262 25.481 -8.872 -19.364 1.00 25.26 ATOM 1823 N VAL A 263 25.336 -9.161 -21.580 1.00 27.12 ATOM 1824 CA VAL A 263 26.189 -10.347 -21.566 1.00 27.81 ATOM 1825 CB VAL A 263 26.352 -10.948 -22.987 1.00 29.01 ATOM 1826 CG1 VAL A 263 27.340 -12.113 -22.942 1.00 30.65 ATOM 1827 CG2 VAL A 263 25.009 -11.409 -23.513 1.00 30.19 ATOM 1828 C VAL A 263 27.579 -10.018 -21.016 1.00 26.79 ATOM 1829 O VAL A 263 28.121 -10.769 -20.203 1.00 26.59 ATOM 1830 N ASP A 264 28.147 -8.896 -21.457 1.00 26.07 ATOM 1831 CA ASP A 264 29.472 -8.481 -21.003 1.00 26.36 ATOM 1832 CB ASP A 264 29.920 -7.220 -21.736 1.00 27.76 ATOM 1833 CG ASP A 264 30.183 -7.467 -23.209 1.00 30.84 ATOM 1834 OD1 ASP A 264 30.015 -6.520 -24.005 1.00 32.52 ATOM 1835 OD2 ASP A 264 30.553 -8.606 -23.570 1.00 30.73 ATOM 1836 C ASP A 264 29.478 -8.219 -19.506 1.00 26.01 ATOM 1837 O ASP A 264 30.381 -8.658 -18.797 1.00 25.69 ATOM 1838 N GLN A 265 28.473 -7.486 -19.039 1.00 25.63 ATOM 1839 CA GLN A 265 28.334 -7.179 -17.621 1.00 26.02 ATOM 1840 CB GLN A 265 27.068 -6.353 -17.384 1.00 26.12 ATOM 1841 CG GLN A 265 27.217 -4.874 -17.718 1.00 28.57 ATOM 1842 CD GLN A 265 25.885 -4.197 -18.024 1.00 29.22 ATOM 1843 OE1 GLN A 265 25.824 -3.272 -18.828 1.00 32.42 ATOM 1844 NE2 GLN A 265 24.822 -4.657 -17.392 1.00 29.38 ATOM 1845 C GLN A 265 28.253 -8.476 -16.811 1.00 25.77 ATOM 1846 O GLN A 265 28.926 -8.619 -15.795 1.00 25.33 ATOM 1847 N LEU A 266 27.430 -9.418 -17.269 1.00 26.24 ATOM 1848 CA LEU A 266 27.269 -10.706 -16.589 1.00 26.80 ATOM 1849 CB LEU A 266 26.187 -11.544 -17.270 1.00 26.90 ATOM 1850 CG LEU A 266 24.753 -11.194 -16.873 1.00 27.03 ATOM 1851 CD1 LEU A 266 23.790 -11.992 -17.723 1.00 27.40 ATOM 1852 CD2 LEU A 266 24.538 -11.488 -15.393 1.00 27.05 ATOM 1853 C LEU A 266 28.566 -11.495 -16.556 1.00 27.38 ATOM 1854 O LEU A 266 28.867 -12.168 -15.574 1.00 27.91 ATOM 1855 N VAL A 267 29.338 -11.420 -17.631 1.00 28.01 ATOM 1856 CA VAL A 267 30.609 -12.131 -17.676 1.00 28.96 ATOM 1857 CB VAL A 267 31.261 -12.040 -19.082 1.00 29.65 ATOM 1858 CG1 VAL A 267 32.735 -12.424 -19.005 1.00 29.89 ATOM 1859 CG2 VAL A 267 30.522 -12.954 -20.058 1.00 29.77 ATOM 1860 C VAL A 267 31.558 -11.541 -16.636 1.00 29.03 ATOM 1861 O VAL A 267 32.305 -12.269 -15.987 1.00 28.97 ATOM 1862 N GLU A 268 31.526 -10.219 -16.484 1.00 28.89 ATOM 1863 CA GLU A 268 32.376 -9.535 -15.513 1.00 29.15 ATOM 1864 CB GLU A 268 32.277 -8.018 -15.688 1.00 30.10 ATOM 1865 CG GLU A 268 32.830 -7.495 -17.005 1.00 32.57 ATOM 1866 CD GLU A 268 34.304 -7.821 -17.193 1.00 33.83 ATOM 1867 OE1 GLU A 268 34.999 -8.074 -16.189 1.00 34.94 ATOM 1868 OE2 GLU A 268 34.772 -7.822 -18.351 1.00 35.92 ATOM 1869 C GLU A 268 31.950 -9.904 -14.092 1.00 28.50 ATOM 1870 O GLU A 268 32.772 -9.950 -13.179 1.00 28.41 ATOM 1871 N ILE A 269 30.659 -10.161 -13.908 1.00 28.62 ATOM 1872 CA ILE A 269 30.147 -10.534 -12.596 1.00 28.60 ATOM 1873 CB ILE A 269 28.605 -10.432 -12.537 1.00 27.34 ATOM 1874 CG2 ILE A 269 28.076 -11.059 -11.245 1.00 26.78 ATOM 1875 CG1 ILE A 269 28.181 -8.966 -12.594 1.00 25.81 ATOM 1876 CD1 ILE A 269 26.687 -8.774 -12.686 1.00 24.23 ATOM 1877 C ILE A 269 30.566 -11.973 -12.312 1.00 29.72 ATOM 1878 O ILE A 269 31.012 -12.300 -11.214 1.00 29.46 ATOM 1879 N ILE A 270 30.432 -12.823 -13.324 1.00 30.53 ATOM 1880 CA ILE A 270 30.792 -14.227 -13.191 1.00 31.40 ATOM 1881 CB ILE A 270 30.380 -15.012 -14.460 1.00 31.05 ATOM 1882 CG2 ILE A 270 31.121 -16.342 -14.524 1.00 31.54 ATOM 1883 CG1 ILE A 270 28.866 -15.242 -14.434 1.00 30.38 ATOM 1884 CD1 ILE A 270 28.259 -15.600 -15.773 1.00 29.33 ATOM 1885 C ILE A 270 32.285 -14.402 -12.915 1.00 32.02 ATOM 1886 O ILE A 270 32.684 -15.301 -12.176 1.00 32.55 ATOM 1887 N LYS A 271 33.110 -13.538 -13.490 1.00 32.50 ATOM 1888 CA LYS A 271 34.544 -13.631 -13.268 1.00 33.95 ATOM 1889 CB LYS A 271 35.277 -12.600 -14.122 1.00 34.47 ATOM 1890 CG LYS A 271 35.253 -12.926 -15.603 1.00 36.34 ATOM 1891 CD LYS A 271 36.460 -12.353 -16.310 1.00 37.59 ATOM 1892 CE LYS A 271 36.063 -11.740 -17.632 1.00 38.86 ATOM 1893 NZ LYS A 271 36.886 -10.538 -17.927 1.00 40.46 ATOM 1894 C LYS A 271 34.888 -13.423 -11.795 1.00 34.73 ATOM 1895 O LYS A 271 35.833 -14.026 -11.278 1.00 35.15 ATOM 1896 N VAL A 272 34.118 -12.577 -11.116 1.00 34.44 ATOM 1897 CA VAL A 272 34.367 -12.307 -9.707 1.00 34.55 ATOM 1898 CB VAL A 272 33.966 -10.861 -9.320 1.00 33.98 ATOM 1899 CG1 VAL A 272 34.153 -10.655 -7.819 1.00 34.16 ATOM 1900 CG2 VAL A 272 34.802 -9.858 -10.089 1.00 33.30 ATOM 1901 C VAL A 272 33.604 -13.270 -8.805 1.00 35.00 ATOM 1902 O VAL A 272 34.195 -13.912 -7.940 1.00 35.39 ATOM 1903 N LEU A 273 32.296 -13.379 -9.014 1.00 35.19 ATOM 1904 CA LEU A 273 31.458 -14.247 -8.189 1.00 35.64 ATOM 1905 CB LEU A 273 30.010 -13.738 -8.173 1.00 34.72 ATOM 1906 CG LEU A 273 29.695 -12.324 -7.662 1.00 34.10 ATOM 1907 CD1 LEU A 273 28.200 -12.191 -7.441 1.00 33.44 ATOM 1908 CD2 LEU A 273 30.444 -12.054 -6.380 1.00 34.20 ATOM 1909 C LEU A 273 31.440 -15.713 -8.598 1.00 36.34 ATOM 1910 O LEU A 273 30.957 -16.551 -7.848 1.00 36.80 ATOM 1911 N GLY A 274 31.963 -16.030 -9.775 1.00 37.21 ATOM 1912 CA GLY A 274 31.930 -17.408 -10.224 1.00 37.99 ATOM 1913 C GLY A 274 30.571 -17.677 -10.846 1.00 39.00 ATOM 1914 O GLY A 274 29.648 -16.882 -10.689 1.00 38.89 ATOM 1915 N THR A 275 30.436 -18.793 -11.554 1.00 40.09 ATOM 1916 CA THR A 275 29.174 -19.134 -12.207 1.00 41.26 ATOM 1917 CB THR A 275 29.329 -20.418 -13.049 1.00 41.39 ATOM 1918 OG1 THR A 275 30.382 -20.232 -14.004 1.00 41.23 ATOM 1919 CG2 THR A 275 28.037 -20.740 -13.784 1.00 40.96 ATOM 1920 C THR A 275 28.030 -19.316 -11.212 1.00 42.23 ATOM 1921 O THR A 275 28.186 -19.962 -10.179 1.00 42.29 ATOM 1922 N PRO A 276 26.859 -18.737 -11.509 1.00 43.11 ATOM 1923 CD PRO A 276 26.531 -17.923 -12.693 1.00 42.98 ATOM 1924 CA PRO A 276 25.715 -18.863 -10.605 1.00 44.36 ATOM 1925 CB PRO A 276 24.746 -17.799 -11.103 1.00 43.58 ATOM 1926 CG PRO A 276 25.047 -17.692 -12.554 1.00 43.14 ATOM 1927 C PRO A 276 25.081 -20.253 -10.612 1.00 46.11 ATOM 1928 O PRO A 276 24.840 -20.841 -11.665 1.00 46.18 ATOM 1929 N THR A 277 24.813 -20.758 -9.415 1.00 47.89 ATOM 1930 CA THR A 277 24.192 -22.059 -9.215 1.00 49.05 ATOM 1931 CB THR A 277 23.998 -22.305 -7.706 1.00 48.94 ATOM 1932 OG1 THR A 277 25.120 -23.035 -7.206 1.00 49.58 ATOM 1933 CG2 THR A 277 22.724 -23.070 -7.422 1.00 49.72 ATOM 1934 C THR A 277 22.843 -22.066 -9.913 1.00 50.09 ATOM 1935 O THR A 277 22.316 -21.011 -10.258 1.00 50.56 ATOM 1936 N ARG A 278 22.284 -23.251 -10.132 1.00 51.32 ATOM 1937 CA ARG A 278 20.984 -23.344 -10.777 1.00 52.37 ATOM 1938 CB ARG A 278 20.620 -24.808 -11.038 1.00 54.12 ATOM 1939 CG ARG A 278 20.055 -25.063 -12.427 1.00 56.69 ATOM 1940 CD ARG A 278 19.779 -26.546 -12.643 1.00 59.31 ATOM 1941 NE ARG A 278 18.731 -26.778 -13.637 1.00 61.46 ATOM 1942 CZ ARG A 278 18.111 -27.945 -13.815 1.00 62.58 ATOM 1943 NH1 ARG A 278 18.430 -28.995 -13.063 1.00 62.82 ATOM 1944 NH2 ARG A 278 17.172 -28.064 -14.748 1.00 62.97 ATOM 1945 C ARG A 278 19.945 -22.693 -9.867 1.00 52.10 ATOM 1946 O ARG A 278 19.047 -21.995 -10.338 1.00 51.84 ATOM 1947 N GLU A 279 20.077 -22.919 -8.562 1.00 52.06 ATOM 1948 CA GLU A 279 19.156 -22.337 -7.586 1.00 52.48 ATOM 1949 CB GLU A 279 19.426 -22.898 -6.182 1.00 54.05 ATOM 1950 CG GLU A 279 18.221 -23.582 -5.531 1.00 56.86 ATOM 1951 CD GLU A 279 17.145 -22.601 -5.054 1.00 58.64 ATOM 1952 OE1 GLU A 279 16.399 -22.058 -5.905 1.00 59.30 ATOM 1953 OE2 GLU A 279 17.042 -22.379 -3.824 1.00 59.52 ATOM 1954 C GLU A 279 19.314 -20.815 -7.566 1.00 51.47 ATOM 1955 O GLU A 279 18.330 -20.082 -7.491 1.00 51.46 ATOM 1956 N GLN A 280 20.557 -20.349 -7.634 1.00 50.20 ATOM 1957 CA GLN A 280 20.839 -18.920 -7.635 1.00 48.85 ATOM 1958 CB GLN A 280 22.344 -18.689 -7.650 1.00 47.47 ATOM 1959 CG GLN A 280 22.982 -18.900 -6.304 1.00 45.99 ATOM 1960 CD GLN A 280 24.475 -18.744 -6.349 1.00 45.46 ATOM 1961 OE1 GLN A 280 25.123 -19.148 -7.312 1.00 45.26 ATOM 1962 NE2 GLN A 280 25.038 -18.155 -5.306 1.00 45.57 ATOM 1963 C GLN A 280 20.196 -18.255 -8.843 1.00 48.85 ATOM 1964 O GLN A 280 19.614 -17.180 -8.732 1.00 48.30 ATOM 1965 N ILE A 281 20.304 -18.897 -9.999 1.00 49.28 ATOM 1966 CA ILE A 281 19.706 -18.368 -11.215 1.00 50.11 ATOM 1967 CB ILE A 281 20.040 -19.259 -12.425 1.00 49.95 ATOM 1968 CG2 ILE A 281 19.129 -18.920 -13.592 1.00 49.82 ATOM 1969 CG1 ILE A 281 21.505 -19.066 -12.815 1.00 49.84 ATOM 1970 CD1 ILE A 281 22.042 -20.145 -13.723 1.00 50.29 ATOM 1971 C ILE A 281 18.194 -18.326 -11.027 1.00 50.79 ATOM 1972 O ILE A 281 17.523 -17.390 -11.456 1.00 50.17 ATOM 1973 N ARG A 282 17.673 -19.356 -10.372 1.00 52.50 ATOM 1974 CA ARG A 282 16.248 -19.476 -10.098 1.00 54.20 ATOM 1975 CB ARG A 282 15.966 -20.858 -9.495 1.00 56.08 ATOM 1976 CG ARG A 282 14.505 -21.156 -9.189 1.00 58.70 ATOM 1977 CD ARG A 282 14.381 -22.397 -8.301 1.00 61.15 ATOM 1978 NE ARG A 282 13.090 -22.471 -7.614 1.00 63.47 ATOM 1979 CZ ARG A 282 12.820 -23.296 -6.601 1.00 64.59 ATOM 1980 NH1 ARG A 282 13.753 -24.126 -6.144 1.00 64.84 ATOM 1981 NH2 ARG A 282 11.613 -23.296 -6.044 1.00 64.76 ATOM 1982 C ARG A 282 15.818 -18.369 -9.133 1.00 54.50 ATOM 1983 O ARG A 282 14.718 -17.825 -9.246 1.00 54.07 ATOM 1984 N GLU A 283 16.697 -18.043 -8.189 1.00 55.35 ATOM 1985 CA GLU A 283 16.443 -16.996 -7.199 1.00 56.58 ATOM 1986 CB GLU A 283 17.581 -16.945 -6.176 1.00 57.23 ATOM 1987 CG GLU A 283 17.845 -18.250 -5.458 1.00 58.84 ATOM 1988 CD GLU A 283 17.131 -18.328 -4.126 1.00 60.04 ATOM 1989 OE1 GLU A 283 17.615 -19.064 -3.234 1.00 60.70 ATOM 1990 OE2 GLU A 283 16.087 -17.653 -3.971 1.00 60.51 ATOM 1991 C GLU A 283 16.323 -15.623 -7.864 1.00 56.96 ATOM 1992 O GLU A 283 15.480 -14.808 -7.491 1.00 56.57 ATOM 1993 N MET A 284 17.180 -15.375 -8.846 1.00 57.64 ATOM 1994 CA MET A 284 17.181 -14.108 -9.560 1.00 59.11 ATOM 1995 CB MET A 284 18.468 -13.974 -10.364 1.00 56.78 ATOM 1996 CG MET A 284 19.699 -14.092 -9.513 1.00 55.02 ATOM 1997 SD MET A 284 21.195 -14.143 -10.468 1.00 52.21 ATOM 1998 CE MET A 284 22.150 -13.180 -9.521 1.00 53.52 ATOM 1999 C MET A 284 15.986 -13.978 -10.487 1.00 61.44 ATOM 2000 O MET A 284 15.235 -13.008 -10.418 1.00 61.21 ATOM 2001 N ASN A 285 15.824 -14.960 -11.363 1.00 64.96 ATOM 2002 CA ASN A 285 14.725 -14.967 -12.317 1.00 68.61 ATOM 2003 CB ASN A 285 14.992 -13.980 -13.456 1.00 68.36 ATOM 2004 CG ASN A 285 13.838 -13.898 -14.434 1.00 68.41 ATOM 2005 OD1 ASN A 285 14.017 -14.041 -15.644 1.00 67.90 ATOM 2006 ND2 ASN A 285 12.640 -13.667 -13.911 1.00 68.45 ATOM 2007 C ASN A 285 14.590 -16.365 -12.888 1.00 71.56 ATOM 2008 O ASN A 285 15.363 -16.768 -13.761 1.00 71.52 ATOM 2009 N PRO A 286 13.603 -17.128 -12.398 1.00 74.64 ATOM 2010 CD PRO A 286 12.631 -16.736 -11.361 1.00 75.04 ATOM 2011 CA PRO A 286 13.382 -18.495 -12.880 1.00 77.37 ATOM 2012 CB PRO A 286 12.516 -19.116 -11.791 1.00 76.79 ATOM 2013 CG PRO A 286 11.749 -17.954 -11.230 1.00 76.05 ATOM 2014 C PRO A 286 12.685 -18.493 -14.236 1.00 80.02 ATOM 2015 O PRO A 286 11.578 -19.013 -14.372 1.00 80.39 ATOM 2016 N ASN A 287 13.340 -17.908 -15.237 1.00 82.95 ATOM 2017 CA ASN A 287 12.760 -17.828 -16.570 1.00 85.82 ATOM 2018 CB ASN A 287 11.929 -16.546 -16.701 1.00 86.15 ATOM 2019 CG ASN A 287 10.788 -16.482 -15.700 1.00 86.78 ATOM 2020 OD1 ASN A 287 9.790 -17.195 -15.830 1.00 86.95 ATOM 2021 ND2 ASN A 287 10.927 -15.621 -14.698 1.00 87.01 ATOM 2022 C ASN A 287 13.780 -17.879 -17.701 1.00 87.77 ATOM 2023 O ASN A 287 13.772 -18.814 -18.501 1.00 88.15 ATOM 2024 N TYR A 288 14.654 -16.874 -17.766 1.00 89.95 ATOM 2025 CA TYR A 288 15.656 -16.786 -18.831 1.00 91.78 ATOM 2026 CB TYR A 288 16.768 -15.819 -18.439 1.00 92.56 ATOM 2027 CG TYR A 288 16.485 -14.422 -18.924 1.00 93.87 ATOM 2028 CD1 TYR A 288 15.188 -13.909 -18.897 1.00 94.63 ATOM 2029 CE1 TYR A 288 14.919 -12.616 -19.322 1.00 95.23 ATOM 2030 CD2 TYR A 288 17.504 -13.605 -19.397 1.00 94.45 ATOM 2031 CE2 TYR A 288 17.243 -12.306 -19.826 1.00 95.18 ATOM 2032 CZ TYR A 288 15.952 -11.817 -19.781 1.00 95.48 ATOM 2033 OH TYR A 288 15.703 -10.515 -20.137 1.00 96.00 ATOM 2034 C TYR A 288 16.249 -18.109 -19.283 1.00 92.48 ATOM 2035 O TYR A 288 16.817 -18.865 -18.490 1.00 92.80 ATOM 2036 N THR A 289 16.114 -18.356 -20.584 1.00 92.92 ATOM 2037 CA THR A 289 16.568 -19.581 -21.227 1.00 93.33 ATOM 2038 CB THR A 289 16.051 -19.638 -22.674 1.00 93.42 ATOM 2039 OG1 THR A 289 15.037 -18.640 -22.852 1.00 93.51 ATOM 2040 CG2 THR A 289 15.466 -21.011 -22.976 1.00 93.37 ATOM 2041 C THR A 289 18.072 -19.847 -21.241 1.00 93.51 ATOM 2042 O THR A 289 18.524 -20.861 -20.707 1.00 93.46 ATOM 2043 N GLU A 290 18.844 -18.957 -21.860 1.00 93.71 ATOM 2044 CA GLU A 290 20.292 -19.144 -21.936 1.00 93.85 ATOM 2045 CB GLU A 290 20.987 -17.871 -22.429 1.00 93.81 ATOM 2046 CG GLU A 290 22.386 -18.089 -22.985 1.00 93.52 ATOM 2047 CD GLU A 290 22.575 -17.464 -24.360 1.00 93.31 ATOM 2048 OE1 GLU A 290 23.344 -16.484 -24.468 1.00 93.15 ATOM 2049 OE2 GLU A 290 21.956 -17.955 -25.328 1.00 92.73 ATOM 2050 C GLU A 290 20.877 -19.537 -20.592 1.00 93.96 ATOM 2051 O GLU A 290 20.788 -18.789 -19.616 1.00 94.40 ATOM 2052 N PHE A 291 21.468 -20.723 -20.549 1.00 93.78 ATOM 2053 CA PHE A 291 22.087 -21.230 -19.335 1.00 93.59 ATOM 2054 CB PHE A 291 21.346 -22.479 -18.842 1.00 93.80 ATOM 2055 CG PHE A 291 20.159 -22.182 -17.952 1.00 94.02 ATOM 2056 CD1 PHE A 291 19.541 -23.203 -17.236 1.00 93.85 ATOM 2057 CD2 PHE A 291 19.657 -20.885 -17.830 1.00 94.17 ATOM 2058 CE1 PHE A 291 18.444 -22.940 -16.412 1.00 93.76 ATOM 2059 CE2 PHE A 291 18.559 -20.611 -17.008 1.00 93.98 ATOM 2060 CZ PHE A 291 17.953 -21.642 -16.299 1.00 93.84 ATOM 2061 C PHE A 291 23.533 -21.564 -19.678 1.00 93.27 ATOM 2062 O PHE A 291 24.273 -22.116 -18.861 1.00 93.36 ATOM 2063 N LYS A 292 23.921 -21.213 -20.902 1.00 92.66 ATOM 2064 CA LYS A 292 25.271 -21.453 -21.395 1.00 92.05 ATOM 2065 CB LYS A 292 25.257 -21.565 -22.926 1.00 92.38 ATOM 2066 CG LYS A 292 26.568 -21.186 -23.615 1.00 92.72 ATOM 2067 CD LYS A 292 26.333 -20.778 -25.065 1.00 92.83 ATOM 2068 CE LYS A 292 27.356 -21.415 -25.998 1.00 92.77 ATOM 2069 NZ LYS A 292 27.054 -22.846 -26.291 1.00 92.60 ATOM 2070 C LYS A 292 26.194 -20.322 -20.962 1.00 91.38 ATOM 2071 O LYS A 292 26.215 -19.255 -21.574 1.00 91.23 ATOM 2072 N PHE A 293 26.948 -20.557 -19.894 1.00 90.72 ATOM 2073 CA PHE A 293 27.875 -19.556 -19.391 1.00 90.04 ATOM 2074 CB PHE A 293 27.190 -18.653 -18.364 1.00 90.41 ATOM 2075 CG PHE A 293 27.064 -17.226 -18.813 1.00 90.82 ATOM 2076 CD1 PHE A 293 25.816 -16.615 -18.901 1.00 90.90 ATOM 2077 CD2 PHE A 293 28.194 -16.498 -19.182 1.00 90.92 ATOM 2078 CE1 PHE A 293 25.694 -15.300 -19.353 1.00 90.91 ATOM 2079 CE2 PHE A 293 28.084 -15.185 -19.636 1.00 90.97 ATOM 2080 CZ PHE A 293 26.831 -14.585 -19.722 1.00 90.96 ATOM 2081 C PHE A 293 29.100 -20.203 -18.774 1.00 89.29 ATOM 2082 O PHE A 293 28.994 -20.983 -17.827 1.00 89.28 ATOM 2083 N PRO A 294 30.284 -19.885 -19.316 1.00 88.62 ATOM 2084 CD PRO A 294 30.453 -18.973 -20.456 1.00 88.59 ATOM 2085 CA PRO A 294 31.572 -20.410 -18.853 1.00 87.94 ATOM 2086 CB PRO A 294 32.587 -19.366 -19.330 1.00 88.22 ATOM 2087 CG PRO A 294 31.824 -18.417 -20.241 1.00 88.48 ATOM 2088 C PRO A 294 31.635 -20.619 -17.345 1.00 87.02 ATOM 2089 O PRO A 294 31.454 -19.679 -16.570 1.00 86.86 ATOM 2090 N GLN A 295 31.889 -21.859 -16.938 1.00 85.88 ATOM 2091 CA GLN A 295 31.986 -22.188 -15.525 1.00 84.68 ATOM 2092 CB GLN A 295 31.934 -23.705 -15.315 1.00 85.11 ATOM 2093 CG GLN A 295 31.552 -24.496 -16.551 1.00 85.45 ATOM 2094 CD GLN A 295 30.130 -24.224 -16.989 1.00 85.87 ATOM 2095 OE1 GLN A 295 29.845 -24.121 -18.184 1.00 86.06 ATOM 2096 NE2 GLN A 295 29.226 -24.104 -16.022 1.00 85.88 ATOM 2097 C GLN A 295 33.292 -21.645 -14.969 1.00 83.40 ATOM 2098 O GLN A 295 34.343 -22.266 -15.119 1.00 83.51 ATOM 2099 N ILE A 296 33.228 -20.476 -14.341 1.00 81.73 ATOM 2100 CA ILE A 296 34.414 -19.870 -13.758 1.00 80.04 ATOM 2101 CB ILE A 296 34.540 -18.379 -14.148 1.00 79.87 ATOM 2102 CG2 ILE A 296 35.249 -17.600 -13.048 1.00 79.81 ATOM 2103 CG1 ILE A 296 35.330 -18.251 -15.450 1.00 79.82 ATOM 2104 CD1 ILE A 296 34.495 -18.441 -16.691 1.00 79.53 ATOM 2105 C ILE A 296 34.327 -19.987 -12.248 1.00 78.91 ATOM 2106 O ILE A 296 33.264 -19.788 -11.662 1.00 78.75 ATOM 2107 N LYS A 297 35.446 -20.326 -11.624 1.00 77.60 ATOM 2108 CA LYS A 297 35.491 -20.455 -10.179 1.00 76.20 ATOM 2109 CB LYS A 297 36.766 -21.191 -9.749 1.00 77.20 ATOM 2110 CG LYS A 297 38.061 -20.436 -10.043 1.00 78.38 ATOM 2111 CD LYS A 297 38.550 -20.688 -11.466 1.00 79.34 ATOM 2112 CE LYS A 297 39.343 -19.500 -12.004 1.00 80.02 ATOM 2113 NZ LYS A 297 39.300 -19.423 -13.494 1.00 80.33 ATOM 2114 C LYS A 297 35.466 -19.053 -9.587 1.00 74.61 ATOM 2115 O LYS A 297 35.975 -18.106 -10.190 1.00 74.19 ATOM 2116 N ALA A 298 34.859 -18.918 -8.414 1.00 72.90 ATOM 2117 CA ALA A 298 34.783 -17.625 -7.757 1.00 71.06 ATOM 2118 CB ALA A 298 34.146 -17.771 -6.384 1.00 71.19 ATOM 2119 C ALA A 298 36.187 -17.057 -7.625 1.00 69.77 ATOM 2120 O ALA A 298 37.121 -17.768 -7.255 1.00 69.73 ATOM 2121 N HIS A 299 36.335 -15.778 -7.946 1.00 68.14 ATOM 2122 CA HIS A 299 37.627 -15.117 -7.843 1.00 66.55 ATOM 2123 CB HIS A 299 37.711 -13.982 -8.863 1.00 67.02 ATOM 2124 CG HIS A 299 39.075 -13.383 -8.988 1.00 67.42 ATOM 2125 CD2 HIS A 299 39.481 -12.182 -9.464 1.00 68.02 ATOM 2126 ND1 HIS A 299 40.217 -14.041 -8.585 1.00 67.64 ATOM 2127 CE1 HIS A 299 41.268 -13.272 -8.809 1.00 67.80 ATOM 2128 NE2 HIS A 299 40.849 -12.138 -9.341 1.00 68.11 ATOM 2129 C HIS A 299 37.785 -14.566 -6.423 1.00 65.14 ATOM 2130 O HIS A 299 37.006 -13.714 -5.989 1.00 65.15 ATOM 2131 N PRO A 300 38.795 -15.051 -5.680 1.00 63.57 ATOM 2132 CD PRO A 300 39.789 -16.052 -6.097 1.00 63.34 ATOM 2133 CA PRO A 300 39.032 -14.594 -4.305 1.00 61.99 ATOM 2134 CB PRO A 300 40.457 -15.073 -3.997 1.00 62.42 ATOM 2135 CG PRO A 300 40.988 -15.668 -5.296 1.00 62.83 ATOM 2136 C PRO A 300 38.888 -13.080 -4.172 1.00 60.22 ATOM 2137 O PRO A 300 39.703 -12.317 -4.695 1.00 60.13 ATOM 2138 N TRP A 301 37.840 -12.661 -3.469 1.00 58.14 ATOM 2139 CA TRP A 301 37.551 -11.249 -3.264 1.00 55.93 ATOM 2140 CB TRP A 301 36.445 -11.091 -2.217 1.00 53.87 ATOM 2141 CG TRP A 301 35.056 -11.015 -2.792 1.00 51.58 ATOM 2142 CD2 TRP A 301 34.508 -9.953 -3.583 1.00 50.26 ATOM 2143 CE2 TRP A 301 33.167 -10.292 -3.865 1.00 49.68 ATOM 2144 CE3 TRP A 301 35.023 -8.750 -4.084 1.00 49.86 ATOM 2145 CD1 TRP A 301 34.052 -11.928 -2.632 1.00 50.76 ATOM 2146 NE1 TRP A 301 32.914 -11.500 -3.272 1.00 49.81 ATOM 2147 CZ2 TRP A 301 32.330 -9.468 -4.621 1.00 49.33 ATOM 2148 CZ3 TRP A 301 34.189 -7.929 -4.838 1.00 49.43 ATOM 2149 CH2 TRP A 301 32.857 -8.295 -5.101 1.00 49.28 ATOM 2150 C TRP A 301 38.782 -10.447 -2.843 1.00 55.52 ATOM 2151 O TRP A 301 38.872 -9.249 -3.117 1.00 55.41 ATOM 2152 N THR A 302 39.731 -11.108 -2.185 1.00 55.13 ATOM 2153 CA THR A 302 40.946 -10.435 -1.737 1.00 54.68 ATOM 2154 CB THR A 302 41.748 -11.316 -0.758 1.00 54.88 ATOM 2155 OG1 THR A 302 40.962 -11.556 0.417 1.00 54.85 ATOM 2156 CG2 THR A 302 43.046 -10.624 -0.353 1.00 54.61 ATOM 2157 C THR A 302 41.849 -10.043 -2.906 1.00 54.21 ATOM 2158 O THR A 302 42.491 -8.990 -2.871 1.00 54.51 ATOM 2159 N LYS A 303 41.894 -10.885 -3.936 1.00 53.25 ATOM 2160 CA LYS A 303 42.721 -10.604 -5.108 1.00 52.57 ATOM 2161 CB LYS A 303 42.992 -11.895 -5.896 1.00 54.40 ATOM 2162 CG LYS A 303 43.879 -11.694 -7.138 1.00 56.26 ATOM 2163 CD LYS A 303 44.444 -13.007 -7.687 1.00 57.37 ATOM 2164 CE LYS A 303 44.865 -12.855 -9.151 1.00 58.49 ATOM 2165 NZ LYS A 303 44.752 -14.122 -9.944 1.00 58.94 ATOM 2166 C LYS A 303 42.057 -9.573 -6.022 1.00 51.06 ATOM 2167 O LYS A 303 42.677 -9.070 -6.958 1.00 50.71 ATOM 2168 N VAL A 304 40.797 -9.255 -5.741 1.00 49.52 ATOM 2169 CA VAL A 304 40.054 -8.285 -6.538 1.00 47.52 ATOM 2170 CB VAL A 304 38.541 -8.358 -6.235 1.00 47.39 ATOM 2171 CG1 VAL A 304 37.821 -7.195 -6.895 1.00 47.26 ATOM 2172 CG2 VAL A 304 37.973 -9.678 -6.727 1.00 47.02 ATOM 2173 C VAL A 304 40.530 -6.856 -6.286 1.00 46.65 ATOM 2174 O VAL A 304 40.646 -6.061 -7.217 1.00 46.01 ATOM 2175 N PHE A 305 40.812 -6.537 -5.026 1.00 45.57 ATOM 2176 CA PHE A 305 41.255 -5.194 -4.665 1.00 45.14 ATOM 2177 CB PHE A 305 40.490 -4.719 -3.426 1.00 43.11 ATOM 2178 CG PHE A 305 38.999 -4.783 -3.575 1.00 40.70 ATOM 2179 CD1 PHE A 305 38.283 -5.844 -3.043 1.00 39.45 ATOM 2180 CD2 PHE A 305 38.313 -3.786 -4.263 1.00 40.00 ATOM 2181 CE1 PHE A 305 36.902 -5.914 -3.197 1.00 39.33 ATOM 2182 CE2 PHE A 305 36.931 -3.846 -4.422 1.00 38.44 ATOM 2183 CZ PHE A 305 36.225 -4.910 -3.889 1.00 38.61 ATOM 2184 C PHE A 305 42.758 -5.098 -4.395 1.00 46.09 ATOM 2185 O PHE A 305 43.434 -6.116 -4.241 1.00 46.26 ATOM 2186 N ARG A 306 43.269 -3.869 -4.342 1.00 47.01 ATOM 2187 CA ARG A 306 44.684 -3.630 -4.064 1.00 48.19 ATOM 2188 CB ARG A 306 44.982 -2.128 -4.082 1.00 49.43 ATOM 2189 CG ARG A 306 44.633 -1.406 -2.791 1.00 52.11 ATOM 2190 CD ARG A 306 44.721 0.106 -2.950 1.00 54.45 ATOM 2191 NE ARG A 306 44.626 0.796 -1.664 1.00 56.91 ATOM 2192 CZ ARG A 306 43.530 0.834 -0.908 1.00 58.37 ATOM 2193 NH1 ARG A 306 42.420 0.219 -1.305 1.00 58.89 ATOM 2194 NH2 ARG A 306 43.540 1.489 0.251 1.00 58.84 ATOM 2195 C ARG A 306 45.019 -4.225 -2.690 1.00 48.41 ATOM 2196 O ARG A 306 44.139 -4.391 -1.842 1.00 47.94 ATOM 2197 N PRO A 307 46.300 -4.548 -2.449 1.00 48.75 ATOM 2198 CD PRO A 307 47.435 -4.378 -3.373 1.00 49.04 ATOM 2199 CA PRO A 307 46.726 -5.132 -1.170 1.00 48.81 ATOM 2200 CB PRO A 307 48.236 -5.327 -1.343 1.00 48.69 ATOM 2201 CG PRO A 307 48.452 -5.334 -2.821 1.00 49.15 ATOM 2202 C PRO A 307 46.391 -4.332 0.091 1.00 48.58 ATOM 2203 O PRO A 307 46.026 -4.905 1.116 1.00 48.53 ATOM 2204 N ARG A 308 46.515 -3.014 0.017 1.00 48.74 ATOM 2205 CA ARG A 308 46.237 -2.158 1.168 1.00 49.27 ATOM 2206 CB ARG A 308 46.639 -0.713 0.855 1.00 51.84 ATOM 2207 CG ARG A 308 48.128 -0.480 0.644 1.00 55.42 ATOM 2208 CD ARG A 308 48.355 0.903 0.039 1.00 58.48 ATOM 2209 NE ARG A 308 49.764 1.293 0.045 1.00 61.53 ATOM 2210 CZ ARG A 308 50.241 2.377 -0.565 1.00 62.90 ATOM 2211 NH1 ARG A 308 51.539 2.660 -0.512 1.00 63.50 ATOM 2212 NH2 ARG A 308 49.415 3.179 -1.231 1.00 63.57 ATOM 2213 C ARG A 308 44.773 -2.164 1.631 1.00 47.63 ATOM 2214 O ARG A 308 44.480 -1.813 2.776 1.00 47.68 ATOM 2215 N THR A 309 43.862 -2.554 0.741 1.00 45.26 ATOM 2216 CA THR A 309 42.430 -2.575 1.041 1.00 42.40 ATOM 2217 CB THR A 309 41.649 -3.247 -0.098 1.00 41.82 ATOM 2218 OG1 THR A 309 42.024 -2.643 -1.340 1.00 41.09 ATOM 2219 CG2 THR A 309 40.149 -3.079 0.108 1.00 40.95 ATOM 2220 C THR A 309 42.036 -3.250 2.350 1.00 40.90 ATOM 2221 O THR A 309 42.322 -4.424 2.563 1.00 40.48 ATOM 2222 N PRO A 310 41.353 -2.509 3.239 1.00 39.82 ATOM 2223 CD PRO A 310 40.953 -1.102 3.059 1.00 39.18 ATOM 2224 CA PRO A 310 40.914 -3.047 4.535 1.00 38.56 ATOM 2225 CB PRO A 310 40.119 -1.898 5.158 1.00 38.61 ATOM 2226 CG PRO A 310 40.571 -0.676 4.438 1.00 38.74 ATOM 2227 C PRO A 310 40.061 -4.302 4.375 1.00 37.85 ATOM 2228 O PRO A 310 39.128 -4.328 3.575 1.00 37.86 ATOM 2229 N PRO A 311 40.376 -5.367 5.134 1.00 37.21 ATOM 2230 CD PRO A 311 41.468 -5.466 6.117 1.00 37.01 ATOM 2231 CA PRO A 311 39.613 -6.614 5.050 1.00 36.25 ATOM 2232 CB PRO A 311 40.271 -7.522 6.093 1.00 36.15 ATOM 2233 CG PRO A 311 41.031 -6.612 6.979 1.00 36.57 ATOM 2234 C PRO A 311 38.127 -6.421 5.324 1.00 35.50 ATOM 2235 O PRO A 311 37.289 -7.117 4.753 1.00 35.49 ATOM 2236 N GLU A 312 37.796 -5.484 6.204 1.00 34.54 ATOM 2237 CA GLU A 312 36.394 -5.231 6.519 1.00 34.34 ATOM 2238 CB GLU A 312 36.278 -4.232 7.672 1.00 36.20 ATOM 2239 CG GLU A 312 36.611 -4.828 9.030 1.00 39.55 ATOM 2240 CD GLU A 312 35.876 -6.132 9.295 1.00 42.16 ATOM 2241 OE1 GLU A 312 36.275 -6.863 10.229 1.00 44.23 ATOM 2242 OE2 GLU A 312 34.897 -6.431 8.575 1.00 43.94 ATOM 2243 C GLU A 312 35.637 -4.708 5.295 1.00 32.49 ATOM 2244 O GLU A 312 34.476 -5.056 5.085 1.00 31.68 ATOM 2245 N ALA A 313 36.297 -3.874 4.495 1.00 30.91 ATOM 2246 CA ALA A 313 35.674 -3.333 3.290 1.00 30.37 ATOM 2247 CB ALA A 313 36.581 -2.297 2.643 1.00 29.45 ATOM 2248 C ALA A 313 35.390 -4.467 2.304 1.00 30.20 ATOM 2249 O ALA A 313 34.339 -4.502 1.668 1.00 29.63 ATOM 2250 N ILE A 314 36.338 -5.389 2.176 1.00 30.12 ATOM 2251 CA ILE A 314 36.180 -6.521 1.274 1.00 29.93 ATOM 2252 CB ILE A 314 37.499 -7.333 1.182 1.00 30.54 ATOM 2253 CG2 ILE A 314 37.338 -8.500 0.217 1.00 30.36 ATOM 2254 CG1 ILE A 314 38.632 -6.418 0.712 1.00 30.48 ATOM 2255 CD1 ILE A 314 39.958 -7.127 0.470 1.00 31.35 ATOM 2256 C ILE A 314 35.042 -7.418 1.769 1.00 29.90 ATOM 2257 O ILE A 314 34.182 -7.847 0.988 1.00 29.87 ATOM 2258 N ALA A 315 35.029 -7.687 3.072 1.00 29.15 ATOM 2259 CA ALA A 315 33.993 -8.529 3.671 1.00 29.00 ATOM 2260 CB ALA A 315 34.253 -8.688 5.167 1.00 29.33 ATOM 2261 C ALA A 315 32.595 -7.949 3.440 1.00 28.56 ATOM 2262 O ALA A 315 31.674 -8.675 3.070 1.00 28.57 ATOM 2263 N LEU A 316 32.438 -6.647 3.671 1.00 27.37 ATOM 2264 CA LEU A 316 31.149 -5.988 3.463 1.00 26.65 ATOM 2265 CB LEU A 316 31.252 -4.498 3.805 1.00 24.60 ATOM 2266 CG LEU A 316 30.065 -3.622 3.387 1.00 23.73 ATOM 2267 CD1 LEU A 316 28.774 -4.170 3.996 1.00 22.40 ATOM 2268 CD2 LEU A 316 30.310 -2.185 3.826 1.00 22.00 ATOM 2269 C LEU A 316 30.750 -6.156 1.994 1.00 27.11 ATOM 2270 O LEU A 316 29.617 -6.510 1.668 1.00 26.70 ATOM 2271 N CYS A 317 31.706 -5.912 1.109 1.00 27.56 ATOM 2272 CA CYS A 317 31.478 -6.039 -0.317 1.00 29.44 ATOM 2273 CB CYS A 317 32.791 -5.819 -1.048 1.00 31.59 ATOM 2274 SG CYS A 317 32.621 -4.794 -2.469 1.00 39.09 ATOM 2275 C CYS A 317 30.900 -7.394 -0.718 1.00 28.71 ATOM 2276 O CYS A 317 29.919 -7.471 -1.459 1.00 28.02 ATOM 2277 N SER A 318 31.517 -8.464 -0.230 1.00 28.62 ATOM 2278 CA SER A 318 31.072 -9.813 -0.552 1.00 28.69 ATOM 2279 CB SER A 318 32.040 -10.832 0.030 1.00 29.27 ATOM 2280 OG SER A 318 31.888 -10.884 1.435 1.00 31.20 ATOM 2281 C SER A 318 29.677 -10.103 -0.036 1.00 28.16 ATOM 2282 O SER A 318 29.008 -11.021 -0.520 1.00 28.72 ATOM 2283 N ARG A 319 29.236 -9.319 0.943 1.00 27.55 ATOM 2284 CA ARG A 319 27.910 -9.494 1.532 1.00 26.84 ATOM 2285 CB ARG A 319 27.953 -9.164 3.029 1.00 28.50 ATOM 2286 CG ARG A 319 28.850 -10.102 3.831 1.00 31.35 ATOM 2287 CD ARG A 319 28.335 -11.528 3.782 1.00 34.11 ATOM 2288 NE ARG A 319 27.107 -11.671 4.560 1.00 37.45 ATOM 2289 CZ ARG A 319 25.910 -11.918 4.034 1.00 38.58 ATOM 2290 NH1 ARG A 319 25.772 -12.053 2.719 1.00 38.77 ATOM 2291 NH2 ARG A 319 24.846 -12.020 4.824 1.00 39.92 ATOM 2292 C ARG A 319 26.834 -8.655 0.848 1.00 25.10 ATOM 2293 O ARG A 319 25.648 -8.811 1.126 1.00 24.70 ATOM 2294 N LEU A 320 27.249 -7.759 -0.039 1.00 23.96 ATOM 2295 CA LEU A 320 26.301 -6.926 -0.772 1.00 22.99 ATOM 2296 CB LEU A 320 26.797 -5.477 -0.851 1.00 21.80 ATOM 2297 CG LEU A 320 26.999 -4.748 0.478 1.00 21.35 ATOM 2298 CD1 LEU A 320 27.793 -3.479 0.236 1.00 21.80 ATOM 2299 CD2 LEU A 320 25.661 -4.423 1.097 1.00 20.58 ATOM 2300 C LEU A 320 26.140 -7.479 -2.182 1.00 23.00 ATOM 2301 O LEU A 320 25.026 -7.594 -2.700 1.00 22.20 ATOM 2302 N LEU A 321 27.265 -7.818 -2.800 1.00 23.74 ATOM 2303 CA LEU A 321 27.255 -8.347 -4.156 1.00 24.29 ATOM 2304 CB LEU A 321 28.545 -7.935 -4.861 1.00 22.91 ATOM 2305 CG LEU A 321 28.725 -6.409 -4.893 1.00 22.10 ATOM 2306 CD1 LEU A 321 30.063 -6.039 -5.509 1.00 21.82 ATOM 2307 CD2 LEU A 321 27.587 -5.785 -5.682 1.00 20.60 ATOM 2308 C LEU A 321 27.075 -9.868 -4.161 1.00 25.65 ATOM 2309 O LEU A 321 28.013 -10.621 -4.421 1.00 26.65 ATOM 2310 N GLU A 322 25.854 -10.300 -3.854 1.00 26.77 ATOM 2311 CA GLU A 322 25.494 -11.718 -3.812 1.00 27.73 ATOM 2312 CB GLU A 322 24.879 -12.083 -2.452 1.00 29.03 ATOM 2313 CG GLU A 322 25.800 -11.881 -1.260 1.00 32.25 ATOM 2314 CD GLU A 322 26.353 -13.181 -0.707 1.00 34.09 ATOM 2315 OE1 GLU A 322 26.374 -14.190 -1.445 1.00 36.01 ATOM 2316 OE2 GLU A 322 26.776 -13.192 0.469 1.00 35.35 ATOM 2317 C GLU A 322 24.463 -11.995 -4.897 1.00 27.14 ATOM 2318 O GLU A 322 23.582 -11.172 -5.128 1.00 26.21 ATOM 2319 N TYR A 323 24.566 -13.153 -5.550 1.00 27.04 ATOM 2320 CA TYR A 323 23.618 -13.534 -6.598 1.00 27.27 ATOM 2321 CB TYR A 323 23.997 -14.896 -7.206 1.00 27.27 ATOM 2322 CG TYR A 323 25.106 -14.873 -8.244 1.00 27.42 ATOM 2323 CD1 TYR A 323 25.037 -14.044 -9.364 1.00 27.96 ATOM 2324 CE1 TYR A 323 26.047 -14.043 -10.324 1.00 28.00 ATOM 2325 CD2 TYR A 323 26.216 -15.701 -8.114 1.00 27.97 ATOM 2326 CE2 TYR A 323 27.232 -15.707 -9.070 1.00 28.54 ATOM 2327 CZ TYR A 323 27.141 -14.875 -10.171 1.00 28.28 ATOM 2328 OH TYR A 323 28.150 -14.876 -11.110 1.00 28.75 ATOM 2329 C TYR A 323 22.181 -13.621 -6.055 1.00 27.29 ATOM 2330 O TYR A 323 21.261 -13.013 -6.595 1.00 27.58 ATOM 2331 N THR A 324 21.982 -14.393 -4.992 1.00 27.87 ATOM 2332 CA THR A 324 20.645 -14.537 -4.421 1.00 28.21 ATOM 2333 CB THR A 324 20.584 -15.690 -3.396 1.00 28.87 ATOM 2334 OG1 THR A 324 21.106 -16.884 -3.990 1.00 30.23 ATOM 2335 CG2 THR A 324 19.154 -15.926 -2.959 1.00 28.56 ATOM 2336 C THR A 324 20.240 -13.248 -3.729 1.00 27.66 ATOM 2337 O THR A 324 20.828 -12.867 -2.717 1.00 27.93 ATOM 2338 N PRO A 325 19.223 -12.562 -4.262 1.00 27.92 ATOM 2339 CD PRO A 325 18.468 -12.963 -5.463 1.00 28.09 ATOM 2340 CA PRO A 325 18.735 -11.296 -3.696 1.00 27.92 ATOM 2341 CB PRO A 325 17.442 -11.031 -4.468 1.00 27.98 ATOM 2342 CG PRO A 325 17.656 -11.727 -5.791 1.00 28.64 ATOM 2343 C PRO A 325 18.515 -11.291 -2.180 1.00 28.47 ATOM 2344 O PRO A 325 18.943 -10.366 -1.484 1.00 27.37 ATOM 2345 N THR A 326 17.852 -12.327 -1.672 1.00 28.30 ATOM 2346 CA THR A 326 17.564 -12.431 -0.249 1.00 27.74 ATOM 2347 CB THR A 326 16.575 -13.580 0.030 1.00 28.21 ATOM 2348 OG1 THR A 326 17.102 -14.802 -0.496 1.00 29.51 ATOM 2349 CG2 THR A 326 15.242 -13.303 -0.627 1.00 28.02 ATOM 2350 C THR A 326 18.807 -12.659 0.596 1.00 27.18 ATOM 2351 O THR A 326 18.768 -12.489 1.811 1.00 28.05 ATOM 2352 N ALA A 327 19.911 -13.041 -0.034 1.00 26.42 ATOM 2353 CA ALA A 327 21.141 -13.287 0.708 1.00 25.77 ATOM 2354 CB ALA A 327 22.026 -14.245 -0.051 1.00 25.51 ATOM 2355 C ALA A 327 21.913 -12.007 1.013 1.00 26.00 ATOM 2356 O ALA A 327 22.782 -11.994 1.888 1.00 26.61 ATOM 2357 N ARG A 328 21.599 -10.930 0.300 1.00 25.49 ATOM 2358 CA ARG A 328 22.291 -9.660 0.514 1.00 24.66 ATOM 2359 CB ARG A 328 21.994 -8.695 -0.640 1.00 24.45 ATOM 2360 CG ARG A 328 22.310 -9.276 -2.007 1.00 23.81 ATOM 2361 CD ARG A 328 21.803 -8.415 -3.151 1.00 23.78 ATOM 2362 NE ARG A 328 21.870 -9.168 -4.399 1.00 22.98 ATOM 2363 CZ ARG A 328 21.080 -8.968 -5.446 1.00 23.28 ATOM 2364 NH1 ARG A 328 20.148 -8.023 -5.414 1.00 22.10 ATOM 2365 NH2 ARG A 328 21.207 -9.744 -6.517 1.00 23.59 ATOM 2366 C ARG A 328 21.896 -9.003 1.832 1.00 24.26 ATOM 2367 O ARG A 328 20.766 -9.144 2.295 1.00 23.90 ATOM 2368 N LEU A 329 22.841 -8.288 2.434 1.00 24.26 ATOM 2369 CA LEU A 329 22.582 -7.580 3.683 1.00 23.29 ATOM 2370 CB LEU A 329 23.829 -6.817 4.127 1.00 23.00 ATOM 2371 CG LEU A 329 25.028 -7.592 4.655 1.00 23.73 ATOM 2372 CD1 LEU A 329 26.146 -6.613 4.992 1.00 22.52 ATOM 2373 CD2 LEU A 329 24.619 -8.391 5.883 1.00 23.85 ATOM 2374 C LEU A 329 21.479 -6.561 3.443 1.00 23.04 ATOM 2375 O LEU A 329 21.297 -6.099 2.319 1.00 23.30 ATOM 2376 N THR A 330 20.725 -6.219 4.480 1.00 22.04 ATOM 2377 CA THR A 330 19.713 -5.184 4.329 1.00 22.37 ATOM 2378 CB THR A 330 18.633 -5.256 5.410 1.00 22.84 ATOM 2379 OG1 THR A 330 19.260 -5.111 6.687 1.00 23.53 ATOM 2380 CG2 THR A 330 17.877 -6.579 5.348 1.00 23.90 ATOM 2381 C THR A 330 20.512 -3.902 4.589 1.00 21.46 ATOM 2382 O THR A 330 21.611 -3.957 5.145 1.00 21.47 ATOM 2383 N PRO A 331 19.995 -2.742 4.165 1.00 20.86 ATOM 2384 CD PRO A 331 18.778 -2.509 3.369 1.00 20.91 ATOM 2385 CA PRO A 331 20.730 -1.496 4.409 1.00 20.36 ATOM 2386 CB PRO A 331 19.806 -0.420 3.845 1.00 20.17 ATOM 2387 CG PRO A 331 19.019 -1.133 2.793 1.00 20.92 ATOM 2388 C PRO A 331 21.062 -1.262 5.885 1.00 19.82 ATOM 2389 O PRO A 331 22.162 -0.821 6.209 1.00 18.98 ATOM 2390 N LEU A 332 20.118 -1.557 6.778 1.00 20.47 ATOM 2391 CA LEU A 332 20.365 -1.362 8.208 1.00 20.98 ATOM 2392 CB LEU A 332 19.085 -1.615 9.025 1.00 20.60 ATOM 2393 CG LEU A 332 19.038 -0.954 10.408 1.00 20.67 ATOM 2394 CD1 LEU A 332 19.141 0.563 10.269 1.00 20.62 ATOM 2395 CD2 LEU A 332 17.740 -1.313 11.097 1.00 21.04 ATOM 2396 C LEU A 332 21.502 -2.275 8.690 1.00 21.47 ATOM 2397 O LEU A 332 22.347 -1.852 9.477 1.00 21.30 ATOM 2398 N GLU A 333 21.533 -3.516 8.209 1.00 21.87 ATOM 2399 CA GLU A 333 22.593 -4.443 8.588 1.00 22.85 ATOM 2400 CB GLU A 333 22.327 -5.837 8.012 1.00 24.71 ATOM 2401 CG GLU A 333 21.180 -6.575 8.701 1.00 28.13 ATOM 2402 CD GLU A 333 20.730 -7.821 7.946 1.00 30.12 ATOM 2403 OE1 GLU A 333 21.158 -8.026 6.787 1.00 30.20 ATOM 2404 OE2 GLU A 333 19.941 -8.603 8.519 1.00 31.59 ATOM 2405 C GLU A 333 23.937 -3.927 8.080 1.00 22.66 ATOM 2406 O GLU A 333 24.960 -4.051 8.765 1.00 22.18 ATOM 2407 N ALA A 334 23.936 -3.350 6.877 1.00 21.98 ATOM 2408 CA ALA A 334 25.161 -2.801 6.303 1.00 21.38 ATOM 2409 CB ALA A 334 24.891 -2.235 4.890 1.00 20.79 ATOM 2410 C ALA A 334 25.680 -1.699 7.228 1.00 20.76 ATOM 2411 O ALA A 334 26.861 -1.665 7.550 1.00 20.84 ATOM 2412 N CYS A 335 24.789 -0.814 7.670 1.00 20.84 ATOM 2413 CA CYS A 335 25.170 0.280 8.568 1.00 20.58 ATOM 2414 CB CYS A 335 23.927 1.088 8.982 1.00 20.48 ATOM 2415 SG CYS A 335 23.286 2.240 7.744 1.00 20.41 ATOM 2416 C CYS A 335 25.867 -0.251 9.831 1.00 21.42 ATOM 2417 O CYS A 335 26.801 0.368 10.346 1.00 20.25 ATOM 2418 N ALA A 336 25.409 -1.406 10.314 1.00 21.93 ATOM 2419 CA ALA A 336 25.958 -2.019 11.524 1.00 22.73 ATOM 2420 CB ALA A 336 24.889 -2.899 12.176 1.00 22.45 ATOM 2421 C ALA A 336 27.241 -2.826 11.307 1.00 23.52 ATOM 2422 O ALA A 336 27.843 -3.315 12.271 1.00 23.81 ATOM 2423 N HIS A 337 27.666 -2.954 10.051 1.00 23.84 ATOM 2424 CA HIS A 337 28.874 -3.707 9.708 1.00 23.72 ATOM 2425 CB HIS A 337 29.029 -3.773 8.184 1.00 23.77 ATOM 2426 CG HIS A 337 30.057 -4.758 7.723 1.00 23.56 ATOM 2427 CD2 HIS A 337 31.406 -4.671 7.648 1.00 23.04 ATOM 2428 ND1 HIS A 337 29.729 -6.021 7.275 1.00 23.69 ATOM 2429 CE1 HIS A 337 30.831 -6.669 6.947 1.00 23.05 ATOM 2430 NE2 HIS A 337 31.864 -5.873 7.164 1.00 23.83 ATOM 2431 C HIS A 337 30.151 -3.130 10.322 1.00 24.13 ATOM 2432 O HIS A 337 30.278 -1.917 10.505 1.00 24.01 ATOM 2433 N SER A 338 31.103 -4.013 10.614 1.00 24.85 ATOM 2434 CA SER A 338 32.388 -3.634 11.206 1.00 25.77 ATOM 2435 CB SER A 338 33.258 -4.875 11.394 1.00 27.29 ATOM 2436 OG SER A 338 32.697 -5.708 12.393 1.00 31.63 ATOM 2437 C SER A 338 33.172 -2.601 10.411 1.00 24.78 ATOM 2438 O SER A 338 33.958 -1.842 10.978 1.00 25.45 ATOM 2439 N PHE A 339 32.971 -2.575 9.099 1.00 23.59 ATOM 2440 CA PHE A 339 33.674 -1.615 8.257 1.00 22.62 ATOM 2441 CB PHE A 339 33.246 -1.783 6.788 1.00 22.14 ATOM 2442 CG PHE A 339 33.863 -0.777 5.848 1.00 22.07 ATOM 2443 CD1 PHE A 339 35.247 -0.658 5.733 1.00 22.02 ATOM 2444 CD2 PHE A 339 33.053 0.055 5.071 1.00 21.91 ATOM 2445 CE1 PHE A 339 35.821 0.277 4.858 1.00 22.07 ATOM 2446 CE2 PHE A 339 33.612 0.993 4.194 1.00 21.40 ATOM 2447 CZ PHE A 339 35.002 1.106 4.086 1.00 22.06 ATOM 2448 C PHE A 339 33.382 -0.192 8.726 1.00 21.83 ATOM 2449 O PHE A 339 34.203 0.700 8.567 1.00 22.20 ATOM 2450 N PHE A 340 32.217 0.020 9.324 1.00 21.52 ATOM 2451 CA PHE A 340 31.851 1.360 9.781 1.00 21.27 ATOM 2452 CB PHE A 340 30.362 1.612 9.509 1.00 20.14 ATOM 2453 CG PHE A 340 29.997 1.531 8.049 1.00 19.83 ATOM 2454 CD1 PHE A 340 30.555 2.420 7.129 1.00 19.47 ATOM 2455 CD2 PHE A 340 29.120 0.555 7.590 1.00 19.02 ATOM 2456 CE1 PHE A 340 30.244 2.340 5.766 1.00 19.77 ATOM 2457 CE2 PHE A 340 28.798 0.460 6.226 1.00 19.64 ATOM 2458 CZ PHE A 340 29.362 1.357 5.312 1.00 19.52 ATOM 2459 C PHE A 340 32.162 1.636 11.248 1.00 21.92 ATOM 2460 O PHE A 340 31.736 2.660 11.787 1.00 22.39 ATOM 2461 N ASP A 341 32.916 0.743 11.888 1.00 22.31 ATOM 2462 CA ASP A 341 33.257 0.905 13.302 1.00 22.58 ATOM 2463 CB ASP A 341 34.064 -0.299 13.794 1.00 23.86 ATOM 2464 CG ASP A 341 33.199 -1.522 14.029 1.00 25.06 ATOM 2465 OD1 ASP A 341 31.957 -1.388 14.051 1.00 26.19 ATOM 2466 OD2 ASP A 341 33.759 -2.629 14.189 1.00 26.78 ATOM 2467 C ASP A 341 34.010 2.195 13.625 1.00 22.55 ATOM 2468 O ASP A 341 33.798 2.787 14.686 1.00 23.03 ATOM 2469 N GLU A 342 34.884 2.639 12.729 1.00 22.03 ATOM 2470 CA GLU A 342 35.626 3.870 12.971 1.00 22.43 ATOM 2471 CB GLU A 342 36.615 4.150 11.836 1.00 23.59 ATOM 2472 CG GLU A 342 37.243 5.539 11.918 1.00 26.04 ATOM 2473 CD GLU A 342 38.423 5.734 10.974 1.00 27.61 ATOM 2474 OE1 GLU A 342 38.534 4.998 9.966 1.00 28.14 ATOM 2475 OE2 GLU A 342 39.242 6.640 11.240 1.00 29.03 ATOM 2476 C GLU A 342 34.689 5.066 13.116 1.00 22.02 ATOM 2477 O GLU A 342 34.970 5.993 13.876 1.00 22.20 ATOM 2478 N LEU A 343 33.579 5.054 12.382 1.00 20.52 ATOM 2479 CA LEU A 343 32.620 6.153 12.453 1.00 19.72 ATOM 2480 CB LEU A 343 31.529 5.985 11.384 1.00 18.48 ATOM 2481 CG LEU A 343 31.983 5.895 9.920 1.00 17.97 ATOM 2482 CD1 LEU A 343 30.772 6.057 9.002 1.00 19.03 ATOM 2483 CD2 LEU A 343 33.021 6.970 9.617 1.00 17.84 ATOM 2484 C LEU A 343 31.978 6.233 13.840 1.00 20.37 ATOM 2485 O LEU A 343 31.524 7.297 14.257 1.00 20.38 ATOM 2486 N ARG A 344 31.953 5.110 14.550 1.00 20.97 ATOM 2487 CA ARG A 344 31.363 5.065 15.886 1.00 22.54 ATOM 2488 CB ARG A 344 30.699 3.700 16.111 1.00 21.72 ATOM 2489 CG ARG A 344 29.401 3.528 15.317 1.00 21.23 ATOM 2490 CD ARG A 344 28.802 2.143 15.489 1.00 21.44 ATOM 2491 NE ARG A 344 29.472 1.127 14.670 1.00 21.76 ATOM 2492 CZ ARG A 344 29.070 0.745 13.458 1.00 21.52 ATOM 2493 NH1 ARG A 344 27.998 1.289 12.905 1.00 20.98 ATOM 2494 NH2 ARG A 344 29.736 -0.191 12.802 1.00 22.23 ATOM 2495 C ARG A 344 32.377 5.360 17.004 1.00 24.58 ATOM 2496 O ARG A 344 32.045 5.285 18.195 1.00 25.02 ATOM 2497 N ASP A 345 33.605 5.696 16.618 1.00 25.91 ATOM 2498 CA ASP A 345 34.661 6.021 17.577 1.00 27.76 ATOM 2499 CB ASP A 345 36.033 5.924 16.897 1.00 29.23 ATOM 2500 CG ASP A 345 37.201 6.086 17.878 1.00 31.54 ATOM 2501 OD1 ASP A 345 37.197 7.023 18.708 1.00 32.30 ATOM 2502 OD2 ASP A 345 38.138 5.268 17.806 1.00 32.93 ATOM 2503 C ASP A 345 34.425 7.448 18.056 1.00 28.56 ATOM 2504 O ASP A 345 34.305 8.365 17.249 1.00 28.55 ATOM 2505 N PRO A 346 34.377 7.660 19.382 1.00 29.61 ATOM 2506 CD PRO A 346 34.552 6.651 20.437 1.00 29.82 ATOM 2507 CA PRO A 346 34.150 8.996 19.943 1.00 30.02 ATOM 2508 CB PRO A 346 34.147 8.756 21.452 1.00 30.05 ATOM 2509 CG PRO A 346 34.885 7.485 21.636 1.00 29.55 ATOM 2510 C PRO A 346 35.168 10.063 19.542 1.00 31.11 ATOM 2511 O PRO A 346 34.868 11.257 19.586 1.00 31.55 ATOM 2512 N ASN A 347 36.367 9.647 19.146 1.00 31.84 ATOM 2513 CA ASN A 347 37.397 10.612 18.760 1.00 32.63 ATOM 2514 CB ASN A 347 38.742 10.193 19.341 1.00 34.12 ATOM 2515 CG ASN A 347 38.665 9.912 20.812 1.00 35.24 ATOM 2516 OD1 ASN A 347 38.953 8.801 21.259 1.00 37.43 ATOM 2517 ND2 ASN A 347 38.267 10.914 21.582 1.00 35.33 ATOM 2518 C ASN A 347 37.564 10.830 17.262 1.00 32.27 ATOM 2519 O ASN A 347 38.476 11.540 16.843 1.00 32.43 ATOM 2520 N VAL A 348 36.696 10.224 16.457 1.00 31.60 ATOM 2521 CA VAL A 348 36.788 10.376 15.011 1.00 30.70 ATOM 2522 CB VAL A 348 35.758 9.468 14.277 1.00 30.91 ATOM 2523 CG1 VAL A 348 34.347 10.020 14.447 1.00 30.72 ATOM 2524 CG2 VAL A 348 36.122 9.359 12.800 1.00 30.78 ATOM 2525 C VAL A 348 36.574 11.832 14.601 1.00 30.02 ATOM 2526 O VAL A 348 35.750 12.544 15.176 1.00 29.81 ATOM 2527 N LYS A 349 37.338 12.264 13.606 1.00 29.56 ATOM 2528 CA LYS A 349 37.261 13.624 13.094 1.00 29.31 ATOM 2529 CB LYS A 349 38.354 14.484 13.729 1.00 30.96 ATOM 2530 CG LYS A 349 38.080 14.877 15.157 1.00 33.30 ATOM 2531 CD LYS A 349 37.414 16.239 15.217 1.00 36.02 ATOM 2532 CE LYS A 349 37.113 16.643 16.652 1.00 37.89 ATOM 2533 NZ LYS A 349 35.902 15.947 17.187 1.00 39.42 ATOM 2534 C LYS A 349 37.462 13.610 11.586 1.00 28.21 ATOM 2535 O LYS A 349 38.040 12.671 11.038 1.00 28.14 ATOM 2536 N LEU A 350 36.990 14.649 10.913 1.00 27.23 ATOM 2537 CA LEU A 350 37.167 14.733 9.471 1.00 26.95 ATOM 2538 CB LEU A 350 36.195 15.751 8.865 1.00 25.94 ATOM 2539 CG LEU A 350 34.696 15.463 8.952 1.00 25.35 ATOM 2540 CD1 LEU A 350 33.931 16.561 8.227 1.00 24.40 ATOM 2541 CD2 LEU A 350 34.394 14.096 8.343 1.00 24.66 ATOM 2542 C LEU A 350 38.603 15.182 9.181 1.00 27.76 ATOM 2543 O LEU A 350 39.232 15.860 10.001 1.00 27.43 ATOM 2544 N PRO A 351 39.150 14.779 8.026 1.00 28.60 ATOM 2545 CD PRO A 351 38.587 13.878 7.006 1.00 28.60 ATOM 2546 CA PRO A 351 40.517 15.192 7.691 1.00 28.97 ATOM 2547 CB PRO A 351 40.739 14.596 6.301 1.00 28.98 ATOM 2548 CG PRO A 351 39.814 13.405 6.272 1.00 28.93 ATOM 2549 C PRO A 351 40.696 16.714 7.713 1.00 29.14 ATOM 2550 O PRO A 351 41.807 17.203 7.924 1.00 29.61 ATOM 2551 N ASN A 352 39.617 17.466 7.504 1.00 28.89 ATOM 2552 CA ASN A 352 39.734 18.920 7.524 1.00 28.97 ATOM 2553 CB ASN A 352 38.709 19.573 6.578 1.00 29.50 ATOM 2554 CG ASN A 352 37.270 19.435 7.058 1.00 29.50 ATOM 2555 OD1 ASN A 352 36.344 19.866 6.371 1.00 30.82 ATOM 2556 ND2 ASN A 352 37.076 18.842 8.226 1.00 29.01 ATOM 2557 C ASN A 352 39.613 19.491 8.934 1.00 28.66 ATOM 2558 O ASN A 352 39.513 20.701 9.117 1.00 28.26 ATOM 2559 N GLY A 353 39.630 18.611 9.928 1.00 28.79 ATOM 2560 CA GLY A 353 39.552 19.061 11.305 1.00 30.12 ATOM 2561 C GLY A 353 38.159 19.208 11.881 1.00 30.77 ATOM 2562 O GLY A 353 38.000 19.318 13.093 1.00 31.69 ATOM 2563 N ARG A 354 37.144 19.211 11.028 1.00 31.33 ATOM 2564 CA ARG A 354 35.764 19.349 11.494 1.00 31.90 ATOM 2565 CB ARG A 354 34.847 19.695 10.328 1.00 33.26 ATOM 2566 CG ARG A 354 35.040 21.067 9.745 1.00 35.89 ATOM 2567 CD ARG A 354 33.849 21.395 8.873 1.00 38.88 ATOM 2568 NE ARG A 354 34.010 22.632 8.118 1.00 40.85 ATOM 2569 CZ ARG A 354 32.994 23.292 7.572 1.00 42.36 ATOM 2570 NH1 ARG A 354 31.755 22.830 7.705 1.00 43.46 ATOM 2571 NH2 ARG A 354 33.212 24.403 6.885 1.00 43.34 ATOM 2572 C ARG A 354 35.248 18.065 12.136 1.00 31.36 ATOM 2573 O ARG A 354 35.837 16.997 11.982 1.00 30.25 ATOM 2574 N ASP A 355 34.146 18.172 12.869 1.00 31.41 ATOM 2575 CA ASP A 355 33.557 16.985 13.473 1.00 31.83 ATOM 2576 CB ASP A 355 32.571 17.356 14.578 1.00 34.99 ATOM 2577 CG ASP A 355 33.235 18.067 15.730 1.00 38.01 ATOM 2578 OD1 ASP A 355 34.291 17.581 16.193 1.00 39.73 ATOM 2579 OD2 ASP A 355 32.698 19.111 16.166 1.00 40.58 ATOM 2580 C ASP A 355 32.792 16.285 12.358 1.00 30.36 ATOM 2581 O ASP A 355 32.459 16.895 11.338 1.00 29.51 ATOM 2582 N THR A 356 32.519 15.005 12.548 1.00 28.83 ATOM 2583 CA THR A 356 31.771 14.259 11.548 1.00 27.94 ATOM 2584 CB THR A 356 31.738 12.769 11.908 1.00 28.39 ATOM 2585 OG1 THR A 356 31.337 12.624 13.275 1.00 29.61 ATOM 2586 CG2 THR A 356 33.116 12.145 11.722 1.00 29.08 ATOM 2587 C THR A 356 30.335 14.806 11.532 1.00 26.44 ATOM 2588 O THR A 356 29.880 15.405 12.508 1.00 25.93 ATOM 2589 N PRO A 357 29.613 14.626 10.413 1.00 24.63 ATOM 2590 CD PRO A 357 30.039 13.975 9.162 1.00 24.14 ATOM 2591 CA PRO A 357 28.232 15.119 10.344 1.00 23.96 ATOM 2592 CB PRO A 357 27.898 15.040 8.855 1.00 23.87 ATOM 2593 CG PRO A 357 28.774 13.931 8.343 1.00 23.09 ATOM 2594 C PRO A 357 27.324 14.214 11.176 1.00 23.22 ATOM 2595 O PRO A 357 27.803 13.320 11.873 1.00 22.84 ATOM 2596 N ALA A 358 26.019 14.445 11.104 1.00 23.59 ATOM 2597 CA ALA A 358 25.058 13.623 11.846 1.00 23.21 ATOM 2598 CB ALA A 358 23.644 14.170 11.646 1.00 23.32 ATOM 2599 C ALA A 358 25.143 12.176 11.348 1.00 22.74 ATOM 2600 O ALA A 358 25.121 11.928 10.138 1.00 23.02 ATOM 2601 N LEU A 359 25.235 11.225 12.274 1.00 20.64 ATOM 2602 CA LEU A 359 25.341 9.815 11.904 1.00 20.22 ATOM 2603 CB LEU A 359 26.789 9.338 12.042 1.00 20.68 ATOM 2604 CG LEU A 359 27.901 9.972 11.216 1.00 20.76 ATOM 2605 CD1 LEU A 359 29.233 9.476 11.755 1.00 21.18 ATOM 2606 CD2 LEU A 359 27.751 9.602 9.758 1.00 20.51 ATOM 2607 C LEU A 359 24.496 8.886 12.756 1.00 19.31 ATOM 2608 O LEU A 359 24.266 7.730 12.387 1.00 18.97 ATOM 2609 N PHE A 360 24.044 9.380 13.901 1.00 19.23 ATOM 2610 CA PHE A 360 23.307 8.523 14.824 1.00 19.47 ATOM 2611 CB PHE A 360 24.140 8.351 16.101 1.00 19.92 ATOM 2612 CG PHE A 360 25.606 8.098 15.841 1.00 20.76 ATOM 2613 CD1 PHE A 360 26.571 9.012 16.256 1.00 21.61 ATOM 2614 CD2 PHE A 360 26.017 6.952 15.174 1.00 20.58 ATOM 2615 CE1 PHE A 360 27.928 8.787 16.004 1.00 22.55 ATOM 2616 CE2 PHE A 360 27.364 6.713 14.918 1.00 22.08 ATOM 2617 CZ PHE A 360 28.324 7.632 15.332 1.00 22.43 ATOM 2618 C PHE A 360 21.887 8.933 15.196 1.00 19.94 ATOM 2619 O PHE A 360 21.284 8.311 16.079 1.00 19.83 ATOM 2620 N ASN A 361 21.342 9.950 14.530 1.00 20.16 ATOM 2621 CA ASN A 361 19.990 10.395 14.840 1.00 21.31 ATOM 2622 CB ASN A 361 19.799 11.869 14.444 1.00 21.58 ATOM 2623 CG ASN A 361 20.164 12.159 12.994 1.00 23.84 ATOM 2624 OD1 ASN A 361 19.747 13.178 12.437 1.00 27.29 ATOM 2625 ND2 ASN A 361 20.939 11.281 12.380 1.00 22.41 ATOM 2626 C ASN A 361 18.922 9.514 14.194 1.00 21.02 ATOM 2627 O ASN A 361 18.068 9.988 13.451 1.00 21.55 ATOM 2628 N PHE A 362 18.980 8.220 14.490 1.00 21.35 ATOM 2629 CA PHE A 362 18.018 7.267 13.951 1.00 22.25 ATOM 2630 CB PHE A 362 18.464 5.836 14.240 1.00 21.79 ATOM 2631 CG PHE A 362 19.652 5.391 13.442 1.00 22.45 ATOM 2632 CD1 PHE A 362 19.485 4.823 12.179 1.00 22.52 ATOM 2633 CD2 PHE A 362 20.940 5.524 13.956 1.00 21.64 ATOM 2634 CE1 PHE A 362 20.590 4.391 11.436 1.00 21.72 ATOM 2635 CE2 PHE A 362 22.051 5.096 13.224 1.00 22.32 ATOM 2636 CZ PHE A 362 21.874 4.528 11.960 1.00 21.52 ATOM 2637 C PHE A 362 16.640 7.461 14.576 1.00 22.59 ATOM 2638 O PHE A 362 16.521 7.843 15.744 1.00 22.76 ATOM 2639 N THR A 363 15.604 7.182 13.789 1.00 22.87 ATOM 2640 CA THR A 363 14.224 7.271 14.256 1.00 22.58 ATOM 2641 CB THR A 363 13.334 8.090 13.294 1.00 22.26 ATOM 2642 OG1 THR A 363 13.347 7.474 12.001 1.00 22.03 ATOM 2643 CG2 THR A 363 13.830 9.510 13.171 1.00 21.25 ATOM 2644 C THR A 363 13.676 5.845 14.301 1.00 23.05 ATOM 2645 O THR A 363 14.277 4.910 13.758 1.00 22.28 ATOM 2646 N THR A 364 12.538 5.675 14.963 1.00 23.23 ATOM 2647 CA THR A 364 11.909 4.369 15.055 1.00 23.84 ATOM 2648 CB THR A 364 10.580 4.471 15.811 1.00 24.26 ATOM 2649 OG1 THR A 364 10.842 4.881 17.160 1.00 26.24 ATOM 2650 CG2 THR A 364 9.860 3.135 15.806 1.00 24.47 ATOM 2651 C THR A 364 11.649 3.817 13.654 1.00 23.69 ATOM 2652 O THR A 364 11.919 2.646 13.376 1.00 24.32 ATOM 2653 N GLN A 365 11.129 4.671 12.779 1.00 23.80 ATOM 2654 CA GLN A 365 10.826 4.290 11.399 1.00 23.65 ATOM 2655 CB GLN A 365 10.310 5.509 10.631 1.00 24.34 ATOM 2656 CG GLN A 365 10.060 5.259 9.145 1.00 26.76 ATOM 2657 CD GLN A 365 8.843 4.384 8.892 1.00 27.43 ATOM 2658 OE1 GLN A 365 7.911 4.344 9.698 1.00 29.13 ATOM 2659 NE2 GLN A 365 8.844 3.680 7.775 1.00 26.82 ATOM 2660 C GLN A 365 12.067 3.731 10.697 1.00 23.26 ATOM 2661 O GLN A 365 12.018 2.679 10.062 1.00 22.58 ATOM 2662 N GLU A 366 13.184 4.438 10.825 1.00 22.54 ATOM 2663 CA GLU A 366 14.441 4.021 10.190 1.00 22.32 ATOM 2664 CB GLU A 366 15.500 5.116 10.393 1.00 22.20 ATOM 2665 CG GLU A 366 16.717 5.000 9.480 1.00 22.76 ATOM 2666 CD GLU A 366 17.663 6.184 9.628 1.00 23.87 ATOM 2667 OE1 GLU A 366 18.730 6.171 8.977 1.00 23.14 ATOM 2668 OE2 GLU A 366 17.338 7.121 10.395 1.00 23.36 ATOM 2669 C GLU A 366 14.979 2.681 10.708 1.00 22.25 ATOM 2670 O GLU A 366 15.601 1.920 9.961 1.00 20.58 ATOM 2671 N LEU A 367 14.740 2.391 11.987 1.00 22.47 ATOM 2672 CA LEU A 367 15.221 1.150 12.594 1.00 22.87 ATOM 2673 CB LEU A 367 15.575 1.387 14.069 1.00 23.18 ATOM 2674 CG LEU A 367 16.772 2.288 14.377 1.00 23.26 ATOM 2675 CD1 LEU A 367 16.598 2.924 15.770 1.00 24.08 ATOM 2676 CD2 LEU A 367 18.049 1.471 14.302 1.00 22.28 ATOM 2677 C LEU A 367 14.205 0.020 12.537 1.00 23.66 ATOM 2678 O LEU A 367 14.508 -1.105 12.928 1.00 23.90 ATOM 2679 N SER A 368 13.009 0.314 12.043 1.00 25.09 ATOM 2680 CA SER A 368 11.927 -0.670 12.018 1.00 26.71 ATOM 2681 CB SER A 368 10.680 -0.066 11.354 1.00 26.67 ATOM 2682 OG SER A 368 10.873 0.160 9.973 1.00 27.42 ATOM 2683 C SER A 368 12.212 -2.053 11.440 1.00 27.68 ATOM 2684 O SER A 368 11.613 -3.036 11.880 1.00 28.18 ATOM 2685 N SER A 369 13.127 -2.159 10.485 1.00 28.08 ATOM 2686 CA SER A 369 13.412 -3.469 9.906 1.00 28.52 ATOM 2687 CB SER A 369 14.212 -3.318 8.604 1.00 28.17 ATOM 2688 OG SER A 369 15.606 -3.273 8.862 1.00 27.80 ATOM 2689 C SER A 369 14.167 -4.391 10.865 1.00 29.40 ATOM 2690 O SER A 369 14.248 -5.599 10.630 1.00 29.75 ATOM 2691 N ASN A 370 14.714 -3.831 11.943 1.00 29.19 ATOM 2692 CA ASN A 370 15.476 -4.620 12.915 1.00 29.09 ATOM 2693 CB ASN A 370 16.718 -5.207 12.235 1.00 30.03 ATOM 2694 CG ASN A 370 17.362 -6.317 13.038 1.00 31.07 ATOM 2695 OD1 ASN A 370 17.170 -6.426 14.252 1.00 32.05 ATOM 2696 ND2 ASN A 370 18.137 -7.153 12.360 1.00 32.10 ATOM 2697 C ASN A 370 15.891 -3.715 14.078 1.00 28.73 ATOM 2698 O ASN A 370 17.063 -3.365 14.225 1.00 28.09 ATOM 2699 N PRO A 371 14.922 -3.323 14.920 1.00 28.65 ATOM 2700 CD PRO A 371 13.497 -3.701 14.829 1.00 28.09 ATOM 2701 CA PRO A 371 15.181 -2.449 16.071 1.00 28.13 ATOM 2702 CB PRO A 371 13.872 -2.501 16.854 1.00 28.10 ATOM 2703 CG PRO A 371 12.836 -2.773 15.812 1.00 28.06 ATOM 2704 C PRO A 371 16.396 -2.798 16.931 1.00 27.75 ATOM 2705 O PRO A 371 17.144 -1.914 17.337 1.00 27.90 ATOM 2706 N PRO A 372 16.608 -4.087 17.233 1.00 27.57 ATOM 2707 CD PRO A 372 15.777 -5.254 16.883 1.00 27.70 ATOM 2708 CA PRO A 372 17.761 -4.468 18.057 1.00 27.44 ATOM 2709 CB PRO A 372 17.703 -5.995 18.073 1.00 27.53 ATOM 2710 CG PRO A 372 16.257 -6.309 17.837 1.00 27.99 ATOM 2711 C PRO A 372 19.128 -3.959 17.603 1.00 27.58 ATOM 2712 O PRO A 372 20.081 -3.948 18.387 1.00 27.57 ATOM 2713 N LEU A 373 19.241 -3.547 16.345 1.00 26.92 ATOM 2714 CA LEU A 373 20.520 -3.048 15.844 1.00 26.94 ATOM 2715 CB LEU A 373 20.485 -2.946 14.316 1.00 26.66 ATOM 2716 CG LEU A 373 20.536 -4.280 13.565 1.00 27.04 ATOM 2717 CD1 LEU A 373 20.539 -4.019 12.061 1.00 26.48 ATOM 2718 CD2 LEU A 373 21.776 -5.065 13.978 1.00 26.59 ATOM 2719 C LEU A 373 20.895 -1.692 16.451 1.00 26.75 ATOM 2720 O LEU A 373 22.047 -1.261 16.362 1.00 26.56 ATOM 2721 N ALA A 374 19.923 -1.026 17.072 1.00 27.26 ATOM 2722 CA ALA A 374 20.161 0.275 17.697 1.00 27.96 ATOM 2723 CB ALA A 374 18.904 0.751 18.405 1.00 27.56 ATOM 2724 C ALA A 374 21.312 0.189 18.690 1.00 28.51 ATOM 2725 O ALA A 374 22.036 1.155 18.906 1.00 28.80 ATOM 2726 N THR A 375 21.471 -0.982 19.293 1.00 29.23 ATOM 2727 CA THR A 375 22.522 -1.230 20.268 1.00 29.85 ATOM 2728 CB THR A 375 22.391 -2.651 20.815 1.00 30.84 ATOM 2729 OG1 THR A 375 21.361 -2.666 21.804 1.00 34.26 ATOM 2730 CG2 THR A 375 23.684 -3.121 21.436 1.00 33.07 ATOM 2731 C THR A 375 23.903 -1.049 19.659 1.00 29.43 ATOM 2732 O THR A 375 24.865 -0.699 20.354 1.00 29.19 ATOM 2733 N ILE A 376 24.003 -1.304 18.359 1.00 28.66 ATOM 2734 CA ILE A 376 25.269 -1.153 17.651 1.00 28.03 ATOM 2735 CB ILE A 376 25.432 -2.208 16.543 1.00 28.68 ATOM 2736 CG2 ILE A 376 26.646 -1.875 15.675 1.00 29.53 ATOM 2737 CG1 ILE A 376 25.583 -3.595 17.155 1.00 28.44 ATOM 2738 CD1 ILE A 376 25.248 -4.698 16.184 1.00 28.94 ATOM 2739 C ILE A 376 25.325 0.209 16.984 1.00 27.34 ATOM 2740 O ILE A 376 26.340 0.905 17.051 1.00 27.30 ATOM 2741 N LEU A 377 24.213 0.578 16.349 1.00 26.06 ATOM 2742 CA LEU A 377 24.102 1.824 15.601 1.00 24.88 ATOM 2743 CB LEU A 377 22.800 1.816 14.799 1.00 23.45 ATOM 2744 CG LEU A 377 22.761 0.694 13.758 1.00 23.82 ATOM 2745 CD1 LEU A 377 21.368 0.616 13.135 1.00 22.21 ATOM 2746 CD2 LEU A 377 23.832 0.948 12.680 1.00 22.41 ATOM 2747 C LEU A 377 24.227 3.126 16.376 1.00 24.72 ATOM 2748 O LEU A 377 24.730 4.114 15.836 1.00 24.32 ATOM 2749 N ILE A 378 23.757 3.151 17.619 1.00 23.94 ATOM 2750 CA ILE A 378 23.873 4.361 18.422 1.00 24.66 ATOM 2751 CB ILE A 378 22.516 4.773 19.047 1.00 25.40 ATOM 2752 CG2 ILE A 378 22.645 6.120 19.751 1.00 24.40 ATOM 2753 CG1 ILE A 378 21.449 4.866 17.948 1.00 25.25 ATOM 2754 CD1 ILE A 378 20.138 5.505 18.403 1.00 25.99 ATOM 2755 C ILE A 378 24.882 4.060 19.521 1.00 25.46 ATOM 2756 O ILE A 378 24.547 3.431 20.524 1.00 25.58 ATOM 2757 N PRO A 379 26.144 4.479 19.327 1.00 25.55 ATOM 2758 CD PRO A 379 26.644 5.205 18.146 1.00 25.72 ATOM 2759 CA PRO A 379 27.205 4.245 20.311 1.00 25.97 ATOM 2760 CB PRO A 379 28.469 4.748 19.609 1.00 25.55 ATOM 2761 CG PRO A 379 27.981 5.706 18.593 1.00 25.32 ATOM 2762 C PRO A 379 26.956 4.940 21.652 1.00 26.18 ATOM 2763 O PRO A 379 26.177 5.886 21.744 1.00 25.49 ATOM 2764 N PRO A 380 27.615 4.459 22.716 1.00 27.30 ATOM 2765 CD PRO A 380 28.533 3.305 22.700 1.00 26.88 ATOM 2766 CA PRO A 380 27.474 5.022 24.067 1.00 28.29 ATOM 2767 CB PRO A 380 28.589 4.335 24.854 1.00 27.49 ATOM 2768 CG PRO A 380 28.746 3.014 24.177 1.00 27.06 ATOM 2769 C PRO A 380 27.540 6.544 24.183 1.00 29.56 ATOM 2770 O PRO A 380 26.744 7.152 24.895 1.00 29.85 ATOM 2771 N HIS A 381 28.479 7.161 23.475 1.00 30.81 ATOM 2772 CA HIS A 381 28.658 8.609 23.534 1.00 32.55 ATOM 2773 CB HIS A 381 30.068 8.965 23.069 1.00 31.69 ATOM 2774 CG HIS A 381 30.282 8.763 21.603 1.00 31.32 ATOM 2775 CD2 HIS A 381 30.173 9.618 20.559 1.00 30.72 ATOM 2776 ND1 HIS A 381 30.633 7.543 21.065 1.00 31.33 ATOM 2777 CE1 HIS A 381 30.732 7.655 19.753 1.00 30.69 ATOM 2778 NE2 HIS A 381 30.458 8.904 19.420 1.00 30.67 ATOM 2779 C HIS A 381 27.669 9.428 22.724 1.00 34.64 ATOM 2780 O HIS A 381 27.476 10.615 22.989 1.00 34.58 ATOM 2781 N ALA A 382 27.038 8.802 21.741 1.00 37.33 ATOM 2782 CA ALA A 382 26.115 9.503 20.856 1.00 41.07 ATOM 2783 CB ALA A 382 25.899 8.670 19.604 1.00 40.35 ATOM 2784 C ALA A 382 24.764 9.927 21.423 1.00 44.20 ATOM 2785 O ALA A 382 24.137 9.204 22.198 1.00 43.99 ATOM 2786 N ARG A 383 24.332 11.117 21.015 1.00 48.34 ATOM 2787 CA ARG A 383 23.044 11.678 21.401 1.00 53.05 ATOM 2788 CB ARG A 383 21.925 10.884 20.723 1.00 53.17 ATOM 2789 CG ARG A 383 22.052 10.784 19.214 1.00 53.98 ATOM 2790 CD ARG A 383 20.871 10.038 18.619 1.00 55.01 ATOM 2791 NE ARG A 383 19.604 10.772 18.700 1.00 55.60 ATOM 2792 CZ ARG A 383 19.438 12.011 18.238 1.00 55.79 ATOM 2793 NH1 ARG A 383 20.452 12.658 17.663 1.00 56.05 ATOM 2794 NH2 ARG A 383 18.253 12.608 18.332 1.00 56.05 ATOM 2795 C ARG A 383 22.766 11.755 22.897 1.00 56.29 ATOM 2796 O ARG A 383 21.607 11.735 23.316 1.00 56.96 ATOM 2797 N ILE A 384 23.818 11.836 23.707 1.00 60.04 ATOM 2798 CA ILE A 384 23.625 11.923 25.150 1.00 63.74 ATOM 2799 CB ILE A 384 24.958 11.711 25.918 1.00 63.70 ATOM 2800 CG2 ILE A 384 24.802 12.125 27.369 1.00 63.94 ATOM 2801 CG1 ILE A 384 25.365 10.237 25.875 1.00 63.75 ATOM 2802 CD1 ILE A 384 24.302 9.298 26.397 1.00 63.98 ATOM 2803 C ILE A 384 23.079 13.312 25.468 1.00 66.41 ATOM 2804 O ILE A 384 23.754 14.324 25.244 1.00 66.91 ATOM 2805 N GLN A 385 21.848 13.355 25.971 1.00 69.29 ATOM 2806 CA GLN A 385 21.215 14.621 26.320 1.00 71.88 ATOM 2807 CB GLN A 385 20.459 15.181 25.103 1.00 72.44 ATOM 2808 CG GLN A 385 18.965 14.879 25.054 1.00 73.59 ATOM 2809 CD GLN A 385 18.153 16.038 24.513 1.00 74.32 ATOM 2810 OE1 GLN A 385 17.437 15.907 23.516 1.00 74.85 ATOM 2811 NE2 GLN A 385 18.272 17.191 25.162 1.00 74.56 ATOM 2812 C GLN A 385 20.277 14.491 27.528 1.00 73.23 ATOM 2813 O GLN A 385 19.319 13.714 27.516 1.00 73.41 ATOM 2814 N ALA A 386 20.580 15.251 28.576 1.00 74.89 ATOM 2815 CA ALA A 386 19.777 15.249 29.796 1.00 76.31 ATOM 2816 CB ALA A 386 20.655 15.589 30.998 1.00 76.07 ATOM 2817 C ALA A 386 18.630 16.253 29.672 1.00 77.33 ATOM 2818 O ALA A 386 18.573 17.031 28.719 1.00 77.53 ATOM 2819 N ALA A 387 17.722 16.232 30.642 1.00 78.58 ATOM 2820 CA ALA A 387 16.577 17.135 30.637 1.00 79.69 ATOM 2821 CB ALA A 387 15.097 16.425 30.885 1.00 79.22 ATOM 2822 C ALA A 387 16.790 18.334 31.560 1.00 80.52 ATOM 2823 O ALA A 387 15.827 18.970 31.993 1.00 80.83 ATOM 2824 N ALA A 388 18.055 18.635 31.856 1.00 81.27 ATOM 2825 CA ALA A 388 18.411 19.765 32.712 1.00 82.09 ATOM 2826 CB ALA A 388 18.029 21.085 32.024 1.00 82.14 ATOM 2827 C ALA A 388 17.773 19.691 34.103 1.00 82.61 ATOM 2828 O ALA A 388 16.557 19.960 34.217 1.00 82.95 ATOM 2829 OT ALA A 388 18.497 19.374 35.076 1.00 82.86 ATOM 2830 CB PHE B 523 43.029 -31.574 -26.588 1.00 93.55 ATOM 2831 CG PHE B 523 42.384 -32.779 -27.246 1.00 94.36 ATOM 2832 CD1 PHE B 523 41.676 -32.668 -28.444 1.00 94.74 ATOM 2833 CD2 PHE B 523 42.475 -34.032 -26.642 1.00 94.56 ATOM 2834 CE1 PHE B 523 41.068 -33.783 -29.028 1.00 94.92 ATOM 2835 CE2 PHE B 523 41.871 -35.153 -27.217 1.00 94.82 ATOM 2836 CZ PHE B 523 41.167 -35.027 -28.412 1.00 94.92 ATOM 2837 C PHE B 523 44.307 -30.568 -28.503 1.00 92.52 ATOM 2838 O PHE B 523 44.535 -31.685 -28.970 1.00 92.61 ATOM 2839 N PHE B 523 41.874 -30.025 -28.159 1.00 92.76 ATOM 2840 CA PHE B 523 43.174 -30.344 -27.502 1.00 92.81 ATOM 2841 N GLY B 524 45.015 -29.489 -28.824 1.00 92.02 ATOM 2842 CA GLY B 524 46.123 -29.566 -29.759 1.00 91.28 ATOM 2843 C GLY B 524 47.349 -28.882 -29.186 1.00 90.72 ATOM 2844 O GLY B 524 47.380 -28.560 -27.999 1.00 90.71 ATOM 2845 N SER B 525 48.357 -28.651 -30.022 1.00 90.14 ATOM 2846 CA SER B 525 49.584 -28.005 -29.568 1.00 89.44 ATOM 2847 CB SER B 525 50.555 -29.055 -29.029 1.00 89.41 ATOM 2848 OG SER B 525 50.816 -30.046 -30.009 1.00 89.34 ATOM 2849 C SER B 525 50.269 -27.207 -30.672 1.00 88.95 ATOM 2850 O SER B 525 49.906 -27.302 -31.845 1.00 88.90 ATOM 2851 N MET B 526 51.270 -26.423 -30.283 1.00 88.30 ATOM 2852 CA MET B 526 52.019 -25.604 -31.228 1.00 87.66 ATOM 2853 CB MET B 526 51.824 -24.119 -30.926 1.00 87.65 ATOM 2854 CG MET B 526 50.413 -23.725 -30.554 1.00 87.69 ATOM 2855 SD MET B 526 50.353 -21.991 -30.104 1.00 87.57 ATOM 2856 CE MET B 526 51.604 -21.938 -28.814 1.00 87.75 ATOM 2857 C MET B 526 53.506 -25.916 -31.183 1.00 87.18 ATOM 2858 O MET B 526 53.962 -26.729 -30.381 1.00 87.12 ATOM 2859 N LYS B 527 54.257 -25.252 -32.051 1.00 86.59 ATOM 2860 CA LYS B 527 55.697 -25.432 -32.123 1.00 86.11 ATOM 2861 CB LYS B 527 56.055 -26.399 -33.255 1.00 85.68 ATOM 2862 CG LYS B 527 55.539 -27.814 -33.050 1.00 85.12 ATOM 2863 CD LYS B 527 56.650 -28.836 -33.219 1.00 84.68 ATOM 2864 CE LYS B 527 56.107 -30.253 -33.182 1.00 84.38 ATOM 2865 NZ LYS B 527 55.953 -30.824 -34.547 1.00 83.90 ATOM 2866 C LYS B 527 56.340 -24.075 -32.372 1.00 86.14 ATOM 2867 O LYS B 527 56.198 -23.496 -33.448 1.00 86.11 ATOM 2868 N VAL B 528 57.040 -23.567 -31.367 1.00 86.35 ATOM 2869 CA VAL B 528 57.700 -22.275 -31.475 1.00 86.61 ATOM 2870 CB VAL B 528 57.560 -21.478 -30.165 1.00 86.42 ATOM 2871 CG1 VAL B 528 58.038 -20.055 -30.373 1.00 86.64 ATOM 2872 CG2 VAL B 528 56.111 -21.492 -29.701 1.00 86.35 ATOM 2873 C VAL B 528 59.182 -22.441 -31.798 1.00 86.95 ATOM 2874 O VAL B 528 59.831 -23.370 -31.320 1.00 86.99 ATOM 2875 N SER B 529 59.710 -21.539 -32.618 1.00 87.42 ATOM 2876 CA SER B 529 61.116 -21.577 -33.005 1.00 87.98 ATOM 2877 CB SER B 529 61.319 -22.549 -34.169 1.00 87.66 ATOM 2878 OG SER B 529 60.699 -22.075 -35.352 1.00 87.31 ATOM 2879 C SER B 529 61.570 -20.181 -33.408 1.00 88.71 ATOM 2880 O SER B 529 60.864 -19.204 -33.166 1.00 88.78 ATOM 2881 N ARG B 530 62.749 -20.087 -34.016 1.00 89.64 ATOM 2882 CA ARG B 530 63.287 -18.801 -34.453 1.00 90.53 ATOM 2883 CB ARG B 530 64.417 -18.346 -33.524 1.00 91.05 ATOM 2884 CG ARG B 530 63.954 -17.877 -32.156 1.00 92.16 ATOM 2885 CD ARG B 530 65.138 -17.618 -31.238 1.00 93.25 ATOM 2886 NE ARG B 530 64.736 -17.476 -29.840 1.00 94.28 ATOM 2887 CZ ARG B 530 65.575 -17.215 -28.840 1.00 94.73 ATOM 2888 NH1 ARG B 530 66.872 -17.066 -29.078 1.00 94.88 ATOM 2889 NH2 ARG B 530 65.117 -17.102 -27.598 1.00 95.02 ATOM 2890 C ARG B 530 63.817 -18.901 -35.876 1.00 90.75 ATOM 2891 O ARG B 530 64.964 -19.295 -36.088 1.00 90.88 ATOM 2892 N ASP B 531 62.979 -18.540 -36.846 1.00 90.95 ATOM 2893 CA ASP B 531 63.359 -18.592 -38.255 1.00 91.14 ATOM 2894 CB ASP B 531 62.361 -17.799 -39.104 1.00 91.87 ATOM 2895 CG ASP B 531 61.508 -18.694 -39.987 1.00 92.69 ATOM 2896 OD1 ASP B 531 61.298 -18.345 -41.170 1.00 92.97 ATOM 2897 OD2 ASP B 531 61.049 -19.750 -39.497 1.00 93.20 ATOM 2898 C ASP B 531 64.763 -18.041 -38.467 1.00 90.84 ATOM 2899 O ASP B 531 65.654 -18.748 -38.940 1.00 90.99 ATOM 2900 N LYS B 532 64.953 -16.775 -38.115 1.00 90.23 ATOM 2901 CA LYS B 532 66.250 -16.124 -38.250 1.00 89.47 ATOM 2902 CB LYS B 532 66.676 -16.064 -39.723 1.00 89.73 ATOM 2903 CG LYS B 532 65.713 -15.324 -40.630 1.00 90.09 ATOM 2904 CD LYS B 532 66.439 -14.772 -41.844 1.00 90.37 ATOM 2905 CE LYS B 532 65.542 -14.767 -43.070 1.00 90.69 ATOM 2906 NZ LYS B 532 66.309 -14.482 -44.315 1.00 90.75 ATOM 2907 C LYS B 532 66.186 -14.720 -37.663 1.00 88.60 ATOM 2908 O LYS B 532 65.116 -14.109 -37.610 1.00 88.58 ATOM 2909 N ASP B 533 67.336 -14.218 -37.222 1.00 87.41 ATOM 2910 CA ASP B 533 67.431 -12.892 -36.617 1.00 85.93 ATOM 2911 CB ASP B 533 66.768 -11.839 -37.516 1.00 86.68 ATOM 2912 CG ASP B 533 67.152 -11.991 -38.978 1.00 87.36 ATOM 2913 OD1 ASP B 533 68.238 -11.502 -39.363 1.00 87.81 ATOM 2914 OD2 ASP B 533 66.366 -12.597 -39.741 1.00 87.57 ATOM 2915 C ASP B 533 66.756 -12.905 -35.249 1.00 84.24 ATOM 2916 O ASP B 533 66.466 -11.853 -34.676 1.00 84.38 ATOM 2917 N GLY B 534 66.514 -14.107 -34.732 1.00 82.04 ATOM 2918 CA GLY B 534 65.867 -14.246 -33.441 1.00 78.95 ATOM 2919 C GLY B 534 64.359 -14.220 -33.593 1.00 76.71 ATOM 2920 O GLY B 534 63.628 -14.392 -32.617 1.00 77.00 ATOM 2921 N SER B 535 63.901 -14.012 -34.826 1.00 74.00 ATOM 2922 CA SER B 535 62.474 -13.951 -35.139 1.00 71.03 ATOM 2923 CB SER B 535 62.274 -13.754 -36.644 1.00 71.51 ATOM 2924 OG SER B 535 60.936 -13.385 -36.934 1.00 71.80 ATOM 2925 C SER B 535 61.719 -15.198 -34.694 1.00 68.53 ATOM 2926 O SER B 535 61.947 -16.288 -35.216 1.00 68.56 ATOM 2927 N LYS B 536 60.814 -15.024 -33.737 1.00 65.23 ATOM 2928 CA LYS B 536 60.019 -16.129 -33.216 1.00 61.84 ATOM 2929 CB LYS B 536 59.366 -15.728 -31.890 1.00 61.97 ATOM 2930 CG LYS B 536 58.395 -16.763 -31.337 1.00 62.12 ATOM 2931 CD LYS B 536 57.718 -16.268 -30.067 1.00 62.41 ATOM 2932 CE LYS B 536 56.500 -17.113 -29.722 1.00 62.45 ATOM 2933 NZ LYS B 536 56.419 -17.399 -28.264 1.00 62.66 ATOM 2934 C LYS B 536 58.942 -16.564 -34.207 1.00 59.46 ATOM 2935 O LYS B 536 58.136 -15.751 -34.664 1.00 59.51 ATOM 2936 N VAL B 537 58.933 -17.852 -34.531 1.00 56.14 ATOM 2937 CA VAL B 537 57.963 -18.413 -35.461 1.00 52.49 ATOM 2938 CB VAL B 537 58.668 -19.085 -36.656 1.00 52.41 ATOM 2939 CG1 VAL B 537 57.664 -19.875 -37.483 1.00 52.09 ATOM 2940 CG2 VAL B 537 59.353 -18.038 -37.503 1.00 51.83 ATOM 2941 C VAL B 537 57.112 -19.460 -34.754 1.00 50.15 ATOM 2942 O VAL B 537 57.637 -20.363 -34.110 1.00 49.66 ATOM 2943 N THR B 538 55.795 -19.331 -34.869 1.00 47.44 ATOM 2944 CA THR B 538 54.890 -20.287 -34.252 1.00 44.90 ATOM 2945 CB THR B 538 53.765 -19.591 -33.471 1.00 44.96 ATOM 2946 OG1 THR B 538 54.331 -18.818 -32.406 1.00 44.88 ATOM 2947 CG2 THR B 538 52.817 -20.621 -32.886 1.00 44.57 ATOM 2948 C THR B 538 54.263 -21.140 -35.342 1.00 43.23 ATOM 2949 O THR B 538 53.684 -20.625 -36.296 1.00 42.83 ATOM 2950 N THR B 539 54.399 -22.450 -35.207 1.00 41.33 ATOM 2951 CA THR B 539 53.839 -23.361 -36.186 1.00 39.35 ATOM 2952 CB THR B 539 54.907 -24.307 -36.759 1.00 39.12 ATOM 2953 OG1 THR B 539 55.850 -23.547 -37.523 1.00 39.25 ATOM 2954 CG2 THR B 539 54.265 -25.353 -37.659 1.00 38.92 ATOM 2955 C THR B 539 52.762 -24.180 -35.520 1.00 37.80 ATOM 2956 O THR B 539 52.972 -24.745 -34.449 1.00 37.03 ATOM 2957 N VAL B 540 51.600 -24.227 -36.160 1.00 36.73 ATOM 2958 CA VAL B 540 50.469 -24.977 -35.638 1.00 35.44 ATOM 2959 CB VAL B 540 49.387 -24.018 -35.087 1.00 35.18 ATOM 2960 CG1 VAL B 540 49.993 -23.081 -34.056 1.00 34.54 ATOM 2961 CG2 VAL B 540 48.783 -23.214 -36.224 1.00 34.74 ATOM 2962 C VAL B 540 49.862 -25.817 -36.757 1.00 35.16 ATOM 2963 O VAL B 540 50.160 -25.607 -37.931 1.00 34.35 ATOM 2964 N VAL B 541 49.031 -26.782 -36.381 1.00 34.74 ATOM 2965 CA VAL B 541 48.347 -27.619 -37.355 1.00 35.22 ATOM 2966 CB VAL B 541 48.553 -29.135 -37.053 1.00 35.02 ATOM 2967 CG1 VAL B 541 47.675 -29.990 -37.973 1.00 34.29 ATOM 2968 CG2 VAL B 541 50.020 -29.501 -37.244 1.00 33.43 ATOM 2969 C VAL B 541 46.876 -27.227 -37.216 1.00 35.47 ATOM 2970 O VAL B 541 46.252 -27.483 -36.185 1.00 35.53 ATOM 2971 N ALA B 542 46.335 -26.591 -38.251 1.00 36.28 ATOM 2972 CA ALA B 542 44.951 -26.116 -38.226 1.00 37.28 ATOM 2973 CB ALA B 542 44.930 -24.613 -38.492 1.00 36.73 ATOM 2974 C ALA B 542 43.988 -26.811 -39.182 1.00 38.01 ATOM 2975 O ALA B 542 44.391 -27.360 -40.203 1.00 37.78 ATOM 2976 N THR B 543 42.705 -26.764 -38.836 1.00 39.03 ATOM 2977 CA THR B 543 41.644 -27.352 -39.649 1.00 40.91 ATOM 2978 CB THR B 543 40.511 -27.901 -38.775 1.00 40.99 ATOM 2979 OG1 THR B 543 41.032 -28.892 -37.885 1.00 41.95 ATOM 2980 CG2 THR B 543 39.422 -28.513 -39.636 1.00 41.30 ATOM 2981 C THR B 543 41.054 -26.274 -40.552 1.00 42.21 ATOM 2982 O THR B 543 40.622 -25.222 -40.072 1.00 41.60 ATOM 2983 N PRO B 544 41.006 -26.526 -41.870 1.00 43.71 ATOM 2984 CD PRO B 544 41.426 -27.746 -42.582 1.00 43.81 ATOM 2985 CA PRO B 544 40.453 -25.526 -42.788 1.00 45.11 ATOM 2986 CB PRO B 544 40.382 -26.265 -44.122 1.00 44.94 ATOM 2987 CG PRO B 544 41.440 -27.310 -44.016 1.00 44.20 ATOM 2988 C PRO B 544 39.088 -25.027 -42.319 1.00 46.66 ATOM 2989 O PRO B 544 38.267 -25.806 -41.827 1.00 46.12 ATOM 2990 N GLY B 545 38.861 -23.724 -42.465 1.00 48.46 ATOM 2991 CA GLY B 545 37.604 -23.137 -42.042 1.00 50.98 ATOM 2992 C GLY B 545 36.401 -23.558 -42.861 1.00 52.93 ATOM 2993 O GLY B 545 35.353 -23.885 -42.306 1.00 53.06 ATOM 2994 N GLN B 546 36.544 -23.561 -44.182 1.00 54.87 ATOM 2995 CA GLN B 546 35.433 -23.931 -45.045 1.00 57.00 ATOM 2996 CB GLN B 546 35.170 -22.817 -46.068 1.00 57.98 ATOM 2997 CG GLN B 546 33.875 -22.990 -46.874 1.00 59.74 ATOM 2998 CD GLN B 546 32.625 -22.572 -46.103 1.00 60.52 ATOM 2999 OE1 GLN B 546 31.512 -23.004 -46.419 1.00 60.99 ATOM 3000 NE2 GLN B 546 32.806 -21.727 -45.091 1.00 60.71 ATOM 3001 C GLN B 546 35.633 -25.260 -45.766 1.00 57.82 ATOM 3002 O GLN B 546 34.728 -26.095 -45.788 1.00 58.39 ATOM 3003 N GLY B 547 36.811 -25.462 -46.347 1.00 58.40 ATOM 3004 CA GLY B 547 37.072 -26.695 -47.073 1.00 59.23 ATOM 3005 C GLY B 547 36.917 -27.965 -46.252 1.00 59.50 ATOM 3006 O GLY B 547 36.513 -27.900 -45.089 1.00 60.04 ATOM 3007 N PRO B 548 37.214 -29.144 -46.836 1.00 59.24 ATOM 3008 CD PRO B 548 37.669 -29.326 -48.229 1.00 59.23 ATOM 3009 CA PRO B 548 37.103 -30.423 -46.120 1.00 58.56 ATOM 3010 CB PRO B 548 37.239 -31.468 -47.223 1.00 58.80 ATOM 3011 CG PRO B 548 38.035 -30.785 -48.289 1.00 59.08 ATOM 3012 C PRO B 548 38.220 -30.529 -45.082 1.00 57.91 ATOM 3013 O PRO B 548 39.246 -29.860 -45.211 1.00 58.16 ATOM 3014 N ASP B 549 38.029 -31.370 -44.066 1.00 57.03 ATOM 3015 CA ASP B 549 39.021 -31.523 -42.996 1.00 55.94 ATOM 3016 CB ASP B 549 38.457 -32.367 -41.850 1.00 56.52 ATOM 3017 CG ASP B 549 39.353 -32.348 -40.614 1.00 57.17 ATOM 3018 OD1 ASP B 549 40.366 -31.611 -40.606 1.00 57.17 ATOM 3019 OD2 ASP B 549 39.045 -33.072 -39.644 1.00 57.84 ATOM 3020 C ASP B 549 40.378 -32.092 -43.395 1.00 54.70 ATOM 3021 O ASP B 549 40.651 -33.275 -43.202 1.00 54.48 ATOM 3022 N ARG B 550 41.226 -31.231 -43.941 1.00 53.35 ATOM 3023 CA ARG B 550 42.573 -31.609 -44.340 1.00 52.05 ATOM 3024 CB ARG B 550 42.806 -31.304 -45.817 1.00 53.48 ATOM 3025 CG ARG B 550 42.304 -32.365 -46.767 1.00 55.60 ATOM 3026 CD ARG B 550 42.308 -31.835 -48.192 1.00 57.56 ATOM 3027 NE ARG B 550 41.312 -32.507 -49.019 1.00 59.06 ATOM 3028 CZ ARG B 550 41.092 -32.218 -50.295 1.00 59.85 ATOM 3029 NH1 ARG B 550 41.802 -31.264 -50.887 1.00 60.38 ATOM 3030 NH2 ARG B 550 40.173 -32.891 -50.977 1.00 60.35 ATOM 3031 C ARG B 550 43.463 -30.709 -43.501 1.00 49.87 ATOM 3032 O ARG B 550 43.690 -29.554 -43.851 1.00 49.67 ATOM 3033 N PRO B 551 43.984 -31.227 -42.382 1.00 48.04 ATOM 3034 CD PRO B 551 43.853 -32.591 -41.844 1.00 47.60 ATOM 3035 CA PRO B 551 44.838 -30.380 -41.547 1.00 46.43 ATOM 3036 CB PRO B 551 45.284 -31.304 -40.416 1.00 46.77 ATOM 3037 CG PRO B 551 44.299 -32.433 -40.423 1.00 47.75 ATOM 3038 C PRO B 551 46.015 -29.816 -42.314 1.00 45.13 ATOM 3039 O PRO B 551 46.649 -30.515 -43.106 1.00 44.47 ATOM 3040 N GLN B 552 46.297 -28.540 -42.093 1.00 43.86 ATOM 3041 CA GLN B 552 47.425 -27.907 -42.747 1.00 43.10 ATOM 3042 CB GLN B 552 46.961 -26.863 -43.768 1.00 44.58 ATOM 3043 CG GLN B 552 45.710 -26.107 -43.377 1.00 47.30 ATOM 3044 CD GLN B 552 45.285 -25.106 -44.440 1.00 49.02 ATOM 3045 OE1 GLN B 552 46.126 -24.454 -45.074 1.00 49.87 ATOM 3046 NE2 GLN B 552 43.975 -24.979 -44.641 1.00 49.84 ATOM 3047 C GLN B 552 48.310 -27.257 -41.697 1.00 41.70 ATOM 3048 O GLN B 552 47.855 -26.883 -40.616 1.00 40.72 ATOM 3049 N GLU B 553 49.585 -27.148 -42.025 1.00 40.58 ATOM 3050 CA GLU B 553 50.564 -26.551 -41.145 1.00 39.99 ATOM 3051 CB GLU B 553 51.934 -27.147 -41.440 1.00 40.61 ATOM 3052 CG GLU B 553 52.773 -27.441 -40.234 1.00 41.26 ATOM 3053 CD GLU B 553 53.984 -28.269 -40.591 1.00 41.90 ATOM 3054 OE1 GLU B 553 54.751 -27.845 -41.479 1.00 43.11 ATOM 3055 OE2 GLU B 553 54.169 -29.347 -39.990 1.00 42.88 ATOM 3056 C GLU B 553 50.576 -25.059 -41.433 1.00 39.35 ATOM 3057 O GLU B 553 50.679 -24.647 -42.586 1.00 39.19 ATOM 3058 N VAL B 554 50.468 -24.253 -40.384 1.00 38.57 ATOM 3059 CA VAL B 554 50.461 -22.800 -40.529 1.00 37.78 ATOM 3060 CB VAL B 554 49.073 -22.214 -40.171 1.00 37.64 ATOM 3061 CG1 VAL B 554 49.052 -20.717 -40.440 1.00 37.32 ATOM 3062 CG2 VAL B 554 47.989 -22.915 -40.973 1.00 37.42 ATOM 3063 C VAL B 554 51.508 -22.173 -39.613 1.00 37.27 ATOM 3064 O VAL B 554 51.532 -22.438 -38.413 1.00 37.44 ATOM 3065 N SER B 555 52.372 -21.344 -40.186 1.00 37.11 ATOM 3066 CA SER B 555 53.419 -20.676 -39.423 1.00 37.51 ATOM 3067 CB SER B 555 54.799 -21.046 -39.974 1.00 38.18 ATOM 3068 OG SER B 555 55.101 -22.406 -39.719 1.00 39.03 ATOM 3069 C SER B 555 53.235 -19.165 -39.491 1.00 37.28 ATOM 3070 O SER B 555 52.981 -18.609 -40.561 1.00 36.76 ATOM 3071 N TYR B 556 53.371 -18.501 -38.350 1.00 37.39 ATOM 3072 CA TYR B 556 53.202 -17.059 -38.311 1.00 38.37 ATOM 3073 CB TYR B 556 51.746 -16.711 -37.997 1.00 37.18 ATOM 3074 CG TYR B 556 51.234 -17.328 -36.722 1.00 35.86 ATOM 3075 CD1 TYR B 556 50.486 -18.502 -36.746 1.00 35.00 ATOM 3076 CE1 TYR B 556 49.990 -19.058 -35.576 1.00 34.90 ATOM 3077 CD2 TYR B 556 51.478 -16.726 -35.492 1.00 35.49 ATOM 3078 CE2 TYR B 556 50.989 -17.273 -34.317 1.00 35.28 ATOM 3079 CZ TYR B 556 50.246 -18.437 -34.365 1.00 35.21 ATOM 3080 OH TYR B 556 49.769 -18.979 -33.199 1.00 35.53 ATOM 3081 C TYR B 556 54.122 -16.373 -37.312 1.00 39.38 ATOM 3082 O TYR B 556 54.628 -16.997 -36.374 1.00 39.27 ATOM 3083 N THR B 557 54.322 -15.077 -37.524 1.00 40.85 ATOM 3084 CA THR B 557 55.188 -14.275 -36.674 1.00 42.47 ATOM 3085 CB THR B 557 56.537 -14.009 -37.368 1.00 42.88 ATOM 3086 OG1 THR B 557 56.321 -13.168 -38.510 1.00 43.88 ATOM 3087 CG2 THR B 557 57.170 -15.310 -37.834 1.00 43.81 ATOM 3088 C THR B 557 54.557 -12.922 -36.365 1.00 43.09 ATOM 3089 O THR B 557 53.407 -12.664 -36.712 1.00 42.98 ATOM 3090 N ASP B 558 55.338 -12.068 -35.711 1.00 44.12 ATOM 3091 CA ASP B 558 54.929 -10.716 -35.351 1.00 45.02 ATOM 3092 CB ASP B 558 55.077 -9.803 -36.567 1.00 46.24 ATOM 3093 CG ASP B 558 56.471 -9.860 -37.164 1.00 47.49 ATOM 3094 OD1 ASP B 558 57.447 -9.721 -36.397 1.00 48.17 ATOM 3095 OD2 ASP B 558 56.593 -10.047 -38.395 1.00 48.59 ATOM 3096 C ASP B 558 53.525 -10.593 -34.780 1.00 45.16 ATOM 3097 O ASP B 558 52.697 -9.846 -35.295 1.00 45.32 ATOM 3098 N THR B 559 53.272 -11.324 -33.702 1.00 45.36 ATOM 3099 CA THR B 559 51.977 -11.306 -33.040 1.00 46.08 ATOM 3100 CB THR B 559 51.813 -12.558 -32.143 1.00 46.48 ATOM 3101 OG1 THR B 559 51.471 -13.685 -32.959 1.00 47.15 ATOM 3102 CG2 THR B 559 50.725 -12.349 -31.105 1.00 47.30 ATOM 3103 C THR B 559 51.835 -10.043 -32.185 1.00 46.11 ATOM 3104 O THR B 559 52.811 -9.553 -31.617 1.00 46.38 ATOM 3105 N LYS B 560 50.615 -9.519 -32.109 1.00 45.78 ATOM 3106 CA LYS B 560 50.329 -8.326 -31.318 1.00 45.47 ATOM 3107 CB LYS B 560 50.874 -7.079 -32.014 1.00 45.75 ATOM 3108 CG LYS B 560 50.528 -7.000 -33.484 1.00 46.99 ATOM 3109 CD LYS B 560 50.890 -5.643 -34.062 1.00 48.02 ATOM 3110 CE LYS B 560 49.707 -4.682 -34.014 1.00 48.65 ATOM 3111 NZ LYS B 560 49.608 -3.843 -35.250 1.00 49.09 ATOM 3112 C LYS B 560 48.822 -8.192 -31.127 1.00 44.84 ATOM 3113 O LYS B 560 48.049 -8.381 -32.068 1.00 44.85 ATOM 3114 N VAL B 561 48.406 -7.871 -29.908 1.00 43.98 ATOM 3115 CA VAL B 561 46.989 -7.723 -29.617 1.00 43.42 ATOM 3116 CB VAL B 561 46.748 -7.495 -28.111 1.00 42.98 ATOM 3117 CG1 VAL B 561 45.272 -7.236 -27.849 1.00 42.26 ATOM 3118 CG2 VAL B 561 47.213 -8.712 -27.331 1.00 42.64 ATOM 3119 C VAL B 561 46.401 -6.560 -30.401 1.00 43.45 ATOM 3120 O VAL B 561 46.999 -5.489 -30.482 1.00 43.15 ATOM 3121 N ILE B 562 45.231 -6.781 -30.991 1.00 43.60 ATOM 3122 CA ILE B 562 44.566 -5.745 -31.769 1.00 44.34 ATOM 3123 CB ILE B 562 44.634 -6.037 -33.292 1.00 43.52 ATOM 3124 CG2 ILE B 562 46.084 -6.018 -33.758 1.00 43.21 ATOM 3125 CG1 ILE B 562 43.976 -7.384 -33.607 1.00 42.75 ATOM 3126 CD1 ILE B 562 43.754 -7.623 -35.089 1.00 41.15 ATOM 3127 C ILE B 562 43.105 -5.614 -31.362 1.00 45.23 ATOM 3128 O ILE B 562 42.358 -4.826 -31.936 1.00 45.02 ATOM 3129 N GLY B 563 42.704 -6.390 -30.363 1.00 46.52 ATOM 3130 CA GLY B 563 41.329 -6.335 -29.911 1.00 48.75 ATOM 3131 C GLY B 563 41.116 -7.093 -28.622 1.00 50.41 ATOM 3132 O GLY B 563 41.967 -7.874 -28.198 1.00 50.21 ATOM 3133 N ASN B 564 39.969 -6.868 -27.995 1.00 52.47 ATOM 3134 CA ASN B 564 39.661 -7.539 -26.744 1.00 54.69 ATOM 3135 CB ASN B 564 40.316 -6.801 -25.574 1.00 55.99 ATOM 3136 CG ASN B 564 41.203 -7.704 -24.737 1.00 57.59 ATOM 3137 OD1 ASN B 564 42.428 -7.538 -24.706 1.00 58.69 ATOM 3138 ND2 ASN B 564 40.590 -8.670 -24.052 1.00 58.08 ATOM 3139 C ASN B 564 38.165 -7.636 -26.500 1.00 55.54 ATOM 3140 O ASN B 564 37.358 -6.997 -27.184 1.00 55.40 ATOM 3141 N GLY B 565 37.819 -8.447 -25.506 1.00 56.19 ATOM 3142 CA GLY B 565 36.436 -8.656 -25.126 1.00 57.22 ATOM 3143 C GLY B 565 36.434 -9.540 -23.895 1.00 57.92 ATOM 3144 O GLY B 565 37.417 -10.241 -23.639 1.00 58.05 ATOM 3145 N SER B 566 35.347 -9.511 -23.130 1.00 58.43 ATOM 3146 CA SER B 566 35.254 -10.327 -21.922 1.00 58.92 ATOM 3147 CB SER B 566 33.918 -10.067 -21.201 1.00 58.98 ATOM 3148 OG SER B 566 32.841 -9.890 -22.110 1.00 58.14 ATOM 3149 C SER B 566 35.399 -11.816 -22.250 1.00 59.15 ATOM 3150 O SER B 566 35.684 -12.630 -21.368 1.00 59.46 ATOM 3151 N PHE B 567 35.220 -12.159 -23.525 1.00 59.41 ATOM 3152 CA PHE B 567 35.316 -13.547 -23.982 1.00 59.09 ATOM 3153 CB PHE B 567 34.391 -13.797 -25.192 1.00 60.54 ATOM 3154 CG PHE B 567 32.995 -13.216 -25.048 1.00 62.08 ATOM 3155 CD1 PHE B 567 32.196 -13.016 -26.175 1.00 62.59 ATOM 3156 CD2 PHE B 567 32.485 -12.854 -23.798 1.00 62.82 ATOM 3157 CE1 PHE B 567 30.912 -12.464 -26.064 1.00 62.94 ATOM 3158 CE2 PHE B 567 31.204 -12.300 -23.676 1.00 63.22 ATOM 3159 CZ PHE B 567 30.417 -12.105 -24.813 1.00 63.29 ATOM 3160 C PHE B 567 36.746 -13.927 -24.363 1.00 57.75 ATOM 3161 O PHE B 567 37.206 -15.028 -24.050 1.00 58.14 ATOM 3162 N GLY B 568 37.447 -13.021 -25.041 1.00 55.98 ATOM 3163 CA GLY B 568 38.811 -13.322 -25.439 1.00 53.60 ATOM 3164 C GLY B 568 39.670 -12.158 -25.900 1.00 51.65 ATOM 3165 O GLY B 568 39.446 -11.006 -25.523 1.00 51.32 ATOM 3166 N VAL B 569 40.670 -12.482 -26.719 1.00 49.52 ATOM 3167 CA VAL B 569 41.602 -11.501 -27.264 1.00 47.32 ATOM 3168 CB VAL B 569 42.972 -11.571 -26.551 1.00 47.23 ATOM 3169 CG1 VAL B 569 43.913 -10.520 -27.116 1.00 46.96 ATOM 3170 CG2 VAL B 569 42.790 -11.367 -25.064 1.00 47.77 ATOM 3171 C VAL B 569 41.835 -11.768 -28.747 1.00 45.70 ATOM 3172 O VAL B 569 41.891 -12.920 -29.177 1.00 45.60 ATOM 3173 N VAL B 570 41.966 -10.703 -29.527 1.00 43.29 ATOM 3174 CA VAL B 570 42.217 -10.842 -30.953 1.00 41.38 ATOM 3175 CB VAL B 570 41.202 -10.040 -31.788 1.00 40.40 ATOM 3176 CG1 VAL B 570 41.463 -10.254 -33.271 1.00 39.00 ATOM 3177 CG2 VAL B 570 39.791 -10.468 -31.431 1.00 39.25 ATOM 3178 C VAL B 570 43.622 -10.336 -31.258 1.00 41.21 ATOM 3179 O VAL B 570 43.967 -9.202 -30.932 1.00 40.74 ATOM 3180 N TYR B 571 44.434 -11.189 -31.872 1.00 40.63 ATOM 3181 CA TYR B 571 45.796 -10.817 -32.220 1.00 40.43 ATOM 3182 CB TYR B 571 46.798 -11.900 -31.821 1.00 40.90 ATOM 3183 CG TYR B 571 46.742 -12.341 -30.392 1.00 41.93 ATOM 3184 CD1 TYR B 571 47.623 -11.814 -29.450 1.00 42.27 ATOM 3185 CE1 TYR B 571 47.610 -12.250 -28.134 1.00 43.23 ATOM 3186 CD2 TYR B 571 45.838 -13.317 -29.984 1.00 42.27 ATOM 3187 CE2 TYR B 571 45.812 -13.764 -28.669 1.00 43.52 ATOM 3188 CZ TYR B 571 46.703 -13.226 -27.749 1.00 43.82 ATOM 3189 OH TYR B 571 46.689 -13.671 -26.447 1.00 45.03 ATOM 3190 C TYR B 571 45.940 -10.649 -33.707 1.00 39.97 ATOM 3191 O TYR B 571 45.143 -11.169 -34.487 1.00 39.85 ATOM 3192 N GLN B 572 46.971 -9.915 -34.095 1.00 39.61 ATOM 3193 CA GLN B 572 47.283 -9.758 -35.496 1.00 39.77 ATOM 3194 CB GLN B 572 47.614 -8.316 -35.850 1.00 40.10 ATOM 3195 CG GLN B 572 47.964 -8.164 -37.316 1.00 41.01 ATOM 3196 CD GLN B 572 48.675 -6.871 -37.615 1.00 41.84 ATOM 3197 OE1 GLN B 572 49.788 -6.638 -37.141 1.00 42.38 ATOM 3198 NE2 GLN B 572 48.040 -6.017 -38.408 1.00 42.55 ATOM 3199 C GLN B 572 48.537 -10.608 -35.633 1.00 39.67 ATOM 3200 O GLN B 572 49.332 -10.698 -34.699 1.00 39.62 ATOM 3201 N ALA B 573 48.706 -11.249 -36.778 1.00 39.80 ATOM 3202 CA ALA B 573 49.881 -12.078 -36.993 1.00 40.10 ATOM 3203 CB ALA B 573 49.629 -13.502 -36.490 1.00 40.02 ATOM 3204 C ALA B 573 50.203 -12.088 -38.475 1.00 40.49 ATOM 3205 O ALA B 573 49.328 -11.864 -39.312 1.00 39.85 ATOM 3206 N LYS B 574 51.466 -12.337 -38.797 1.00 40.99 ATOM 3207 CA LYS B 574 51.887 -12.371 -40.181 1.00 41.78 ATOM 3208 CB LYS B 574 53.104 -11.471 -40.382 1.00 42.77 ATOM 3209 CG LYS B 574 53.411 -11.185 -41.839 1.00 44.19 ATOM 3210 CD LYS B 574 54.880 -10.884 -42.036 1.00 46.14 ATOM 3211 CE LYS B 574 55.295 -9.651 -41.250 1.00 47.57 ATOM 3212 NZ LYS B 574 56.737 -9.318 -41.461 1.00 49.05 ATOM 3213 C LYS B 574 52.223 -13.796 -40.596 1.00 42.07 ATOM 3214 O LYS B 574 53.006 -14.478 -39.932 1.00 41.81 ATOM 3215 N LEU B 575 51.614 -14.242 -41.690 1.00 42.07 ATOM 3216 CA LEU B 575 51.864 -15.580 -42.197 1.00 42.84 ATOM 3217 CB LEU B 575 50.845 -15.935 -43.276 1.00 41.54 ATOM 3218 CG LEU B 575 49.421 -16.105 -42.749 1.00 40.73 ATOM 3219 CD1 LEU B 575 48.545 -16.670 -43.846 1.00 40.16 ATOM 3220 CD2 LEU B 575 49.423 -17.012 -41.532 1.00 39.64 ATOM 3221 C LEU B 575 53.275 -15.600 -42.763 1.00 44.01 ATOM 3222 O LEU B 575 53.620 -14.799 -43.629 1.00 44.03 ATOM 3223 N CYS B 576 54.083 -16.526 -42.258 1.00 45.47 ATOM 3224 CA CYS B 576 55.479 -16.661 -42.650 1.00 47.39 ATOM 3225 CB CYS B 576 56.070 -17.908 -42.004 1.00 46.95 ATOM 3226 SG CYS B 576 56.513 -17.639 -40.301 1.00 47.61 ATOM 3227 C CYS B 576 55.813 -16.677 -44.131 1.00 48.87 ATOM 3228 O CYS B 576 56.788 -16.055 -44.556 1.00 49.64 ATOM 3229 N ASP B 577 55.025 -17.378 -44.931 1.00 50.26 ATOM 3230 CA ASP B 577 55.352 -17.442 -46.344 1.00 51.58 ATOM 3231 CB ASP B 577 55.056 -18.846 -46.872 1.00 52.55 ATOM 3232 CG ASP B 577 56.135 -19.844 -46.470 1.00 53.65 ATOM 3233 OD1 ASP B 577 57.329 -19.558 -46.722 1.00 54.40 ATOM 3234 OD2 ASP B 577 55.799 -20.904 -45.895 1.00 54.05 ATOM 3235 C ASP B 577 54.684 -16.376 -47.196 1.00 51.83 ATOM 3236 O ASP B 577 55.365 -15.603 -47.871 1.00 52.35 ATOM 3237 N SER B 578 53.359 -16.319 -47.164 1.00 51.58 ATOM 3238 CA SER B 578 52.654 -15.324 -47.954 1.00 50.90 ATOM 3239 CB SER B 578 51.143 -15.555 -47.875 1.00 51.37 ATOM 3240 OG SER B 578 50.668 -15.364 -46.556 1.00 51.78 ATOM 3241 C SER B 578 52.993 -13.929 -47.451 1.00 50.25 ATOM 3242 O SER B 578 52.976 -12.966 -48.216 1.00 50.65 ATOM 3243 N GLY B 579 53.321 -13.828 -46.165 1.00 49.24 ATOM 3244 CA GLY B 579 53.631 -12.534 -45.582 1.00 47.45 ATOM 3245 C GLY B 579 52.321 -11.842 -45.258 1.00 46.13 ATOM 3246 O GLY B 579 52.288 -10.735 -44.732 1.00 46.07 ATOM 3247 N GLU B 580 51.232 -12.527 -45.584 1.00 44.82 ATOM 3248 CA GLU B 580 49.878 -12.038 -45.359 1.00 43.67 ATOM 3249 CB GLU B 580 48.876 -13.045 -45.907 1.00 45.15 ATOM 3250 CG GLU B 580 47.955 -12.516 -46.959 1.00 47.44 ATOM 3251 CD GLU B 580 47.090 -13.616 -47.531 1.00 49.23 ATOM 3252 OE1 GLU B 580 45.948 -13.315 -47.943 1.00 50.82 ATOM 3253 OE2 GLU B 580 47.554 -14.780 -47.563 1.00 49.63 ATOM 3254 C GLU B 580 49.579 -11.835 -43.885 1.00 41.76 ATOM 3255 O GLU B 580 50.034 -12.600 -43.036 1.00 41.47 ATOM 3256 N LEU B 581 48.794 -10.806 -43.591 1.00 39.82 ATOM 3257 CA LEU B 581 48.408 -10.523 -42.219 1.00 37.86 ATOM 3258 CB LEU B 581 48.249 -9.015 -42.000 1.00 38.14 ATOM 3259 CG LEU B 581 49.526 -8.185 -41.833 1.00 38.24 ATOM 3260 CD1 LEU B 581 49.179 -6.711 -41.845 1.00 38.09 ATOM 3261 CD2 LEU B 581 50.212 -8.551 -40.531 1.00 38.58 ATOM 3262 C LEU B 581 47.074 -11.213 -41.985 1.00 36.49 ATOM 3263 O LEU B 581 46.258 -11.337 -42.900 1.00 36.34 ATOM 3264 N VAL B 582 46.864 -11.682 -40.765 1.00 34.75 ATOM 3265 CA VAL B 582 45.621 -12.341 -40.406 1.00 33.31 ATOM 3266 CB VAL B 582 45.731 -13.896 -40.456 1.00 33.32 ATOM 3267 CG1 VAL B 582 45.950 -14.364 -41.891 1.00 32.45 ATOM 3268 CG2 VAL B 582 46.861 -14.375 -39.549 1.00 32.79 ATOM 3269 C VAL B 582 45.323 -11.939 -38.984 1.00 32.44 ATOM 3270 O VAL B 582 46.166 -11.351 -38.306 1.00 32.27 ATOM 3271 N ALA B 583 44.116 -12.245 -38.537 1.00 32.13 ATOM 3272 CA ALA B 583 43.722 -11.945 -37.171 1.00 31.52 ATOM 3273 CB ALA B 583 42.467 -11.077 -37.157 1.00 30.85 ATOM 3274 C ALA B 583 43.441 -13.295 -36.536 1.00 31.28 ATOM 3275 O ALA B 583 42.928 -14.193 -37.196 1.00 31.50 ATOM 3276 N ILE B 584 43.798 -13.453 -35.271 1.00 30.83 ATOM 3277 CA ILE B 584 43.542 -14.704 -34.581 1.00 31.25 ATOM 3278 CB ILE B 584 44.860 -15.405 -34.168 1.00 31.65 ATOM 3279 CG2 ILE B 584 44.553 -16.711 -33.449 1.00 31.25 ATOM 3280 CG1 ILE B 584 45.724 -15.665 -35.404 1.00 31.94 ATOM 3281 CD1 ILE B 584 47.115 -16.162 -35.076 1.00 32.20 ATOM 3282 C ILE B 584 42.719 -14.418 -33.333 1.00 31.45 ATOM 3283 O ILE B 584 43.219 -13.818 -32.381 1.00 31.29 ATOM 3284 N LYS B 585 41.454 -14.833 -33.347 1.00 31.58 ATOM 3285 CA LYS B 585 40.572 -14.625 -32.203 1.00 32.02 ATOM 3286 CB LYS B 585 39.116 -14.476 -32.665 1.00 30.77 ATOM 3287 CG LYS B 585 38.131 -14.199 -31.536 1.00 29.28 ATOM 3288 CD LYS B 585 36.769 -13.742 -32.060 1.00 28.90 ATOM 3289 CE LYS B 585 35.796 -13.498 -30.914 1.00 27.66 ATOM 3290 NZ LYS B 585 34.506 -12.935 -31.387 1.00 28.53 ATOM 3291 C LYS B 585 40.704 -15.816 -31.261 1.00 33.38 ATOM 3292 O LYS B 585 40.312 -16.932 -31.597 1.00 33.08 ATOM 3293 N LYS B 586 41.266 -15.570 -30.082 1.00 34.96 ATOM 3294 CA LYS B 586 41.473 -16.617 -29.089 1.00 36.96 ATOM 3295 CB LYS B 586 42.850 -16.461 -28.446 1.00 37.42 ATOM 3296 CG LYS B 586 43.241 -17.605 -27.541 1.00 38.04 ATOM 3297 CD LYS B 586 44.698 -17.499 -27.143 1.00 38.75 ATOM 3298 CE LYS B 586 45.209 -18.817 -26.596 1.00 39.59 ATOM 3299 NZ LYS B 586 46.699 -18.881 -26.632 1.00 41.32 ATOM 3300 C LYS B 586 40.396 -16.571 -28.017 1.00 38.37 ATOM 3301 O LYS B 586 40.253 -15.578 -27.304 1.00 37.52 ATOM 3302 N VAL B 587 39.652 -17.666 -27.902 1.00 40.15 ATOM 3303 CA VAL B 587 38.564 -17.771 -26.942 1.00 42.57 ATOM 3304 CB VAL B 587 37.205 -17.747 -27.683 1.00 42.46 ATOM 3305 CG1 VAL B 587 36.122 -18.376 -26.827 1.00 43.21 ATOM 3306 CG2 VAL B 587 36.841 -16.315 -28.046 1.00 41.98 ATOM 3307 C VAL B 587 38.667 -19.054 -26.114 1.00 44.52 ATOM 3308 O VAL B 587 39.025 -20.110 -26.636 1.00 44.09 ATOM 3309 N LEU B 588 38.356 -18.958 -24.824 1.00 46.86 ATOM 3310 CA LEU B 588 38.404 -20.127 -23.954 1.00 49.52 ATOM 3311 CB LEU B 588 38.173 -19.728 -22.500 1.00 49.52 ATOM 3312 CG LEU B 588 38.521 -20.811 -21.482 1.00 49.74 ATOM 3313 CD1 LEU B 588 39.978 -20.680 -21.069 1.00 49.53 ATOM 3314 CD2 LEU B 588 37.603 -20.687 -20.280 1.00 50.26 ATOM 3315 C LEU B 588 37.324 -21.104 -24.400 1.00 51.67 ATOM 3316 O LEU B 588 36.162 -20.726 -24.567 1.00 51.61 ATOM 3317 N GLN B 589 37.713 -22.359 -24.594 1.00 54.29 ATOM 3318 CA GLN B 589 36.774 -23.373 -25.047 1.00 57.23 ATOM 3319 CB GLN B 589 37.429 -24.263 -26.107 1.00 58.05 ATOM 3320 CG GLN B 589 36.464 -25.241 -26.771 1.00 59.63 ATOM 3321 CD GLN B 589 35.107 -24.620 -27.055 1.00 60.45 ATOM 3322 OE1 GLN B 589 34.064 -25.183 -26.713 1.00 60.97 ATOM 3323 NE2 GLN B 589 35.115 -23.450 -27.683 1.00 61.25 ATOM 3324 C GLN B 589 36.234 -24.248 -23.930 1.00 58.83 ATOM 3325 O GLN B 589 36.994 -24.795 -23.132 1.00 59.12 ATOM 3326 N ASP B 590 34.911 -24.376 -23.892 1.00 60.67 ATOM 3327 CA ASP B 590 34.232 -25.198 -22.899 1.00 62.70 ATOM 3328 CB ASP B 590 32.783 -24.718 -22.724 1.00 63.77 ATOM 3329 CG ASP B 590 32.154 -25.198 -21.418 1.00 65.38 ATOM 3330 OD1 ASP B 590 31.065 -24.692 -21.063 1.00 65.85 ATOM 3331 OD2 ASP B 590 32.744 -26.077 -20.748 1.00 66.42 ATOM 3332 C ASP B 590 34.242 -26.645 -23.394 1.00 63.41 ATOM 3333 O ASP B 590 33.661 -26.954 -24.435 1.00 63.59 ATOM 3334 N LYS B 591 34.908 -27.527 -22.657 1.00 64.23 ATOM 3335 CA LYS B 591 34.970 -28.934 -23.045 1.00 65.03 ATOM 3336 CB LYS B 591 35.913 -29.705 -22.109 1.00 65.50 ATOM 3337 CG LYS B 591 37.402 -29.531 -22.416 1.00 65.98 ATOM 3338 CD LYS B 591 38.016 -28.366 -21.637 1.00 66.54 ATOM 3339 CE LYS B 591 37.967 -28.594 -20.130 1.00 66.75 ATOM 3340 NZ LYS B 591 36.621 -28.294 -19.560 1.00 66.73 ATOM 3341 C LYS B 591 33.564 -29.539 -22.987 1.00 65.00 ATOM 3342 O LYS B 591 33.330 -30.647 -23.470 1.00 65.21 ATOM 3343 N ARG B 592 32.633 -28.788 -22.404 1.00 64.84 ATOM 3344 CA ARG B 592 31.242 -29.213 -22.256 1.00 64.60 ATOM 3345 CB ARG B 592 30.518 -28.250 -21.308 1.00 66.23 ATOM 3346 CG ARG B 592 29.106 -28.663 -20.934 1.00 68.27 ATOM 3347 CD ARG B 592 29.026 -30.114 -20.485 1.00 70.65 ATOM 3348 NE ARG B 592 27.681 -30.467 -20.033 1.00 72.39 ATOM 3349 CZ ARG B 592 27.357 -31.633 -19.478 1.00 73.07 ATOM 3350 NH1 ARG B 592 28.279 -32.574 -19.300 1.00 73.31 ATOM 3351 NH2 ARG B 592 26.107 -31.860 -19.092 1.00 73.68 ATOM 3352 C ARG B 592 30.476 -29.319 -23.579 1.00 63.54 ATOM 3353 O ARG B 592 29.984 -30.392 -23.925 1.00 63.79 ATOM 3354 N PHE B 593 30.355 -28.210 -24.306 1.00 61.96 ATOM 3355 CA PHE B 593 29.651 -28.222 -25.591 1.00 59.89 ATOM 3356 CB PHE B 593 28.362 -27.386 -25.542 1.00 61.21 ATOM 3357 CG PHE B 593 27.898 -27.033 -24.152 1.00 62.51 ATOM 3358 CD1 PHE B 593 26.974 -27.839 -23.490 1.00 63.09 ATOM 3359 CD2 PHE B 593 28.352 -25.873 -23.521 1.00 63.09 ATOM 3360 CE1 PHE B 593 26.501 -27.498 -22.217 1.00 63.48 ATOM 3361 CE2 PHE B 593 27.888 -25.521 -22.247 1.00 63.56 ATOM 3362 CZ PHE B 593 26.959 -26.336 -21.594 1.00 63.55 ATOM 3363 C PHE B 593 30.531 -27.681 -26.712 1.00 57.71 ATOM 3364 O PHE B 593 31.688 -27.321 -26.496 1.00 57.54 ATOM 3365 N LYS B 594 29.968 -27.624 -27.912 1.00 54.88 ATOM 3366 CA LYS B 594 30.687 -27.115 -29.071 1.00 51.86 ATOM 3367 CB LYS B 594 30.095 -27.697 -30.355 1.00 53.21 ATOM 3368 CG LYS B 594 30.034 -29.213 -30.367 1.00 54.88 ATOM 3369 CD LYS B 594 29.960 -29.756 -31.781 1.00 56.39 ATOM 3370 CE LYS B 594 29.419 -31.177 -31.790 1.00 57.46 ATOM 3371 NZ LYS B 594 28.826 -31.523 -33.114 1.00 58.45 ATOM 3372 C LYS B 594 30.586 -25.600 -29.109 1.00 48.79 ATOM 3373 O LYS B 594 29.642 -25.020 -28.571 1.00 48.03 ATOM 3374 N ASN B 595 31.562 -24.961 -29.748 1.00 45.47 ATOM 3375 CA ASN B 595 31.563 -23.505 -29.853 1.00 42.06 ATOM 3376 CB ASN B 595 32.961 -23.014 -30.207 1.00 41.25 ATOM 3377 CG ASN B 595 33.089 -21.518 -30.075 1.00 40.68 ATOM 3378 OD1 ASN B 595 33.328 -21.001 -28.985 1.00 40.48 ATOM 3379 ND2 ASN B 595 32.922 -20.813 -31.182 1.00 39.13 ATOM 3380 C ASN B 595 30.568 -23.049 -30.921 1.00 39.88 ATOM 3381 O ASN B 595 30.750 -23.317 -32.105 1.00 39.20 ATOM 3382 N ARG B 596 29.512 -22.356 -30.490 1.00 37.44 ATOM 3383 CA ARG B 596 28.478 -21.885 -31.408 1.00 35.72 ATOM 3384 CB ARG B 596 27.342 -21.225 -30.627 1.00 35.93 ATOM 3385 CG ARG B 596 26.140 -20.867 -31.479 1.00 37.17 ATOM 3386 CD ARG B 596 25.037 -20.234 -30.641 1.00 39.04 ATOM 3387 NE ARG B 596 24.404 -21.215 -29.763 1.00 41.22 ATOM 3388 CZ ARG B 596 23.583 -20.889 -28.764 1.00 42.76 ATOM 3389 NH1 ARG B 596 23.295 -19.608 -28.513 1.00 43.05 ATOM 3390 NH2 ARG B 596 23.041 -21.843 -28.007 1.00 42.99 ATOM 3391 C ARG B 596 29.021 -20.904 -32.442 1.00 34.32 ATOM 3392 O ARG B 596 28.607 -20.920 -33.603 1.00 33.38 ATOM 3393 N GLU B 597 29.946 -20.049 -32.017 1.00 32.78 ATOM 3394 CA GLU B 597 30.543 -19.070 -32.914 1.00 31.60 ATOM 3395 CB GLU B 597 31.537 -18.192 -32.139 1.00 31.36 ATOM 3396 CG GLU B 597 32.173 -17.072 -32.965 1.00 32.30 ATOM 3397 CD GLU B 597 32.970 -16.084 -32.115 1.00 33.01 ATOM 3398 OE1 GLU B 597 33.478 -15.089 -32.677 1.00 32.57 ATOM 3399 OE2 GLU B 597 33.092 -16.303 -30.889 1.00 32.96 ATOM 3400 C GLU B 597 31.254 -19.795 -34.064 1.00 31.16 ATOM 3401 O GLU B 597 31.063 -19.456 -35.234 1.00 30.05 ATOM 3402 N LEU B 598 32.069 -20.793 -33.728 1.00 31.00 ATOM 3403 CA LEU B 598 32.801 -21.559 -34.727 1.00 31.67 ATOM 3404 CB LEU B 598 33.701 -22.593 -34.043 1.00 31.37 ATOM 3405 CG LEU B 598 34.385 -23.615 -34.960 1.00 30.61 ATOM 3406 CD1 LEU B 598 35.276 -22.909 -35.955 1.00 29.99 ATOM 3407 CD2 LEU B 598 35.210 -24.589 -34.129 1.00 30.20 ATOM 3408 C LEU B 598 31.832 -22.274 -35.670 1.00 32.40 ATOM 3409 O LEU B 598 31.953 -22.182 -36.894 1.00 32.52 ATOM 3410 N GLN B 599 30.866 -22.983 -35.100 1.00 32.89 ATOM 3411 CA GLN B 599 29.897 -23.712 -35.905 1.00 34.02 ATOM 3412 CB GLN B 599 28.876 -24.390 -34.990 1.00 36.06 ATOM 3413 CG GLN B 599 29.485 -25.402 -33.998 1.00 40.12 ATOM 3414 CD GLN B 599 30.822 -25.999 -34.464 1.00 42.71 ATOM 3415 OE1 GLN B 599 30.946 -26.510 -35.589 1.00 44.16 ATOM 3416 NE2 GLN B 599 31.829 -25.937 -33.590 1.00 43.58 ATOM 3417 C GLN B 599 29.188 -22.802 -36.914 1.00 33.80 ATOM 3418 O GLN B 599 28.891 -23.217 -38.035 1.00 32.91 ATOM 3419 N ILE B 600 28.924 -21.559 -36.522 1.00 33.42 ATOM 3420 CA ILE B 600 28.257 -20.623 -37.415 1.00 32.86 ATOM 3421 CB ILE B 600 27.636 -19.449 -36.608 1.00 32.68 ATOM 3422 CG2 ILE B 600 27.387 -18.245 -37.511 1.00 31.97 ATOM 3423 CG1 ILE B 600 26.321 -19.906 -35.965 1.00 32.22 ATOM 3424 CD1 ILE B 600 25.796 -18.982 -34.877 1.00 31.74 ATOM 3425 C ILE B 600 29.252 -20.095 -38.451 1.00 33.29 ATOM 3426 O ILE B 600 28.980 -20.120 -39.655 1.00 33.29 ATOM 3427 N MET B 601 30.405 -19.626 -37.985 1.00 33.64 ATOM 3428 CA MET B 601 31.432 -19.091 -38.879 1.00 34.97 ATOM 3429 CB MET B 601 32.704 -18.752 -38.095 1.00 36.66 ATOM 3430 CG MET B 601 32.590 -17.587 -37.135 1.00 38.72 ATOM 3431 SD MET B 601 33.180 -16.045 -37.824 1.00 43.53 ATOM 3432 CE MET B 601 34.750 -16.403 -38.314 1.00 41.22 ATOM 3433 C MET B 601 31.806 -20.081 -39.979 1.00 35.28 ATOM 3434 O MET B 601 32.124 -19.685 -41.103 1.00 34.49 ATOM 3435 N ARG B 602 31.782 -21.366 -39.640 1.00 35.41 ATOM 3436 CA ARG B 602 32.153 -22.422 -40.574 1.00 36.34 ATOM 3437 CB ARG B 602 32.241 -23.752 -39.840 1.00 36.64 ATOM 3438 CG ARG B 602 33.411 -23.828 -38.895 1.00 38.25 ATOM 3439 CD ARG B 602 33.506 -25.217 -38.308 1.00 39.47 ATOM 3440 NE ARG B 602 34.108 -26.125 -39.266 1.00 40.29 ATOM 3441 CZ ARG B 602 34.325 -27.409 -39.013 1.00 40.70 ATOM 3442 NH1 ARG B 602 33.987 -27.929 -37.834 1.00 40.88 ATOM 3443 NH2 ARG B 602 34.896 -28.176 -39.934 1.00 41.37 ATOM 3444 C ARG B 602 31.243 -22.584 -41.777 1.00 36.12 ATOM 3445 O ARG B 602 31.691 -22.999 -42.843 1.00 37.03 ATOM 3446 N LYS B 603 29.967 -22.265 -41.624 1.00 36.09 ATOM 3447 CA LYS B 603 29.058 -22.417 -42.741 1.00 36.26 ATOM 3448 CB LYS B 603 27.733 -22.991 -42.244 1.00 38.30 ATOM 3449 CG LYS B 603 26.974 -22.100 -41.288 1.00 41.24 ATOM 3450 CD LYS B 603 25.731 -22.803 -40.757 1.00 43.37 ATOM 3451 CE LYS B 603 26.092 -23.823 -39.681 1.00 45.06 ATOM 3452 NZ LYS B 603 25.093 -24.934 -39.578 1.00 46.49 ATOM 3453 C LYS B 603 28.816 -21.123 -43.522 1.00 35.28 ATOM 3454 O LYS B 603 28.031 -21.102 -44.469 1.00 35.94 ATOM 3455 N LEU B 604 29.505 -20.048 -43.148 1.00 33.16 ATOM 3456 CA LEU B 604 29.318 -18.774 -43.831 1.00 31.45 ATOM 3457 CB LEU B 604 29.355 -17.622 -42.823 1.00 31.74 ATOM 3458 CG LEU B 604 28.357 -17.694 -41.659 1.00 31.08 ATOM 3459 CD1 LEU B 604 28.456 -16.429 -40.821 1.00 30.92 ATOM 3460 CD2 LEU B 604 26.943 -17.870 -42.187 1.00 30.51 ATOM 3461 C LEU B 604 30.336 -18.506 -44.931 1.00 30.70 ATOM 3462 O LEU B 604 31.522 -18.785 -44.781 1.00 30.82 ATOM 3463 N ASP B 605 29.860 -17.949 -46.035 1.00 30.06 ATOM 3464 CA ASP B 605 30.720 -17.615 -47.167 1.00 30.01 ATOM 3465 CB ASP B 605 30.868 -18.826 -48.089 1.00 31.60 ATOM 3466 CG ASP B 605 31.861 -18.587 -49.206 1.00 33.46 ATOM 3467 OD1 ASP B 605 32.666 -17.635 -49.104 1.00 34.26 ATOM 3468 OD2 ASP B 605 31.833 -19.349 -50.197 1.00 35.05 ATOM 3469 C ASP B 605 30.087 -16.446 -47.924 1.00 29.08 ATOM 3470 O ASP B 605 29.213 -16.645 -48.770 1.00 28.82 ATOM 3471 N HIS B 606 30.535 -15.227 -47.604 1.00 27.12 ATOM 3472 CA HIS B 606 29.994 -14.023 -48.225 1.00 24.80 ATOM 3473 CB HIS B 606 28.779 -13.540 -47.423 1.00 23.96 ATOM 3474 CG HIS B 606 28.008 -12.442 -48.091 1.00 22.74 ATOM 3475 CD2 HIS B 606 26.878 -12.478 -48.835 1.00 22.63 ATOM 3476 ND1 HIS B 606 28.367 -11.117 -47.991 1.00 22.27 ATOM 3477 CE1 HIS B 606 27.483 -10.378 -48.649 1.00 23.21 ATOM 3478 NE2 HIS B 606 26.572 -11.176 -49.168 1.00 22.32 ATOM 3479 C HIS B 606 31.076 -12.953 -48.248 1.00 24.29 ATOM 3480 O HIS B 606 31.893 -12.864 -47.322 1.00 23.77 ATOM 3481 N CYS B 607 31.076 -12.129 -49.290 1.00 23.45 ATOM 3482 CA CYS B 607 32.092 -11.092 -49.449 1.00 23.34 ATOM 3483 CB CYS B 607 32.029 -10.509 -50.867 1.00 24.25 ATOM 3484 SG CYS B 607 30.431 -9.775 -51.321 1.00 28.61 ATOM 3485 C CYS B 607 32.031 -9.964 -48.420 1.00 22.52 ATOM 3486 O CYS B 607 32.975 -9.183 -48.298 1.00 22.02 ATOM 3487 N ASN B 608 30.922 -9.876 -47.689 1.00 21.64 ATOM 3488 CA ASN B 608 30.763 -8.843 -46.669 1.00 20.84 ATOM 3489 CB ASN B 608 29.502 -8.020 -46.943 1.00 20.58 ATOM 3490 CG ASN B 608 29.624 -7.204 -48.215 1.00 21.27 ATOM 3491 OD1 ASN B 608 30.606 -6.479 -48.404 1.00 21.80 ATOM 3492 ND2 ASN B 608 28.650 -7.330 -49.100 1.00 19.13 ATOM 3493 C ASN B 608 30.749 -9.422 -45.254 1.00 20.97 ATOM 3494 O ASN B 608 30.200 -8.829 -44.323 1.00 20.99 ATOM 3495 N ILE B 609 31.362 -10.592 -45.103 1.00 20.47 ATOM 3496 CA ILE B 609 31.475 -11.249 -43.807 1.00 20.80 ATOM 3497 CB ILE B 609 30.511 -12.451 -43.679 1.00 21.00 ATOM 3498 CG2 ILE B 609 30.802 -13.216 -42.383 1.00 20.81 ATOM 3499 CG1 ILE B 609 29.062 -11.954 -43.715 1.00 20.52 ATOM 3500 CD1 ILE B 609 28.025 -13.028 -43.499 1.00 21.55 ATOM 3501 C ILE B 609 32.916 -11.735 -43.737 1.00 21.86 ATOM 3502 O ILE B 609 33.415 -12.370 -44.675 1.00 21.15 ATOM 3503 N VAL B 610 33.596 -11.421 -42.642 1.00 22.12 ATOM 3504 CA VAL B 610 34.988 -11.807 -42.498 1.00 23.75 ATOM 3505 CB VAL B 610 35.572 -11.284 -41.145 1.00 23.49 ATOM 3506 CG1 VAL B 610 35.050 -12.113 -39.976 1.00 23.84 ATOM 3507 CG2 VAL B 610 37.098 -11.292 -41.203 1.00 24.19 ATOM 3508 C VAL B 610 35.138 -13.324 -42.627 1.00 24.56 ATOM 3509 O VAL B 610 34.362 -14.091 -42.060 1.00 24.14 ATOM 3510 N ARG B 611 36.139 -13.747 -43.390 1.00 25.97 ATOM 3511 CA ARG B 611 36.367 -15.167 -43.622 1.00 27.52 ATOM 3512 CB ARG B 611 37.050 -15.375 -44.985 1.00 29.49 ATOM 3513 CG ARG B 611 37.413 -16.838 -45.299 1.00 33.29 ATOM 3514 CD ARG B 611 38.168 -16.976 -46.621 1.00 35.37 ATOM 3515 NE ARG B 611 39.374 -16.151 -46.632 1.00 39.30 ATOM 3516 CZ ARG B 611 40.299 -16.167 -47.591 1.00 41.74 ATOM 3517 NH1 ARG B 611 40.167 -16.974 -48.640 1.00 43.02 ATOM 3518 NH2 ARG B 611 41.362 -15.371 -47.505 1.00 42.29 ATOM 3519 C ARG B 611 37.175 -15.891 -42.554 1.00 26.99 ATOM 3520 O ARG B 611 38.171 -15.375 -42.049 1.00 26.61 ATOM 3521 N LEU B 612 36.723 -17.092 -42.208 1.00 27.33 ATOM 3522 CA LEU B 612 37.437 -17.926 -41.248 1.00 27.98 ATOM 3523 CB LEU B 612 36.460 -18.805 -40.454 1.00 27.31 ATOM 3524 CG LEU B 612 37.089 -19.906 -39.587 1.00 27.32 ATOM 3525 CD1 LEU B 612 37.771 -19.285 -38.383 1.00 26.97 ATOM 3526 CD2 LEU B 612 36.024 -20.895 -39.141 1.00 27.25 ATOM 3527 C LEU B 612 38.363 -18.808 -42.100 1.00 29.18 ATOM 3528 O LEU B 612 37.896 -19.691 -42.822 1.00 29.02 ATOM 3529 N ARG B 613 39.663 -18.547 -42.042 1.00 30.21 ATOM 3530 CA ARG B 613 40.632 -19.329 -42.814 1.00 32.08 ATOM 3531 CB ARG B 613 41.991 -18.652 -42.769 1.00 32.86 ATOM 3532 CG ARG B 613 42.026 -17.323 -43.483 1.00 35.08 ATOM 3533 CD ARG B 613 43.458 -16.923 -43.759 1.00 37.50 ATOM 3534 NE ARG B 613 43.539 -15.748 -44.616 1.00 40.17 ATOM 3535 CZ ARG B 613 44.665 -15.300 -45.161 1.00 41.01 ATOM 3536 NH1 ARG B 613 44.646 -14.221 -45.928 1.00 41.80 ATOM 3537 NH2 ARG B 613 45.811 -15.933 -44.943 1.00 42.61 ATOM 3538 C ARG B 613 40.730 -20.745 -42.251 1.00 32.68 ATOM 3539 O ARG B 613 40.582 -21.730 -42.975 1.00 32.53 ATOM 3540 N TYR B 614 40.999 -20.840 -40.953 1.00 33.42 ATOM 3541 CA TYR B 614 41.063 -22.128 -40.273 1.00 34.29 ATOM 3542 CB TYR B 614 42.348 -22.906 -40.599 1.00 35.30 ATOM 3543 CG TYR B 614 43.453 -22.099 -41.219 1.00 36.47 ATOM 3544 CD1 TYR B 614 43.813 -22.289 -42.551 1.00 36.95 ATOM 3545 CE1 TYR B 614 44.822 -21.539 -43.139 1.00 38.19 ATOM 3546 CD2 TYR B 614 44.133 -21.139 -40.482 1.00 37.70 ATOM 3547 CE2 TYR B 614 45.146 -20.378 -41.060 1.00 38.62 ATOM 3548 CZ TYR B 614 45.483 -20.582 -42.386 1.00 38.79 ATOM 3549 OH TYR B 614 46.473 -19.818 -42.958 1.00 41.01 ATOM 3550 C TYR B 614 40.992 -21.877 -38.787 1.00 34.02 ATOM 3551 O TYR B 614 40.945 -20.734 -38.346 1.00 34.10 ATOM 3552 N PHE B 615 40.970 -22.952 -38.017 1.00 33.70 ATOM 3553 CA PHE B 615 40.915 -22.835 -36.574 1.00 33.75 ATOM 3554 CB PHE B 615 39.473 -22.950 -36.084 1.00 33.07 ATOM 3555 CG PHE B 615 38.811 -24.257 -36.428 1.00 33.59 ATOM 3556 CD1 PHE B 615 38.252 -24.460 -37.689 1.00 33.67 ATOM 3557 CD2 PHE B 615 38.702 -25.269 -35.474 1.00 33.35 ATOM 3558 CE1 PHE B 615 37.586 -25.653 -37.996 1.00 33.41 ATOM 3559 CE2 PHE B 615 38.039 -26.464 -35.769 1.00 33.34 ATOM 3560 CZ PHE B 615 37.479 -26.653 -37.033 1.00 33.31 ATOM 3561 C PHE B 615 41.758 -23.936 -35.965 1.00 34.56 ATOM 3562 O PHE B 615 41.998 -24.964 -36.594 1.00 34.31 ATOM 3563 N PHE B 616 42.223 -23.709 -34.744 1.00 35.02 ATOM 3564 CA PHE B 616 43.031 -24.694 -34.053 1.00 35.86 ATOM 3565 CB PHE B 616 44.498 -24.598 -34.496 1.00 34.91 ATOM 3566 CG PHE B 616 45.162 -23.294 -34.148 1.00 34.58 ATOM 3567 CD1 PHE B 616 45.188 -22.248 -35.060 1.00 34.01 ATOM 3568 CD2 PHE B 616 45.782 -23.119 -32.914 1.00 34.45 ATOM 3569 CE1 PHE B 616 45.823 -21.045 -34.752 1.00 34.30 ATOM 3570 CE2 PHE B 616 46.420 -21.922 -32.595 1.00 34.53 ATOM 3571 CZ PHE B 616 46.440 -20.880 -33.518 1.00 34.26 ATOM 3572 C PHE B 616 42.918 -24.475 -32.560 1.00 37.34 ATOM 3573 O PHE B 616 42.560 -23.389 -32.105 1.00 36.51 ATOM 3574 N TYR B 617 43.215 -25.519 -31.799 1.00 39.35 ATOM 3575 CA TYR B 617 43.155 -25.425 -30.356 1.00 41.80 ATOM 3576 CB TYR B 617 42.447 -26.651 -29.784 1.00 40.98 ATOM 3577 CG TYR B 617 40.999 -26.734 -30.201 1.00 40.81 ATOM 3578 CD1 TYR B 617 39.997 -26.166 -29.417 1.00 40.53 ATOM 3579 CE1 TYR B 617 38.662 -26.212 -29.810 1.00 40.66 ATOM 3580 CD2 TYR B 617 40.631 -27.355 -31.395 1.00 40.68 ATOM 3581 CE2 TYR B 617 39.298 -27.407 -31.799 1.00 40.48 ATOM 3582 CZ TYR B 617 38.320 -26.835 -31.002 1.00 40.67 ATOM 3583 OH TYR B 617 37.000 -26.890 -31.386 1.00 40.67 ATOM 3584 C TYR B 617 44.565 -25.303 -29.796 1.00 44.26 ATOM 3585 O TYR B 617 45.526 -25.826 -30.367 1.00 44.11 ATOM 3586 N SER B 618 44.684 -24.582 -28.688 1.00 47.10 ATOM 3587 CA SER B 618 45.967 -24.383 -28.042 1.00 50.24 ATOM 3588 CB SER B 618 46.525 -22.997 -28.375 1.00 49.55 ATOM 3589 OG SER B 618 45.671 -21.977 -27.894 1.00 48.94 ATOM 3590 C SER B 618 45.772 -24.523 -26.544 1.00 53.07 ATOM 3591 O SER B 618 44.807 -24.003 -25.978 1.00 52.74 ATOM 3592 N SER B 619 46.686 -25.246 -25.908 1.00 56.97 ATOM 3593 CA SER B 619 46.611 -25.465 -24.473 1.00 60.55 ATOM 3594 CB SER B 619 47.497 -26.648 -24.063 1.00 60.69 ATOM 3595 OG SER B 619 48.348 -27.054 -25.127 1.00 61.60 ATOM 3596 C SER B 619 47.048 -24.213 -23.735 1.00 62.93 ATOM 3597 O SER B 619 48.195 -23.774 -23.853 1.00 63.11 ATOM 3598 N GLY B 620 46.116 -23.625 -22.991 1.00 65.86 ATOM 3599 CA GLY B 620 46.436 -22.438 -22.223 1.00 69.36 ATOM 3600 C GLY B 620 47.377 -22.850 -21.107 1.00 71.69 ATOM 3601 O GLY B 620 46.966 -23.541 -20.171 1.00 72.19 ATOM 3602 N GLU B 621 48.638 -22.439 -21.213 1.00 73.65 ATOM 3603 CA GLU B 621 49.656 -22.776 -20.220 1.00 75.54 ATOM 3604 CB GLU B 621 50.993 -22.119 -20.593 1.00 76.43 ATOM 3605 CG GLU B 621 51.588 -22.606 -21.913 1.00 77.92 ATOM 3606 CD GLU B 621 51.849 -24.106 -21.926 1.00 78.87 ATOM 3607 OE1 GLU B 621 52.238 -24.657 -20.871 1.00 79.56 ATOM 3608 OE2 GLU B 621 51.665 -24.733 -22.994 1.00 79.18 ATOM 3609 C GLU B 621 49.261 -22.357 -18.806 1.00 76.21 ATOM 3610 O GLU B 621 50.084 -22.394 -17.890 1.00 76.51 ATOM 3611 N LYS B 622 48.001 -21.965 -18.633 1.00 76.84 ATOM 3612 CA LYS B 622 47.491 -21.532 -17.337 1.00 77.18 ATOM 3613 CB LYS B 622 46.449 -20.426 -17.525 1.00 77.49 ATOM 3614 CG LYS B 622 47.022 -19.098 -17.995 1.00 77.77 ATOM 3615 CD LYS B 622 45.934 -18.201 -18.565 1.00 78.03 ATOM 3616 CE LYS B 622 46.526 -17.087 -19.418 1.00 78.22 ATOM 3617 NZ LYS B 622 45.645 -15.886 -19.458 1.00 78.05 ATOM 3618 C LYS B 622 46.875 -22.672 -16.530 1.00 77.18 ATOM 3619 O LYS B 622 46.840 -22.615 -15.301 1.00 77.55 ATOM 3620 N LYS B 623 46.387 -23.701 -17.214 1.00 76.96 ATOM 3621 CA LYS B 623 45.774 -24.839 -16.535 1.00 76.75 ATOM 3622 CB LYS B 623 44.585 -24.370 -15.692 1.00 77.55 ATOM 3623 CG LYS B 623 44.352 -25.190 -14.430 1.00 78.77 ATOM 3624 CD LYS B 623 43.044 -24.806 -13.748 1.00 79.60 ATOM 3625 CE LYS B 623 42.476 -25.969 -12.939 1.00 80.10 ATOM 3626 NZ LYS B 623 41.234 -25.595 -12.203 1.00 80.28 ATOM 3627 C LYS B 623 45.301 -25.871 -17.549 1.00 76.08 ATOM 3628 O LYS B 623 45.852 -25.975 -18.645 1.00 76.32 ATOM 3629 N ASP B 624 44.281 -26.637 -17.170 1.00 74.86 ATOM 3630 CA ASP B 624 43.711 -27.649 -18.054 1.00 73.36 ATOM 3631 CB ASP B 624 43.030 -28.753 -17.236 1.00 74.57 ATOM 3632 CG ASP B 624 42.001 -28.209 -16.255 1.00 75.72 ATOM 3633 OD1 ASP B 624 41.229 -29.022 -15.694 1.00 76.44 ATOM 3634 OD2 ASP B 624 41.961 -26.975 -16.043 1.00 75.99 ATOM 3635 C ASP B 624 42.691 -26.958 -18.959 1.00 71.54 ATOM 3636 O ASP B 624 41.723 -27.571 -19.422 1.00 71.61 ATOM 3637 N GLU B 625 42.922 -25.670 -19.197 1.00 68.90 ATOM 3638 CA GLU B 625 42.050 -24.860 -20.036 1.00 66.17 ATOM 3639 CB GLU B 625 42.075 -23.409 -19.553 1.00 67.35 ATOM 3640 CG GLU B 625 43.465 -22.782 -19.574 1.00 69.00 ATOM 3641 CD GLU B 625 43.593 -21.602 -18.627 1.00 70.17 ATOM 3642 OE1 GLU B 625 43.253 -21.758 -17.434 1.00 71.07 ATOM 3643 OE2 GLU B 625 44.033 -20.520 -19.074 1.00 70.69 ATOM 3644 C GLU B 625 42.480 -24.922 -21.506 1.00 63.41 ATOM 3645 O GLU B 625 43.657 -24.752 -21.832 1.00 63.04 ATOM 3646 N VAL B 626 41.515 -25.172 -22.385 1.00 59.82 ATOM 3647 CA VAL B 626 41.779 -25.246 -23.817 1.00 55.98 ATOM 3648 CB VAL B 626 41.095 -26.475 -24.459 1.00 56.48 ATOM 3649 CG1 VAL B 626 41.790 -26.832 -25.765 1.00 56.34 ATOM 3650 CG2 VAL B 626 41.123 -27.653 -23.498 1.00 56.78 ATOM 3651 C VAL B 626 41.243 -23.995 -24.500 1.00 52.85 ATOM 3652 O VAL B 626 40.171 -23.499 -24.155 1.00 52.17 ATOM 3653 N TYR B 627 41.989 -23.493 -25.473 1.00 49.39 ATOM 3654 CA TYR B 627 41.573 -22.304 -26.194 1.00 46.30 ATOM 3655 CB TYR B 627 42.647 -21.227 -26.105 1.00 46.68 ATOM 3656 CG TYR B 627 42.728 -20.561 -24.755 1.00 47.79 ATOM 3657 CD1 TYR B 627 43.504 -21.108 -23.730 1.00 48.33 ATOM 3658 CE1 TYR B 627 43.590 -20.491 -22.483 1.00 48.54 ATOM 3659 CD2 TYR B 627 42.038 -19.380 -24.502 1.00 47.82 ATOM 3660 CE2 TYR B 627 42.116 -18.756 -23.262 1.00 48.50 ATOM 3661 CZ TYR B 627 42.893 -19.314 -22.256 1.00 48.80 ATOM 3662 OH TYR B 627 42.969 -18.689 -21.030 1.00 49.33 ATOM 3663 C TYR B 627 41.304 -22.599 -27.658 1.00 43.94 ATOM 3664 O TYR B 627 42.062 -23.324 -28.302 1.00 43.79 ATOM 3665 N LEU B 628 40.213 -22.042 -28.174 1.00 40.64 ATOM 3666 CA LEU B 628 39.871 -22.200 -29.578 1.00 37.33 ATOM 3667 CB LEU B 628 38.356 -22.288 -29.763 1.00 36.80 ATOM 3668 CG LEU B 628 37.840 -22.048 -31.188 1.00 36.22 ATOM 3669 CD1 LEU B 628 38.250 -23.203 -32.097 1.00 35.58 ATOM 3670 CD2 LEU B 628 36.323 -21.898 -31.158 1.00 36.06 ATOM 3671 C LEU B 628 40.415 -20.953 -30.269 1.00 35.60 ATOM 3672 O LEU B 628 40.178 -19.830 -29.814 1.00 34.83 ATOM 3673 N ASN B 629 41.167 -21.150 -31.347 1.00 33.26 ATOM 3674 CA ASN B 629 41.752 -20.042 -32.092 1.00 31.34 ATOM 3675 CB ASN B 629 43.264 -20.207 -32.199 1.00 30.86 ATOM 3676 CG ASN B 629 43.940 -20.271 -30.849 1.00 31.35 ATOM 3677 OD1 ASN B 629 44.534 -19.291 -30.393 1.00 30.50 ATOM 3678 ND2 ASN B 629 43.855 -21.431 -30.197 1.00 30.79 ATOM 3679 C ASN B 629 41.179 -19.973 -33.491 1.00 30.63 ATOM 3680 O ASN B 629 41.374 -20.887 -34.282 1.00 29.78 ATOM 3681 N LEU B 630 40.471 -18.889 -33.791 1.00 29.74 ATOM 3682 CA LEU B 630 39.891 -18.700 -35.114 1.00 28.84 ATOM 3683 CB LEU B 630 38.499 -18.072 -35.014 1.00 28.72 ATOM 3684 CG LEU B 630 37.501 -18.704 -34.045 1.00 28.61 ATOM 3685 CD1 LEU B 630 36.277 -17.809 -33.920 1.00 28.26 ATOM 3686 CD2 LEU B 630 37.096 -20.077 -34.540 1.00 29.07 ATOM 3687 C LEU B 630 40.809 -17.771 -35.900 1.00 28.70 ATOM 3688 O LEU B 630 41.035 -16.631 -35.494 1.00 28.46 ATOM 3689 N VAL B 631 41.351 -18.270 -37.009 1.00 28.04 ATOM 3690 CA VAL B 631 42.232 -17.474 -37.857 1.00 28.27 ATOM 3691 CB VAL B 631 43.321 -18.352 -38.512 1.00 28.18 ATOM 3692 CG1 VAL B 631 44.285 -17.482 -39.302 1.00 26.65 ATOM 3693 CG2 VAL B 631 44.059 -19.143 -37.441 1.00 27.11 ATOM 3694 C VAL B 631 41.383 -16.813 -38.947 1.00 28.82 ATOM 3695 O VAL B 631 40.826 -17.490 -39.815 1.00 29.25 ATOM 3696 N LEU B 632 41.291 -15.489 -38.895 1.00 28.64 ATOM 3697 CA LEU B 632 40.483 -14.739 -39.847 1.00 28.64 ATOM 3698 CB LEU B 632 39.483 -13.860 -39.096 1.00 28.15 ATOM 3699 CG LEU B 632 38.832 -14.453 -37.855 1.00 28.05 ATOM 3700 CD1 LEU B 632 38.215 -13.342 -37.010 1.00 28.19 ATOM 3701 CD2 LEU B 632 37.779 -15.459 -38.285 1.00 27.64 ATOM 3702 C LEU B 632 41.288 -13.839 -40.761 1.00 29.17 ATOM 3703 O LEU B 632 42.458 -13.545 -40.499 1.00 28.71 ATOM 3704 N ASP B 633 40.646 -13.398 -41.840 1.00 29.84 ATOM 3705 CA ASP B 633 41.283 -12.470 -42.756 1.00 30.59 ATOM 3706 CB ASP B 633 40.373 -12.167 -43.945 1.00 32.03 ATOM 3707 CG ASP B 633 40.505 -13.185 -45.064 1.00 33.27 ATOM 3708 OD1 ASP B 633 39.668 -13.151 -45.987 1.00 33.68 ATOM 3709 OD2 ASP B 633 41.438 -14.014 -45.022 1.00 34.91 ATOM 3710 C ASP B 633 41.431 -11.206 -41.910 1.00 30.72 ATOM 3711 O ASP B 633 40.547 -10.882 -41.110 1.00 30.47 ATOM 3712 N TYR B 634 42.541 -10.500 -42.073 1.00 30.80 ATOM 3713 CA TYR B 634 42.767 -9.276 -41.318 1.00 30.70 ATOM 3714 CB TYR B 634 44.268 -9.078 -41.077 1.00 31.52 ATOM 3715 CG TYR B 634 44.611 -7.726 -40.493 1.00 32.67 ATOM 3716 CD1 TYR B 634 45.031 -6.680 -41.312 1.00 32.80 ATOM 3717 CE1 TYR B 634 45.295 -5.419 -40.787 1.00 33.38 ATOM 3718 CD2 TYR B 634 44.467 -7.478 -39.127 1.00 32.89 ATOM 3719 CE2 TYR B 634 44.727 -6.220 -38.592 1.00 33.41 ATOM 3720 CZ TYR B 634 45.138 -5.196 -39.430 1.00 33.52 ATOM 3721 OH TYR B 634 45.382 -3.943 -38.913 1.00 34.89 ATOM 3722 C TYR B 634 42.203 -8.079 -42.086 1.00 30.09 ATOM 3723 O TYR B 634 42.429 -7.950 -43.283 1.00 30.17 ATOM 3724 N VAL B 635 41.440 -7.229 -41.401 1.00 28.90 ATOM 3725 CA VAL B 635 40.875 -6.020 -42.006 1.00 27.92 ATOM 3726 CB VAL B 635 39.333 -6.052 -42.019 1.00 27.40 ATOM 3727 CG1 VAL B 635 38.797 -4.897 -42.846 1.00 26.60 ATOM 3728 CG2 VAL B 635 38.854 -7.368 -42.614 1.00 27.29 ATOM 3729 C VAL B 635 41.408 -4.902 -41.105 1.00 27.76 ATOM 3730 O VAL B 635 41.261 -4.953 -39.888 1.00 27.13 ATOM 3731 N PRO B 636 42.008 -3.859 -41.701 1.00 27.92 ATOM 3732 CD PRO B 636 42.082 -3.684 -43.165 1.00 28.24 ATOM 3733 CA PRO B 636 42.608 -2.718 -40.992 1.00 27.88 ATOM 3734 CB PRO B 636 43.376 -1.989 -42.095 1.00 28.22 ATOM 3735 CG PRO B 636 42.577 -2.269 -43.323 1.00 28.42 ATOM 3736 C PRO B 636 41.790 -1.740 -40.154 1.00 27.70 ATOM 3737 O PRO B 636 42.299 -1.201 -39.163 1.00 27.99 ATOM 3738 N GLU B 637 40.545 -1.493 -40.536 1.00 27.10 ATOM 3739 CA GLU B 637 39.738 -0.533 -39.804 1.00 26.85 ATOM 3740 CB GLU B 637 39.513 0.711 -40.664 1.00 29.28 ATOM 3741 CG GLU B 637 40.701 1.627 -40.741 1.00 33.78 ATOM 3742 CD GLU B 637 40.866 2.459 -39.493 1.00 36.30 ATOM 3743 OE1 GLU B 637 41.827 3.252 -39.440 1.00 39.33 ATOM 3744 OE2 GLU B 637 40.037 2.329 -38.565 1.00 37.41 ATOM 3745 C GLU B 637 38.385 -1.057 -39.375 1.00 25.43 ATOM 3746 O GLU B 637 38.014 -2.198 -39.657 1.00 24.25 ATOM 3747 N THR B 638 37.657 -0.195 -38.677 1.00 24.14 ATOM 3748 CA THR B 638 36.314 -0.497 -38.226 1.00 23.45 ATOM 3749 CB THR B 638 36.253 -0.859 -36.719 1.00 23.55 ATOM 3750 OG1 THR B 638 36.649 0.273 -35.936 1.00 23.46 ATOM 3751 CG2 THR B 638 37.148 -2.042 -36.407 1.00 22.39 ATOM 3752 C THR B 638 35.496 0.771 -38.448 1.00 23.65 ATOM 3753 O THR B 638 36.040 1.883 -38.444 1.00 23.22 ATOM 3754 N VAL B 639 34.197 0.605 -38.660 1.00 22.53 ATOM 3755 CA VAL B 639 33.327 1.749 -38.844 1.00 22.83 ATOM 3756 CB VAL B 639 31.850 1.291 -39.035 1.00 22.69 ATOM 3757 CG1 VAL B 639 30.889 2.456 -38.818 1.00 22.81 ATOM 3758 CG2 VAL B 639 31.671 0.723 -40.443 1.00 22.27 ATOM 3759 C VAL B 639 33.454 2.634 -37.596 1.00 23.56 ATOM 3760 O VAL B 639 33.424 3.861 -37.688 1.00 23.64 ATOM 3761 N TYR B 640 33.612 2.005 -36.436 1.00 23.72 ATOM 3762 CA TYR B 640 33.739 2.740 -35.184 1.00 25.46 ATOM 3763 CB TYR B 640 33.930 1.770 -34.022 1.00 25.98 ATOM 3764 CG TYR B 640 34.191 2.459 -32.704 1.00 28.08 ATOM 3765 CD1 TYR B 640 35.491 2.620 -32.226 1.00 29.48 ATOM 3766 CE1 TYR B 640 35.739 3.259 -31.007 1.00 30.66 ATOM 3767 CD2 TYR B 640 33.138 2.953 -31.933 1.00 28.99 ATOM 3768 CE2 TYR B 640 33.370 3.591 -30.717 1.00 30.14 ATOM 3769 CZ TYR B 640 34.673 3.741 -30.260 1.00 31.07 ATOM 3770 OH TYR B 640 34.912 4.369 -29.057 1.00 32.57 ATOM 3771 C TYR B 640 34.902 3.736 -35.198 1.00 26.28 ATOM 3772 O TYR B 640 34.729 4.915 -34.880 1.00 24.65 ATOM 3773 N ARG B 641 36.084 3.256 -35.569 1.00 27.12 ATOM 3774 CA ARG B 641 37.272 4.106 -35.603 1.00 29.00 ATOM 3775 CB ARG B 641 38.522 3.260 -35.849 1.00 31.65 ATOM 3776 CG ARG B 641 38.950 2.452 -34.632 1.00 36.26 ATOM 3777 CD ARG B 641 40.182 1.604 -34.933 1.00 40.32 ATOM 3778 NE ARG B 641 41.190 2.343 -35.698 1.00 43.78 ATOM 3779 CZ ARG B 641 42.315 1.808 -36.170 1.00 45.41 ATOM 3780 NH1 ARG B 641 42.582 0.525 -35.958 1.00 46.58 ATOM 3781 NH2 ARG B 641 43.178 2.558 -36.848 1.00 46.21 ATOM 3782 C ARG B 641 37.173 5.193 -36.656 1.00 28.46 ATOM 3783 O ARG B 641 37.546 6.334 -36.411 1.00 27.65 ATOM 3784 N VAL B 642 36.661 4.840 -37.828 1.00 27.82 ATOM 3785 CA VAL B 642 36.520 5.804 -38.901 1.00 27.95 ATOM 3786 CB VAL B 642 36.014 5.126 -40.187 1.00 28.04 ATOM 3787 CG1 VAL B 642 35.531 6.176 -41.192 1.00 28.11 ATOM 3788 CG2 VAL B 642 37.130 4.269 -40.781 1.00 28.13 ATOM 3789 C VAL B 642 35.550 6.901 -38.494 1.00 28.25 ATOM 3790 O VAL B 642 35.860 8.082 -38.623 1.00 28.01 ATOM 3791 N ALA B 643 34.382 6.512 -37.991 1.00 28.18 ATOM 3792 CA ALA B 643 33.381 7.485 -37.579 1.00 29.65 ATOM 3793 CB ALA B 643 32.119 6.770 -37.089 1.00 29.08 ATOM 3794 C ALA B 643 33.913 8.419 -36.490 1.00 30.71 ATOM 3795 O ALA B 643 33.579 9.602 -36.464 1.00 31.25 ATOM 3796 N ARG B 644 34.735 7.881 -35.594 1.00 32.08 ATOM 3797 CA ARG B 644 35.313 8.661 -34.507 1.00 34.44 ATOM 3798 CB ARG B 644 35.988 7.720 -33.503 1.00 36.24 ATOM 3799 CG ARG B 644 36.404 8.372 -32.195 1.00 39.38 ATOM 3800 CD ARG B 644 37.226 7.409 -31.334 1.00 42.64 ATOM 3801 NE ARG B 644 38.225 6.680 -32.119 1.00 45.66 ATOM 3802 CZ ARG B 644 39.028 5.734 -31.629 1.00 47.22 ATOM 3803 NH1 ARG B 644 38.956 5.391 -30.346 1.00 48.12 ATOM 3804 NH2 ARG B 644 39.909 5.134 -32.423 1.00 47.91 ATOM 3805 C ARG B 644 36.320 9.685 -35.041 1.00 35.13 ATOM 3806 O ARG B 644 36.433 10.782 -34.509 1.00 35.00 ATOM 3807 N HIS B 645 37.052 9.321 -36.089 1.00 36.48 ATOM 3808 CA HIS B 645 38.029 10.226 -36.693 1.00 37.77 ATOM 3809 CB HIS B 645 38.757 9.539 -37.853 1.00 39.68 ATOM 3810 CG HIS B 645 39.865 8.626 -37.423 1.00 42.92 ATOM 3811 CD2 HIS B 645 40.704 8.678 -36.359 1.00 44.11 ATOM 3812 ND1 HIS B 645 40.217 7.495 -38.132 1.00 44.44 ATOM 3813 CE1 HIS B 645 41.225 6.891 -37.526 1.00 44.75 ATOM 3814 NE2 HIS B 645 41.539 7.589 -36.447 1.00 44.86 ATOM 3815 C HIS B 645 37.313 11.468 -37.216 1.00 37.83 ATOM 3816 O HIS B 645 37.766 12.591 -37.010 1.00 37.53 ATOM 3817 N TYR B 646 36.189 11.261 -37.894 1.00 37.51 ATOM 3818 CA TYR B 646 35.417 12.370 -38.438 1.00 37.79 ATOM 3819 CB TYR B 646 34.373 11.862 -39.433 1.00 35.52 ATOM 3820 CG TYR B 646 34.938 11.527 -40.791 1.00 33.22 ATOM 3821 CD1 TYR B 646 35.559 10.303 -41.022 1.00 32.24 ATOM 3822 CE1 TYR B 646 36.092 9.991 -42.265 1.00 31.14 ATOM 3823 CD2 TYR B 646 34.860 12.437 -41.845 1.00 32.59 ATOM 3824 CE2 TYR B 646 35.388 12.137 -43.094 1.00 31.41 ATOM 3825 CZ TYR B 646 36.004 10.911 -43.294 1.00 31.30 ATOM 3826 OH TYR B 646 36.544 10.610 -44.517 1.00 30.89 ATOM 3827 C TYR B 646 34.715 13.143 -37.336 1.00 39.21 ATOM 3828 O TYR B 646 34.633 14.366 -37.379 1.00 39.65 ATOM 3829 N SER B 647 34.200 12.428 -36.348 1.00 41.01 ATOM 3830 CA SER B 647 33.501 13.075 -35.254 1.00 43.62 ATOM 3831 CB SER B 647 32.955 12.029 -34.286 1.00 44.35 ATOM 3832 OG SER B 647 31.654 12.391 -33.857 1.00 46.43 ATOM 3833 C SER B 647 34.438 14.018 -34.517 1.00 45.22 ATOM 3834 O SER B 647 34.086 15.162 -34.225 1.00 45.33 ATOM 3835 N ARG B 648 35.634 13.529 -34.216 1.00 46.94 ATOM 3836 CA ARG B 648 36.621 14.338 -33.522 1.00 48.89 ATOM 3837 CB ARG B 648 37.922 13.555 -33.357 1.00 50.14 ATOM 3838 CG ARG B 648 37.883 12.541 -32.224 1.00 52.59 ATOM 3839 CD ARG B 648 39.242 11.888 -32.034 1.00 55.33 ATOM 3840 NE ARG B 648 39.177 10.724 -31.154 1.00 58.17 ATOM 3841 CZ ARG B 648 40.246 10.064 -30.708 1.00 59.91 ATOM 3842 NH1 ARG B 648 41.466 10.456 -31.062 1.00 60.75 ATOM 3843 NH2 ARG B 648 40.100 9.013 -29.905 1.00 60.21 ATOM 3844 C ARG B 648 36.868 15.613 -34.317 1.00 49.37 ATOM 3845 O ARG B 648 36.768 16.714 -33.780 1.00 49.90 ATOM 3846 N ALA B 649 37.175 15.461 -35.602 1.00 49.73 ATOM 3847 CA ALA B 649 37.427 16.605 -36.477 1.00 50.12 ATOM 3848 CB ALA B 649 38.018 16.132 -37.807 1.00 49.72 ATOM 3849 C ALA B 649 36.147 17.397 -36.728 1.00 50.15 ATOM 3850 O ALA B 649 36.118 18.300 -37.561 1.00 50.16 ATOM 3851 N LYS B 650 35.092 17.056 -35.999 1.00 50.81 ATOM 3852 CA LYS B 650 33.804 17.724 -36.141 1.00 51.61 ATOM 3853 CB LYS B 650 33.873 19.149 -35.580 1.00 52.95 ATOM 3854 CG LYS B 650 33.447 19.250 -34.116 1.00 54.54 ATOM 3855 CD LYS B 650 33.178 20.692 -33.692 1.00 56.04 ATOM 3856 CE LYS B 650 33.253 20.846 -32.170 1.00 57.43 ATOM 3857 NZ LYS B 650 32.747 22.171 -31.683 1.00 57.71 ATOM 3858 C LYS B 650 33.345 17.753 -37.597 1.00 51.33 ATOM 3859 O LYS B 650 32.718 18.715 -38.049 1.00 51.46 ATOM 3860 N GLN B 651 33.676 16.690 -38.326 1.00 50.58 ATOM 3861 CA GLN B 651 33.281 16.545 -39.722 1.00 49.40 ATOM 3862 CB GLN B 651 34.495 16.300 -40.617 1.00 50.22 ATOM 3863 CG GLN B 651 35.711 17.127 -40.274 1.00 51.84 ATOM 3864 CD GLN B 651 36.864 16.877 -41.228 1.00 53.24 ATOM 3865 OE1 GLN B 651 36.751 16.082 -42.164 1.00 53.83 ATOM 3866 NE2 GLN B 651 37.983 17.559 -40.997 1.00 53.84 ATOM 3867 C GLN B 651 32.358 15.339 -39.805 1.00 47.96 ATOM 3868 O GLN B 651 32.166 14.620 -38.824 1.00 47.93 ATOM 3869 N THR B 652 31.788 15.119 -40.981 1.00 46.33 ATOM 3870 CA THR B 652 30.892 13.990 -41.186 1.00 44.29 ATOM 3871 CB THR B 652 29.433 14.481 -41.413 1.00 45.01 ATOM 3872 OG1 THR B 652 28.601 13.999 -40.350 1.00 46.24 ATOM 3873 CG2 THR B 652 28.888 13.997 -42.749 1.00 45.89 ATOM 3874 C THR B 652 31.392 13.171 -42.378 1.00 41.78 ATOM 3875 O THR B 652 31.971 13.707 -43.320 1.00 41.15 ATOM 3876 N LEU B 653 31.183 11.866 -42.321 1.00 38.90 ATOM 3877 CA LEU B 653 31.619 10.987 -43.394 1.00 35.93 ATOM 3878 CB LEU B 653 31.385 9.539 -42.966 1.00 35.23 ATOM 3879 CG LEU B 653 31.903 8.390 -43.819 1.00 34.09 ATOM 3880 CD1 LEU B 653 33.414 8.309 -43.752 1.00 33.69 ATOM 3881 CD2 LEU B 653 31.274 7.109 -43.305 1.00 34.01 ATOM 3882 C LEU B 653 30.841 11.294 -44.675 1.00 34.24 ATOM 3883 O LEU B 653 29.624 11.451 -44.638 1.00 33.96 ATOM 3884 N PRO B 654 31.539 11.423 -45.818 1.00 32.56 ATOM 3885 CD PRO B 654 32.997 11.339 -46.009 1.00 32.34 ATOM 3886 CA PRO B 654 30.826 11.706 -47.073 1.00 31.67 ATOM 3887 CB PRO B 654 31.911 11.616 -48.149 1.00 31.10 ATOM 3888 CG PRO B 654 33.197 11.843 -47.419 1.00 31.73 ATOM 3889 C PRO B 654 29.732 10.656 -47.278 1.00 30.98 ATOM 3890 O PRO B 654 29.948 9.463 -47.052 1.00 30.41 ATOM 3891 N VAL B 655 28.566 11.103 -47.718 1.00 29.67 ATOM 3892 CA VAL B 655 27.438 10.211 -47.911 1.00 28.86 ATOM 3893 CB VAL B 655 26.217 11.003 -48.425 1.00 29.43 ATOM 3894 CG1 VAL B 655 24.982 10.108 -48.457 1.00 30.52 ATOM 3895 CG2 VAL B 655 25.967 12.191 -47.499 1.00 29.93 ATOM 3896 C VAL B 655 27.715 9.006 -48.808 1.00 27.97 ATOM 3897 O VAL B 655 27.140 7.943 -48.598 1.00 28.02 ATOM 3898 N ILE B 656 28.596 9.146 -49.795 1.00 26.62 ATOM 3899 CA ILE B 656 28.882 8.008 -50.664 1.00 24.93 ATOM 3900 CB ILE B 656 29.905 8.367 -51.771 1.00 25.01 ATOM 3901 CG2 ILE B 656 31.233 8.776 -51.154 1.00 25.16 ATOM 3902 CG1 ILE B 656 30.095 7.169 -52.706 1.00 24.40 ATOM 3903 CD1 ILE B 656 28.823 6.732 -53.418 1.00 24.74 ATOM 3904 C ILE B 656 29.410 6.825 -49.846 1.00 23.93 ATOM 3905 O ILE B 656 29.096 5.674 -50.139 1.00 23.06 ATOM 3906 N TYR B 657 30.204 7.108 -48.819 1.00 23.11 ATOM 3907 CA TYR B 657 30.741 6.045 -47.967 1.00 22.95 ATOM 3908 CB TYR B 657 31.886 6.582 -47.109 1.00 24.32 ATOM 3909 CG TYR B 657 33.139 6.814 -47.917 1.00 27.37 ATOM 3910 CD1 TYR B 657 33.670 8.097 -48.068 1.00 28.12 ATOM 3911 CE1 TYR B 657 34.815 8.316 -48.846 1.00 29.77 ATOM 3912 CD2 TYR B 657 33.780 5.751 -48.563 1.00 27.72 ATOM 3913 CE2 TYR B 657 34.921 5.958 -49.341 1.00 29.17 ATOM 3914 CZ TYR B 657 35.431 7.241 -49.475 1.00 30.12 ATOM 3915 OH TYR B 657 36.572 7.444 -50.223 1.00 33.01 ATOM 3916 C TYR B 657 29.631 5.481 -47.083 1.00 22.14 ATOM 3917 O TYR B 657 29.571 4.276 -46.842 1.00 21.17 ATOM 3918 N VAL B 658 28.756 6.361 -46.602 1.00 21.25 ATOM 3919 CA VAL B 658 27.636 5.940 -45.774 1.00 21.00 ATOM 3920 CB VAL B 658 26.748 7.140 -45.373 1.00 21.04 ATOM 3921 CG1 VAL B 658 25.506 6.646 -44.623 1.00 21.32 ATOM 3922 CG2 VAL B 658 27.548 8.121 -44.503 1.00 20.36 ATOM 3923 C VAL B 658 26.794 4.956 -46.584 1.00 20.90 ATOM 3924 O VAL B 658 26.372 3.913 -46.080 1.00 20.00 ATOM 3925 N LYS B 659 26.547 5.299 -47.845 1.00 20.31 ATOM 3926 CA LYS B 659 25.763 4.445 -48.731 1.00 20.13 ATOM 3927 CB LYS B 659 25.570 5.127 -50.088 1.00 20.85 ATOM 3928 CG LYS B 659 24.415 6.101 -50.138 1.00 21.64 ATOM 3929 CD LYS B 659 24.333 6.765 -51.495 1.00 23.05 ATOM 3930 CE LYS B 659 23.695 8.133 -51.376 1.00 23.69 ATOM 3931 NZ LYS B 659 23.365 8.685 -52.718 1.00 25.59 ATOM 3932 C LYS B 659 26.466 3.104 -48.935 1.00 20.03 ATOM 3933 O LYS B 659 25.866 2.042 -48.779 1.00 19.79 ATOM 3934 N LEU B 660 27.748 3.153 -49.274 1.00 19.91 ATOM 3935 CA LEU B 660 28.510 1.929 -49.502 1.00 19.79 ATOM 3936 CB LEU B 660 29.927 2.267 -49.970 1.00 20.50 ATOM 3937 CG LEU B 660 30.123 2.525 -51.466 1.00 21.52 ATOM 3938 CD1 LEU B 660 31.504 3.180 -51.672 1.00 22.17 ATOM 3939 CD2 LEU B 660 30.018 1.220 -52.253 1.00 20.67 ATOM 3940 C LEU B 660 28.599 1.007 -48.282 1.00 19.08 ATOM 3941 O LEU B 660 28.420 -0.200 -48.401 1.00 17.82 ATOM 3942 N TYR B 661 28.901 1.570 -47.116 1.00 18.79 ATOM 3943 CA TYR B 661 29.024 0.765 -45.903 1.00 18.63 ATOM 3944 CB TYR B 661 29.566 1.610 -44.741 1.00 19.89 ATOM 3945 CG TYR B 661 30.953 2.164 -44.968 1.00 21.90 ATOM 3946 CD1 TYR B 661 31.782 1.637 -45.955 1.00 23.78 ATOM 3947 CE1 TYR B 661 33.055 2.157 -46.186 1.00 26.21 ATOM 3948 CD2 TYR B 661 31.429 3.234 -44.206 1.00 24.25 ATOM 3949 CE2 TYR B 661 32.703 3.765 -44.428 1.00 25.48 ATOM 3950 CZ TYR B 661 33.507 3.219 -45.420 1.00 26.66 ATOM 3951 OH TYR B 661 34.769 3.724 -45.655 1.00 29.89 ATOM 3952 C TYR B 661 27.696 0.152 -45.485 1.00 18.11 ATOM 3953 O TYR B 661 27.624 -1.043 -45.193 1.00 17.63 ATOM 3954 N MET B 662 26.650 0.969 -45.449 1.00 16.98 ATOM 3955 CA MET B 662 25.338 0.481 -45.036 1.00 17.60 ATOM 3956 CB MET B 662 24.351 1.649 -44.901 1.00 18.21 ATOM 3957 CG MET B 662 24.616 2.563 -43.701 1.00 21.38 ATOM 3958 SD MET B 662 24.750 1.681 -42.123 1.00 22.64 ATOM 3959 CE MET B 662 23.107 0.906 -42.053 1.00 23.06 ATOM 3960 C MET B 662 24.793 -0.563 -46.012 1.00 16.99 ATOM 3961 O MET B 662 24.179 -1.551 -45.595 1.00 15.83 ATOM 3962 N TYR B 663 25.019 -0.350 -47.305 1.00 16.47 ATOM 3963 CA TYR B 663 24.543 -1.302 -48.312 1.00 16.52 ATOM 3964 CB TYR B 663 24.914 -0.824 -49.721 1.00 17.61 ATOM 3965 CG TYR B 663 24.522 -1.792 -50.820 1.00 17.77 ATOM 3966 CD1 TYR B 663 25.430 -2.746 -51.297 1.00 18.64 ATOM 3967 CE1 TYR B 663 25.076 -3.632 -52.325 1.00 17.84 ATOM 3968 CD2 TYR B 663 23.249 -1.746 -51.391 1.00 18.50 ATOM 3969 CE2 TYR B 663 22.883 -2.628 -52.421 1.00 19.06 ATOM 3970 CZ TYR B 663 23.806 -3.564 -52.879 1.00 18.70 ATOM 3971 OH TYR B 663 23.452 -4.418 -53.903 1.00 20.30 ATOM 3972 C TYR B 663 25.178 -2.670 -48.073 1.00 16.81 ATOM 3973 O TYR B 663 24.497 -3.704 -48.082 1.00 16.34 ATOM 3974 N GLN B 664 26.488 -2.669 -47.866 1.00 16.69 ATOM 3975 CA GLN B 664 27.220 -3.903 -47.634 1.00 17.22 ATOM 3976 CB GLN B 664 28.730 -3.623 -47.631 1.00 17.72 ATOM 3977 CG GLN B 664 29.294 -3.331 -49.028 1.00 17.53 ATOM 3978 CD GLN B 664 30.728 -2.818 -49.004 1.00 18.48 ATOM 3979 OE1 GLN B 664 30.981 -1.622 -48.821 1.00 20.16 ATOM 3980 NE2 GLN B 664 31.668 -3.718 -49.190 1.00 16.09 ATOM 3981 C GLN B 664 26.775 -4.562 -46.322 1.00 17.46 ATOM 3982 O GLN B 664 26.718 -5.792 -46.227 1.00 17.02 ATOM 3983 N LEU B 665 26.460 -3.756 -45.310 1.00 16.26 ATOM 3984 CA LEU B 665 25.996 -4.321 -44.041 1.00 16.57 ATOM 3985 CB LEU B 665 25.833 -3.219 -42.983 1.00 16.40 ATOM 3986 CG LEU B 665 25.008 -3.584 -41.737 1.00 16.23 ATOM 3987 CD1 LEU B 665 25.580 -4.817 -41.060 1.00 16.37 ATOM 3988 CD2 LEU B 665 25.006 -2.395 -40.769 1.00 17.50 ATOM 3989 C LEU B 665 24.652 -5.041 -44.265 1.00 16.91 ATOM 3990 O LEU B 665 24.447 -6.170 -43.798 1.00 17.36 ATOM 3991 N PHE B 666 23.740 -4.400 -44.988 1.00 16.20 ATOM 3992 CA PHE B 666 22.449 -5.022 -45.244 1.00 17.89 ATOM 3993 CB PHE B 666 21.519 -4.021 -45.926 1.00 18.41 ATOM 3994 CG PHE B 666 20.920 -3.014 -44.969 1.00 19.55 ATOM 3995 CD1 PHE B 666 21.027 -1.647 -45.212 1.00 19.61 ATOM 3996 CD2 PHE B 666 20.261 -3.441 -43.813 1.00 19.66 ATOM 3997 CE1 PHE B 666 20.491 -0.720 -44.321 1.00 19.41 ATOM 3998 CE2 PHE B 666 19.721 -2.519 -42.914 1.00 19.79 ATOM 3999 CZ PHE B 666 19.839 -1.157 -43.174 1.00 19.39 ATOM 4000 C PHE B 666 22.599 -6.314 -46.062 1.00 18.01 ATOM 4001 O PHE B 666 21.857 -7.274 -45.852 1.00 18.77 ATOM 4002 N ARG B 667 23.568 -6.355 -46.973 1.00 18.04 ATOM 4003 CA ARG B 667 23.795 -7.567 -47.760 1.00 18.19 ATOM 4004 CB ARG B 667 24.901 -7.344 -48.797 1.00 18.53 ATOM 4005 CG ARG B 667 24.401 -6.797 -50.116 1.00 19.91 ATOM 4006 CD ARG B 667 25.416 -7.042 -51.225 1.00 20.69 ATOM 4007 NE ARG B 667 25.439 -8.436 -51.667 1.00 21.50 ATOM 4008 CZ ARG B 667 26.346 -8.939 -52.501 1.00 22.10 ATOM 4009 NH1 ARG B 667 27.311 -8.168 -52.986 1.00 22.19 ATOM 4010 NH2 ARG B 667 26.274 -10.207 -52.872 1.00 22.96 ATOM 4011 C ARG B 667 24.208 -8.701 -46.827 1.00 17.99 ATOM 4012 O ARG B 667 23.677 -9.815 -46.907 1.00 18.42 ATOM 4013 N SER B 668 25.158 -8.423 -45.939 1.00 17.08 ATOM 4014 CA SER B 668 25.626 -9.435 -45.004 1.00 17.73 ATOM 4015 CB SER B 668 26.799 -8.883 -44.167 1.00 17.00 ATOM 4016 OG SER B 668 26.361 -8.003 -43.149 1.00 17.72 ATOM 4017 C SER B 668 24.472 -9.932 -44.106 1.00 17.38 ATOM 4018 O SER B 668 24.407 -11.116 -43.776 1.00 18.47 ATOM 4019 N LEU B 669 23.556 -9.044 -43.731 1.00 17.44 ATOM 4020 CA LEU B 669 22.409 -9.430 -42.898 1.00 17.91 ATOM 4021 CB LEU B 669 21.715 -8.193 -42.321 1.00 16.80 ATOM 4022 CG LEU B 669 22.521 -7.373 -41.293 1.00 17.62 ATOM 4023 CD1 LEU B 669 21.649 -6.234 -40.737 1.00 16.59 ATOM 4024 CD2 LEU B 669 23.019 -8.292 -40.166 1.00 16.01 ATOM 4025 C LEU B 669 21.388 -10.254 -43.700 1.00 18.68 ATOM 4026 O LEU B 669 20.780 -11.188 -43.174 1.00 18.78 ATOM 4027 N ALA B 670 21.178 -9.897 -44.961 1.00 18.94 ATOM 4028 CA ALA B 670 20.244 -10.654 -45.785 1.00 19.37 ATOM 4029 CB ALA B 670 20.161 -10.046 -47.182 1.00 19.07 ATOM 4030 C ALA B 670 20.780 -12.085 -45.860 1.00 19.64 ATOM 4031 O ALA B 670 20.018 -13.051 -45.791 1.00 20.24 ATOM 4032 N TYR B 671 22.098 -12.213 -45.974 1.00 19.95 ATOM 4033 CA TYR B 671 22.733 -13.522 -46.070 1.00 21.01 ATOM 4034 CB TYR B 671 24.211 -13.368 -46.457 1.00 21.35 ATOM 4035 CG TYR B 671 24.964 -14.680 -46.554 1.00 22.82 ATOM 4036 CD1 TYR B 671 25.853 -15.064 -45.555 1.00 22.66 ATOM 4037 CE1 TYR B 671 26.546 -16.270 -45.629 1.00 24.11 ATOM 4038 CD2 TYR B 671 24.781 -15.543 -47.646 1.00 23.59 ATOM 4039 CE2 TYR B 671 25.472 -16.760 -47.729 1.00 23.71 ATOM 4040 CZ TYR B 671 26.352 -17.112 -46.716 1.00 24.29 ATOM 4041 OH TYR B 671 27.045 -18.299 -46.768 1.00 25.56 ATOM 4042 C TYR B 671 22.610 -14.387 -44.813 1.00 21.50 ATOM 4043 O TYR B 671 22.142 -15.524 -44.891 1.00 22.49 ATOM 4044 N ILE B 672 23.027 -13.880 -43.655 1.00 20.85 ATOM 4045 CA ILE B 672 22.921 -14.693 -42.448 1.00 19.71 ATOM 4046 CB ILE B 672 23.689 -14.063 -41.240 1.00 19.56 ATOM 4047 CG2 ILE B 672 25.174 -14.001 -41.545 1.00 19.26 ATOM 4048 CG1 ILE B 672 23.144 -12.672 -40.920 1.00 19.18 ATOM 4049 CD1 ILE B 672 23.620 -12.134 -39.563 1.00 19.71 ATOM 4050 C ILE B 672 21.460 -14.948 -42.058 1.00 20.26 ATOM 4051 O ILE B 672 21.126 -16.029 -41.571 1.00 20.44 ATOM 4052 N HIS B 673 20.585 -13.973 -42.287 1.00 20.24 ATOM 4053 CA HIS B 673 19.179 -14.134 -41.943 1.00 21.43 ATOM 4054 CB HIS B 673 18.425 -12.819 -42.127 1.00 21.17 ATOM 4055 CG HIS B 673 18.712 -11.800 -41.062 1.00 20.71 ATOM 4056 CD2 HIS B 673 19.584 -11.812 -40.023 1.00 19.53 ATOM 4057 ND1 HIS B 673 18.070 -10.581 -41.007 1.00 20.05 ATOM 4058 CE1 HIS B 673 18.532 -9.887 -39.979 1.00 18.61 ATOM 4059 NE2 HIS B 673 19.452 -10.611 -39.367 1.00 17.86 ATOM 4060 C HIS B 673 18.518 -15.218 -42.795 1.00 23.76 ATOM 4061 O HIS B 673 17.570 -15.878 -42.349 1.00 23.86 ATOM 4062 N SER B 674 19.018 -15.397 -44.018 1.00 24.99 ATOM 4063 CA SER B 674 18.468 -16.401 -44.931 1.00 26.09 ATOM 4064 CB SER B 674 19.125 -16.280 -46.311 1.00 25.24 ATOM 4065 OG SER B 674 20.372 -16.945 -46.330 1.00 25.27 ATOM 4066 C SER B 674 18.683 -17.803 -44.364 1.00 27.17 ATOM 4067 O SER B 674 18.065 -18.766 -44.819 1.00 27.85 ATOM 4068 N PHE B 675 19.569 -17.906 -43.378 1.00 27.62 ATOM 4069 CA PHE B 675 19.861 -19.171 -42.706 1.00 28.12 ATOM 4070 CB PHE B 675 21.363 -19.323 -42.456 1.00 29.88 ATOM 4071 CG PHE B 675 22.163 -19.578 -43.692 1.00 32.59 ATOM 4072 CD1 PHE B 675 22.173 -20.839 -44.283 1.00 33.41 ATOM 4073 CD2 PHE B 675 22.904 -18.557 -44.272 1.00 33.05 ATOM 4074 CE1 PHE B 675 22.913 -21.077 -45.441 1.00 34.57 ATOM 4075 CE2 PHE B 675 23.649 -18.781 -45.431 1.00 34.49 ATOM 4076 CZ PHE B 675 23.654 -20.042 -46.017 1.00 34.60 ATOM 4077 C PHE B 675 19.156 -19.192 -41.351 1.00 27.71 ATOM 4078 O PHE B 675 19.271 -20.158 -40.601 1.00 28.36 ATOM 4079 N GLY B 676 18.440 -18.116 -41.035 1.00 27.55 ATOM 4080 CA GLY B 676 17.756 -18.034 -39.754 1.00 26.78 ATOM 4081 C GLY B 676 18.690 -17.574 -38.639 1.00 26.60 ATOM 4082 O GLY B 676 18.311 -17.559 -37.461 1.00 26.46 ATOM 4083 N ILE B 677 19.912 -17.193 -39.007 1.00 25.07 ATOM 4084 CA ILE B 677 20.899 -16.738 -38.030 1.00 24.08 ATOM 4085 CB ILE B 677 22.339 -17.076 -38.497 1.00 24.56 ATOM 4086 CG2 ILE B 677 23.370 -16.484 -37.533 1.00 23.01 ATOM 4087 CG1 ILE B 677 22.517 -18.592 -38.569 1.00 24.51 ATOM 4088 CD1 ILE B 677 23.675 -19.014 -39.425 1.00 25.94 ATOM 4089 C ILE B 677 20.806 -15.227 -37.773 1.00 23.58 ATOM 4090 O ILE B 677 20.861 -14.423 -38.705 1.00 22.78 ATOM 4091 N CYS B 678 20.650 -14.856 -36.502 1.00 22.17 ATOM 4092 CA CYS B 678 20.565 -13.451 -36.099 1.00 21.09 ATOM 4093 CB CYS B 678 19.423 -13.255 -35.098 1.00 20.41 ATOM 4094 SG CYS B 678 19.165 -11.538 -34.577 1.00 20.89 ATOM 4095 C CYS B 678 21.906 -13.108 -35.444 1.00 20.07 ATOM 4096 O CYS B 678 22.394 -13.862 -34.595 1.00 20.70 ATOM 4097 N HIS B 679 22.509 -11.988 -35.845 1.00 18.74 ATOM 4098 CA HIS B 679 23.809 -11.595 -35.296 1.00 18.14 ATOM 4099 CB HIS B 679 24.395 -10.427 -36.100 1.00 16.87 ATOM 4100 CG HIS B 679 25.764 -10.010 -35.648 1.00 18.24 ATOM 4101 CD2 HIS B 679 26.161 -9.242 -34.605 1.00 17.04 ATOM 4102 ND1 HIS B 679 26.914 -10.371 -36.315 1.00 19.04 ATOM 4103 CE1 HIS B 679 27.961 -9.843 -35.704 1.00 17.40 ATOM 4104 NE2 HIS B 679 27.530 -9.153 -34.664 1.00 18.30 ATOM 4105 C HIS B 679 23.710 -11.219 -33.813 1.00 17.52 ATOM 4106 O HIS B 679 24.535 -11.648 -33.010 1.00 17.33 ATOM 4107 N ARG B 680 22.701 -10.418 -33.472 1.00 17.44 ATOM 4108 CA ARG B 680 22.446 -9.980 -32.092 1.00 18.80 ATOM 4109 CB ARG B 680 22.263 -11.195 -31.170 1.00 18.19 ATOM 4110 CG ARG B 680 21.215 -12.187 -31.698 1.00 18.28 ATOM 4111 CD ARG B 680 20.587 -13.010 -30.585 1.00 17.88 ATOM 4112 NE ARG B 680 21.579 -13.843 -29.915 1.00 19.38 ATOM 4113 CZ ARG B 680 21.307 -14.660 -28.903 1.00 19.55 ATOM 4114 NH1 ARG B 680 20.069 -14.758 -28.435 1.00 20.96 ATOM 4115 NH2 ARG B 680 22.277 -15.377 -28.362 1.00 20.40 ATOM 4116 C ARG B 680 23.460 -9.014 -31.471 1.00 19.40 ATOM 4117 O ARG B 680 23.372 -8.701 -30.281 1.00 20.91 ATOM 4118 N ASP B 681 24.419 -8.539 -32.256 1.00 19.76 ATOM 4119 CA ASP B 681 25.381 -7.577 -31.733 1.00 19.48 ATOM 4120 CB ASP B 681 26.573 -8.279 -31.078 1.00 20.66 ATOM 4121 CG ASP B 681 27.368 -7.345 -30.155 1.00 22.63 ATOM 4122 OD1 ASP B 681 26.790 -6.336 -29.685 1.00 22.51 ATOM 4123 OD2 ASP B 681 28.565 -7.619 -29.904 1.00 23.13 ATOM 4124 C ASP B 681 25.877 -6.636 -32.822 1.00 18.80 ATOM 4125 O ASP B 681 27.071 -6.365 -32.916 1.00 18.76 ATOM 4126 N ILE B 682 24.959 -6.147 -33.649 1.00 18.00 ATOM 4127 CA ILE B 682 25.333 -5.222 -34.712 1.00 18.44 ATOM 4128 CB ILE B 682 24.180 -5.031 -35.725 1.00 17.89 ATOM 4129 CG2 ILE B 682 24.538 -3.943 -36.729 1.00 17.46 ATOM 4130 CG1 ILE B 682 23.883 -6.356 -36.436 1.00 17.58 ATOM 4131 CD1 ILE B 682 25.077 -6.946 -37.173 1.00 17.77 ATOM 4132 C ILE B 682 25.678 -3.866 -34.083 1.00 18.97 ATOM 4133 O ILE B 682 24.861 -3.270 -33.390 1.00 19.76 ATOM 4134 N LYS B 683 26.894 -3.397 -34.330 1.00 18.79 ATOM 4135 CA LYS B 683 27.382 -2.127 -33.797 1.00 19.53 ATOM 4136 CB LYS B 683 27.729 -2.271 -32.308 1.00 18.91 ATOM 4137 CG LYS B 683 28.916 -3.181 -32.034 1.00 19.87 ATOM 4138 CD LYS B 683 29.167 -3.384 -30.549 1.00 21.25 ATOM 4139 CE LYS B 683 30.325 -4.336 -30.332 1.00 21.75 ATOM 4140 NZ LYS B 683 30.268 -5.022 -29.010 1.00 25.25 ATOM 4141 C LYS B 683 28.627 -1.737 -34.598 1.00 19.64 ATOM 4142 O LYS B 683 29.257 -2.590 -35.212 1.00 19.33 ATOM 4143 N PRO B 684 28.995 -0.444 -34.601 1.00 20.45 ATOM 4144 CD PRO B 684 28.304 0.661 -33.915 1.00 20.57 ATOM 4145 CA PRO B 684 30.172 0.029 -35.345 1.00 20.88 ATOM 4146 CB PRO B 684 30.295 1.494 -34.922 1.00 21.36 ATOM 4147 CG PRO B 684 28.902 1.879 -34.557 1.00 21.32 ATOM 4148 C PRO B 684 31.474 -0.749 -35.130 1.00 21.17 ATOM 4149 O PRO B 684 32.244 -0.949 -36.070 1.00 20.45 ATOM 4150 N GLN B 685 31.721 -1.196 -33.905 1.00 21.52 ATOM 4151 CA GLN B 685 32.948 -1.934 -33.617 1.00 22.47 ATOM 4152 CB GLN B 685 33.157 -2.029 -32.101 1.00 25.81 ATOM 4153 CG GLN B 685 33.699 -0.736 -31.492 1.00 30.66 ATOM 4154 CD GLN B 685 33.248 -0.512 -30.058 1.00 34.53 ATOM 4155 OE1 GLN B 685 32.063 -0.637 -29.734 1.00 37.75 ATOM 4156 NE2 GLN B 685 34.196 -0.175 -29.187 1.00 35.76 ATOM 4157 C GLN B 685 32.995 -3.331 -34.240 1.00 21.25 ATOM 4158 O GLN B 685 34.058 -3.946 -34.316 1.00 21.85 ATOM 4159 N ASN B 686 31.844 -3.826 -34.685 1.00 20.00 ATOM 4160 CA ASN B 686 31.769 -5.147 -35.304 1.00 19.14 ATOM 4161 CB ASN B 686 30.575 -5.922 -34.738 1.00 18.85 ATOM 4162 CG ASN B 686 30.861 -6.488 -33.366 1.00 19.28 ATOM 4163 OD1 ASN B 686 32.019 -6.597 -32.971 1.00 20.56 ATOM 4164 ND2 ASN B 686 29.813 -6.840 -32.626 1.00 18.85 ATOM 4165 C ASN B 686 31.675 -5.060 -36.829 1.00 18.81 ATOM 4166 O ASN B 686 31.368 -6.045 -37.501 1.00 18.23 ATOM 4167 N LEU B 687 31.946 -3.875 -37.366 1.00 17.59 ATOM 4168 CA LEU B 687 31.914 -3.661 -38.802 1.00 17.92 ATOM 4169 CB LEU B 687 30.927 -2.540 -39.154 1.00 17.74 ATOM 4170 CG LEU B 687 29.527 -2.694 -38.548 1.00 17.16 ATOM 4171 CD1 LEU B 687 28.665 -1.462 -38.875 1.00 17.80 ATOM 4172 CD2 LEU B 687 28.871 -3.958 -39.094 1.00 17.99 ATOM 4173 C LEU B 687 33.329 -3.292 -39.252 1.00 19.35 ATOM 4174 O LEU B 687 33.785 -2.165 -39.050 1.00 18.95 ATOM 4175 N LEU B 688 34.030 -4.261 -39.834 1.00 19.88 ATOM 4176 CA LEU B 688 35.389 -4.041 -40.306 1.00 20.99 ATOM 4177 CB LEU B 688 36.126 -5.376 -40.411 1.00 21.00 ATOM 4178 CG LEU B 688 36.066 -6.261 -39.164 1.00 21.27 ATOM 4179 CD1 LEU B 688 36.773 -7.583 -39.447 1.00 21.77 ATOM 4180 CD2 LEU B 688 36.703 -5.543 -37.980 1.00 21.18 ATOM 4181 C LEU B 688 35.383 -3.336 -41.659 1.00 21.59 ATOM 4182 O LEU B 688 34.483 -3.541 -42.472 1.00 21.40 ATOM 4183 N LEU B 689 36.401 -2.514 -41.898 1.00 23.06 ATOM 4184 CA LEU B 689 36.500 -1.753 -43.140 1.00 25.27 ATOM 4185 CB LEU B 689 36.108 -0.286 -42.912 1.00 26.18 ATOM 4186 CG LEU B 689 34.684 0.145 -42.590 1.00 27.55 ATOM 4187 CD1 LEU B 689 34.689 1.622 -42.182 1.00 27.76 ATOM 4188 CD2 LEU B 689 33.804 -0.085 -43.808 1.00 28.14 ATOM 4189 C LEU B 689 37.895 -1.719 -43.726 1.00 26.27 ATOM 4190 O LEU B 689 38.884 -1.670 -43.003 1.00 25.10 ATOM 4191 N ASP B 690 37.957 -1.734 -45.050 1.00 28.89 ATOM 4192 CA ASP B 690 39.220 -1.587 -45.752 1.00 32.28 ATOM 4193 CB ASP B 690 39.424 -2.679 -46.793 1.00 34.33 ATOM 4194 CG ASP B 690 40.835 -2.684 -47.341 1.00 36.86 ATOM 4195 OD1 ASP B 690 41.230 -1.679 -47.964 1.00 37.95 ATOM 4196 OD2 ASP B 690 41.553 -3.684 -47.141 1.00 39.30 ATOM 4197 C ASP B 690 39.014 -0.232 -46.427 1.00 33.38 ATOM 4198 O ASP B 690 38.316 -0.129 -47.428 1.00 33.15 ATOM 4199 N PRO B 691 39.613 0.828 -45.867 1.00 35.60 ATOM 4200 CD PRO B 691 40.495 0.724 -44.689 1.00 36.57 ATOM 4201 CA PRO B 691 39.526 2.212 -46.354 1.00 36.62 ATOM 4202 CB PRO B 691 40.582 2.945 -45.532 1.00 37.33 ATOM 4203 CG PRO B 691 40.670 2.153 -44.266 1.00 37.40 ATOM 4204 C PRO B 691 39.732 2.432 -47.848 1.00 37.21 ATOM 4205 O PRO B 691 38.991 3.188 -48.480 1.00 37.78 ATOM 4206 N ASP B 692 40.734 1.766 -48.406 1.00 37.58 ATOM 4207 CA ASP B 692 41.063 1.910 -49.818 1.00 38.01 ATOM 4208 CB ASP B 692 42.420 1.262 -50.096 1.00 39.86 ATOM 4209 CG ASP B 692 43.560 1.975 -49.386 1.00 42.30 ATOM 4210 OD1 ASP B 692 44.611 1.331 -49.162 1.00 43.71 ATOM 4211 OD2 ASP B 692 43.406 3.175 -49.051 1.00 43.16 ATOM 4212 C ASP B 692 40.031 1.338 -50.773 1.00 36.92 ATOM 4213 O ASP B 692 39.660 1.982 -51.757 1.00 37.73 ATOM 4214 N THR B 693 39.569 0.130 -50.484 1.00 34.97 ATOM 4215 CA THR B 693 38.599 -0.530 -51.338 1.00 32.67 ATOM 4216 CB THR B 693 38.794 -2.058 -51.310 1.00 32.91 ATOM 4217 OG1 THR B 693 38.652 -2.538 -49.965 1.00 32.46 ATOM 4218 CG2 THR B 693 40.181 -2.423 -51.818 1.00 32.83 ATOM 4219 C THR B 693 37.164 -0.224 -50.940 1.00 31.20 ATOM 4220 O THR B 693 36.243 -0.488 -51.706 1.00 31.06 ATOM 4221 N ALA B 694 36.985 0.335 -49.747 1.00 29.22 ATOM 4222 CA ALA B 694 35.660 0.663 -49.226 1.00 27.89 ATOM 4223 CB ALA B 694 34.909 1.571 -50.202 1.00 27.76 ATOM 4224 C ALA B 694 34.840 -0.600 -48.950 1.00 26.75 ATOM 4225 O ALA B 694 33.616 -0.553 -48.889 1.00 27.16 ATOM 4226 N VAL B 695 35.522 -1.726 -48.784 1.00 25.73 ATOM 4227 CA VAL B 695 34.848 -2.987 -48.502 1.00 24.05 ATOM 4228 CB VAL B 695 35.716 -4.196 -48.922 1.00 24.27 ATOM 4229 CG1 VAL B 695 35.164 -5.478 -48.310 1.00 24.71 ATOM 4230 CG2 VAL B 695 35.736 -4.318 -50.442 1.00 24.40 ATOM 4231 C VAL B 695 34.556 -3.093 -47.010 1.00 23.09 ATOM 4232 O VAL B 695 35.401 -2.761 -46.170 1.00 22.78 ATOM 4233 N LEU B 696 33.348 -3.537 -46.683 1.00 21.74 ATOM 4234 CA LEU B 696 32.961 -3.709 -45.286 1.00 20.80 ATOM 4235 CB LEU B 696 31.674 -2.929 -44.981 1.00 19.95 ATOM 4236 CG LEU B 696 31.088 -3.116 -43.575 1.00 19.80 ATOM 4237 CD1 LEU B 696 30.326 -1.863 -43.176 1.00 19.12 ATOM 4238 CD2 LEU B 696 30.150 -4.327 -43.544 1.00 19.15 ATOM 4239 C LEU B 696 32.726 -5.198 -45.042 1.00 21.04 ATOM 4240 O LEU B 696 32.153 -5.887 -45.888 1.00 20.70 ATOM 4241 N LYS B 697 33.185 -5.695 -43.899 1.00 20.89 ATOM 4242 CA LYS B 697 32.990 -7.095 -43.552 1.00 20.67 ATOM 4243 CB LYS B 697 34.299 -7.878 -43.677 1.00 22.63 ATOM 4244 CG LYS B 697 34.694 -8.177 -45.123 1.00 24.54 ATOM 4245 CD LYS B 697 36.150 -8.584 -45.202 1.00 27.28 ATOM 4246 CE LYS B 697 36.611 -8.720 -46.647 1.00 28.49 ATOM 4247 NZ LYS B 697 35.547 -9.317 -47.519 1.00 31.50 ATOM 4248 C LYS B 697 32.473 -7.186 -42.128 1.00 20.39 ATOM 4249 O LYS B 697 33.066 -6.650 -41.194 1.00 19.91 ATOM 4250 N LEU B 698 31.351 -7.867 -41.972 1.00 20.29 ATOM 4251 CA LEU B 698 30.742 -8.056 -40.666 1.00 19.61 ATOM 4252 CB LEU B 698 29.307 -8.566 -40.851 1.00 18.50 ATOM 4253 CG LEU B 698 28.471 -8.940 -39.627 1.00 18.76 ATOM 4254 CD1 LEU B 698 28.226 -7.712 -38.750 1.00 17.60 ATOM 4255 CD2 LEU B 698 27.145 -9.529 -40.100 1.00 18.66 ATOM 4256 C LEU B 698 31.582 -9.069 -39.890 1.00 19.71 ATOM 4257 O LEU B 698 32.064 -10.048 -40.461 1.00 20.14 ATOM 4258 N CYS B 699 31.785 -8.825 -38.598 1.00 19.33 ATOM 4259 CA CYS B 699 32.556 -9.756 -37.781 1.00 20.06 ATOM 4260 CB CYS B 699 33.996 -9.255 -37.578 1.00 20.41 ATOM 4261 SG CYS B 699 34.224 -7.903 -36.370 1.00 23.61 ATOM 4262 C CYS B 699 31.898 -9.996 -36.430 1.00 20.17 ATOM 4263 O CYS B 699 30.810 -9.490 -36.161 1.00 19.38 ATOM 4264 N ASP B 700 32.572 -10.787 -35.600 1.00 20.45 ATOM 4265 CA ASP B 700 32.124 -11.126 -34.248 1.00 21.21 ATOM 4266 CB ASP B 700 32.044 -9.872 -33.380 1.00 21.72 ATOM 4267 CG ASP B 700 31.734 -10.196 -31.927 1.00 23.25 ATOM 4268 OD1 ASP B 700 31.702 -11.392 -31.577 1.00 22.45 ATOM 4269 OD2 ASP B 700 31.519 -9.263 -31.133 1.00 24.97 ATOM 4270 C ASP B 700 30.799 -11.869 -34.158 1.00 21.26 ATOM 4271 O ASP B 700 29.756 -11.273 -33.881 1.00 21.72 ATOM 4272 N PHE B 701 30.845 -13.181 -34.359 1.00 21.03 ATOM 4273 CA PHE B 701 29.637 -13.980 -34.282 1.00 20.80 ATOM 4274 CB PHE B 701 29.623 -14.997 -35.421 1.00 20.26 ATOM 4275 CG PHE B 701 29.383 -14.362 -36.755 1.00 21.02 ATOM 4276 CD1 PHE B 701 30.430 -13.772 -37.452 1.00 20.35 ATOM 4277 CD2 PHE B 701 28.093 -14.265 -37.272 1.00 20.29 ATOM 4278 CE1 PHE B 701 30.198 -13.086 -38.642 1.00 21.25 ATOM 4279 CE2 PHE B 701 27.855 -13.578 -38.463 1.00 20.75 ATOM 4280 CZ PHE B 701 28.912 -12.987 -39.145 1.00 20.04 ATOM 4281 C PHE B 701 29.508 -14.648 -32.922 1.00 21.45 ATOM 4282 O PHE B 701 28.864 -15.691 -32.780 1.00 21.73 ATOM 4283 N GLY B 702 30.103 -14.011 -31.918 1.00 21.54 ATOM 4284 CA GLY B 702 30.061 -14.536 -30.565 1.00 21.81 ATOM 4285 C GLY B 702 28.714 -14.448 -29.872 1.00 22.27 ATOM 4286 O GLY B 702 28.535 -15.069 -28.829 1.00 23.26 ATOM 4287 N SER B 703 27.774 -13.678 -30.426 1.00 22.39 ATOM 4288 CA SER B 703 26.429 -13.537 -29.846 1.00 22.56 ATOM 4289 CB SER B 703 26.080 -12.063 -29.608 1.00 22.92 ATOM 4290 OG SER B 703 26.894 -11.468 -28.615 1.00 23.81 ATOM 4291 C SER B 703 25.389 -14.101 -30.807 1.00 22.75 ATOM 4292 O SER B 703 24.208 -14.194 -30.474 1.00 22.71 ATOM 4293 N ALA B 704 25.839 -14.463 -32.005 1.00 22.89 ATOM 4294 CA ALA B 704 24.962 -14.981 -33.045 1.00 24.03 ATOM 4295 CB ALA B 704 25.756 -15.160 -34.344 1.00 22.38 ATOM 4296 C ALA B 704 24.261 -16.284 -32.667 1.00 24.93 ATOM 4297 O ALA B 704 24.815 -17.127 -31.960 1.00 24.91 ATOM 4298 N LYS B 705 23.037 -16.442 -33.149 1.00 26.47 ATOM 4299 CA LYS B 705 22.266 -17.639 -32.856 1.00 28.24 ATOM 4300 CB LYS B 705 21.705 -17.552 -31.438 1.00 28.98 ATOM 4301 CG LYS B 705 20.962 -18.787 -30.971 1.00 30.40 ATOM 4302 CD LYS B 705 20.533 -18.614 -29.522 1.00 32.14 ATOM 4303 CE LYS B 705 19.940 -19.891 -28.953 1.00 32.77 ATOM 4304 NZ LYS B 705 18.539 -20.043 -29.400 1.00 33.75 ATOM 4305 C LYS B 705 21.124 -17.814 -33.840 1.00 29.04 ATOM 4306 O LYS B 705 20.533 -16.842 -34.307 1.00 27.91 ATOM 4307 N GLN B 706 20.820 -19.065 -34.161 1.00 30.46 ATOM 4308 CA GLN B 706 19.722 -19.352 -35.066 1.00 32.45 ATOM 4309 CB GLN B 706 19.838 -20.771 -35.609 1.00 34.05 ATOM 4310 CG GLN B 706 18.516 -21.322 -36.090 1.00 37.83 ATOM 4311 CD GLN B 706 18.686 -22.364 -37.164 1.00 39.60 ATOM 4312 OE1 GLN B 706 19.531 -23.253 -37.049 1.00 40.34 ATOM 4313 NE2 GLN B 706 17.883 -22.263 -38.223 1.00 40.86 ATOM 4314 C GLN B 706 18.424 -19.201 -34.278 1.00 32.40 ATOM 4315 O GLN B 706 18.200 -19.905 -33.295 1.00 32.78 ATOM 4316 N LEU B 707 17.573 -18.280 -34.704 1.00 32.48 ATOM 4317 CA LEU B 707 16.323 -18.051 -34.009 1.00 33.44 ATOM 4318 CB LEU B 707 15.910 -16.585 -34.134 1.00 32.86 ATOM 4319 CG LEU B 707 16.901 -15.527 -33.628 1.00 32.16 ATOM 4320 CD1 LEU B 707 16.223 -14.167 -33.657 1.00 32.08 ATOM 4321 CD2 LEU B 707 17.377 -15.860 -32.220 1.00 31.23 ATOM 4322 C LEU B 707 15.226 -18.942 -34.565 1.00 35.29 ATOM 4323 O LEU B 707 14.895 -18.868 -35.751 1.00 35.71 ATOM 4324 N VAL B 708 14.673 -19.787 -33.698 1.00 36.53 ATOM 4325 CA VAL B 708 13.601 -20.700 -34.073 1.00 37.71 ATOM 4326 CB VAL B 708 13.910 -22.138 -33.622 1.00 37.88 ATOM 4327 CG1 VAL B 708 12.866 -23.091 -34.184 1.00 37.97 ATOM 4328 CG2 VAL B 708 15.303 -22.540 -34.080 1.00 37.24 ATOM 4329 C VAL B 708 12.302 -20.259 -33.419 1.00 38.61 ATOM 4330 O VAL B 708 12.214 -20.174 -32.196 1.00 38.52 ATOM 4331 N ARG B 709 11.301 -19.969 -34.240 1.00 40.16 ATOM 4332 CA ARG B 709 10.000 -19.539 -33.743 1.00 41.77 ATOM 4333 CB ARG B 709 8.984 -19.542 -34.888 1.00 43.89 ATOM 4334 CG ARG B 709 7.635 -18.937 -34.544 1.00 46.86 ATOM 4335 CD ARG B 709 6.724 -18.917 -35.767 1.00 50.55 ATOM 4336 NE ARG B 709 6.519 -20.255 -36.329 1.00 54.11 ATOM 4337 CZ ARG B 709 5.685 -20.535 -37.332 1.00 55.40 ATOM 4338 NH1 ARG B 709 4.968 -19.569 -37.898 1.00 55.86 ATOM 4339 NH2 ARG B 709 5.566 -21.784 -37.771 1.00 55.94 ATOM 4340 C ARG B 709 9.546 -20.481 -32.632 1.00 41.90 ATOM 4341 O ARG B 709 9.742 -21.695 -32.715 1.00 42.11 ATOM 4342 N GLY B 710 8.956 -19.918 -31.584 1.00 41.69 ATOM 4343 CA GLY B 710 8.496 -20.734 -30.478 1.00 41.58 ATOM 4344 C GLY B 710 9.568 -20.982 -29.432 1.00 41.59 ATOM 4345 O GLY B 710 9.273 -21.409 -28.313 1.00 42.23 ATOM 4346 N GLU B 711 10.821 -20.726 -29.789 1.00 40.84 ATOM 4347 CA GLU B 711 11.919 -20.919 -28.850 1.00 39.84 ATOM 4348 CB GLU B 711 13.144 -21.467 -29.574 1.00 41.60 ATOM 4349 CG GLU B 711 13.132 -22.954 -29.823 1.00 43.94 ATOM 4350 CD GLU B 711 14.380 -23.400 -30.566 1.00 45.50 ATOM 4351 OE1 GLU B 711 15.402 -22.676 -30.491 1.00 45.79 ATOM 4352 OE2 GLU B 711 14.337 -24.465 -31.223 1.00 46.76 ATOM 4353 C GLU B 711 12.278 -19.580 -28.208 1.00 38.12 ATOM 4354 O GLU B 711 12.437 -18.572 -28.899 1.00 37.68 ATOM 4355 N PRO B 712 12.408 -19.551 -26.874 1.00 36.45 ATOM 4356 CD PRO B 712 12.229 -20.664 -25.923 1.00 35.70 ATOM 4357 CA PRO B 712 12.753 -18.294 -26.197 1.00 34.87 ATOM 4358 CB PRO B 712 12.334 -18.545 -24.752 1.00 34.59 ATOM 4359 CG PRO B 712 12.499 -20.028 -24.579 1.00 35.52 ATOM 4360 C PRO B 712 14.243 -17.966 -26.310 1.00 33.11 ATOM 4361 O PRO B 712 15.078 -18.862 -26.388 1.00 32.72 ATOM 4362 N ASN B 713 14.575 -16.680 -26.331 1.00 31.38 ATOM 4363 CA ASN B 713 15.975 -16.278 -26.407 1.00 30.31 ATOM 4364 CB ASN B 713 16.328 -15.873 -27.836 1.00 30.48 ATOM 4365 CG ASN B 713 16.367 -17.064 -28.777 1.00 30.43 ATOM 4366 OD1 ASN B 713 17.254 -17.914 -28.687 1.00 30.62 ATOM 4367 ND2 ASN B 713 15.398 -17.134 -29.678 1.00 30.58 ATOM 4368 C ASN B 713 16.220 -15.130 -25.434 1.00 28.83 ATOM 4369 O ASN B 713 15.323 -14.329 -25.184 1.00 28.44 ATOM 4370 N VAL B 714 17.428 -15.061 -24.883 1.00 28.03 ATOM 4371 CA VAL B 714 17.759 -14.021 -23.906 1.00 27.76 ATOM 4372 CB VAL B 714 19.161 -14.228 -23.315 1.00 27.22 ATOM 4373 CG1 VAL B 714 19.208 -15.561 -22.621 1.00 26.65 ATOM 4374 CG2 VAL B 714 20.224 -14.138 -24.397 1.00 27.23 ATOM 4375 C VAL B 714 17.656 -12.610 -24.451 1.00 27.88 ATOM 4376 O VAL B 714 17.982 -12.350 -25.608 1.00 27.50 ATOM 4377 N SER B 715 17.191 -11.691 -23.613 1.00 27.49 ATOM 4378 CA SER B 715 17.048 -10.319 -24.056 1.00 26.86 ATOM 4379 CB SER B 715 15.710 -9.750 -23.585 1.00 27.82 ATOM 4380 OG SER B 715 15.663 -9.699 -22.176 1.00 29.73 ATOM 4381 C SER B 715 18.181 -9.424 -23.585 1.00 25.78 ATOM 4382 O SER B 715 18.103 -8.212 -23.738 1.00 27.06 ATOM 4383 N TYR B 716 19.236 -9.998 -23.019 1.00 24.63 ATOM 4384 CA TYR B 716 20.341 -9.160 -22.560 1.00 24.63 ATOM 4385 CB TYR B 716 20.824 -9.584 -21.162 1.00 25.42 ATOM 4386 CG TYR B 716 21.143 -11.051 -21.005 1.00 27.13 ATOM 4387 CD1 TYR B 716 22.373 -11.571 -21.407 1.00 28.36 ATOM 4388 CE1 TYR B 716 22.683 -12.921 -21.216 1.00 28.68 ATOM 4389 CD2 TYR B 716 20.230 -11.912 -20.417 1.00 28.31 ATOM 4390 CE2 TYR B 716 20.526 -13.253 -20.223 1.00 29.33 ATOM 4391 CZ TYR B 716 21.750 -13.749 -20.620 1.00 30.03 ATOM 4392 OH TYR B 716 22.032 -15.078 -20.398 1.00 32.28 ATOM 4393 C TYR B 716 21.523 -9.107 -23.526 1.00 23.82 ATOM 4394 O TYR B 716 22.641 -8.752 -23.141 1.00 23.92 ATOM 4395 N ILE B 717 21.279 -9.467 -24.783 1.00 23.12 ATOM 4396 CA ILE B 717 22.329 -9.402 -25.790 1.00 22.59 ATOM 4397 CB ILE B 717 22.159 -10.497 -26.903 1.00 22.28 ATOM 4398 CG2 ILE B 717 22.903 -11.763 -26.497 1.00 22.07 ATOM 4399 CG1 ILE B 717 20.677 -10.801 -27.157 1.00 21.83 ATOM 4400 CD1 ILE B 717 19.941 -9.746 -27.935 1.00 20.34 ATOM 4401 C ILE B 717 22.254 -8.017 -26.438 1.00 22.41 ATOM 4402 O ILE B 717 21.337 -7.233 -26.150 1.00 21.17 ATOM 4403 N CYS B 718 23.220 -7.728 -27.306 1.00 22.28 ATOM 4404 CA CYS B 718 23.296 -6.464 -28.030 1.00 23.80 ATOM 4405 CB CYS B 718 21.943 -6.107 -28.641 1.00 23.47 ATOM 4406 SG CYS B 718 22.106 -5.029 -30.073 1.00 26.20 ATOM 4407 C CYS B 718 23.790 -5.298 -27.189 1.00 24.71 ATOM 4408 O CYS B 718 23.394 -5.138 -26.044 1.00 24.83 ATOM 4409 N SER B 719 24.653 -4.476 -27.777 1.00 25.92 ATOM 4410 CA SER B 719 25.220 -3.335 -27.079 1.00 26.86 ATOM 4411 CB SER B 719 26.487 -2.889 -27.791 1.00 27.71 ATOM 4412 OG SER B 719 27.398 -3.968 -27.813 1.00 33.06 ATOM 4413 C SER B 719 24.278 -2.155 -26.928 1.00 26.85 ATOM 4414 O SER B 719 23.507 -1.838 -27.834 1.00 25.69 ATOM 4415 N ARG B 720 24.347 -1.510 -25.768 1.00 28.23 ATOM 4416 CA ARG B 720 23.517 -0.346 -25.489 1.00 30.84 ATOM 4417 CB ARG B 720 23.879 0.257 -24.122 1.00 34.41 ATOM 4418 CG ARG B 720 25.267 0.883 -24.056 1.00 39.03 ATOM 4419 CD ARG B 720 25.419 1.806 -22.840 1.00 44.03 ATOM 4420 NE ARG B 720 26.488 2.785 -23.048 1.00 47.69 ATOM 4421 CZ ARG B 720 26.722 3.826 -22.253 1.00 49.51 ATOM 4422 NH1 ARG B 720 27.721 4.661 -22.529 1.00 50.09 ATOM 4423 NH2 ARG B 720 25.963 4.032 -21.180 1.00 50.66 ATOM 4424 C ARG B 720 23.728 0.691 -26.591 1.00 29.98 ATOM 4425 O ARG B 720 24.837 0.858 -27.103 1.00 32.15 ATOM 4426 N TYR B 721 22.652 1.385 -26.929 1.00 28.63 ATOM 4427 CA TYR B 721 22.594 2.395 -27.985 1.00 26.95 ATOM 4428 CB TYR B 721 23.970 2.980 -28.355 1.00 28.78 ATOM 4429 CG TYR B 721 24.634 3.870 -27.322 1.00 30.95 ATOM 4430 CD1 TYR B 721 24.231 3.859 -25.983 1.00 31.80 ATOM 4431 CE1 TYR B 721 24.908 4.617 -25.022 1.00 33.34 ATOM 4432 CD2 TYR B 721 25.725 4.668 -27.677 1.00 32.13 ATOM 4433 CE2 TYR B 721 26.407 5.426 -26.729 1.00 32.34 ATOM 4434 CZ TYR B 721 25.997 5.396 -25.408 1.00 33.67 ATOM 4435 OH TYR B 721 26.693 6.129 -24.468 1.00 35.72 ATOM 4436 C TYR B 721 22.023 1.727 -29.232 1.00 24.18 ATOM 4437 O TYR B 721 21.260 2.342 -29.959 1.00 23.62 ATOM 4438 N TYR B 722 22.396 0.466 -29.465 1.00 22.34 ATOM 4439 CA TYR B 722 21.952 -0.270 -30.657 1.00 21.08 ATOM 4440 CB TYR B 722 23.172 -0.923 -31.335 1.00 19.95 ATOM 4441 CG TYR B 722 24.294 0.064 -31.525 1.00 19.96 ATOM 4442 CD1 TYR B 722 24.247 1.003 -32.556 1.00 18.95 ATOM 4443 CE1 TYR B 722 25.203 2.006 -32.667 1.00 19.44 ATOM 4444 CD2 TYR B 722 25.346 0.143 -30.605 1.00 19.85 ATOM 4445 CE2 TYR B 722 26.317 1.151 -30.705 1.00 20.49 ATOM 4446 CZ TYR B 722 26.234 2.081 -31.734 1.00 20.02 ATOM 4447 OH TYR B 722 27.156 3.109 -31.812 1.00 21.14 ATOM 4448 C TYR B 722 20.859 -1.315 -30.418 1.00 20.85 ATOM 4449 O TYR B 722 20.448 -1.999 -31.348 1.00 19.93 ATOM 4450 N ARG B 723 20.380 -1.413 -29.182 1.00 21.01 ATOM 4451 CA ARG B 723 19.334 -2.372 -28.805 1.00 21.97 ATOM 4452 CB ARG B 723 19.270 -2.497 -27.282 1.00 24.17 ATOM 4453 CG ARG B 723 20.377 -3.289 -26.666 1.00 27.96 ATOM 4454 CD ARG B 723 20.501 -2.965 -25.187 1.00 31.18 ATOM 4455 NE ARG B 723 19.383 -3.457 -24.381 1.00 34.23 ATOM 4456 CZ ARG B 723 19.088 -4.745 -24.193 1.00 35.36 ATOM 4457 NH1 ARG B 723 19.822 -5.695 -24.757 1.00 35.41 ATOM 4458 NH2 ARG B 723 18.074 -5.085 -23.404 1.00 36.11 ATOM 4459 C ARG B 723 17.934 -1.996 -29.289 1.00 21.40 ATOM 4460 O ARG B 723 17.489 -0.866 -29.086 1.00 20.56 ATOM 4461 N ALA B 724 17.233 -2.951 -29.903 1.00 20.99 ATOM 4462 CA ALA B 724 15.867 -2.718 -30.371 1.00 20.81 ATOM 4463 CB ALA B 724 15.366 -3.925 -31.180 1.00 20.41 ATOM 4464 C ALA B 724 14.993 -2.515 -29.130 1.00 20.61 ATOM 4465 O ALA B 724 15.278 -3.068 -28.072 1.00 20.59 ATOM 4466 N PRO B 725 13.914 -1.725 -29.248 1.00 21.23 ATOM 4467 CD PRO B 725 13.474 -1.031 -30.474 1.00 21.42 ATOM 4468 CA PRO B 725 13.023 -1.466 -28.108 1.00 21.60 ATOM 4469 CB PRO B 725 11.945 -0.541 -28.675 1.00 21.62 ATOM 4470 CG PRO B 725 12.066 -0.639 -30.163 1.00 22.27 ATOM 4471 C PRO B 725 12.432 -2.715 -27.464 1.00 22.35 ATOM 4472 O PRO B 725 12.187 -2.725 -26.258 1.00 22.48 ATOM 4473 N GLU B 726 12.200 -3.767 -28.250 1.00 22.57 ATOM 4474 CA GLU B 726 11.648 -5.005 -27.689 1.00 22.43 ATOM 4475 CB GLU B 726 11.181 -5.966 -28.803 1.00 22.13 ATOM 4476 CG GLU B 726 12.260 -6.432 -29.777 1.00 22.87 ATOM 4477 CD GLU B 726 12.291 -5.610 -31.055 1.00 23.28 ATOM 4478 OE1 GLU B 726 12.016 -4.390 -30.981 1.00 22.93 ATOM 4479 OE2 GLU B 726 12.592 -6.181 -32.130 1.00 23.54 ATOM 4480 C GLU B 726 12.670 -5.688 -26.772 1.00 22.33 ATOM 4481 O GLU B 726 12.300 -6.414 -25.840 1.00 22.09 ATOM 4482 N LEU B 727 13.956 -5.455 -27.022 1.00 21.69 ATOM 4483 CA LEU B 727 14.989 -6.027 -26.163 1.00 21.57 ATOM 4484 CB LEU B 727 16.367 -5.929 -26.824 1.00 21.34 ATOM 4485 CG LEU B 727 16.594 -6.816 -28.052 1.00 21.09 ATOM 4486 CD1 LEU B 727 18.065 -6.731 -28.460 1.00 21.34 ATOM 4487 CD2 LEU B 727 16.212 -8.258 -27.738 1.00 21.25 ATOM 4488 C LEU B 727 14.999 -5.239 -24.853 1.00 21.93 ATOM 4489 O LEU B 727 15.120 -5.811 -23.766 1.00 22.22 ATOM 4490 N ILE B 728 14.881 -3.920 -24.970 1.00 22.01 ATOM 4491 CA ILE B 728 14.865 -3.048 -23.801 1.00 22.11 ATOM 4492 CB ILE B 728 14.747 -1.559 -24.212 1.00 21.32 ATOM 4493 CG2 ILE B 728 14.683 -0.657 -22.962 1.00 21.52 ATOM 4494 CG1 ILE B 728 15.955 -1.163 -25.067 1.00 21.31 ATOM 4495 CD1 ILE B 728 15.851 0.247 -25.640 1.00 21.71 ATOM 4496 C ILE B 728 13.681 -3.447 -22.932 1.00 23.18 ATOM 4497 O ILE B 728 13.785 -3.472 -21.709 1.00 23.52 ATOM 4498 N PHE B 729 12.564 -3.780 -23.575 1.00 24.61 ATOM 4499 CA PHE B 729 11.352 -4.199 -22.867 1.00 26.37 ATOM 4500 CB PHE B 729 10.129 -4.037 -23.769 1.00 27.17 ATOM 4501 CG PHE B 729 9.641 -2.620 -23.887 1.00 28.55 ATOM 4502 CD1 PHE B 729 9.434 -2.046 -25.135 1.00 29.36 ATOM 4503 CD2 PHE B 729 9.352 -1.869 -22.753 1.00 29.87 ATOM 4504 CE1 PHE B 729 8.942 -0.741 -25.258 1.00 28.91 ATOM 4505 CE2 PHE B 729 8.857 -0.565 -22.866 1.00 30.04 ATOM 4506 CZ PHE B 729 8.653 -0.005 -24.123 1.00 29.79 ATOM 4507 C PHE B 729 11.415 -5.646 -22.372 1.00 27.16 ATOM 4508 O PHE B 729 10.425 -6.173 -21.871 1.00 28.60 ATOM 4509 N GLY B 730 12.561 -6.296 -22.536 1.00 27.87 ATOM 4510 CA GLY B 730 12.718 -7.664 -22.064 1.00 27.99 ATOM 4511 C GLY B 730 12.059 -8.795 -22.840 1.00 28.76 ATOM 4512 O GLY B 730 11.788 -9.854 -22.270 1.00 28.86 ATOM 4513 N ALA B 731 11.797 -8.604 -24.130 1.00 28.86 ATOM 4514 CA ALA B 731 11.171 -9.667 -24.919 1.00 28.65 ATOM 4515 CB ALA B 731 10.686 -9.115 -26.260 1.00 28.78 ATOM 4516 C ALA B 731 12.135 -10.827 -25.154 1.00 28.53 ATOM 4517 O ALA B 731 13.341 -10.622 -25.298 1.00 28.58 ATOM 4518 N THR B 732 11.600 -12.047 -25.181 1.00 28.38 ATOM 4519 CA THR B 732 12.411 -13.240 -25.424 1.00 28.55 ATOM 4520 CB THR B 732 12.360 -14.226 -24.235 1.00 29.27 ATOM 4521 OG1 THR B 732 11.018 -14.698 -24.060 1.00 29.63 ATOM 4522 CG2 THR B 732 12.834 -13.543 -22.958 1.00 29.43 ATOM 4523 C THR B 732 11.920 -13.966 -26.682 1.00 28.33 ATOM 4524 O THR B 732 12.435 -15.024 -27.044 1.00 28.13 ATOM 4525 N ASP B 733 10.923 -13.377 -27.335 1.00 28.26 ATOM 4526 CA ASP B 733 10.336 -13.929 -28.552 1.00 29.06 ATOM 4527 CB ASP B 733 8.815 -14.033 -28.402 1.00 30.46 ATOM 4528 CG ASP B 733 8.141 -12.673 -28.354 1.00 32.97 ATOM 4529 OD1 ASP B 733 8.780 -11.698 -27.894 1.00 34.48 ATOM 4530 OD2 ASP B 733 6.971 -12.570 -28.778 1.00 34.69 ATOM 4531 C ASP B 733 10.665 -13.037 -29.751 1.00 28.24 ATOM 4532 O ASP B 733 9.917 -12.994 -30.736 1.00 28.03 ATOM 4533 N TYR B 734 11.783 -12.326 -29.666 1.00 26.75 ATOM 4534 CA TYR B 734 12.180 -11.437 -30.750 1.00 25.75 ATOM 4535 CB TYR B 734 13.258 -10.455 -30.268 1.00 24.22 ATOM 4536 CG TYR B 734 14.489 -11.120 -29.688 1.00 23.17 ATOM 4537 CD1 TYR B 734 15.527 -11.549 -30.513 1.00 22.93 ATOM 4538 CE1 TYR B 734 16.667 -12.159 -29.979 1.00 22.30 ATOM 4539 CD2 TYR B 734 14.615 -11.316 -28.307 1.00 22.81 ATOM 4540 CE2 TYR B 734 15.745 -11.922 -27.763 1.00 22.14 ATOM 4541 CZ TYR B 734 16.767 -12.340 -28.601 1.00 21.70 ATOM 4542 OH TYR B 734 17.892 -12.928 -28.068 1.00 22.34 ATOM 4543 C TYR B 734 12.676 -12.219 -31.966 1.00 25.41 ATOM 4544 O TYR B 734 12.976 -13.412 -31.879 1.00 24.25 ATOM 4545 N THR B 735 12.764 -11.519 -33.095 1.00 25.52 ATOM 4546 CA THR B 735 13.198 -12.098 -34.359 1.00 24.86 ATOM 4547 CB THR B 735 12.104 -11.939 -35.419 1.00 25.34 ATOM 4548 OG1 THR B 735 11.963 -10.551 -35.749 1.00 25.89 ATOM 4549 CG2 THR B 735 10.771 -12.440 -34.880 1.00 25.34 ATOM 4550 C THR B 735 14.472 -11.423 -34.879 1.00 24.66 ATOM 4551 O THR B 735 15.090 -10.610 -34.192 1.00 24.20 ATOM 4552 N SER B 736 14.847 -11.761 -36.106 1.00 23.43 ATOM 4553 CA SER B 736 16.044 -11.208 -36.721 1.00 23.19 ATOM 4554 CB SER B 736 16.344 -11.957 -38.021 1.00 24.10 ATOM 4555 OG SER B 736 16.840 -13.254 -37.732 1.00 26.24 ATOM 4556 C SER B 736 15.915 -9.721 -36.997 1.00 22.02 ATOM 4557 O SER B 736 16.909 -9.045 -37.268 1.00 21.74 ATOM 4558 N SER B 737 14.695 -9.200 -36.924 1.00 21.26 ATOM 4559 CA SER B 737 14.500 -7.788 -37.180 1.00 20.80 ATOM 4560 CB SER B 737 13.014 -7.449 -37.279 1.00 21.71 ATOM 4561 OG SER B 737 12.366 -7.601 -36.031 1.00 23.86 ATOM 4562 C SER B 737 15.179 -6.923 -36.115 1.00 20.71 ATOM 4563 O SER B 737 15.194 -5.704 -36.246 1.00 20.93 ATOM 4564 N ILE B 738 15.726 -7.527 -35.057 1.00 19.35 ATOM 4565 CA ILE B 738 16.423 -6.703 -34.067 1.00 18.60 ATOM 4566 CB ILE B 738 16.744 -7.451 -32.739 1.00 17.88 ATOM 4567 CG2 ILE B 738 15.439 -7.837 -32.039 1.00 18.18 ATOM 4568 CG1 ILE B 738 17.654 -8.653 -32.988 1.00 18.07 ATOM 4569 CD1 ILE B 738 18.388 -9.147 -31.719 1.00 18.38 ATOM 4570 C ILE B 738 17.733 -6.238 -34.712 1.00 18.36 ATOM 4571 O ILE B 738 18.258 -5.183 -34.368 1.00 18.26 ATOM 4572 N ASP B 739 18.252 -7.021 -35.658 1.00 17.89 ATOM 4573 CA ASP B 739 19.491 -6.646 -36.353 1.00 17.91 ATOM 4574 CB ASP B 739 20.013 -7.790 -37.223 1.00 17.97 ATOM 4575 CG ASP B 739 20.757 -8.853 -36.435 1.00 17.94 ATOM 4576 OD1 ASP B 739 20.938 -9.949 -37.002 1.00 18.30 ATOM 4577 OD2 ASP B 739 21.159 -8.617 -35.274 1.00 16.10 ATOM 4578 C ASP B 739 19.219 -5.451 -37.264 1.00 17.93 ATOM 4579 O ASP B 739 20.105 -4.621 -37.504 1.00 17.70 ATOM 4580 N VAL B 740 17.998 -5.368 -37.788 1.00 17.91 ATOM 4581 CA VAL B 740 17.646 -4.266 -38.672 1.00 17.70 ATOM 4582 CB VAL B 740 16.324 -4.537 -39.411 1.00 18.01 ATOM 4583 CG1 VAL B 740 15.895 -3.303 -40.213 1.00 18.03 ATOM 4584 CG2 VAL B 740 16.508 -5.726 -40.339 1.00 18.51 ATOM 4585 C VAL B 740 17.557 -2.976 -37.875 1.00 17.52 ATOM 4586 O VAL B 740 17.996 -1.929 -38.349 1.00 16.84 ATOM 4587 N TRP B 741 16.995 -3.042 -36.666 1.00 17.13 ATOM 4588 CA TRP B 741 16.915 -1.839 -35.822 1.00 17.16 ATOM 4589 CB TRP B 741 16.237 -2.144 -34.468 1.00 17.63 ATOM 4590 CG TRP B 741 16.281 -0.987 -33.478 1.00 17.49 ATOM 4591 CD2 TRP B 741 15.274 0.021 -33.270 1.00 17.85 ATOM 4592 CE2 TRP B 741 15.771 0.912 -32.285 1.00 18.06 ATOM 4593 CE3 TRP B 741 14.005 0.260 -33.818 1.00 18.33 ATOM 4594 CD1 TRP B 741 17.310 -0.674 -32.632 1.00 17.03 ATOM 4595 NE1 TRP B 741 17.011 0.464 -31.915 1.00 17.73 ATOM 4596 CZ2 TRP B 741 15.042 2.027 -31.835 1.00 17.64 ATOM 4597 CZ3 TRP B 741 13.278 1.374 -33.370 1.00 20.03 ATOM 4598 CH2 TRP B 741 13.806 2.241 -32.387 1.00 19.15 ATOM 4599 C TRP B 741 18.346 -1.339 -35.574 1.00 16.88 ATOM 4600 O TRP B 741 18.635 -0.153 -35.751 1.00 17.24 ATOM 4601 N SER B 742 19.236 -2.250 -35.183 1.00 16.58 ATOM 4602 CA SER B 742 20.633 -1.899 -34.915 1.00 16.79 ATOM 4603 CB SER B 742 21.427 -3.136 -34.500 1.00 16.84 ATOM 4604 OG SER B 742 20.805 -3.804 -33.409 1.00 20.06 ATOM 4605 C SER B 742 21.312 -1.260 -36.124 1.00 16.84 ATOM 4606 O SER B 742 22.031 -0.268 -35.983 1.00 16.45 ATOM 4607 N ALA B 743 21.098 -1.830 -37.310 1.00 16.76 ATOM 4608 CA ALA B 743 21.700 -1.287 -38.524 1.00 16.89 ATOM 4609 CB ALA B 743 21.360 -2.181 -39.737 1.00 17.75 ATOM 4610 C ALA B 743 21.154 0.126 -38.726 1.00 16.89 ATOM 4611 O ALA B 743 21.865 1.020 -39.182 1.00 17.86 ATOM 4612 N GLY B 744 19.887 0.323 -38.385 1.00 16.78 ATOM 4613 CA GLY B 744 19.286 1.642 -38.513 1.00 16.95 ATOM 4614 C GLY B 744 19.953 2.634 -37.563 1.00 17.42 ATOM 4615 O GLY B 744 20.114 3.815 -37.882 1.00 17.99 ATOM 4616 N CYS B 745 20.340 2.157 -36.383 1.00 17.86 ATOM 4617 CA CYS B 745 21.015 3.015 -35.409 1.00 17.68 ATOM 4618 CB CYS B 745 21.142 2.290 -34.067 1.00 17.95 ATOM 4619 SG CYS B 745 19.565 2.140 -33.179 1.00 18.88 ATOM 4620 C CYS B 745 22.406 3.384 -35.937 1.00 17.93 ATOM 4621 O CYS B 745 22.906 4.481 -35.692 1.00 18.14 ATOM 4622 N VAL B 746 23.036 2.460 -36.655 1.00 17.45 ATOM 4623 CA VAL B 746 24.352 2.734 -37.215 1.00 17.86 ATOM 4624 CB VAL B 746 25.005 1.445 -37.779 1.00 17.16 ATOM 4625 CG1 VAL B 746 26.284 1.788 -38.548 1.00 16.61 ATOM 4626 CG2 VAL B 746 25.331 0.486 -36.618 1.00 17.18 ATOM 4627 C VAL B 746 24.228 3.781 -38.323 1.00 18.38 ATOM 4628 O VAL B 746 25.034 4.712 -38.401 1.00 18.74 ATOM 4629 N LEU B 747 23.221 3.637 -39.181 1.00 18.09 ATOM 4630 CA LEU B 747 23.033 4.592 -40.266 1.00 19.05 ATOM 4631 CB LEU B 747 21.853 4.179 -41.153 1.00 19.31 ATOM 4632 CG LEU B 747 21.295 5.271 -42.084 1.00 19.98 ATOM 4633 CD1 LEU B 747 22.379 5.733 -43.053 1.00 20.56 ATOM 4634 CD2 LEU B 747 20.094 4.728 -42.855 1.00 21.29 ATOM 4635 C LEU B 747 22.774 5.988 -39.696 1.00 19.24 ATOM 4636 O LEU B 747 23.403 6.961 -40.101 1.00 19.60 ATOM 4637 N ALA B 748 21.842 6.080 -38.757 1.00 19.32 ATOM 4638 CA ALA B 748 21.510 7.360 -38.152 1.00 20.30 ATOM 4639 CB ALA B 748 20.424 7.174 -37.108 1.00 19.63 ATOM 4640 C ALA B 748 22.748 7.983 -37.523 1.00 20.97 ATOM 4641 O ALA B 748 22.966 9.190 -37.634 1.00 22.20 ATOM 4642 N GLU B 749 23.566 7.153 -36.883 1.00 21.75 ATOM 4643 CA GLU B 749 24.783 7.622 -36.226 1.00 21.86 ATOM 4644 CB GLU B 749 25.416 6.486 -35.416 1.00 21.91 ATOM 4645 CG GLU B 749 26.692 6.883 -34.700 1.00 23.61 ATOM 4646 CD GLU B 749 27.111 5.897 -33.617 1.00 24.67 ATOM 4647 OE1 GLU B 749 26.321 4.991 -33.260 1.00 24.74 ATOM 4648 OE2 GLU B 749 28.246 6.038 -33.115 1.00 24.61 ATOM 4649 C GLU B 749 25.788 8.170 -37.234 1.00 22.08 ATOM 4650 O GLU B 749 26.426 9.193 -36.989 1.00 20.72 ATOM 4651 N LEU B 750 25.937 7.494 -38.368 1.00 22.02 ATOM 4652 CA LEU B 750 26.873 7.964 -39.386 1.00 22.81 ATOM 4653 CB LEU B 750 27.017 6.933 -40.501 1.00 22.82 ATOM 4654 CG LEU B 750 27.713 5.634 -40.098 1.00 23.05 ATOM 4655 CD1 LEU B 750 27.736 4.683 -41.294 1.00 23.41 ATOM 4656 CD2 LEU B 750 29.126 5.936 -39.604 1.00 23.49 ATOM 4657 C LEU B 750 26.415 9.298 -39.975 1.00 23.90 ATOM 4658 O LEU B 750 27.237 10.126 -40.374 1.00 24.38 ATOM 4659 N LEU B 751 25.104 9.512 -40.022 1.00 24.39 ATOM 4660 CA LEU B 751 24.563 10.760 -40.550 1.00 25.26 ATOM 4661 CB LEU B 751 23.113 10.569 -40.995 1.00 24.33 ATOM 4662 CG LEU B 751 22.850 9.655 -42.194 1.00 24.48 ATOM 4663 CD1 LEU B 751 21.352 9.459 -42.337 1.00 24.26 ATOM 4664 CD2 LEU B 751 23.442 10.255 -43.469 1.00 23.77 ATOM 4665 C LEU B 751 24.625 11.880 -39.507 1.00 26.23 ATOM 4666 O LEU B 751 24.869 13.037 -39.845 1.00 26.73 ATOM 4667 N LEU B 752 24.413 11.529 -38.245 1.00 26.41 ATOM 4668 CA LEU B 752 24.419 12.504 -37.156 1.00 27.83 ATOM 4669 CB LEU B 752 23.581 11.988 -35.993 1.00 28.36 ATOM 4670 CG LEU B 752 22.072 12.016 -36.176 1.00 30.20 ATOM 4671 CD1 LEU B 752 21.422 11.175 -35.082 1.00 30.12 ATOM 4672 CD2 LEU B 752 21.577 13.465 -36.126 1.00 30.40 ATOM 4673 C LEU B 752 25.787 12.890 -36.600 1.00 27.83 ATOM 4674 O LEU B 752 25.982 14.018 -36.164 1.00 28.71 ATOM 4675 N GLY B 753 26.722 11.950 -36.589 1.00 27.84 ATOM 4676 CA GLY B 753 28.031 12.230 -36.031 1.00 27.59 ATOM 4677 C GLY B 753 28.083 11.764 -34.582 1.00 28.17 ATOM 4678 O GLY B 753 29.120 11.866 -33.928 1.00 28.16 ATOM 4679 N GLN B 754 26.956 11.260 -34.077 1.00 27.87 ATOM 4680 CA GLN B 754 26.865 10.754 -32.708 1.00 28.38 ATOM 4681 CB GLN B 754 26.615 11.901 -31.716 1.00 29.90 ATOM 4682 CG GLN B 754 25.364 12.721 -32.014 1.00 34.79 ATOM 4683 CD GLN B 754 25.015 13.728 -30.914 1.00 37.88 ATOM 4684 OE1 GLN B 754 25.817 14.003 -30.019 1.00 40.28 ATOM 4685 NE2 GLN B 754 23.808 14.282 -30.984 1.00 39.26 ATOM 4686 C GLN B 754 25.713 9.756 -32.634 1.00 26.96 ATOM 4687 O GLN B 754 24.820 9.777 -33.478 1.00 26.48 ATOM 4688 N PRO B 755 25.730 8.854 -31.636 1.00 26.66 ATOM 4689 CD PRO B 755 26.764 8.685 -30.602 1.00 26.20 ATOM 4690 CA PRO B 755 24.647 7.866 -31.501 1.00 26.32 ATOM 4691 CB PRO B 755 24.981 7.122 -30.209 1.00 26.32 ATOM 4692 CG PRO B 755 26.432 7.343 -30.001 1.00 27.20 ATOM 4693 C PRO B 755 23.289 8.552 -31.418 1.00 25.95 ATOM 4694 O PRO B 755 23.147 9.589 -30.772 1.00 25.83 ATOM 4695 N ILE B 756 22.281 7.978 -32.066 1.00 25.45 ATOM 4696 CA ILE B 756 20.960 8.592 -32.041 1.00 24.65 ATOM 4697 CB ILE B 756 20.125 8.164 -33.280 1.00 25.07 ATOM 4698 CG2 ILE B 756 19.983 6.650 -33.326 1.00 24.39 ATOM 4699 CG1 ILE B 756 18.766 8.878 -33.258 1.00 26.11 ATOM 4700 CD1 ILE B 756 17.968 8.771 -34.561 1.00 27.35 ATOM 4701 C ILE B 756 20.164 8.330 -30.754 1.00 24.18 ATOM 4702 O ILE B 756 19.429 9.207 -30.302 1.00 23.72 ATOM 4703 N PHE B 757 20.322 7.150 -30.153 1.00 23.69 ATOM 4704 CA PHE B 757 19.586 6.817 -28.933 1.00 24.15 ATOM 4705 CB PHE B 757 18.648 5.630 -29.196 1.00 22.51 ATOM 4706 CG PHE B 757 17.661 5.871 -30.310 1.00 22.11 ATOM 4707 CD1 PHE B 757 17.518 4.950 -31.342 1.00 22.01 ATOM 4708 CD2 PHE B 757 16.875 7.024 -30.325 1.00 22.11 ATOM 4709 CE1 PHE B 757 16.608 5.167 -32.379 1.00 22.38 ATOM 4710 CE2 PHE B 757 15.960 7.260 -31.353 1.00 22.97 ATOM 4711 CZ PHE B 757 15.825 6.322 -32.390 1.00 22.97 ATOM 4712 C PHE B 757 20.489 6.499 -27.741 1.00 25.07 ATOM 4713 O PHE B 757 20.493 5.380 -27.228 1.00 25.40 ATOM 4714 N PRO B 758 21.268 7.487 -27.274 1.00 26.19 ATOM 4715 CD PRO B 758 21.400 8.878 -27.748 1.00 26.46 ATOM 4716 CA PRO B 758 22.143 7.204 -26.130 1.00 27.01 ATOM 4717 CB PRO B 758 23.132 8.366 -26.144 1.00 26.84 ATOM 4718 CG PRO B 758 22.356 9.501 -26.742 1.00 26.65 ATOM 4719 C PRO B 758 21.374 7.123 -24.814 1.00 27.88 ATOM 4720 O PRO B 758 20.206 7.500 -24.746 1.00 27.32 ATOM 4721 N GLY B 759 22.037 6.626 -23.775 1.00 29.37 ATOM 4722 CA GLY B 759 21.407 6.512 -22.472 1.00 30.44 ATOM 4723 C GLY B 759 22.153 5.534 -21.584 1.00 31.77 ATOM 4724 O GLY B 759 22.596 4.474 -22.041 1.00 31.89 ATOM 4725 N ASP B 760 22.295 5.877 -20.311 1.00 32.25 ATOM 4726 CA ASP B 760 22.998 5.001 -19.381 1.00 33.17 ATOM 4727 CB ASP B 760 23.606 5.820 -18.243 1.00 35.47 ATOM 4728 CG ASP B 760 24.893 6.513 -18.657 1.00 38.12 ATOM 4729 OD1 ASP B 760 25.348 6.301 -19.810 1.00 39.07 ATOM 4730 OD2 ASP B 760 25.449 7.271 -17.831 1.00 40.20 ATOM 4731 C ASP B 760 22.072 3.925 -18.825 1.00 31.99 ATOM 4732 O ASP B 760 22.528 2.911 -18.298 1.00 32.01 ATOM 4733 N SER B 761 20.768 4.150 -18.947 1.00 31.05 ATOM 4734 CA SER B 761 19.778 3.188 -18.484 1.00 29.93 ATOM 4735 CB SER B 761 19.060 3.715 -17.240 1.00 29.72 ATOM 4736 OG SER B 761 18.044 4.633 -17.595 1.00 29.88 ATOM 4737 C SER B 761 18.766 2.946 -19.605 1.00 29.37 ATOM 4738 O SER B 761 18.689 3.724 -20.557 1.00 28.85 ATOM 4739 N GLY B 762 18.003 1.862 -19.492 1.00 29.20 ATOM 4740 CA GLY B 762 17.000 1.557 -20.498 1.00 28.19 ATOM 4741 C GLY B 762 15.947 2.648 -20.599 1.00 28.43 ATOM 4742 O GLY B 762 15.487 2.965 -21.692 1.00 27.50 ATOM 4743 N VAL B 763 15.556 3.232 -19.465 1.00 28.56 ATOM 4744 CA VAL B 763 14.548 4.290 -19.486 1.00 28.52 ATOM 4745 CB VAL B 763 14.115 4.718 -18.044 1.00 29.63 ATOM 4746 CG1 VAL B 763 13.672 3.505 -17.256 1.00 30.30 ATOM 4747 CG2 VAL B 763 15.252 5.407 -17.326 1.00 29.18 ATOM 4748 C VAL B 763 15.047 5.509 -20.257 1.00 28.12 ATOM 4749 O VAL B 763 14.292 6.128 -21.004 1.00 28.01 ATOM 4750 N ASP B 764 16.319 5.849 -20.086 1.00 27.97 ATOM 4751 CA ASP B 764 16.896 6.998 -20.780 1.00 27.90 ATOM 4752 CB ASP B 764 18.325 7.251 -20.296 1.00 29.57 ATOM 4753 CG ASP B 764 18.373 7.886 -18.909 1.00 31.79 ATOM 4754 OD1 ASP B 764 19.470 7.918 -18.316 1.00 33.74 ATOM 4755 OD2 ASP B 764 17.323 8.346 -18.407 1.00 32.31 ATOM 4756 C ASP B 764 16.910 6.736 -22.282 1.00 27.66 ATOM 4757 O ASP B 764 16.673 7.642 -23.081 1.00 27.23 ATOM 4758 N GLN B 765 17.202 5.494 -22.658 1.00 26.66 ATOM 4759 CA GLN B 765 17.234 5.119 -24.065 1.00 26.28 ATOM 4760 CB GLN B 765 17.815 3.710 -24.227 1.00 27.52 ATOM 4761 CG GLN B 765 19.328 3.650 -24.053 1.00 29.79 ATOM 4762 CD GLN B 765 19.855 2.236 -23.803 1.00 32.26 ATOM 4763 OE1 GLN B 765 20.883 2.051 -23.142 1.00 34.90 ATOM 4764 NE2 GLN B 765 19.160 1.239 -24.330 1.00 32.31 ATOM 4765 C GLN B 765 15.823 5.183 -24.634 1.00 25.74 ATOM 4766 O GLN B 765 15.605 5.705 -25.731 1.00 25.15 ATOM 4767 N LEU B 766 14.855 4.668 -23.887 1.00 25.04 ATOM 4768 CA LEU B 766 13.472 4.700 -24.350 1.00 25.76 ATOM 4769 CB LEU B 766 12.554 3.989 -23.365 1.00 26.32 ATOM 4770 CG LEU B 766 12.557 2.467 -23.469 1.00 27.44 ATOM 4771 CD1 LEU B 766 11.652 1.890 -22.385 1.00 27.98 ATOM 4772 CD2 LEU B 766 12.095 2.040 -24.857 1.00 26.82 ATOM 4773 C LEU B 766 13.009 6.138 -24.531 1.00 25.89 ATOM 4774 O LEU B 766 12.254 6.441 -25.451 1.00 25.08 ATOM 4775 N VAL B 767 13.466 7.024 -23.651 1.00 26.56 ATOM 4776 CA VAL B 767 13.098 8.433 -23.739 1.00 27.35 ATOM 4777 CB VAL B 767 13.627 9.227 -22.519 1.00 28.18 ATOM 4778 CG1 VAL B 767 13.629 10.719 -22.828 1.00 28.02 ATOM 4779 CG2 VAL B 767 12.772 8.932 -21.301 1.00 28.19 ATOM 4780 C VAL B 767 13.634 9.082 -25.020 1.00 27.23 ATOM 4781 O VAL B 767 12.934 9.870 -25.662 1.00 27.41 ATOM 4782 N GLU B 768 14.877 8.769 -25.380 1.00 26.59 ATOM 4783 CA GLU B 768 15.474 9.317 -26.596 1.00 26.25 ATOM 4784 CB GLU B 768 16.955 8.932 -26.694 1.00 26.92 ATOM 4785 CG GLU B 768 17.841 9.529 -25.612 1.00 29.59 ATOM 4786 CD GLU B 768 17.844 11.049 -25.623 1.00 31.83 ATOM 4787 OE1 GLU B 768 17.819 11.644 -26.719 1.00 32.94 ATOM 4788 OE2 GLU B 768 17.867 11.658 -24.530 1.00 34.62 ATOM 4789 C GLU B 768 14.728 8.779 -27.815 1.00 25.53 ATOM 4790 O GLU B 768 14.538 9.491 -28.796 1.00 26.15 ATOM 4791 N ILE B 769 14.313 7.516 -27.751 1.00 24.71 ATOM 4792 CA ILE B 769 13.578 6.887 -28.843 1.00 24.73 ATOM 4793 CB ILE B 769 13.370 5.373 -28.584 1.00 23.62 ATOM 4794 CG2 ILE B 769 12.407 4.789 -29.607 1.00 23.07 ATOM 4795 CG1 ILE B 769 14.715 4.643 -28.652 1.00 23.83 ATOM 4796 CD1 ILE B 769 14.657 3.193 -28.214 1.00 21.92 ATOM 4797 C ILE B 769 12.206 7.549 -29.000 1.00 25.87 ATOM 4798 O ILE B 769 11.788 7.897 -30.110 1.00 25.43 ATOM 4799 N ILE B 770 11.517 7.722 -27.875 1.00 26.56 ATOM 4800 CA ILE B 770 10.194 8.334 -27.867 1.00 28.03 ATOM 4801 CB ILE B 770 9.576 8.298 -26.446 1.00 28.22 ATOM 4802 CG2 ILE B 770 8.319 9.163 -26.387 1.00 27.72 ATOM 4803 CG1 ILE B 770 9.232 6.851 -26.083 1.00 27.96 ATOM 4804 CD1 ILE B 770 8.751 6.658 -24.670 1.00 28.92 ATOM 4805 C ILE B 770 10.262 9.770 -28.377 1.00 29.09 ATOM 4806 O ILE B 770 9.352 10.232 -29.061 1.00 29.73 ATOM 4807 N LYS B 771 11.344 10.473 -28.061 1.00 29.99 ATOM 4808 CA LYS B 771 11.499 11.847 -28.519 1.00 31.50 ATOM 4809 CB LYS B 771 12.837 12.407 -28.053 1.00 32.54 ATOM 4810 CG LYS B 771 12.815 13.027 -26.667 1.00 34.63 ATOM 4811 CD LYS B 771 14.026 13.931 -26.476 1.00 36.36 ATOM 4812 CE LYS B 771 14.473 13.953 -25.029 1.00 37.34 ATOM 4813 NZ LYS B 771 15.921 14.261 -24.913 1.00 38.61 ATOM 4814 C LYS B 771 11.430 11.923 -30.044 1.00 31.90 ATOM 4815 O LYS B 771 10.862 12.860 -30.607 1.00 32.47 ATOM 4816 N VAL B 772 12.006 10.924 -30.706 1.00 32.18 ATOM 4817 CA VAL B 772 12.037 10.870 -32.163 1.00 31.85 ATOM 4818 CB VAL B 772 13.321 10.165 -32.664 1.00 31.13 ATOM 4819 CG1 VAL B 772 13.341 10.137 -34.180 1.00 30.07 ATOM 4820 CG2 VAL B 772 14.550 10.886 -32.136 1.00 30.47 ATOM 4821 C VAL B 772 10.833 10.161 -32.775 1.00 32.49 ATOM 4822 O VAL B 772 10.179 10.698 -33.673 1.00 33.03 ATOM 4823 N LEU B 773 10.536 8.961 -32.289 1.00 32.25 ATOM 4824 CA LEU B 773 9.425 8.181 -32.823 1.00 32.71 ATOM 4825 CB LEU B 773 9.667 6.683 -32.592 1.00 31.82 ATOM 4826 CG LEU B 773 10.935 6.003 -33.130 1.00 31.50 ATOM 4827 CD1 LEU B 773 10.660 4.515 -33.309 1.00 30.52 ATOM 4828 CD2 LEU B 773 11.363 6.628 -34.444 1.00 32.48 ATOM 4829 C LEU B 773 8.075 8.551 -32.229 1.00 33.89 ATOM 4830 O LEU B 773 7.032 8.223 -32.792 1.00 34.06 ATOM 4831 N GLY B 774 8.092 9.231 -31.092 1.00 34.76 ATOM 4832 CA GLY B 774 6.844 9.581 -30.444 1.00 35.97 ATOM 4833 C GLY B 774 6.455 8.428 -29.541 1.00 37.01 ATOM 4834 O GLY B 774 7.046 7.351 -29.614 1.00 36.47 ATOM 4835 N THR B 775 5.464 8.647 -28.685 1.00 38.35 ATOM 4836 CA THR B 775 5.008 7.613 -27.765 1.00 39.38 ATOM 4837 CB THR B 775 3.940 8.170 -26.797 1.00 40.04 ATOM 4838 OG1 THR B 775 4.553 9.119 -25.916 1.00 40.74 ATOM 4839 CG2 THR B 775 3.318 7.046 -25.967 1.00 40.57 ATOM 4840 C THR B 775 4.423 6.425 -28.522 1.00 39.63 ATOM 4841 O THR B 775 3.608 6.597 -29.428 1.00 39.65 ATOM 4842 N PRO B 776 4.840 5.202 -28.164 1.00 39.85 ATOM 4843 CD PRO B 776 5.821 4.859 -27.118 1.00 39.61 ATOM 4844 CA PRO B 776 4.324 4.010 -28.841 1.00 40.94 ATOM 4845 CB PRO B 776 5.270 2.903 -28.388 1.00 40.17 ATOM 4846 CG PRO B 776 5.744 3.352 -27.049 1.00 39.69 ATOM 4847 C PRO B 776 2.878 3.704 -28.465 1.00 42.51 ATOM 4848 O PRO B 776 2.523 3.705 -27.284 1.00 42.91 ATOM 4849 N THR B 777 2.047 3.443 -29.468 1.00 43.85 ATOM 4850 CA THR B 777 0.649 3.112 -29.220 1.00 45.25 ATOM 4851 CB THR B 777 -0.123 2.844 -30.525 1.00 45.06 ATOM 4852 OG1 THR B 777 0.302 1.591 -31.081 1.00 44.88 ATOM 4853 CG2 THR B 777 0.110 3.958 -31.528 1.00 44.91 ATOM 4854 C THR B 777 0.599 1.836 -28.393 1.00 46.62 ATOM 4855 O THR B 777 1.573 1.079 -28.334 1.00 46.58 ATOM 4856 N ARG B 778 -0.542 1.598 -27.759 1.00 48.24 ATOM 4857 CA ARG B 778 -0.733 0.412 -26.938 1.00 49.79 ATOM 4858 CB ARG B 778 -2.146 0.422 -26.350 1.00 52.33 ATOM 4859 CG ARG B 778 -2.513 -0.819 -25.560 1.00 56.05 ATOM 4860 CD ARG B 778 -3.857 -0.636 -24.870 1.00 59.16 ATOM 4861 NE ARG B 778 -4.252 -1.823 -24.116 1.00 62.01 ATOM 4862 CZ ARG B 778 -5.383 -1.926 -23.421 1.00 63.56 ATOM 4863 NH1 ARG B 778 -6.239 -0.908 -23.383 1.00 64.34 ATOM 4864 NH2 ARG B 778 -5.660 -3.048 -22.762 1.00 64.38 ATOM 4865 C ARG B 778 -0.526 -0.840 -27.789 1.00 49.59 ATOM 4866 O ARG B 778 -0.042 -1.868 -27.304 1.00 49.01 ATOM 4867 N GLU B 779 -0.894 -0.739 -29.063 1.00 49.34 ATOM 4868 CA GLU B 779 -0.758 -1.852 -29.989 1.00 49.79 ATOM 4869 CB GLU B 779 -1.540 -1.570 -31.272 1.00 51.61 ATOM 4870 CG GLU B 779 -1.635 -2.772 -32.199 1.00 55.00 ATOM 4871 CD GLU B 779 -2.049 -2.391 -33.609 1.00 57.42 ATOM 4872 OE1 GLU B 779 -2.691 -1.325 -33.778 1.00 58.99 ATOM 4873 OE2 GLU B 779 -1.734 -3.157 -34.552 1.00 58.34 ATOM 4874 C GLU B 779 0.708 -2.111 -30.328 1.00 48.85 ATOM 4875 O GLU B 779 1.149 -3.261 -30.372 1.00 48.46 ATOM 4876 N GLN B 780 1.455 -1.039 -30.574 1.00 47.55 ATOM 4877 CA GLN B 780 2.871 -1.158 -30.898 1.00 46.24 ATOM 4878 CB GLN B 780 3.462 0.220 -31.193 1.00 44.61 ATOM 4879 CG GLN B 780 3.407 0.612 -32.656 1.00 42.36 ATOM 4880 CD GLN B 780 3.597 2.096 -32.861 1.00 41.43 ATOM 4881 OE1 GLN B 780 3.368 2.891 -31.952 1.00 41.36 ATOM 4882 NE2 GLN B 780 4.021 2.481 -34.058 1.00 40.91 ATOM 4883 C GLN B 780 3.601 -1.796 -29.719 1.00 46.66 ATOM 4884 O GLN B 780 4.504 -2.615 -29.902 1.00 46.10 ATOM 4885 N ILE B 781 3.202 -1.418 -28.509 1.00 47.19 ATOM 4886 CA ILE B 781 3.812 -1.959 -27.304 1.00 48.32 ATOM 4887 CB ILE B 781 3.200 -1.315 -26.041 1.00 47.97 ATOM 4888 CG2 ILE B 781 3.638 -2.074 -24.802 1.00 47.78 ATOM 4889 CG1 ILE B 781 3.635 0.149 -25.949 1.00 47.98 ATOM 4890 CD1 ILE B 781 3.102 0.883 -24.739 1.00 47.51 ATOM 4891 C ILE B 781 3.584 -3.465 -27.267 1.00 49.47 ATOM 4892 O ILE B 781 4.482 -4.243 -26.940 1.00 49.15 ATOM 4893 N ARG B 782 2.371 -3.864 -27.621 1.00 51.35 ATOM 4894 CA ARG B 782 1.980 -5.265 -27.645 1.00 53.23 ATOM 4895 CB ARG B 782 0.496 -5.354 -28.003 1.00 55.13 ATOM 4896 CG ARG B 782 -0.073 -6.751 -28.060 1.00 58.09 ATOM 4897 CD ARG B 782 -1.475 -6.719 -28.652 1.00 60.64 ATOM 4898 NE ARG B 782 -2.075 -8.050 -28.701 1.00 63.87 ATOM 4899 CZ ARG B 782 -3.287 -8.310 -29.188 1.00 65.01 ATOM 4900 NH1 ARG B 782 -4.034 -7.322 -29.672 1.00 65.70 ATOM 4901 NH2 ARG B 782 -3.755 -9.557 -29.190 1.00 65.35 ATOM 4902 C ARG B 782 2.817 -6.062 -28.646 1.00 53.57 ATOM 4903 O ARG B 782 3.072 -7.248 -28.444 1.00 52.97 ATOM 4904 N GLU B 783 3.242 -5.398 -29.720 1.00 54.52 ATOM 4905 CA GLU B 783 4.052 -6.015 -30.773 1.00 55.65 ATOM 4906 CB GLU B 783 4.134 -5.085 -31.984 1.00 56.26 ATOM 4907 CG GLU B 783 2.791 -4.612 -32.497 1.00 57.55 ATOM 4908 CD GLU B 783 2.280 -5.468 -33.635 1.00 58.49 ATOM 4909 OE1 GLU B 783 1.288 -5.061 -34.281 1.00 59.27 ATOM 4910 OE2 GLU B 783 2.873 -6.543 -33.885 1.00 58.84 ATOM 4911 C GLU B 783 5.475 -6.347 -30.315 1.00 56.24 ATOM 4912 O GLU B 783 6.026 -7.393 -30.670 1.00 55.85 ATOM 4913 N MET B 784 6.068 -5.448 -29.537 1.00 57.18 ATOM 4914 CA MET B 784 7.424 -5.644 -29.041 1.00 58.63 ATOM 4915 CB MET B 784 7.979 -4.328 -28.519 1.00 56.74 ATOM 4916 CG MET B 784 8.033 -3.277 -29.586 1.00 54.96 ATOM 4917 SD MET B 784 8.249 -1.643 -28.933 1.00 52.33 ATOM 4918 CE MET B 784 9.062 -0.957 -30.196 1.00 53.91 ATOM 4919 C MET B 784 7.457 -6.680 -27.943 1.00 60.58 ATOM 4920 O MET B 784 8.167 -7.678 -28.038 1.00 60.36 ATOM 4921 N ASN B 785 6.692 -6.434 -26.888 1.00 63.67 ATOM 4922 CA ASN B 785 6.635 -7.374 -25.785 1.00 67.21 ATOM 4923 CB ASN B 785 7.758 -7.113 -24.787 1.00 67.07 ATOM 4924 CG ASN B 785 7.724 -8.080 -23.629 1.00 67.18 ATOM 4925 OD1 ASN B 785 7.786 -7.683 -22.465 1.00 67.03 ATOM 4926 ND2 ASN B 785 7.610 -9.365 -23.942 1.00 67.61 ATOM 4927 C ASN B 785 5.302 -7.310 -25.057 1.00 69.84 ATOM 4928 O ASN B 785 4.979 -6.308 -24.416 1.00 69.78 ATOM 4929 N PRO B 786 4.500 -8.383 -25.163 1.00 72.72 ATOM 4930 CD PRO B 786 4.768 -9.616 -25.926 1.00 73.15 ATOM 4931 CA PRO B 786 3.196 -8.434 -24.500 1.00 75.26 ATOM 4932 CB PRO B 786 2.378 -9.344 -25.405 1.00 74.73 ATOM 4933 CG PRO B 786 3.397 -10.248 -26.068 1.00 73.89 ATOM 4934 C PRO B 786 3.322 -8.993 -23.081 1.00 77.77 ATOM 4935 O PRO B 786 2.718 -10.013 -22.759 1.00 78.40 ATOM 4936 N ASN B 787 4.115 -8.323 -22.247 1.00 80.29 ATOM 4937 CA ASN B 787 4.307 -8.777 -20.880 1.00 82.81 ATOM 4938 CB ASN B 787 5.351 -9.896 -20.821 1.00 82.72 ATOM 4939 CG ASN B 787 4.953 -11.117 -21.620 1.00 82.81 ATOM 4940 OD1 ASN B 787 3.941 -11.762 -21.343 1.00 82.86 ATOM 4941 ND2 ASN B 787 5.757 -11.444 -22.623 1.00 83.08 ATOM 4942 C ASN B 787 4.730 -7.683 -19.909 1.00 84.70 ATOM 4943 O ASN B 787 4.331 -7.707 -18.740 1.00 85.35 ATOM 4944 N TYR B 788 5.536 -6.727 -20.365 1.00 86.65 ATOM 4945 CA TYR B 788 6.004 -5.680 -19.455 1.00 88.49 ATOM 4946 CB TYR B 788 7.201 -4.944 -20.066 1.00 88.39 ATOM 4947 CG TYR B 788 8.474 -5.661 -19.691 1.00 88.60 ATOM 4948 CD1 TYR B 788 8.589 -7.040 -19.898 1.00 88.58 ATOM 4949 CE1 TYR B 788 9.714 -7.740 -19.492 1.00 88.47 ATOM 4950 CD2 TYR B 788 9.531 -4.994 -19.066 1.00 88.40 ATOM 4951 CE2 TYR B 788 10.670 -5.693 -18.653 1.00 88.44 ATOM 4952 CZ TYR B 788 10.749 -7.068 -18.872 1.00 88.47 ATOM 4953 OH TYR B 788 11.852 -7.786 -18.464 1.00 88.34 ATOM 4954 C TYR B 788 4.950 -4.706 -18.947 1.00 89.56 ATOM 4955 O TYR B 788 4.022 -4.329 -19.671 1.00 89.92 ATOM 4956 N THR B 789 5.114 -4.319 -17.685 1.00 90.54 ATOM 4957 CA THR B 789 4.177 -3.453 -16.987 1.00 91.49 ATOM 4958 CB THR B 789 4.348 -3.624 -15.461 1.00 91.55 ATOM 4959 OG1 THR B 789 5.286 -4.674 -15.191 1.00 91.33 ATOM 4960 CG2 THR B 789 3.011 -3.965 -14.792 1.00 91.62 ATOM 4961 C THR B 789 4.156 -1.957 -17.295 1.00 92.01 ATOM 4962 O THR B 789 3.186 -1.455 -17.871 1.00 92.05 ATOM 4963 N GLU B 790 5.217 -1.247 -16.919 1.00 92.62 ATOM 4964 CA GLU B 790 5.262 0.197 -17.134 1.00 93.13 ATOM 4965 CB GLU B 790 6.692 0.739 -17.015 1.00 93.62 ATOM 4966 CG GLU B 790 6.767 2.225 -16.677 1.00 94.29 ATOM 4967 CD GLU B 790 7.950 2.921 -17.329 1.00 94.66 ATOM 4968 OE1 GLU B 790 8.962 2.248 -17.607 1.00 95.06 ATOM 4969 OE2 GLU B 790 7.868 4.145 -17.561 1.00 94.74 ATOM 4970 C GLU B 790 4.671 0.659 -18.456 1.00 93.14 ATOM 4971 O GLU B 790 5.159 0.315 -19.531 1.00 93.47 ATOM 4972 N PHE B 791 3.599 1.437 -18.353 1.00 92.80 ATOM 4973 CA PHE B 791 2.922 2.004 -19.509 1.00 92.19 ATOM 4974 CB PHE B 791 1.476 1.504 -19.573 1.00 92.29 ATOM 4975 CG PHE B 791 1.316 0.199 -20.309 1.00 92.30 ATOM 4976 CD1 PHE B 791 0.047 -0.303 -20.579 1.00 92.12 ATOM 4977 CD2 PHE B 791 2.428 -0.528 -20.734 1.00 92.28 ATOM 4978 CE1 PHE B 791 -0.121 -1.509 -21.264 1.00 92.07 ATOM 4979 CE2 PHE B 791 2.271 -1.738 -21.420 1.00 92.26 ATOM 4980 CZ PHE B 791 0.995 -2.228 -21.685 1.00 92.10 ATOM 4981 C PHE B 791 2.955 3.514 -19.294 1.00 91.65 ATOM 4982 O PHE B 791 2.539 4.301 -20.148 1.00 91.60 ATOM 4983 N LYS B 792 3.465 3.899 -18.126 1.00 90.88 ATOM 4984 CA LYS B 792 3.575 5.297 -17.744 1.00 90.08 ATOM 4985 CB LYS B 792 3.710 5.411 -16.217 1.00 90.27 ATOM 4986 CG LYS B 792 4.379 6.694 -15.724 1.00 90.47 ATOM 4987 CD LYS B 792 4.925 6.529 -14.313 1.00 90.30 ATOM 4988 CE LYS B 792 4.804 7.818 -13.515 1.00 89.90 ATOM 4989 NZ LYS B 792 3.559 7.859 -12.696 1.00 89.39 ATOM 4990 C LYS B 792 4.783 5.942 -18.422 1.00 89.34 ATOM 4991 O LYS B 792 5.911 5.835 -17.949 1.00 89.09 ATOM 4992 N PHE B 793 4.536 6.603 -19.551 1.00 88.63 ATOM 4993 CA PHE B 793 5.588 7.284 -20.284 1.00 87.72 ATOM 4994 CB PHE B 793 6.242 6.335 -21.288 1.00 87.76 ATOM 4995 CG PHE B 793 7.691 6.083 -21.010 1.00 87.81 ATOM 4996 CD1 PHE B 793 8.152 4.794 -20.773 1.00 87.80 ATOM 4997 CD2 PHE B 793 8.593 7.140 -20.969 1.00 87.83 ATOM 4998 CE1 PHE B 793 9.497 4.561 -20.499 1.00 87.80 ATOM 4999 CE2 PHE B 793 9.939 6.918 -20.698 1.00 87.72 ATOM 5000 CZ PHE B 793 10.393 5.625 -20.463 1.00 87.65 ATOM 5001 C PHE B 793 5.035 8.506 -21.006 1.00 87.06 ATOM 5002 O PHE B 793 4.084 8.402 -21.784 1.00 86.97 ATOM 5003 N PRO B 794 5.613 9.688 -20.735 1.00 86.29 ATOM 5004 CD PRO B 794 6.733 9.875 -19.789 1.00 86.03 ATOM 5005 CA PRO B 794 5.198 10.956 -21.338 1.00 85.62 ATOM 5006 CB PRO B 794 6.456 11.816 -21.269 1.00 85.76 ATOM 5007 CG PRO B 794 7.276 11.227 -20.154 1.00 85.99 ATOM 5008 C PRO B 794 4.698 10.783 -22.770 1.00 84.91 ATOM 5009 O PRO B 794 5.350 10.134 -23.583 1.00 84.75 ATOM 5010 N GLN B 795 3.538 11.367 -23.061 1.00 84.10 ATOM 5011 CA GLN B 795 2.949 11.271 -24.392 1.00 83.24 ATOM 5012 CB GLN B 795 1.422 11.390 -24.323 1.00 83.71 ATOM 5013 CG GLN B 795 0.837 11.250 -22.927 1.00 84.44 ATOM 5014 CD GLN B 795 0.696 9.805 -22.489 1.00 84.85 ATOM 5015 OE1 GLN B 795 0.504 9.521 -21.306 1.00 85.28 ATOM 5016 NE2 GLN B 795 0.793 8.883 -23.442 1.00 84.85 ATOM 5017 C GLN B 795 3.497 12.355 -25.309 1.00 82.30 ATOM 5018 O GLN B 795 2.909 13.428 -25.442 1.00 82.12 ATOM 5019 N ILE B 796 4.631 12.064 -25.935 1.00 81.19 ATOM 5020 CA ILE B 796 5.278 12.997 -26.846 1.00 79.88 ATOM 5021 CB ILE B 796 6.824 12.868 -26.753 1.00 79.60 ATOM 5022 CG2 ILE B 796 7.466 13.086 -28.114 1.00 79.50 ATOM 5023 CG1 ILE B 796 7.362 13.884 -25.742 1.00 79.39 ATOM 5024 CD1 ILE B 796 7.506 13.333 -24.341 1.00 79.00 ATOM 5025 C ILE B 796 4.815 12.709 -28.272 1.00 79.15 ATOM 5026 O ILE B 796 4.534 11.564 -28.623 1.00 78.72 ATOM 5027 N LYS B 797 4.723 13.755 -29.085 1.00 78.58 ATOM 5028 CA LYS B 797 4.301 13.608 -30.472 1.00 78.16 ATOM 5029 CB LYS B 797 3.678 14.915 -30.980 1.00 78.23 ATOM 5030 CG LYS B 797 4.587 16.131 -30.866 1.00 78.53 ATOM 5031 CD LYS B 797 4.559 16.728 -29.466 1.00 78.53 ATOM 5032 CE LYS B 797 5.929 17.259 -29.072 1.00 78.60 ATOM 5033 NZ LYS B 797 6.192 17.104 -27.614 1.00 78.41 ATOM 5034 C LYS B 797 5.494 13.218 -31.345 1.00 77.59 ATOM 5035 O LYS B 797 6.645 13.482 -30.992 1.00 77.46 ATOM 5036 N ALA B 798 5.216 12.584 -32.481 1.00 76.91 ATOM 5037 CA ALA B 798 6.265 12.151 -33.401 1.00 76.17 ATOM 5038 CB ALA B 798 5.639 11.517 -34.645 1.00 76.40 ATOM 5039 C ALA B 798 7.175 13.310 -33.804 1.00 75.46 ATOM 5040 O ALA B 798 6.702 14.368 -34.226 1.00 75.52 ATOM 5041 N HIS B 799 8.483 13.100 -33.673 1.00 74.38 ATOM 5042 CA HIS B 799 9.470 14.116 -34.026 1.00 73.15 ATOM 5043 CB HIS B 799 10.745 13.920 -33.207 1.00 74.08 ATOM 5044 CG HIS B 799 11.732 15.036 -33.349 1.00 74.78 ATOM 5045 CD2 HIS B 799 13.026 15.135 -32.965 1.00 75.33 ATOM 5046 ND1 HIS B 799 11.410 16.243 -33.932 1.00 75.27 ATOM 5047 CE1 HIS B 799 12.465 17.038 -33.901 1.00 75.42 ATOM 5048 NE2 HIS B 799 13.459 16.391 -33.320 1.00 75.61 ATOM 5049 C HIS B 799 9.819 14.056 -35.510 1.00 71.73 ATOM 5050 O HIS B 799 10.349 13.051 -35.994 1.00 71.72 ATOM 5051 N PRO B 800 9.536 15.142 -36.253 1.00 70.15 ATOM 5052 CD PRO B 800 8.949 16.407 -35.781 1.00 70.00 ATOM 5053 CA PRO B 800 9.832 15.184 -37.689 1.00 68.32 ATOM 5054 CB PRO B 800 9.588 16.647 -38.076 1.00 68.89 ATOM 5055 CG PRO B 800 9.486 17.398 -36.765 1.00 69.65 ATOM 5056 C PRO B 800 11.268 14.753 -37.949 1.00 66.16 ATOM 5057 O PRO B 800 12.211 15.466 -37.611 1.00 66.34 ATOM 5058 N TRP B 801 11.421 13.574 -38.538 1.00 63.42 ATOM 5059 CA TRP B 801 12.735 13.032 -38.834 1.00 60.64 ATOM 5060 CB TRP B 801 12.590 11.795 -39.713 1.00 58.27 ATOM 5061 CG TRP B 801 12.373 10.532 -38.946 1.00 55.71 ATOM 5062 CD2 TRP B 801 13.363 9.781 -38.234 1.00 54.28 ATOM 5063 CE2 TRP B 801 12.725 8.629 -37.722 1.00 53.66 ATOM 5064 CE3 TRP B 801 14.728 9.967 -37.982 1.00 53.37 ATOM 5065 CD1 TRP B 801 11.207 9.829 -38.834 1.00 55.02 ATOM 5066 NE1 TRP B 801 11.411 8.684 -38.102 1.00 53.96 ATOM 5067 CZ2 TRP B 801 13.405 7.668 -36.972 1.00 52.98 ATOM 5068 CZ3 TRP B 801 15.405 9.011 -37.236 1.00 52.99 ATOM 5069 CH2 TRP B 801 14.741 7.875 -36.741 1.00 52.93 ATOM 5070 C TRP B 801 13.646 14.051 -39.516 1.00 60.00 ATOM 5071 O TRP B 801 14.855 14.068 -39.276 1.00 59.88 ATOM 5072 N THR B 802 13.069 14.903 -40.361 1.00 59.14 ATOM 5073 CA THR B 802 13.853 15.915 -41.066 1.00 58.29 ATOM 5074 CB THR B 802 12.988 16.682 -42.093 1.00 58.71 ATOM 5075 OG1 THR B 802 12.565 15.777 -43.123 1.00 58.80 ATOM 5076 CG2 THR B 802 13.784 17.824 -42.729 1.00 58.55 ATOM 5077 C THR B 802 14.486 16.903 -40.089 1.00 57.36 ATOM 5078 O THR B 802 15.550 17.465 -40.361 1.00 57.68 ATOM 5079 N LYS B 803 13.835 17.105 -38.947 1.00 55.89 ATOM 5080 CA LYS B 803 14.355 18.007 -37.926 1.00 54.37 ATOM 5081 CB LYS B 803 13.223 18.478 -37.002 1.00 55.89 ATOM 5082 CG LYS B 803 13.697 19.405 -35.880 1.00 57.93 ATOM 5083 CD LYS B 803 12.545 20.091 -35.148 1.00 59.30 ATOM 5084 CE LYS B 803 12.962 20.494 -33.736 1.00 60.09 ATOM 5085 NZ LYS B 803 11.806 20.937 -32.899 1.00 61.20 ATOM 5086 C LYS B 803 15.435 17.300 -37.102 1.00 52.30 ATOM 5087 O LYS B 803 16.177 17.933 -36.351 1.00 51.94 ATOM 5088 N VAL B 804 15.525 15.984 -37.253 1.00 50.02 ATOM 5089 CA VAL B 804 16.505 15.194 -36.515 1.00 47.40 ATOM 5090 CB VAL B 804 16.110 13.696 -36.495 1.00 47.54 ATOM 5091 CG1 VAL B 804 17.230 12.864 -35.888 1.00 46.99 ATOM 5092 CG2 VAL B 804 14.821 13.510 -35.713 1.00 47.27 ATOM 5093 C VAL B 804 17.915 15.316 -37.089 1.00 45.82 ATOM 5094 O VAL B 804 18.891 15.360 -36.339 1.00 45.06 ATOM 5095 N PHE B 805 18.021 15.379 -38.415 1.00 43.87 ATOM 5096 CA PHE B 805 19.324 15.469 -39.063 1.00 42.56 ATOM 5097 CB PHE B 805 19.369 14.502 -40.247 1.00 40.91 ATOM 5098 CG PHE B 805 19.099 13.076 -39.864 1.00 39.06 ATOM 5099 CD1 PHE B 805 17.860 12.497 -40.114 1.00 37.77 ATOM 5100 CD2 PHE B 805 20.080 12.317 -39.227 1.00 38.23 ATOM 5101 CE1 PHE B 805 17.595 11.181 -39.733 1.00 37.36 ATOM 5102 CE2 PHE B 805 19.827 10.998 -38.841 1.00 37.51 ATOM 5103 CZ PHE B 805 18.581 10.432 -39.096 1.00 36.83 ATOM 5104 C PHE B 805 19.711 16.874 -39.516 1.00 42.95 ATOM 5105 O PHE B 805 18.862 17.757 -39.656 1.00 42.39 ATOM 5106 N ARG B 806 21.009 17.067 -39.738 1.00 43.38 ATOM 5107 CA ARG B 806 21.534 18.351 -40.172 1.00 44.00 ATOM 5108 CB ARG B 806 23.061 18.278 -40.296 1.00 45.67 ATOM 5109 CG ARG B 806 23.562 17.520 -41.514 1.00 48.58 ATOM 5110 CD ARG B 806 25.046 17.741 -41.749 1.00 51.52 ATOM 5111 NE ARG B 806 25.520 17.122 -42.990 1.00 54.67 ATOM 5112 CZ ARG B 806 25.393 15.825 -43.283 1.00 56.58 ATOM 5113 NH1 ARG B 806 24.802 14.989 -42.427 1.00 57.59 ATOM 5114 NH2 ARG B 806 25.863 15.352 -44.435 1.00 57.49 ATOM 5115 C ARG B 806 20.916 18.755 -41.501 1.00 43.51 ATOM 5116 O ARG B 806 20.491 17.905 -42.282 1.00 42.96 ATOM 5117 N PRO B 807 20.848 20.068 -41.776 1.00 43.35 ATOM 5118 CD PRO B 807 21.298 21.206 -40.954 1.00 43.62 ATOM 5119 CA PRO B 807 20.262 20.503 -43.046 1.00 42.56 ATOM 5120 CB PRO B 807 20.296 22.030 -42.966 1.00 42.91 ATOM 5121 CG PRO B 807 21.340 22.339 -41.943 1.00 43.45 ATOM 5122 C PRO B 807 21.070 19.968 -44.220 1.00 41.66 ATOM 5123 O PRO B 807 22.295 19.852 -44.142 1.00 41.45 ATOM 5124 N ARG B 808 20.366 19.635 -45.295 1.00 40.97 ATOM 5125 CA ARG B 808 20.972 19.106 -46.511 1.00 40.62 ATOM 5126 CB ARG B 808 22.286 19.839 -46.823 1.00 41.66 ATOM 5127 CG ARG B 808 22.095 21.187 -47.513 1.00 43.77 ATOM 5128 CD ARG B 808 23.428 21.792 -47.950 1.00 45.77 ATOM 5129 NE ARG B 808 24.289 22.080 -46.806 1.00 47.88 ATOM 5130 CZ ARG B 808 24.067 23.056 -45.928 1.00 49.42 ATOM 5131 NH1 ARG B 808 23.008 23.849 -46.055 1.00 49.89 ATOM 5132 NH2 ARG B 808 24.900 23.232 -44.910 1.00 50.54 ATOM 5133 C ARG B 808 21.202 17.593 -46.453 1.00 39.18 ATOM 5134 O ARG B 808 21.814 17.016 -47.355 1.00 38.68 ATOM 5135 N THR B 809 20.718 16.952 -45.391 1.00 37.71 ATOM 5136 CA THR B 809 20.847 15.506 -45.271 1.00 36.14 ATOM 5137 CB THR B 809 20.359 15.010 -43.903 1.00 35.82 ATOM 5138 OG1 THR B 809 21.272 15.443 -42.894 1.00 34.80 ATOM 5139 CG2 THR B 809 20.272 13.483 -43.883 1.00 35.63 ATOM 5140 C THR B 809 19.942 14.936 -46.354 1.00 35.55 ATOM 5141 O THR B 809 18.781 15.331 -46.460 1.00 35.53 ATOM 5142 N PRO B 810 20.452 13.998 -47.171 1.00 34.94 ATOM 5143 CD PRO B 810 21.796 13.392 -47.161 1.00 34.62 ATOM 5144 CA PRO B 810 19.600 13.440 -48.229 1.00 34.43 ATOM 5145 CB PRO B 810 20.457 12.335 -48.849 1.00 34.10 ATOM 5146 CG PRO B 810 21.865 12.694 -48.491 1.00 34.61 ATOM 5147 C PRO B 810 18.265 12.918 -47.707 1.00 34.12 ATOM 5148 O PRO B 810 18.224 12.131 -46.765 1.00 33.99 ATOM 5149 N PRO B 811 17.153 13.373 -48.308 1.00 33.67 ATOM 5150 CD PRO B 811 17.136 14.347 -49.415 1.00 33.65 ATOM 5151 CA PRO B 811 15.798 12.960 -47.916 1.00 32.91 ATOM 5152 CB PRO B 811 14.900 13.643 -48.947 1.00 33.11 ATOM 5153 CG PRO B 811 15.711 14.808 -49.439 1.00 33.82 ATOM 5154 C PRO B 811 15.618 11.444 -47.925 1.00 32.21 ATOM 5155 O PRO B 811 14.883 10.891 -47.102 1.00 31.80 ATOM 5156 N GLU B 812 16.287 10.782 -48.867 1.00 31.11 ATOM 5157 CA GLU B 812 16.210 9.331 -48.998 1.00 30.59 ATOM 5158 CB GLU B 812 16.922 8.872 -50.276 1.00 31.68 ATOM 5159 CG GLU B 812 16.302 9.416 -51.557 1.00 34.72 ATOM 5160 CD GLU B 812 16.640 10.888 -51.809 1.00 36.77 ATOM 5161 OE1 GLU B 812 15.976 11.502 -52.679 1.00 38.67 ATOM 5162 OE2 GLU B 812 17.562 11.432 -51.148 1.00 36.34 ATOM 5163 C GLU B 812 16.840 8.650 -47.785 1.00 28.89 ATOM 5164 O GLU B 812 16.392 7.587 -47.355 1.00 27.91 ATOM 5165 N ALA B 813 17.884 9.265 -47.240 1.00 28.06 ATOM 5166 CA ALA B 813 18.563 8.715 -46.071 1.00 27.29 ATOM 5167 CB ALA B 813 19.831 9.509 -45.775 1.00 26.76 ATOM 5168 C ALA B 813 17.614 8.774 -44.882 1.00 27.06 ATOM 5169 O ALA B 813 17.519 7.830 -44.100 1.00 26.00 ATOM 5170 N ILE B 814 16.914 9.897 -44.755 1.00 27.46 ATOM 5171 CA ILE B 814 15.953 10.100 -43.677 1.00 28.09 ATOM 5172 CB ILE B 814 15.396 11.538 -43.697 1.00 29.27 ATOM 5173 CG2 ILE B 814 14.382 11.722 -42.579 1.00 29.62 ATOM 5174 CG1 ILE B 814 16.538 12.544 -43.546 1.00 30.04 ATOM 5175 CD1 ILE B 814 16.115 13.987 -43.781 1.00 31.39 ATOM 5176 C ILE B 814 14.784 9.123 -43.819 1.00 27.20 ATOM 5177 O ILE B 814 14.292 8.584 -42.826 1.00 27.36 ATOM 5178 N ALA B 815 14.340 8.903 -45.055 1.00 26.36 ATOM 5179 CA ALA B 815 13.233 7.984 -45.320 1.00 25.39 ATOM 5180 CB ALA B 815 12.846 8.037 -46.794 1.00 25.28 ATOM 5181 C ALA B 815 13.615 6.557 -44.928 1.00 25.00 ATOM 5182 O ALA B 815 12.849 5.864 -44.256 1.00 24.39 ATOM 5183 N LEU B 816 14.796 6.120 -45.358 1.00 24.50 ATOM 5184 CA LEU B 816 15.285 4.782 -45.028 1.00 23.79 ATOM 5185 CB LEU B 816 16.686 4.551 -45.624 1.00 22.65 ATOM 5186 CG LEU B 816 17.450 3.262 -45.258 1.00 22.80 ATOM 5187 CD1 LEU B 816 16.567 2.030 -45.482 1.00 21.38 ATOM 5188 CD2 LEU B 816 18.729 3.146 -46.100 1.00 20.57 ATOM 5189 C LEU B 816 15.341 4.646 -43.509 1.00 24.19 ATOM 5190 O LEU B 816 14.878 3.658 -42.949 1.00 24.09 ATOM 5191 N CYS B 817 15.905 5.642 -42.836 1.00 24.54 ATOM 5192 CA CYS B 817 15.995 5.592 -41.383 1.00 26.39 ATOM 5193 CB CYS B 817 16.547 6.901 -40.832 1.00 28.67 ATOM 5194 SG CYS B 817 18.321 6.915 -40.667 1.00 33.51 ATOM 5195 C CYS B 817 14.636 5.348 -40.743 1.00 25.57 ATOM 5196 O CYS B 817 14.504 4.503 -39.863 1.00 24.97 ATOM 5197 N SER B 818 13.628 6.091 -41.183 1.00 25.49 ATOM 5198 CA SER B 818 12.291 5.947 -40.617 1.00 26.32 ATOM 5199 CB SER B 818 11.362 7.039 -41.156 1.00 26.48 ATOM 5200 OG SER B 818 10.975 6.775 -42.488 1.00 28.90 ATOM 5201 C SER B 818 11.662 4.573 -40.854 1.00 26.57 ATOM 5202 O SER B 818 10.774 4.154 -40.103 1.00 27.22 ATOM 5203 N ARG B 819 12.120 3.868 -41.886 1.00 26.01 ATOM 5204 CA ARG B 819 11.583 2.540 -42.193 1.00 25.66 ATOM 5205 CB ARG B 819 11.550 2.310 -43.708 1.00 27.24 ATOM 5206 CG ARG B 819 10.662 3.304 -44.457 1.00 30.47 ATOM 5207 CD ARG B 819 9.185 3.059 -44.188 1.00 32.55 ATOM 5208 NE ARG B 819 8.710 1.858 -44.874 1.00 35.21 ATOM 5209 CZ ARG B 819 8.391 0.721 -44.261 1.00 36.41 ATOM 5210 NH1 ARG B 819 8.492 0.624 -42.936 1.00 36.79 ATOM 5211 NH2 ARG B 819 7.985 -0.326 -44.972 1.00 37.09 ATOM 5212 C ARG B 819 12.372 1.425 -41.524 1.00 24.58 ATOM 5213 O ARG B 819 11.982 0.256 -41.580 1.00 23.32 ATOM 5214 N LEU B 820 13.483 1.783 -40.887 1.00 23.27 ATOM 5215 CA LEU B 820 14.311 0.801 -40.194 1.00 22.93 ATOM 5216 CB LEU B 820 15.793 1.092 -40.439 1.00 21.51 ATOM 5217 CG LEU B 820 16.286 0.960 -41.877 1.00 21.26 ATOM 5218 CD1 LEU B 820 17.743 1.399 -41.945 1.00 19.94 ATOM 5219 CD2 LEU B 820 16.129 -0.485 -42.345 1.00 20.60 ATOM 5220 C LEU B 820 14.031 0.878 -38.698 1.00 23.24 ATOM 5221 O LEU B 820 13.919 -0.140 -38.005 1.00 23.24 ATOM 5222 N LEU B 821 13.925 2.109 -38.215 1.00 23.69 ATOM 5223 CA LEU B 821 13.680 2.371 -36.808 1.00 23.99 ATOM 5224 CB LEU B 821 14.417 3.650 -36.392 1.00 23.40 ATOM 5225 CG LEU B 821 15.935 3.581 -36.634 1.00 23.43 ATOM 5226 CD1 LEU B 821 16.601 4.888 -36.248 1.00 23.21 ATOM 5227 CD2 LEU B 821 16.527 2.429 -35.824 1.00 23.14 ATOM 5228 C LEU B 821 12.186 2.485 -36.538 1.00 24.81 ATOM 5229 O LEU B 821 11.662 3.576 -36.338 1.00 25.44 ATOM 5230 N GLU B 822 11.507 1.341 -36.556 1.00 25.24 ATOM 5231 CA GLU B 822 10.070 1.275 -36.305 1.00 27.06 ATOM 5232 CB GLU B 822 9.345 0.559 -37.455 1.00 28.32 ATOM 5233 CG GLU B 822 9.520 1.202 -38.820 1.00 32.30 ATOM 5234 CD GLU B 822 8.331 2.063 -39.219 1.00 34.70 ATOM 5235 OE1 GLU B 822 7.530 2.420 -38.326 1.00 36.08 ATOM 5236 OE2 GLU B 822 8.198 2.384 -40.426 1.00 36.36 ATOM 5237 C GLU B 822 9.835 0.489 -35.022 1.00 26.48 ATOM 5238 O GLU B 822 10.564 -0.459 -34.733 1.00 26.24 ATOM 5239 N TYR B 823 8.817 0.879 -34.257 1.00 26.40 ATOM 5240 CA TYR B 823 8.481 0.178 -33.021 1.00 25.60 ATOM 5241 CB TYR B 823 7.344 0.895 -32.283 1.00 25.88 ATOM 5242 CG TYR B 823 7.747 2.113 -31.480 1.00 26.19 ATOM 5243 CD1 TYR B 823 8.734 2.035 -30.495 1.00 26.07 ATOM 5244 CE1 TYR B 823 9.075 3.143 -29.725 1.00 26.35 ATOM 5245 CD2 TYR B 823 7.110 3.337 -31.675 1.00 26.10 ATOM 5246 CE2 TYR B 823 7.443 4.450 -30.912 1.00 26.76 ATOM 5247 CZ TYR B 823 8.425 4.345 -29.939 1.00 26.68 ATOM 5248 OH TYR B 823 8.759 5.444 -29.185 1.00 28.08 ATOM 5249 C TYR B 823 8.031 -1.251 -33.344 1.00 25.53 ATOM 5250 O TYR B 823 8.553 -2.217 -32.792 1.00 25.56 ATOM 5251 N THR B 824 7.059 -1.386 -34.241 1.00 25.29 ATOM 5252 CA THR B 824 6.560 -2.710 -34.612 1.00 25.94 ATOM 5253 CB THR B 824 5.274 -2.595 -35.466 1.00 26.13 ATOM 5254 OG1 THR B 824 4.264 -1.910 -34.712 1.00 26.10 ATOM 5255 CG2 THR B 824 4.768 -3.977 -35.859 1.00 25.73 ATOM 5256 C THR B 824 7.632 -3.464 -35.390 1.00 25.88 ATOM 5257 O THR B 824 7.954 -3.106 -36.518 1.00 26.36 ATOM 5258 N PRO B 825 8.191 -4.532 -34.796 1.00 26.37 ATOM 5259 CD PRO B 825 7.854 -5.060 -33.458 1.00 26.22 ATOM 5260 CA PRO B 825 9.241 -5.328 -35.446 1.00 26.57 ATOM 5261 CB PRO B 825 9.439 -6.510 -34.493 1.00 25.91 ATOM 5262 CG PRO B 825 9.000 -5.988 -33.157 1.00 26.29 ATOM 5263 C PRO B 825 8.951 -5.770 -36.883 1.00 26.85 ATOM 5264 O PRO B 825 9.800 -5.630 -37.766 1.00 26.24 ATOM 5265 N THR B 826 7.757 -6.303 -37.120 1.00 27.01 ATOM 5266 CA THR B 826 7.391 -6.753 -38.457 1.00 26.55 ATOM 5267 CB THR B 826 6.077 -7.574 -38.436 1.00 26.76 ATOM 5268 OG1 THR B 826 5.039 -6.814 -37.809 1.00 27.62 ATOM 5269 CG2 THR B 826 6.271 -8.855 -37.662 1.00 27.02 ATOM 5270 C THR B 826 7.240 -5.602 -39.451 1.00 26.15 ATOM 5271 O THR B 826 7.217 -5.827 -40.662 1.00 26.81 ATOM 5272 N ALA B 827 7.139 -4.373 -38.952 1.00 25.66 ATOM 5273 CA ALA B 827 6.993 -3.208 -39.824 1.00 25.36 ATOM 5274 CB ALA B 827 6.358 -2.064 -39.055 1.00 25.44 ATOM 5275 C ALA B 827 8.330 -2.748 -40.437 1.00 25.13 ATOM 5276 O ALA B 827 8.348 -2.077 -41.469 1.00 26.05 ATOM 5277 N ARG B 828 9.444 -3.107 -39.807 1.00 23.63 ATOM 5278 CA ARG B 828 10.756 -2.720 -40.316 1.00 22.16 ATOM 5279 CB ARG B 828 11.852 -3.086 -39.299 1.00 20.49 ATOM 5280 CG ARG B 828 11.599 -2.542 -37.916 1.00 19.36 ATOM 5281 CD ARG B 828 12.610 -3.003 -36.878 1.00 19.38 ATOM 5282 NE ARG B 828 12.094 -2.627 -35.569 1.00 19.69 ATOM 5283 CZ ARG B 828 12.279 -3.301 -34.441 1.00 20.38 ATOM 5284 NH1 ARG B 828 12.992 -4.414 -34.433 1.00 19.68 ATOM 5285 NH2 ARG B 828 11.694 -2.877 -33.320 1.00 19.35 ATOM 5286 C ARG B 828 11.072 -3.408 -41.647 1.00 22.11 ATOM 5287 O ARG B 828 10.651 -4.543 -41.890 1.00 21.41 ATOM 5288 N LEU B 829 11.829 -2.724 -42.501 1.00 21.52 ATOM 5289 CA LEU B 829 12.242 -3.308 -43.773 1.00 21.41 ATOM 5290 CB LEU B 829 13.080 -2.310 -44.582 1.00 22.35 ATOM 5291 CG LEU B 829 12.431 -1.028 -45.095 1.00 22.42 ATOM 5292 CD1 LEU B 829 13.508 -0.064 -45.590 1.00 22.53 ATOM 5293 CD2 LEU B 829 11.474 -1.369 -46.217 1.00 23.24 ATOM 5294 C LEU B 829 13.131 -4.517 -43.478 1.00 22.35 ATOM 5295 O LEU B 829 13.774 -4.588 -42.418 1.00 21.58 ATOM 5296 N THR B 830 13.163 -5.468 -44.405 1.00 21.63 ATOM 5297 CA THR B 830 14.036 -6.625 -44.267 1.00 22.10 ATOM 5298 CB THR B 830 13.549 -7.828 -45.108 1.00 22.51 ATOM 5299 OG1 THR B 830 13.526 -7.460 -46.493 1.00 23.24 ATOM 5300 CG2 THR B 830 12.148 -8.244 -44.683 1.00 23.55 ATOM 5301 C THR B 830 15.350 -6.130 -44.872 1.00 21.95 ATOM 5302 O THR B 830 15.370 -5.107 -45.564 1.00 21.91 ATOM 5303 N PRO B 831 16.468 -6.814 -44.587 1.00 21.68 ATOM 5304 CD PRO B 831 16.602 -7.967 -43.677 1.00 21.62 ATOM 5305 CA PRO B 831 17.762 -6.403 -45.143 1.00 21.14 ATOM 5306 CB PRO B 831 18.723 -7.480 -44.648 1.00 21.16 ATOM 5307 CG PRO B 831 18.073 -8.006 -43.396 1.00 21.42 ATOM 5308 C PRO B 831 17.749 -6.307 -46.668 1.00 21.29 ATOM 5309 O PRO B 831 18.275 -5.353 -47.238 1.00 20.93 ATOM 5310 N LEU B 832 17.149 -7.292 -47.333 1.00 21.47 ATOM 5311 CA LEU B 832 17.102 -7.281 -48.792 1.00 21.64 ATOM 5312 CB LEU B 832 16.488 -8.589 -49.306 1.00 22.33 ATOM 5313 CG LEU B 832 16.864 -9.041 -50.720 1.00 23.78 ATOM 5314 CD1 LEU B 832 18.376 -9.250 -50.833 1.00 22.96 ATOM 5315 CD2 LEU B 832 16.100 -10.327 -51.043 1.00 23.46 ATOM 5316 C LEU B 832 16.307 -6.077 -49.290 1.00 21.38 ATOM 5317 O LEU B 832 16.690 -5.438 -50.268 1.00 21.93 ATOM 5318 N GLU B 833 15.204 -5.763 -48.614 1.00 21.92 ATOM 5319 CA GLU B 833 14.380 -4.616 -48.988 1.00 22.23 ATOM 5320 CB GLU B 833 13.094 -4.572 -48.155 1.00 23.30 ATOM 5321 CG GLU B 833 12.036 -5.574 -48.611 1.00 24.62 ATOM 5322 CD GLU B 833 10.910 -5.754 -47.608 1.00 26.01 ATOM 5323 OE1 GLU B 833 10.968 -5.150 -46.517 1.00 25.24 ATOM 5324 OE2 GLU B 833 9.958 -6.510 -47.912 1.00 26.83 ATOM 5325 C GLU B 833 15.161 -3.323 -48.773 1.00 22.16 ATOM 5326 O GLU B 833 15.036 -2.368 -49.550 1.00 21.81 ATOM 5327 N ALA B 834 15.957 -3.291 -47.708 1.00 21.02 ATOM 5328 CA ALA B 834 16.765 -2.114 -47.408 1.00 20.22 ATOM 5329 CB ALA B 834 17.506 -2.301 -46.065 1.00 19.05 ATOM 5330 C ALA B 834 17.763 -1.892 -48.555 1.00 19.62 ATOM 5331 O ALA B 834 17.943 -0.767 -49.015 1.00 18.67 ATOM 5332 N CYS B 835 18.389 -2.972 -49.023 1.00 19.47 ATOM 5333 CA CYS B 835 19.350 -2.880 -50.119 1.00 20.39 ATOM 5334 CB CYS B 835 19.869 -4.268 -50.483 1.00 20.89 ATOM 5335 SG CYS B 835 21.095 -4.945 -49.354 1.00 22.54 ATOM 5336 C CYS B 835 18.733 -2.252 -51.366 1.00 21.53 ATOM 5337 O CYS B 835 19.416 -1.552 -52.132 1.00 21.63 ATOM 5338 N ALA B 836 17.443 -2.510 -51.567 1.00 22.28 ATOM 5339 CA ALA B 836 16.717 -2.009 -52.734 1.00 22.34 ATOM 5340 CB ALA B 836 15.592 -2.976 -53.087 1.00 21.77 ATOM 5341 C ALA B 836 16.154 -0.609 -52.539 1.00 22.98 ATOM 5342 O ALA B 836 15.535 -0.052 -53.451 1.00 23.48 ATOM 5343 N HIS B 837 16.357 -0.037 -51.357 1.00 22.62 ATOM 5344 CA HIS B 837 15.853 1.299 -51.084 1.00 23.18 ATOM 5345 CB HIS B 837 16.122 1.686 -49.626 1.00 23.29 ATOM 5346 CG HIS B 837 15.370 2.903 -49.181 1.00 23.82 ATOM 5347 CD2 HIS B 837 14.206 3.035 -48.501 1.00 24.04 ATOM 5348 ND1 HIS B 837 15.806 4.185 -49.443 1.00 23.83 ATOM 5349 CE1 HIS B 837 14.944 5.053 -48.942 1.00 24.07 ATOM 5350 NE2 HIS B 837 13.964 4.381 -48.365 1.00 24.40 ATOM 5351 C HIS B 837 16.502 2.315 -52.031 1.00 23.81 ATOM 5352 O HIS B 837 17.616 2.107 -52.514 1.00 23.32 ATOM 5353 N SER B 838 15.800 3.416 -52.284 1.00 24.57 ATOM 5354 CA SER B 838 16.291 4.456 -53.183 1.00 25.45 ATOM 5355 CB SER B 838 15.168 5.453 -53.473 1.00 26.91 ATOM 5356 OG SER B 838 14.735 6.064 -52.265 1.00 30.45 ATOM 5357 C SER B 838 17.524 5.204 -52.661 1.00 25.30 ATOM 5358 O SER B 838 18.210 5.885 -53.431 1.00 25.38 ATOM 5359 N PHE B 839 17.806 5.095 -51.364 1.00 24.10 ATOM 5360 CA PHE B 839 18.986 5.756 -50.804 1.00 23.41 ATOM 5361 CB PHE B 839 19.044 5.550 -49.279 1.00 23.44 ATOM 5362 CG PHE B 839 20.304 6.088 -48.623 1.00 22.87 ATOM 5363 CD1 PHE B 839 20.663 7.428 -48.754 1.00 22.23 ATOM 5364 CD2 PHE B 839 21.116 5.251 -47.848 1.00 22.21 ATOM 5365 CE1 PHE B 839 21.811 7.927 -48.123 1.00 22.96 ATOM 5366 CE2 PHE B 839 22.266 5.741 -47.214 1.00 22.39 ATOM 5367 CZ PHE B 839 22.613 7.077 -47.350 1.00 22.00 ATOM 5368 C PHE B 839 20.219 5.145 -51.464 1.00 22.55 ATOM 5369 O PHE B 839 21.254 5.799 -51.598 1.00 22.76 ATOM 5370 N PHE B 840 20.105 3.893 -51.901 1.00 22.13 ATOM 5371 CA PHE B 840 21.236 3.223 -52.533 1.00 21.90 ATOM 5372 CB PHE B 840 21.298 1.759 -52.085 1.00 21.08 ATOM 5373 CG PHE B 840 21.436 1.587 -50.595 1.00 20.08 ATOM 5374 CD1 PHE B 840 22.575 2.034 -49.927 1.00 19.68 ATOM 5375 CD2 PHE B 840 20.422 0.989 -49.857 1.00 19.64 ATOM 5376 CE1 PHE B 840 22.701 1.886 -48.535 1.00 18.79 ATOM 5377 CE2 PHE B 840 20.541 0.839 -48.465 1.00 20.03 ATOM 5378 CZ PHE B 840 21.685 1.289 -47.806 1.00 19.12 ATOM 5379 C PHE B 840 21.241 3.296 -54.064 1.00 22.90 ATOM 5380 O PHE B 840 22.069 2.662 -54.720 1.00 22.36 ATOM 5381 N ASP B 841 20.334 4.077 -54.638 1.00 23.97 ATOM 5382 CA ASP B 841 20.279 4.183 -56.095 1.00 25.59 ATOM 5383 CB ASP B 841 19.181 5.160 -56.511 1.00 26.83 ATOM 5384 CG ASP B 841 17.798 4.535 -56.470 1.00 28.80 ATOM 5385 OD1 ASP B 841 17.702 3.299 -56.289 1.00 29.87 ATOM 5386 OD2 ASP B 841 16.805 5.285 -56.612 1.00 29.35 ATOM 5387 C ASP B 841 21.600 4.595 -56.741 1.00 25.93 ATOM 5388 O ASP B 841 21.948 4.100 -57.813 1.00 26.86 ATOM 5389 N GLU B 842 22.340 5.488 -56.090 1.00 25.58 ATOM 5390 CA GLU B 842 23.613 5.953 -56.630 1.00 25.15 ATOM 5391 CB GLU B 842 24.233 7.011 -55.712 1.00 26.51 ATOM 5392 CG GLU B 842 25.610 7.460 -56.176 1.00 29.03 ATOM 5393 CD GLU B 842 26.163 8.627 -55.383 1.00 30.05 ATOM 5394 OE1 GLU B 842 25.576 8.979 -54.336 1.00 31.06 ATOM 5395 OE2 GLU B 842 27.194 9.187 -55.811 1.00 31.60 ATOM 5396 C GLU B 842 24.610 4.812 -56.825 1.00 24.16 ATOM 5397 O GLU B 842 25.431 4.841 -57.747 1.00 23.68 ATOM 5398 N LEU B 843 24.541 3.813 -55.951 1.00 22.59 ATOM 5399 CA LEU B 843 25.436 2.665 -56.033 1.00 21.72 ATOM 5400 CB LEU B 843 25.270 1.784 -54.790 1.00 21.43 ATOM 5401 CG LEU B 843 25.540 2.444 -53.431 1.00 20.46 ATOM 5402 CD1 LEU B 843 25.558 1.377 -52.330 1.00 18.89 ATOM 5403 CD2 LEU B 843 26.882 3.190 -53.476 1.00 19.51 ATOM 5404 C LEU B 843 25.165 1.832 -57.289 1.00 21.72 ATOM 5405 O LEU B 843 26.046 1.130 -57.776 1.00 21.41 ATOM 5406 N ARG B 844 23.944 1.918 -57.804 1.00 22.63 ATOM 5407 CA ARG B 844 23.548 1.162 -58.989 1.00 23.59 ATOM 5408 CB ARG B 844 22.067 0.774 -58.886 1.00 22.43 ATOM 5409 CG ARG B 844 21.785 -0.352 -57.879 1.00 21.99 ATOM 5410 CD ARG B 844 20.292 -0.682 -57.781 1.00 21.49 ATOM 5411 NE ARG B 844 19.541 0.258 -56.943 1.00 22.18 ATOM 5412 CZ ARG B 844 19.403 0.149 -55.621 1.00 22.06 ATOM 5413 NH1 ARG B 844 19.965 -0.861 -54.972 1.00 21.19 ATOM 5414 NH2 ARG B 844 18.705 1.050 -54.949 1.00 22.08 ATOM 5415 C ARG B 844 23.810 1.930 -60.290 1.00 25.51 ATOM 5416 O ARG B 844 23.520 1.435 -61.380 1.00 25.86 ATOM 5417 N ASP B 845 24.352 3.139 -60.169 1.00 27.20 ATOM 5418 CA ASP B 845 24.679 3.951 -61.336 1.00 29.07 ATOM 5419 CB ASP B 845 24.981 5.392 -60.916 1.00 30.21 ATOM 5420 CG ASP B 845 25.162 6.319 -62.105 1.00 32.05 ATOM 5421 OD1 ASP B 845 25.981 6.006 -62.992 1.00 32.18 ATOM 5422 OD2 ASP B 845 24.482 7.365 -62.153 1.00 34.44 ATOM 5423 C ASP B 845 25.907 3.331 -62.004 1.00 29.60 ATOM 5424 O ASP B 845 26.909 3.039 -61.349 1.00 29.51 ATOM 5425 N PRO B 846 25.857 3.144 -63.328 1.00 30.60 ATOM 5426 CD PRO B 846 24.769 3.513 -64.252 1.00 30.82 ATOM 5427 CA PRO B 846 26.997 2.542 -64.026 1.00 31.51 ATOM 5428 CB PRO B 846 26.514 2.429 -65.475 1.00 31.14 ATOM 5429 CG PRO B 846 25.445 3.485 -65.594 1.00 31.78 ATOM 5430 C PRO B 846 28.310 3.319 -63.919 1.00 32.58 ATOM 5431 O PRO B 846 29.392 2.738 -64.032 1.00 33.17 ATOM 5432 N ASN B 847 28.225 4.622 -63.689 1.00 33.17 ATOM 5433 CA ASN B 847 29.436 5.432 -63.613 1.00 35.10 ATOM 5434 CB ASN B 847 29.244 6.732 -64.393 1.00 36.61 ATOM 5435 CG ASN B 847 28.906 6.488 -65.845 1.00 38.05 ATOM 5436 OD1 ASN B 847 28.040 7.160 -66.410 1.00 40.59 ATOM 5437 ND2 ASN B 847 29.583 5.519 -66.460 1.00 37.90 ATOM 5438 C ASN B 847 29.915 5.764 -62.215 1.00 35.03 ATOM 5439 O ASN B 847 30.873 6.515 -62.058 1.00 35.62 ATOM 5440 N VAL B 848 29.258 5.214 -61.201 1.00 35.21 ATOM 5441 CA VAL B 848 29.664 5.482 -59.826 1.00 35.19 ATOM 5442 CB VAL B 848 28.685 4.817 -58.816 1.00 34.88 ATOM 5443 CG1 VAL B 848 28.926 3.314 -58.750 1.00 33.58 ATOM 5444 CG2 VAL B 848 28.845 5.459 -57.440 1.00 34.35 ATOM 5445 C VAL B 848 31.094 4.992 -59.568 1.00 35.75 ATOM 5446 O VAL B 848 31.498 3.933 -60.048 1.00 35.88 ATOM 5447 N LYS B 849 31.866 5.777 -58.824 1.00 36.45 ATOM 5448 CA LYS B 849 33.241 5.410 -58.494 1.00 37.28 ATOM 5449 CB LYS B 849 34.223 6.041 -59.490 1.00 37.90 ATOM 5450 CG LYS B 849 34.087 5.534 -60.918 1.00 39.36 ATOM 5451 CD LYS B 849 34.780 4.194 -61.099 1.00 40.88 ATOM 5452 CE LYS B 849 34.458 3.586 -62.461 1.00 42.54 ATOM 5453 NZ LYS B 849 32.986 3.499 -62.709 1.00 43.68 ATOM 5454 C LYS B 849 33.561 5.908 -57.090 1.00 37.40 ATOM 5455 O LYS B 849 32.860 6.769 -56.562 1.00 36.95 ATOM 5456 N LEU B 850 34.608 5.358 -56.482 1.00 37.36 ATOM 5457 CA LEU B 850 35.011 5.799 -55.153 1.00 38.49 ATOM 5458 CB LEU B 850 36.061 4.856 -54.564 1.00 37.01 ATOM 5459 CG LEU B 850 35.651 3.431 -54.199 1.00 36.88 ATOM 5460 CD1 LEU B 850 36.759 2.801 -53.362 1.00 36.78 ATOM 5461 CD2 LEU B 850 34.337 3.440 -53.435 1.00 35.65 ATOM 5462 C LEU B 850 35.631 7.182 -55.325 1.00 39.95 ATOM 5463 O LEU B 850 36.140 7.507 -56.400 1.00 40.12 ATOM 5464 N PRO B 851 35.580 8.025 -54.281 1.00 41.40 ATOM 5465 CD PRO B 851 34.953 7.833 -52.962 1.00 41.22 ATOM 5466 CA PRO B 851 36.177 9.361 -54.416 1.00 42.75 ATOM 5467 CB PRO B 851 36.017 9.968 -53.022 1.00 42.72 ATOM 5468 CG PRO B 851 34.851 9.235 -52.432 1.00 41.73 ATOM 5469 C PRO B 851 37.645 9.293 -54.862 1.00 44.06 ATOM 5470 O PRO B 851 38.122 10.164 -55.589 1.00 44.08 ATOM 5471 N ASN B 852 38.357 8.253 -54.434 1.00 45.49 ATOM 5472 CA ASN B 852 39.759 8.095 -54.810 1.00 46.54 ATOM 5473 CB ASN B 852 40.468 7.126 -53.852 1.00 47.61 ATOM 5474 CG ASN B 852 39.886 5.721 -53.889 1.00 49.09 ATOM 5475 OD1 ASN B 852 40.210 4.879 -53.042 1.00 49.90 ATOM 5476 ND2 ASN B 852 39.024 5.459 -54.868 1.00 49.34 ATOM 5477 C ASN B 852 39.901 7.607 -56.251 1.00 46.69 ATOM 5478 O ASN B 852 40.930 7.047 -56.621 1.00 47.34 ATOM 5479 N GLY B 853 38.858 7.823 -57.053 1.00 46.42 ATOM 5480 CA GLY B 853 38.877 7.418 -58.449 1.00 45.72 ATOM 5481 C GLY B 853 38.765 5.922 -58.701 1.00 45.38 ATOM 5482 O GLY B 853 38.482 5.493 -59.822 1.00 45.34 ATOM 5483 N ARG B 854 38.986 5.127 -57.659 1.00 45.00 ATOM 5484 CA ARG B 854 38.922 3.671 -57.765 1.00 44.49 ATOM 5485 CB ARG B 854 39.555 3.050 -56.517 1.00 45.94 ATOM 5486 CG ARG B 854 39.733 1.550 -56.578 1.00 48.31 ATOM 5487 CD ARG B 854 40.437 1.040 -55.333 1.00 50.13 ATOM 5488 NE ARG B 854 41.620 1.838 -55.013 1.00 52.32 ATOM 5489 CZ ARG B 854 42.512 1.511 -54.081 1.00 53.21 ATOM 5490 NH1 ARG B 854 42.355 0.398 -53.373 1.00 54.04 ATOM 5491 NH2 ARG B 854 43.561 2.293 -53.856 1.00 53.60 ATOM 5492 C ARG B 854 37.502 3.119 -57.963 1.00 42.90 ATOM 5493 O ARG B 854 36.507 3.801 -57.711 1.00 42.20 ATOM 5494 N ASP B 855 37.419 1.878 -58.426 1.00 41.76 ATOM 5495 CA ASP B 855 36.135 1.216 -58.655 1.00 40.59 ATOM 5496 CB ASP B 855 36.344 -0.066 -59.452 1.00 42.11 ATOM 5497 CG ASP B 855 35.893 0.054 -60.882 1.00 43.63 ATOM 5498 OD1 ASP B 855 36.084 -0.926 -61.634 1.00 45.01 ATOM 5499 OD2 ASP B 855 35.352 1.117 -61.260 1.00 44.45 ATOM 5500 C ASP B 855 35.489 0.845 -57.327 1.00 39.01 ATOM 5501 O ASP B 855 36.186 0.611 -56.336 1.00 38.42 ATOM 5502 N THR B 856 34.162 0.789 -57.306 1.00 37.12 ATOM 5503 CA THR B 856 33.459 0.402 -56.086 1.00 35.95 ATOM 5504 CB THR B 856 31.926 0.666 -56.173 1.00 36.35 ATOM 5505 OG1 THR B 856 31.405 0.085 -57.374 1.00 38.16 ATOM 5506 CG2 THR B 856 31.625 2.154 -56.164 1.00 36.23 ATOM 5507 C THR B 856 33.667 -1.103 -55.922 1.00 34.34 ATOM 5508 O THR B 856 34.053 -1.787 -56.870 1.00 34.11 ATOM 5509 N PRO B 857 33.451 -1.632 -54.711 1.00 33.20 ATOM 5510 CD PRO B 857 33.067 -0.936 -53.474 1.00 32.56 ATOM 5511 CA PRO B 857 33.627 -3.076 -54.512 1.00 32.14 ATOM 5512 CB PRO B 857 33.648 -3.245 -52.991 1.00 32.52 ATOM 5513 CG PRO B 857 33.543 -1.857 -52.410 1.00 33.01 ATOM 5514 C PRO B 857 32.469 -3.853 -55.140 1.00 31.07 ATOM 5515 O PRO B 857 31.552 -3.264 -55.716 1.00 29.95 ATOM 5516 N ALA B 858 32.519 -5.176 -55.024 1.00 30.53 ATOM 5517 CA ALA B 858 31.467 -6.039 -55.559 1.00 29.74 ATOM 5518 CB ALA B 858 31.829 -7.495 -55.325 1.00 30.23 ATOM 5519 C ALA B 858 30.162 -5.702 -54.837 1.00 29.07 ATOM 5520 O ALA B 858 30.104 -5.728 -53.605 1.00 29.10 ATOM 5521 N LEU B 859 29.121 -5.386 -55.599 1.00 27.50 ATOM 5522 CA LEU B 859 27.843 -5.023 -55.006 1.00 26.76 ATOM 5523 CB LEU B 859 27.581 -3.533 -55.226 1.00 26.25 ATOM 5524 CG LEU B 859 28.619 -2.534 -54.715 1.00 26.22 ATOM 5525 CD1 LEU B 859 28.331 -1.158 -55.305 1.00 26.59 ATOM 5526 CD2 LEU B 859 28.583 -2.484 -53.190 1.00 25.78 ATOM 5527 C LEU B 859 26.651 -5.800 -55.547 1.00 26.30 ATOM 5528 O LEU B 859 25.584 -5.808 -54.932 1.00 25.31 ATOM 5529 N PHE B 860 26.820 -6.455 -56.689 1.00 26.07 ATOM 5530 CA PHE B 860 25.686 -7.157 -57.277 1.00 26.69 ATOM 5531 CB PHE B 860 25.273 -6.448 -58.576 1.00 26.92 ATOM 5532 CG PHE B 860 25.414 -4.950 -58.521 1.00 26.78 ATOM 5533 CD1 PHE B 860 26.425 -4.304 -59.232 1.00 26.90 ATOM 5534 CD2 PHE B 860 24.554 -4.184 -57.745 1.00 26.54 ATOM 5535 CE1 PHE B 860 26.575 -2.927 -59.168 1.00 25.76 ATOM 5536 CE2 PHE B 860 24.697 -2.799 -57.676 1.00 26.79 ATOM 5537 CZ PHE B 860 25.710 -2.173 -58.390 1.00 26.29 ATOM 5538 C PHE B 860 25.829 -8.653 -57.529 1.00 26.99 ATOM 5539 O PHE B 860 25.009 -9.239 -58.228 1.00 27.32 ATOM 5540 N ASN B 861 26.849 -9.278 -56.962 1.00 27.20 ATOM 5541 CA ASN B 861 27.016 -10.708 -57.149 1.00 28.55 ATOM 5542 CB ASN B 861 28.491 -11.099 -57.009 1.00 29.57 ATOM 5543 CG ASN B 861 29.141 -10.536 -55.759 1.00 31.93 ATOM 5544 OD1 ASN B 861 30.252 -10.939 -55.399 1.00 33.34 ATOM 5545 ND2 ASN B 861 28.465 -9.604 -55.094 1.00 31.69 ATOM 5546 C ASN B 861 26.146 -11.494 -56.162 1.00 28.44 ATOM 5547 O ASN B 861 26.638 -12.324 -55.396 1.00 28.78 ATOM 5548 N PHE B 862 24.845 -11.219 -56.197 1.00 28.88 ATOM 5549 CA PHE B 862 23.857 -11.870 -55.329 1.00 29.90 ATOM 5550 CB PHE B 862 22.497 -11.177 -55.473 1.00 28.90 ATOM 5551 CG PHE B 862 22.401 -9.851 -54.773 1.00 29.02 ATOM 5552 CD1 PHE B 862 22.067 -9.783 -53.420 1.00 28.46 ATOM 5553 CD2 PHE B 862 22.628 -8.663 -55.467 1.00 28.87 ATOM 5554 CE1 PHE B 862 21.960 -8.551 -52.764 1.00 27.72 ATOM 5555 CE2 PHE B 862 22.525 -7.426 -54.822 1.00 28.88 ATOM 5556 CZ PHE B 862 22.190 -7.371 -53.467 1.00 27.99 ATOM 5557 C PHE B 862 23.670 -13.349 -55.685 1.00 31.21 ATOM 5558 O PHE B 862 23.593 -13.694 -56.864 1.00 31.86 ATOM 5559 N THR B 863 23.588 -14.216 -54.676 1.00 31.61 ATOM 5560 CA THR B 863 23.370 -15.639 -54.926 1.00 32.28 ATOM 5561 CB THR B 863 24.222 -16.540 -54.007 1.00 32.24 ATOM 5562 OG1 THR B 863 23.811 -16.358 -52.647 1.00 32.80 ATOM 5563 CG2 THR B 863 25.709 -16.217 -54.157 1.00 31.83 ATOM 5564 C THR B 863 21.904 -15.950 -54.654 1.00 32.65 ATOM 5565 O THR B 863 21.177 -15.117 -54.100 1.00 32.82 ATOM 5566 N THR B 864 21.468 -17.145 -55.050 1.00 32.33 ATOM 5567 CA THR B 864 20.085 -17.563 -54.839 1.00 31.55 ATOM 5568 CB THR B 864 19.853 -18.991 -55.401 1.00 32.49 ATOM 5569 OG1 THR B 864 20.030 -18.978 -56.827 1.00 32.12 ATOM 5570 CG2 THR B 864 18.448 -19.476 -55.071 1.00 31.94 ATOM 5571 C THR B 864 19.762 -17.537 -53.341 1.00 31.27 ATOM 5572 O THR B 864 18.699 -17.066 -52.928 1.00 30.55 ATOM 5573 N GLN B 865 20.693 -18.044 -52.540 1.00 31.29 ATOM 5574 CA GLN B 865 20.547 -18.077 -51.085 1.00 31.89 ATOM 5575 CB GLN B 865 21.848 -18.584 -50.450 1.00 33.50 ATOM 5576 CG GLN B 865 21.829 -18.659 -48.924 1.00 36.10 ATOM 5577 CD GLN B 865 20.809 -19.659 -48.411 1.00 38.22 ATOM 5578 OE1 GLN B 865 20.446 -20.610 -49.115 1.00 39.26 ATOM 5579 NE2 GLN B 865 20.335 -19.452 -47.182 1.00 38.37 ATOM 5580 C GLN B 865 20.242 -16.665 -50.576 1.00 31.24 ATOM 5581 O GLN B 865 19.228 -16.421 -49.917 1.00 30.77 ATOM 5582 N GLU B 866 21.135 -15.741 -50.910 1.00 30.33 ATOM 5583 CA GLU B 866 21.014 -14.348 -50.511 1.00 29.83 ATOM 5584 CB GLU B 866 22.166 -13.554 -51.130 1.00 30.18 ATOM 5585 CG GLU B 866 22.532 -12.286 -50.393 1.00 31.47 ATOM 5586 CD GLU B 866 23.792 -11.649 -50.954 1.00 31.97 ATOM 5587 OE1 GLU B 866 24.120 -10.521 -50.532 1.00 32.68 ATOM 5588 OE2 GLU B 866 24.454 -12.277 -51.813 1.00 31.99 ATOM 5589 C GLU B 866 19.680 -13.719 -50.909 1.00 29.01 ATOM 5590 O GLU B 866 19.127 -12.899 -50.176 1.00 28.05 ATOM 5591 N LEU B 867 19.156 -14.108 -52.067 1.00 28.45 ATOM 5592 CA LEU B 867 17.893 -13.554 -52.548 1.00 27.86 ATOM 5593 CB LEU B 867 17.911 -13.477 -54.079 1.00 27.68 ATOM 5594 CG LEU B 867 19.027 -12.648 -54.717 1.00 27.46 ATOM 5595 CD1 LEU B 867 19.263 -13.100 -56.158 1.00 27.82 ATOM 5596 CD2 LEU B 867 18.632 -11.184 -54.685 1.00 26.89 ATOM 5597 C LEU B 867 16.658 -14.347 -52.114 1.00 28.21 ATOM 5598 O LEU B 867 15.532 -13.890 -52.300 1.00 26.85 ATOM 5599 N SER B 868 16.870 -15.520 -51.526 1.00 28.94 ATOM 5600 CA SER B 868 15.758 -16.382 -51.131 1.00 30.06 ATOM 5601 CB SER B 868 16.266 -17.528 -50.248 1.00 30.25 ATOM 5602 OG SER B 868 16.942 -17.046 -49.104 1.00 32.37 ATOM 5603 C SER B 868 14.550 -15.710 -50.474 1.00 30.35 ATOM 5604 O SER B 868 13.417 -16.064 -50.773 1.00 30.75 ATOM 5605 N SER B 869 14.773 -14.733 -49.601 1.00 30.46 ATOM 5606 CA SER B 869 13.657 -14.069 -48.928 1.00 30.36 ATOM 5607 CB SER B 869 14.182 -13.077 -47.874 1.00 30.90 ATOM 5608 OG SER B 869 14.341 -11.763 -48.404 1.00 29.52 ATOM 5609 C SER B 869 12.671 -13.348 -49.854 1.00 30.65 ATOM 5610 O SER B 869 11.523 -13.127 -49.479 1.00 30.56 ATOM 5611 N ASN B 870 13.107 -12.977 -51.056 1.00 30.35 ATOM 5612 CA ASN B 870 12.238 -12.259 -51.992 1.00 30.09 ATOM 5613 CB ASN B 870 11.932 -10.859 -51.437 1.00 30.43 ATOM 5614 CG ASN B 870 10.763 -10.185 -52.134 1.00 31.40 ATOM 5615 OD1 ASN B 870 10.411 -10.534 -53.261 1.00 32.22 ATOM 5616 ND2 ASN B 870 10.156 -9.208 -51.467 1.00 31.43 ATOM 5617 C ASN B 870 12.938 -12.161 -53.355 1.00 30.11 ATOM 5618 O ASN B 870 13.411 -11.095 -53.754 1.00 29.81 ATOM 5619 N PRO B 871 13.009 -13.285 -54.090 1.00 30.32 ATOM 5620 CD PRO B 871 12.483 -14.615 -53.729 1.00 29.70 ATOM 5621 CA PRO B 871 13.663 -13.309 -55.402 1.00 29.73 ATOM 5622 CB PRO B 871 13.277 -14.677 -55.959 1.00 30.16 ATOM 5623 CG PRO B 871 13.142 -15.520 -54.732 1.00 30.15 ATOM 5624 C PRO B 871 13.350 -12.167 -56.371 1.00 29.39 ATOM 5625 O PRO B 871 14.251 -11.662 -57.032 1.00 28.92 ATOM 5626 N PRO B 872 12.077 -11.740 -56.467 1.00 29.27 ATOM 5627 CD PRO B 872 10.880 -12.232 -55.768 1.00 29.94 ATOM 5628 CA PRO B 872 11.749 -10.647 -57.390 1.00 29.47 ATOM 5629 CB PRO B 872 10.231 -10.492 -57.250 1.00 29.50 ATOM 5630 CG PRO B 872 9.763 -11.773 -56.657 1.00 29.50 ATOM 5631 C PRO B 872 12.484 -9.325 -57.141 1.00 29.32 ATOM 5632 O PRO B 872 12.540 -8.465 -58.027 1.00 28.49 ATOM 5633 N LEU B 873 13.043 -9.154 -55.945 1.00 28.23 ATOM 5634 CA LEU B 873 13.763 -7.920 -55.644 1.00 27.84 ATOM 5635 CB LEU B 873 14.166 -7.874 -54.166 1.00 27.41 ATOM 5636 CG LEU B 873 13.028 -7.436 -53.245 1.00 27.23 ATOM 5637 CD1 LEU B 873 13.527 -7.306 -51.810 1.00 27.29 ATOM 5638 CD2 LEU B 873 12.469 -6.116 -53.738 1.00 27.65 ATOM 5639 C LEU B 873 15.000 -7.801 -56.522 1.00 27.49 ATOM 5640 O LEU B 873 15.544 -6.711 -56.698 1.00 27.24 ATOM 5641 N ALA B 874 15.441 -8.929 -57.068 1.00 27.49 ATOM 5642 CA ALA B 874 16.610 -8.945 -57.938 1.00 28.02 ATOM 5643 CB ALA B 874 16.887 -10.357 -58.415 1.00 27.52 ATOM 5644 C ALA B 874 16.426 -8.014 -59.138 1.00 28.30 ATOM 5645 O ALA B 874 17.407 -7.529 -59.704 1.00 28.13 ATOM 5646 N THR B 875 15.177 -7.755 -59.522 1.00 28.68 ATOM 5647 CA THR B 875 14.915 -6.880 -60.666 1.00 29.20 ATOM 5648 CB THR B 875 13.427 -6.893 -61.061 1.00 29.30 ATOM 5649 OG1 THR B 875 12.643 -6.339 -59.999 1.00 29.77 ATOM 5650 CG2 THR B 875 12.971 -8.323 -61.346 1.00 28.81 ATOM 5651 C THR B 875 15.346 -5.445 -60.387 1.00 29.38 ATOM 5652 O THR B 875 15.479 -4.636 -61.305 1.00 29.25 ATOM 5653 N ILE B 876 15.556 -5.134 -59.111 1.00 29.49 ATOM 5654 CA ILE B 876 16.004 -3.807 -58.696 1.00 29.34 ATOM 5655 CB ILE B 876 15.198 -3.272 -57.484 1.00 30.12 ATOM 5656 CG2 ILE B 876 15.879 -2.027 -56.904 1.00 30.71 ATOM 5657 CG1 ILE B 876 13.773 -2.941 -57.904 1.00 30.33 ATOM 5658 CD1 ILE B 876 12.874 -2.622 -56.741 1.00 30.79 ATOM 5659 C ILE B 876 17.462 -3.915 -58.262 1.00 28.89 ATOM 5660 O ILE B 876 18.306 -3.113 -58.658 1.00 28.69 ATOM 5661 N LEU B 877 17.745 -4.933 -57.456 1.00 27.61 ATOM 5662 CA LEU B 877 19.080 -5.153 -56.925 1.00 26.42 ATOM 5663 CB LEU B 877 19.058 -6.360 -55.986 1.00 25.52 ATOM 5664 CG LEU B 877 18.226 -6.140 -54.718 1.00 25.56 ATOM 5665 CD1 LEU B 877 18.138 -7.436 -53.927 1.00 24.59 ATOM 5666 CD2 LEU B 877 18.859 -5.030 -53.875 1.00 24.74 ATOM 5667 C LEU B 877 20.184 -5.317 -57.966 1.00 26.48 ATOM 5668 O LEU B 877 21.298 -4.825 -57.778 1.00 25.48 ATOM 5669 N ILE B 878 19.893 -6.025 -59.051 1.00 26.26 ATOM 5670 CA ILE B 878 20.889 -6.211 -60.097 1.00 26.81 ATOM 5671 CB ILE B 878 20.870 -7.654 -60.628 1.00 26.67 ATOM 5672 CG2 ILE B 878 22.034 -7.871 -61.576 1.00 26.13 ATOM 5673 CG1 ILE B 878 20.960 -8.634 -59.450 1.00 26.46 ATOM 5674 CD1 ILE B 878 20.786 -10.080 -59.841 1.00 26.90 ATOM 5675 C ILE B 878 20.568 -5.223 -61.218 1.00 26.97 ATOM 5676 O ILE B 878 19.597 -5.401 -61.955 1.00 27.04 ATOM 5677 N PRO B 879 21.370 -4.149 -61.338 1.00 26.94 ATOM 5678 CD PRO B 879 22.547 -3.835 -60.503 1.00 27.10 ATOM 5679 CA PRO B 879 21.156 -3.133 -62.370 1.00 26.94 ATOM 5680 CB PRO B 879 22.085 -1.995 -61.944 1.00 26.84 ATOM 5681 CG PRO B 879 23.190 -2.680 -61.228 1.00 26.72 ATOM 5682 C PRO B 879 21.453 -3.644 -63.783 1.00 27.05 ATOM 5683 O PRO B 879 22.274 -4.544 -63.972 1.00 26.61 ATOM 5684 N PRO B 880 20.788 -3.060 -64.794 1.00 28.07 ATOM 5685 CD PRO B 880 19.816 -1.960 -64.658 1.00 27.76 ATOM 5686 CA PRO B 880 20.974 -3.457 -66.196 1.00 28.65 ATOM 5687 CB PRO B 880 20.295 -2.339 -66.981 1.00 28.98 ATOM 5688 CG PRO B 880 19.254 -1.820 -66.053 1.00 29.00 ATOM 5689 C PRO B 880 22.426 -3.633 -66.606 1.00 29.56 ATOM 5690 O PRO B 880 22.787 -4.658 -67.184 1.00 30.56 ATOM 5691 N HIS B 881 23.268 -2.645 -66.305 1.00 29.77 ATOM 5692 CA HIS B 881 24.671 -2.738 -66.687 1.00 29.91 ATOM 5693 CB HIS B 881 25.429 -1.446 -66.327 1.00 30.02 ATOM 5694 CG HIS B 881 25.709 -1.271 -64.865 1.00 29.91 ATOM 5695 CD2 HIS B 881 24.981 -0.689 -63.881 1.00 29.83 ATOM 5696 ND1 HIS B 881 26.889 -1.675 -64.280 1.00 30.48 ATOM 5697 CE1 HIS B 881 26.879 -1.348 -62.998 1.00 30.04 ATOM 5698 NE2 HIS B 881 25.733 -0.749 -62.731 1.00 30.16 ATOM 5699 C HIS B 881 25.362 -3.946 -66.088 1.00 30.36 ATOM 5700 O HIS B 881 26.352 -4.423 -66.626 1.00 30.14 ATOM 5701 N ALA B 882 24.831 -4.456 -64.981 1.00 31.45 ATOM 5702 CA ALA B 882 25.424 -5.621 -64.335 1.00 32.43 ATOM 5703 CB ALA B 882 25.075 -5.632 -62.841 1.00 32.51 ATOM 5704 C ALA B 882 24.948 -6.911 -65.001 1.00 33.47 ATOM 5705 O ALA B 882 25.415 -8.001 -64.672 1.00 33.22 ATOM 5706 N ARG B 883 24.024 -6.784 -65.945 1.00 34.91 ATOM 5707 CA ARG B 883 23.495 -7.945 -66.653 1.00 36.58 ATOM 5708 CB ARG B 883 21.973 -7.884 -66.699 1.00 35.55 ATOM 5709 CG ARG B 883 21.333 -7.650 -65.358 1.00 34.75 ATOM 5710 CD ARG B 883 19.843 -7.572 -65.520 1.00 34.53 ATOM 5711 NE ARG B 883 19.205 -6.932 -64.380 1.00 33.71 ATOM 5712 CZ ARG B 883 17.917 -6.620 -64.339 1.00 33.93 ATOM 5713 NH1 ARG B 883 17.140 -6.895 -65.381 1.00 34.49 ATOM 5714 NH2 ARG B 883 17.407 -6.044 -63.260 1.00 33.35 ATOM 5715 C ARG B 883 24.024 -8.036 -68.081 1.00 38.17 ATOM 5716 O ARG B 883 23.602 -8.901 -68.853 1.00 38.14 ATOM 5717 N ILE B 884 24.934 -7.136 -68.436 1.00 40.10 ATOM 5718 CA ILE B 884 25.500 -7.130 -69.777 1.00 42.34 ATOM 5719 CB ILE B 884 26.326 -5.858 -70.024 1.00 41.01 ATOM 5720 CG2 ILE B 884 27.157 -6.011 -71.283 1.00 40.80 ATOM 5721 CG1 ILE B 884 25.390 -4.656 -70.146 1.00 40.21 ATOM 5722 CD1 ILE B 884 26.099 -3.314 -70.091 1.00 39.60 ATOM 5723 C ILE B 884 26.381 -8.353 -70.009 1.00 45.06 ATOM 5724 O ILE B 884 27.266 -8.655 -69.205 1.00 45.16 ATOM 5725 N GLN B 885 26.125 -9.048 -71.118 1.00 47.98 ATOM 5726 CA GLN B 885 26.875 -10.246 -71.489 1.00 50.86 ATOM 5727 CB GLN B 885 26.317 -10.830 -72.790 1.00 51.79 ATOM 5728 CG GLN B 885 25.760 -12.238 -72.660 1.00 53.64 ATOM 5729 CD GLN B 885 25.706 -12.967 -73.987 1.00 54.91 ATOM 5730 OE1 GLN B 885 25.251 -12.422 -74.993 1.00 55.98 ATOM 5731 NE2 GLN B 885 26.173 -14.208 -73.997 1.00 56.22 ATOM 5732 C GLN B 885 28.360 -9.940 -71.661 1.00 52.46 ATOM 5733 O GLN B 885 29.201 -10.511 -70.961 1.00 53.13 ATOM 5734 N ALA B 886 28.670 -9.043 -72.597 1.00 53.94 ATOM 5735 CA ALA B 886 30.046 -8.632 -72.880 1.00 55.43 ATOM 5736 CB ALA B 886 30.670 -7.999 -71.624 1.00 55.96 ATOM 5737 C ALA B 886 30.936 -9.775 -73.391 1.00 56.53 ATOM 5738 O ALA B 886 31.719 -9.523 -74.336 1.00 56.90 ATOM 5739 OT ALA B 886 30.849 -10.905 -72.850 1.00 57.43 HETATM 5740 PG PNP E 430 19.199 11.353 -13.922 1.00 50.73 HETATM 5741 O1G PNP E 430 19.918 12.168 -14.993 1.00 49.59 HETATM 5742 O2G PNP E 430 18.801 9.999 -14.503 1.00 49.93 HETATM 5743 O3G PNP E 430 20.216 11.158 -12.645 1.00 49.39 HETATM 5744 PB PNP E 430 17.384 13.588 -14.014 1.00 45.91 HETATM 5745 O1B PNP E 430 18.329 14.042 -15.138 1.00 47.12 HETATM 5746 O2B PNP E 430 15.972 13.567 -14.612 1.00 46.55 HETATM 5747 N3B PNP E 430 17.820 12.107 -13.384 1.00 47.83 HETATM 5748 PA PNP E 430 18.538 14.588 -11.555 1.00 36.62 HETATM 5749 O1A PNP E 430 17.691 14.731 -10.311 1.00 36.01 HETATM 5750 O2A PNP E 430 19.352 13.314 -11.537 1.00 37.46 HETATM 5751 O3A PNP E 430 17.595 14.660 -12.850 1.00 41.65 HETATM 5752 O5' PNP E 430 19.527 15.805 -11.704 1.00 36.49 HETATM 5753 C5' PNP E 430 20.591 15.704 -12.721 1.00 34.77 HETATM 5754 C4' PNP E 430 21.898 16.224 -12.189 1.00 33.16 HETATM 5755 O4' PNP E 430 21.611 17.573 -11.733 1.00 32.46 HETATM 5756 C3' PNP E 430 22.435 15.467 -10.955 1.00 33.09 HETATM 5757 O3' PNP E 430 23.076 14.216 -11.186 1.00 33.82 HETATM 5758 C2' PNP E 430 23.247 16.581 -10.304 1.00 32.71 HETATM 5759 O2' PNP E 430 24.607 16.668 -10.748 1.00 34.43 HETATM 5760 C1' PNP E 430 22.394 17.865 -10.573 1.00 31.48 HETATM 5761 N9 PNP E 430 21.545 18.057 -9.375 1.00 28.84 HETATM 5762 C8 PNP E 430 20.304 17.503 -8.979 1.00 28.65 HETATM 5763 N7 PNP E 430 19.705 17.823 -7.803 1.00 27.50 HETATM 5764 C5 PNP E 430 20.670 18.694 -7.376 1.00 25.98 HETATM 5765 C6 PNP E 430 20.774 19.475 -6.160 1.00 25.34 HETATM 5766 N6 PNP E 430 19.817 19.408 -5.230 1.00 24.60 HETATM 5767 N1 PNP E 430 21.855 20.297 -5.944 1.00 23.80 HETATM 5768 C2 PNP E 430 22.856 20.403 -6.854 1.00 24.98 HETATM 5769 N3 PNP E 430 22.931 19.766 -8.012 1.00 24.64 HETATM 5770 C4 PNP E 430 21.801 18.848 -8.332 1.00 27.01 HETATM 5771 PG PNP F 930 32.855 -8.133 -28.616 1.00 49.21 HETATM 5772 O1G PNP F 930 33.839 -7.393 -27.735 1.00 48.63 HETATM 5773 O2G PNP F 930 31.605 -8.459 -27.818 1.00 48.84 HETATM 5774 O3G PNP F 930 32.488 -7.178 -29.900 1.00 47.81 HETATM 5775 PB PNP F 930 35.047 -9.966 -28.800 1.00 44.86 HETATM 5776 O1B PNP F 930 35.761 -8.851 -28.032 1.00 45.94 HETATM 5777 O2B PNP F 930 35.111 -11.211 -27.902 1.00 44.88 HETATM 5778 N3B PNP F 930 33.489 -9.550 -29.205 1.00 46.38 HETATM 5779 PA PNP F 930 35.583 -9.379 -31.577 1.00 36.35 HETATM 5780 O1A PNP F 930 35.380 -10.425 -32.658 1.00 36.74 HETATM 5781 O2A PNP F 930 34.412 -8.420 -31.487 1.00 38.01 HETATM 5782 O3A PNP F 930 35.846 -10.101 -30.172 1.00 40.59 HETATM 5783 O5' PNP F 930 36.893 -8.542 -31.855 1.00 35.33 HETATM 5784 C5' PNP F 930 37.149 -7.363 -31.024 1.00 31.95 HETATM 5785 C4' PNP F 930 37.773 -6.267 -31.842 1.00 30.05 HETATM 5786 O4' PNP F 930 38.942 -6.869 -32.447 1.00 29.72 HETATM 5787 C3' PNP F 930 36.908 -5.767 -33.017 1.00 30.00 HETATM 5788 O3' PNP F 930 35.859 -4.849 -32.705 1.00 30.33 HETATM 5789 C2' PNP F 930 38.003 -5.301 -33.968 1.00 29.85 HETATM 5790 O2' PNP F 930 38.399 -3.938 -33.777 1.00 31.20 HETATM 5791 C1' PNP F 930 39.149 -6.336 -33.755 1.00 29.01 HETATM 5792 N9 PNP F 930 39.005 -7.382 -34.806 1.00 27.83 HETATM 5793 C8 PNP F 930 38.199 -8.544 -34.898 1.00 26.53 HETATM 5794 N7 PNP F 930 38.225 -9.370 -35.980 1.00 26.58 HETATM 5795 C5 PNP F 930 39.166 -8.664 -36.691 1.00 26.20 HETATM 5796 C6 PNP F 930 39.765 -8.900 -38.016 1.00 25.72 HETATM 5797 N6 PNP F 930 39.410 -9.952 -38.749 1.00 24.53 HETATM 5798 N1 PNP F 930 40.707 -8.038 -38.521 1.00 25.61 HETATM 5799 C2 PNP F 930 41.111 -6.948 -37.818 1.00 25.16 HETATM 5800 N3 PNP F 930 40.681 -6.573 -36.616 1.00 25.70 HETATM 5801 C4 PNP F 930 39.653 -7.445 -35.977 1.00 26.25 HETATM 5802 O HOH G 1 26.991 7.790 -12.088 1.00 19.36 SOLV O HETATM 5803 O HOH G 2 26.122 -4.513 -11.861 1.00 20.10 SOLV O HETATM 5804 O HOH G 3 14.869 7.142 -8.536 1.00 22.49 SOLV O HETATM 5805 O HOH G 4 20.106 -2.703 -9.306 1.00 18.58 SOLV O HETATM 5806 O HOH G 5 14.638 -0.463 6.277 1.00 21.53 SOLV O HETATM 5807 O HOH G 6 7.758 -0.495 -12.675 1.00 20.62 SOLV O HETATM 5808 O HOH G 7 21.978 4.791 -30.693 1.00 21.00 SOLV O HETATM 5809 O HOH G 8 23.392 5.195 -33.074 1.00 20.26 SOLV O HETATM 5810 O HOH G 9 19.389 0.977 -7.729 1.00 16.89 SOLV O HETATM 5811 O HOH G 10 21.946 -6.641 -33.426 1.00 17.46 SOLV O HETATM 5812 O HOH G 11 24.453 12.088 15.339 1.00 20.30 SOLV O HETATM 5813 O HOH G 12 17.736 -1.777 -19.949 1.00 23.28 SOLV O HETATM 5814 O HOH G 13 18.660 18.670 1.853 1.00 21.18 SOLV O HETATM 5815 O HOH G 14 30.080 -1.777 -11.806 1.00 18.33 SOLV O HETATM 5816 O HOH G 15 26.288 3.659 13.661 1.00 17.00 SOLV O HETATM 5817 O HOH G 16 20.986 -5.842 -20.955 1.00 25.45 SOLV O HETATM 5818 O HOH G 17 14.864 -0.417 8.830 1.00 25.94 SOLV O HETATM 5819 O HOH G 18 17.133 -13.140 -48.592 1.00 29.05 SOLV O HETATM 5820 O HOH G 19 24.965 13.230 7.761 1.00 20.11 SOLV O HETATM 5821 O HOH G 20 13.323 -6.523 -40.460 1.00 21.32 SOLV O HETATM 5822 O HOH G 21 23.990 9.874 8.531 1.00 17.13 SOLV O HETATM 5823 O HOH G 22 38.198 7.047 -7.423 1.00 27.19 SOLV O HETATM 5824 O HOH G 23 19.393 -16.927 -26.494 1.00 17.24 SOLV O HETATM 5825 O HOH G 24 13.814 -14.643 -36.934 1.00 23.89 SOLV O HETATM 5826 O HOH G 25 18.476 -9.148 0.832 1.00 27.18 SOLV O HETATM 5827 O HOH G 26 14.826 14.837 3.245 1.00 17.69 SOLV O HETATM 5828 O HOH G 27 17.521 -12.769 -45.997 1.00 25.08 SOLV O HETATM 5829 O HOH G 28 18.183 16.915 3.827 1.00 24.18 SOLV O HETATM 5830 O HOH G 29 37.543 14.916 -0.846 1.00 36.81 SOLV O HETATM 5831 O HOH G 30 15.702 -3.388 2.325 1.00 24.34 SOLV O HETATM 5832 O HOH G 31 17.162 -2.029 6.165 1.00 21.10 SOLV O HETATM 5833 O HOH G 32 7.428 3.310 -35.120 1.00 25.97 SOLV O HETATM 5834 O HOH G 33 22.382 -5.439 -23.499 1.00 22.05 SOLV O HETATM 5835 O HOH G 34 21.759 -3.173 -55.646 1.00 24.29 SOLV O HETATM 5836 O HOH G 35 12.245 -8.772 -33.152 1.00 19.41 SOLV O HETATM 5837 O HOH G 36 24.677 -2.563 -15.213 1.00 39.19 SOLV O HETATM 5838 O HOH G 37 9.927 -9.097 -36.843 1.00 29.71 SOLV O HETATM 5839 O HOH G 38 31.035 -0.014 -9.856 1.00 21.13 SOLV O HETATM 5840 O HOH G 39 11.588 16.200 1.067 1.00 31.19 SOLV O HETATM 5841 O HOH G 40 31.183 10.465 -37.488 1.00 27.40 SOLV O HETATM 5842 O HOH G 41 35.094 -8.867 -13.718 1.00 29.41 SOLV O HETATM 5843 O HOH G 42 29.741 2.658 -31.004 1.00 28.90 SOLV O HETATM 5844 O HOH G 43 29.174 -10.257 -29.814 1.00 23.35 SOLV O HETATM 5845 O HOH G 44 36.346 -11.274 -35.009 1.00 33.85 SOLV O HETATM 5846 O HOH G 45 9.687 -9.461 -32.363 1.00 24.11 SOLV O HETATM 5847 O HOH G 46 19.236 8.604 -53.948 1.00 41.97 SOLV O HETATM 5848 O HOH G 47 36.183 5.393 -8.061 1.00 27.73 SOLV O HETATM 5849 O HOH G 48 25.757 -6.215 10.174 1.00 36.92 SOLV O HETATM 5850 O HOH G 49 30.490 17.860 9.342 1.00 23.45 SOLV O HETATM 5851 O HOH G 50 37.276 -11.919 -45.242 1.00 29.35 SOLV O HETATM 5852 O HOH G 51 39.224 3.896 -1.575 1.00 22.57 SOLV O HETATM 5853 O HOH G 52 19.056 -6.306 0.672 1.00 23.56 SOLV O HETATM 5854 O HOH G 53 37.698 16.422 5.138 1.00 25.57 SOLV O HETATM 5855 O HOH G 54 32.730 -15.048 -45.445 1.00 28.69 SOLV O HETATM 5856 O HOH G 55 31.462 8.889 16.566 1.00 28.44 SOLV O HETATM 5857 O HOH G 56 39.236 -3.970 8.008 1.00 32.52 SOLV O HETATM 5858 O HOH G 57 18.865 -0.013 -17.576 1.00 25.20 SOLV O HETATM 5859 O HOH G 58 15.765 -8.200 -5.994 1.00 21.78 SOLV O HETATM 5860 O HOH G 59 29.189 -6.747 -58.524 1.00 26.99 SOLV O HETATM 5861 O HOH G 60 29.392 6.279 -12.704 1.00 26.95 SOLV O HETATM 5862 O HOH G 61 31.844 -5.648 -51.267 1.00 23.19 SOLV O HETATM 5863 O HOH G 62 34.639 -12.584 -36.260 1.00 29.68 SOLV O HETATM 5864 O HOH G 63 28.153 14.443 -11.308 1.00 35.15 SOLV O HETATM 5865 O HOH G 64 16.479 8.222 -12.061 1.00 31.08 SOLV O HETATM 5866 O HOH G 65 43.691 16.010 9.325 1.00 32.41 SOLV O HETATM 5867 O HOH G 66 13.530 14.542 0.940 1.00 24.11 SOLV O HETATM 5868 O HOH G 67 15.439 -10.743 -41.876 1.00 26.75 SOLV O HETATM 5869 O HOH G 68 4.964 3.132 -13.641 1.00 47.44 SOLV O HETATM 5870 O HOH G 69 27.322 -12.082 -32.709 1.00 22.50 SOLV O HETATM 5871 O HOH G 70 7.724 10.989 -11.770 1.00 30.21 SOLV O HETATM 5872 O HOH G 71 10.534 20.262 3.444 1.00 48.65 SOLV O HETATM 5873 O HOH G 72 26.205 20.138 4.736 1.00 37.51 SOLV O HETATM 5874 O HOH G 73 25.235 16.963 10.016 1.00 27.97 SOLV O HETATM 5875 O HOH G 74 18.943 -1.257 -22.639 1.00 29.80 SOLV O HETATM 5876 O HOH G 75 27.339 -17.566 -31.459 1.00 26.75 SOLV O HETATM 5877 O HOH G 76 18.859 -4.925 -31.481 1.00 20.61 SOLV O HETATM 5878 O HOH G 77 9.225 8.056 -9.123 1.00 24.20 SOLV O HETATM 5879 O HOH G 78 9.750 7.279 13.506 1.00 29.00 SOLV O HETATM 5880 O HOH G 79 35.233 -12.375 -46.871 1.00 27.03 SOLV O HETATM 5881 O HOH G 80 21.832 3.187 -11.270 1.00 30.44 SOLV O HETATM 5882 O HOH G 81 5.210 4.431 -6.097 1.00 26.64 SOLV O HETATM 5883 O HOH G 82 27.318 -4.528 -14.454 1.00 32.93 SOLV O HETATM 5884 O HOH G 83 22.352 -21.388 -33.124 1.00 27.99 SOLV O HETATM 5885 O HOH G 84 17.591 -4.840 8.726 1.00 30.56 SOLV O HETATM 5886 O HOH G 85 37.057 -1.159 -54.343 1.00 31.24 SOLV O HETATM 5887 O HOH G 86 22.386 19.436 6.018 1.00 55.78 SOLV O HETATM 5888 O HOH G 87 22.192 -4.447 -18.350 1.00 29.49 SOLV O HETATM 5889 O HOH G 88 9.707 10.493 8.204 1.00 32.49 SOLV O HETATM 5890 O HOH G 89 21.400 7.180 -54.057 1.00 30.31 SOLV O HETATM 5891 O HOH G 90 15.444 -9.629 -1.973 1.00 28.97 SOLV O HETATM 5892 O HOH G 91 12.084 0.638 15.069 1.00 26.15 SOLV O HETATM 5893 O HOH G 92 16.455 4.054 -13.813 1.00 24.15 SOLV O HETATM 5894 O HOH G 93 20.912 4.462 -60.369 1.00 38.65 SOLV O HETATM 5895 O HOH G 94 54.054 8.599 1.316 1.00 49.24 SOLV O HETATM 5896 O HOH G 95 12.020 -15.893 -33.152 1.00 39.65 SOLV O HETATM 5897 O HOH G 96 24.873 7.680 -65.100 1.00 45.80 SOLV O HETATM 5898 O HOH G 97 28.464 -5.972 -51.389 1.00 20.78 SOLV O HETATM 5899 O HOH G 98 36.095 0.901 10.600 1.00 28.35 SOLV O HETATM 5900 O HOH G 99 27.012 0.536 -60.294 1.00 27.81 SOLV O HETATM 5901 O HOH G 100 15.261 -3.610 5.066 1.00 36.11 SOLV O HETATM 5902 O HOH G 101 28.481 26.336 -3.435 1.00 40.55 SOLV O HETATM 5903 O HOH G 102 8.790 4.974 -10.935 1.00 44.61 SOLV O HETATM 5904 O HOH G 103 14.058 -11.339 -8.711 1.00 32.32 SOLV O HETATM 5905 O HOH G 104 18.533 1.561 -29.760 1.00 18.98 SOLV O HETATM 5906 O HOH G 105 44.682 0.109 -38.932 1.00 51.91 SOLV O HETATM 5907 O HOH G 106 6.292 -8.877 -8.366 1.00 44.13 SOLV O HETATM 5908 O HOH G 107 39.771 0.575 7.848 1.00 33.50 SOLV O HETATM 5909 O HOH G 108 32.948 -18.074 -28.933 1.00 33.54 SOLV O HETATM 5910 O HOH G 109 9.338 24.518 3.092 1.00 33.74 SOLV O HETATM 5911 O HOH G 110 39.636 6.755 -34.437 1.00 42.24 SOLV O HETATM 5912 O HOH G 111 22.585 0.186 -65.199 1.00 27.74 SOLV O HETATM 5913 O HOH G 112 19.207 15.246 -33.499 1.00 48.57 SOLV O HETATM 5914 O HOH G 113 14.592 -11.638 -44.521 1.00 38.09 SOLV O HETATM 5915 O HOH G 114 17.442 12.241 9.533 1.00 25.09 SOLV O HETATM 5916 O HOH G 115 26.808 -14.913 -4.694 1.00 34.31 SOLV O HETATM 5917 O HOH G 116 13.206 -9.501 -48.259 1.00 26.68 SOLV O HETATM 5918 O HOH G 117 41.267 7.268 5.574 1.00 29.88 SOLV O HETATM 5919 O HOH G 118 21.544 1.493 -63.123 1.00 33.50 SOLV O HETATM 5920 O HOH G 119 33.494 14.022 15.238 1.00 29.30 SOLV O HETATM 5921 O HOH G 120 34.135 -16.480 -47.240 1.00 32.96 SOLV O HETATM 5922 O HOH G 121 51.594 -8.873 -37.331 1.00 44.39 SOLV O HETATM 5923 O HOH G 122 16.249 11.487 -29.031 1.00 31.37 SOLV O HETATM 5924 O HOH G 123 16.247 -9.911 -46.256 1.00 26.92 SOLV O HETATM 5925 O HOH G 124 25.600 -9.278 -27.420 1.00 24.20 SOLV O HETATM 5926 O HOH G 125 23.318 15.478 7.549 1.00 37.25 SOLV O HETATM 5927 O HOH G 126 7.018 -5.932 -6.429 1.00 36.78 SOLV O HETATM 5928 O HOH G 127 33.903 1.648 17.332 1.00 39.96 SOLV O HETATM 5929 O HOH G 128 16.297 14.860 -6.305 1.00 25.54 SOLV O HETATM 5930 O HOH G 129 16.021 -1.448 20.126 1.00 29.34 SOLV O HETATM 5931 O HOH G 130 37.300 -0.174 -33.377 1.00 35.59 SOLV O HETATM 5932 O HOH G 131 2.862 28.159 3.949 1.00 41.80 SOLV O HETATM 5933 O HOH G 132 16.547 -16.741 -54.489 1.00 31.70 SOLV O HETATM 5934 O HOH G 133 29.680 -14.167 0.574 1.00 55.70 SOLV O HETATM 5935 O HOH G 134 12.744 -18.336 -51.942 1.00 46.35 SOLV O HETATM 5936 O HOH G 135 31.287 -11.455 -28.641 1.00 46.48 SOLV O HETATM 5937 O HOH G 136 29.309 -12.961 -51.688 1.00 37.20 SOLV O HETATM 5938 O HOH G 137 30.347 -19.266 -29.057 1.00 38.01 SOLV O HETATM 5939 O HOH G 138 16.231 -14.932 -40.034 1.00 27.99 SOLV O HETATM 5940 O HOH G 139 28.214 0.765 19.228 1.00 37.30 SOLV O HETATM 5941 O HOH G 140 33.375 -14.568 -35.090 1.00 31.11 SOLV O HETATM 5942 O HOH G 141 26.786 -20.115 -48.847 1.00 43.21 SOLV O HETATM 5943 O HOH G 142 16.685 -5.337 1.055 1.00 35.69 SOLV O HETATM 5944 O HOH G 143 37.846 -1.358 8.290 1.00 36.48 SOLV O HETATM 5945 O HOH G 144 10.655 -6.801 -40.079 1.00 28.36 SOLV O HETATM 5946 O HOH G 145 14.976 -9.675 0.481 1.00 39.76 SOLV O HETATM 5947 O HOH G 146 29.356 9.026 -36.151 1.00 34.26 SOLV O HETATM 5948 O HOH G 147 32.706 -16.018 -42.967 1.00 29.33 SOLV O HETATM 5949 O HOH G 148 8.624 8.390 -11.542 1.00 41.50 SOLV O HETATM 5950 O HOH G 149 29.477 8.500 -33.404 1.00 39.12 SOLV O HETATM 5951 O HOH G 150 33.358 -13.980 -28.868 1.00 34.46 SOLV O HETATM 5952 O HOH G 151 46.843 -21.327 -25.258 1.00 45.21 SOLV O HETATM 5953 O HOH G 152 14.201 16.748 4.965 1.00 34.67 SOLV O HETATM 5954 O HOH G 153 32.676 1.517 -59.763 1.00 37.27 SOLV O HETATM 5955 O HOH G 154 13.978 13.887 -6.978 1.00 33.28 SOLV O HETATM 5956 O HOH G 155 5.043 -2.674 -6.946 1.00 28.27 SOLV O HETATM 5957 O HOH G 156 14.390 -10.520 -6.182 1.00 30.30 SOLV O HETATM 5958 O HOH G 157 31.153 0.085 16.730 1.00 29.32 SOLV O HETATM 5959 O HOH G 158 35.315 5.320 -10.914 1.00 33.00 SOLV O HETATM 5960 O HOH G 159 8.818 -6.747 -2.512 1.00 33.59 SOLV O HETATM 5961 O HOH G 160 17.998 -1.236 21.581 1.00 40.18 SOLV O HETATM 5962 O HOH G 161 5.746 0.998 -35.881 1.00 32.90 SOLV O HETATM 5963 O HOH G 162 32.839 -27.007 -31.406 1.00 53.35 SOLV O HETATM 5964 O HOH G 163 12.815 3.365 -51.832 1.00 36.31 SOLV O HETATM 5965 O HOH G 164 11.348 -2.095 0.727 1.00 29.25 SOLV O HETATM 5966 O HOH G 165 -2.527 20.652 4.171 1.00 55.35 SOLV O HETATM 5967 O HOH G 166 36.973 -1.615 10.986 1.00 42.49 SOLV O HETATM 5968 O HOH G 167 44.096 -11.478 -44.500 1.00 41.27 SOLV O HETATM 5969 O HOH G 168 23.988 -15.747 -3.462 1.00 38.78 SOLV O HETATM 5970 O HOH G 169 33.656 -18.246 -42.913 1.00 40.35 SOLV O HETATM 5971 O HOH G 170 8.808 -6.001 -8.581 1.00 28.16 SOLV O HETATM 5972 O HOH G 171 39.682 -0.050 -59.148 1.00 49.29 SOLV O HETATM 5973 O HOH G 172 28.691 -22.259 -47.034 1.00 60.74 SOLV O HETATM 5974 O HOH G 173 32.666 6.256 -33.603 1.00 38.09 SOLV O HETATM 5975 O HOH G 174 12.968 -3.784 2.015 1.00 32.23 SOLV O HETATM 5976 O HOH G 175 14.346 -5.857 5.771 1.00 39.77 SOLV O HETATM 5977 O HOH G 176 12.382 -13.321 -39.209 1.00 35.24 SOLV O HETATM 5978 O HOH G 177 15.750 -20.022 -31.189 1.00 32.28 SOLV O HETATM 5979 O HOH G 178 25.951 19.446 -9.088 1.00 48.66 SOLV O HETATM 5980 O HOH G 179 -0.183 1.479 -33.666 1.00 43.17 SOLV O HETATM 5981 O HOH G 180 8.349 -2.311 3.974 1.00 52.43 SOLV O HETATM 5982 O HOH G 181 15.061 8.436 10.187 1.00 46.06 SOLV O HETATM 5983 O HOH G 182 12.852 -2.138 5.395 1.00 36.16 SOLV O HETATM 5984 O HOH G 183 17.456 16.142 -8.081 1.00 28.00 SOLV O HETATM 5985 O HOH G 184 33.877 -10.598 -25.546 1.00 38.71 SOLV O HETATM 5986 O HOH G 185 25.793 14.215 -11.393 1.00 53.30 SOLV O HETATM 5987 O HOH G 186 25.417 -4.269 -30.406 1.00 37.11 SOLV O HETATM 5988 O HOH G 187 32.895 20.826 14.002 1.00 50.78 SOLV O HETATM 5989 O HOH G 188 9.051 -5.826 -44.118 1.00 50.62 SOLV O HETATM 5990 O HOH G 189 26.010 18.513 -6.852 1.00 49.69 SOLV O HETATM 5991 O HOH G 190 29.894 -3.569 14.227 1.00 35.91 SOLV O HETATM 5992 O HOH G 191 25.950 1.426 21.652 1.00 38.16 SOLV O HETATM 5993 O HOH G 192 30.416 -6.977 10.563 1.00 31.47 SOLV O HETATM 5994 O HOH G 193 40.786 -3.563 -35.980 1.00 48.26 SOLV O HETATM 5995 O HOH G 194 9.360 13.217 -12.515 1.00 29.34 SOLV O HETATM 5996 O HOH G 195 37.061 20.772 3.378 1.00 48.19 SOLV O HETATM 5997 O HOH G 196 20.951 25.816 2.484 1.00 55.57 SOLV O HETATM 5998 O HOH G 197 11.617 3.348 18.918 1.00 37.80 SOLV O HETATM 5999 O HOH G 198 19.141 0.870 -61.614 1.00 36.93 SOLV O HETATM 6000 O HOH G 199 35.932 15.111 -11.286 1.00 42.73 SOLV O HETATM 6001 O HOH G 200 2.788 12.290 -1.157 1.00 35.79 SOLV O HETATM 6002 O HOH G 201 35.192 -14.369 -48.527 1.00 41.53 SOLV O HETATM 6003 O HOH G 202 47.867 -1.500 -2.127 1.00 48.95 SOLV O HETATM 6004 O HOH G 203 26.774 -13.452 -52.352 1.00 45.24 SOLV O HETATM 6005 O HOH G 204 38.431 18.402 3.304 1.00 34.89 SOLV O HETATM 6006 O HOH G 205 33.183 -22.521 -26.204 1.00 42.36 SOLV O HETATM 6007 O HOH G 206 5.697 2.849 -22.426 1.00 55.84 SOLV O HETATM 6008 O HOH G 207 31.092 8.710 -58.661 1.00 36.33 SOLV O HETATM 6009 O HOH G 208 30.110 -3.253 -58.207 1.00 53.43 SOLV O HETATM 6010 O HOH G 209 14.260 -11.781 -3.473 1.00 42.09 SOLV O HETATM 6011 O HOH G 210 14.467 -13.450 -41.286 1.00 36.07 SOLV O HETATM 6012 O HOH G 211 21.248 4.151 -63.862 1.00 48.79 SOLV O HETATM 6013 O HOH G 212 12.019 -16.146 -35.673 1.00 36.45 SOLV O HETATM 6014 O HOH G 213 10.677 -8.894 -48.834 1.00 42.11 SOLV O HETATM 6015 O HOH G 214 41.783 7.597 8.063 1.00 49.94 SOLV O HETATM 6016 O HOH G 215 41.437 16.065 11.433 1.00 35.73 SOLV O HETATM 6017 O HOH G 216 5.134 10.513 -12.571 1.00 31.80 SOLV O HETATM 6018 O HOH G 217 12.076 -12.328 -44.391 1.00 46.88 SOLV O HETATM 6019 O HOH G 218 24.091 33.208 -5.838 1.00 49.29 SOLV O HETATM 6020 O HOH G 219 17.440 -7.437 9.567 1.00 38.41 SOLV O HETATM 6021 O HOH G 220 39.911 -15.785 -24.161 1.00 52.94 SOLV O HETATM 6022 O HOH G 221 18.013 -7.316 -19.946 1.00 48.25 SOLV O HETATM 6023 O HOH G 222 18.187 -1.525 -60.883 1.00 33.88 SOLV O HETATM 6024 O HOH G 223 10.274 5.365 -37.844 1.00 31.24 SOLV O HETATM 6025 O HOH G 224 35.810 -6.756 -12.219 1.00 39.85 SOLV O HETATM 6026 O HOH G 225 7.835 5.216 -41.372 1.00 43.39 SOLV O HETATM 6027 O HOH G 226 16.594 17.440 6.065 1.00 36.55 SOLV O HETATM 6028 O HOH G 227 40.947 -10.125 -47.729 1.00 57.74 SOLV O HETATM 6029 O HOH G 228 39.946 7.833 13.394 1.00 39.91 SOLV O HETATM 6030 O HOH G 229 18.163 11.610 -30.727 1.00 31.92 SOLV O HETATM 6031 O HOH G 230 20.046 9.829 -23.035 1.00 40.03 SOLV O HETATM 6032 O HOH G 231 41.570 -1.590 -4.810 1.00 43.13 SOLV O HETATM 6033 O HOH G 232 9.122 -8.933 -1.142 1.00 58.25 SOLV O HETATM 6034 O HOH G 233 30.251 15.434 -35.506 1.00 53.17 SOLV O HETATM 6035 O HOH G 234 4.163 6.304 -4.429 1.00 48.18 SOLV O HETATM 6036 O HOH G 235 17.727 -21.635 -46.591 1.00 51.94 SOLV O HETATM 6037 O HOH G 236 44.907 9.064 -1.038 1.00 34.85 SOLV O HETATM 6038 O HOH G 237 28.023 -18.058 -28.695 1.00 49.66 SOLV O HETATM 6039 O HOH G 238 12.028 25.774 2.936 1.00 61.76 SOLV O HETATM 6040 O HOH G 239 2.392 25.610 -5.875 1.00 35.15 SOLV O HETATM 6041 O HOH G 240 32.550 -2.711 -59.124 1.00 58.28 SOLV O HETATM 6042 O HOH G 241 16.657 10.163 10.881 1.00 44.33 SOLV O HETATM 6043 O HOH G 242 17.006 -16.226 -57.015 1.00 38.79 SOLV O HETATM 6044 O HOH G 243 13.187 -17.638 -31.584 1.00 36.75 SOLV O HETATM 6045 O HOH G 244 33.322 -5.726 -19.738 1.00 36.73 SOLV O HETATM 6046 O HOH G 245 9.664 -0.740 15.107 1.00 33.20 SOLV O HETATM 6047 O HOH G 246 13.466 -15.382 -29.682 1.00 35.58 SOLV O HETATM 6048 O HOH G 247 9.813 -3.061 13.857 1.00 32.82 SOLV O HETATM 6049 O HOH G 248 29.757 -12.186 -2.841 1.00 37.79 SOLV O HETATM 6050 O HOH G 249 9.362 -9.447 -29.792 1.00 38.78 SOLV O HETATM 6051 O HOH G 250 28.226 -8.165 9.726 1.00 43.75 SOLV O HETATM 6052 O HOH G 251 12.820 -1.018 -50.432 1.00 36.42 SOLV O HETATM 6053 O HOH G 252 3.298 -0.092 -37.452 1.00 55.54 SOLV O HETATM 6054 O HOH G 253 11.998 -25.635 -31.030 1.00 57.25 SOLV O HETATM 6055 O HOH G 254 15.090 -4.057 20.191 1.00 40.66 SOLV O HETATM 6056 O HOH G 255 21.719 12.226 -30.616 1.00 53.27 SOLV O HETATM 6057 O HOH G 256 36.360 19.661 15.272 1.00 44.98 SOLV O HETATM 6058 O HOH G 257 34.231 -5.322 -30.265 1.00 41.85 SOLV O HETATM 6059 O HOH G 258 15.496 -13.985 -44.691 1.00 39.74 SOLV O HETATM 6060 O HOH G 259 3.300 30.262 -9.313 1.00 38.74 SOLV O HETATM 6061 O HOH G 260 11.936 8.561 10.291 1.00 46.36 SOLV O HETATM 6062 O HOH G 261 12.236 -6.138 0.134 1.00 48.29 SOLV O HETATM 6063 O HOH G 262 64.740 -20.918 -40.941 1.00 59.87 SOLV O HETATM 6064 O HOH G 263 28.330 17.648 13.526 1.00 65.55 SOLV O HETATM 6065 O HOH G 264 26.959 15.236 -33.794 1.00 48.56 SOLV O HETATM 6066 O HOH G 265 11.078 5.055 -47.740 1.00 42.09 SOLV O HETATM 6067 O HOH G 266 34.925 -6.269 -54.132 1.00 35.26 SOLV O HETATM 6068 O HOH G 267 29.265 11.917 -50.972 1.00 40.30 SOLV O HETATM 6069 O HOH G 268 42.645 5.044 -9.178 1.00 47.53 SOLV O HETATM 6070 O HOH G 269 15.651 -16.576 -37.475 1.00 53.90 SOLV O HETATM 6071 O HOH G 270 10.367 -12.239 -13.081 1.00 51.83 SOLV O HETATM 6072 O HOH G 271 10.847 27.306 -13.915 1.00 45.10 SOLV O HETATM 6073 O HOH G 272 28.922 -25.620 -38.802 1.00 41.27 SOLV O HETATM 6074 O HOH G 273 23.636 -22.667 -37.471 1.00 50.89 SOLV O HETATM 6075 O HOH G 274 -0.800 22.995 -3.456 1.00 51.30 SOLV O HETATM 6076 O HOH G 275 8.604 37.075 -12.613 1.00 59.07 SOLV O HETATM 6077 O HOH G 276 37.190 -4.491 -53.752 1.00 45.42 SOLV O HETATM 6078 O HOH G 277 18.754 1.826 -58.988 1.00 36.65 SOLV O HETATM 6079 O HOH G 278 10.570 12.494 -15.011 1.00 64.77 SOLV O HETATM 6080 O HOH G 279 27.334 18.941 9.365 1.00 42.85 SOLV O HETATM 6081 O HOH G 280 10.884 -4.958 -1.787 1.00 27.35 SOLV O HETATM 6082 O HOH G 281 40.522 -1.198 -35.454 1.00 57.92 SOLV O HETATM 6083 O HOH G 282 29.201 15.817 -13.489 1.00 42.39 SOLV O HETATM 6084 O HOH G 283 19.979 9.872 -51.616 1.00 40.43 SOLV O HETATM 6085 O HOH G 284 13.341 7.968 -50.977 1.00 47.95 SOLV O HETATM 6086 O HOH G 285 13.983 10.756 9.571 1.00 35.32 SOLV O HETATM 6087 O HOH G 286 37.871 4.390 -50.936 1.00 55.02 SOLV O HETATM 6088 O HOH G 287 7.767 -9.529 -34.523 1.00 35.70 SOLV O HETATM 6089 O HOH G 288 8.106 26.855 -18.116 1.00 60.72 SOLV O HETATM 6090 O HOH G 289 24.743 6.814 -15.286 1.00 44.32 SOLV O HETATM 6091 O HOH G 290 36.207 -0.608 -14.850 1.00 41.84 SOLV O HETATM 6092 O HOH G 291 6.191 10.743 6.055 1.00 56.46 SOLV O HETATM 6093 O HOH G 292 10.715 -1.751 7.763 1.00 39.71 SOLV O HETATM 6094 O HOH G 293 18.081 15.259 14.648 1.00 54.08 SOLV O HETATM 6095 O HOH G 294 22.152 20.974 2.057 1.00 59.78 SOLV O HETATM 6096 O HOH G 295 14.612 -6.996 -0.061 1.00 49.00 SOLV O HETATM 6097 O HOH G 296 11.893 -6.175 6.936 1.00 56.79 SOLV O HETATM 6098 O HOH G 297 29.768 -21.523 -27.608 1.00 43.30 SOLV O HETATM 6099 O HOH G 298 4.948 -5.792 -0.180 1.00 49.85 SOLV O HETATM 6100 O HOH G 299 31.576 26.642 -10.019 1.00 56.99 SOLV O HETATM 6101 O HOH G 300 29.674 -9.156 -26.262 1.00 40.25 SOLV O HETATM 6102 O HOH G 301 13.133 13.040 -13.006 1.00 44.58 SOLV O HETATM 6103 O HOH G 302 27.747 -7.914 -26.487 1.00 40.44 SOLV O HETATM 6104 O HOH G 303 27.408 11.342 -42.976 1.00 40.80 SOLV O HETATM 6105 O HOH G 304 30.115 10.459 -39.823 1.00 38.19 SOLV O HETATM 6106 O HOH G 305 16.179 15.842 8.535 1.00 59.24 SOLV O HETATM 6107 O HOH G 306 17.810 5.945 -15.181 1.00 36.34 SOLV O HETATM 6108 O HOH G 307 7.633 -13.164 -12.527 1.00 45.72 SOLV O HETATM 6109 O HOH G 308 50.615 -27.849 -44.318 1.00 51.53 SOLV O HETATM 6110 O HOH G 309 9.165 4.346 -15.231 1.00 48.35 SOLV O HETATM 6111 O HOH G 310 39.116 -24.975 -21.363 1.00 45.37 SOLV O HETATM 6112 O HOH G 311 8.691 -7.004 -5.137 1.00 37.80 SOLV O HETATM 6113 O HOH G 312 23.083 28.215 0.322 1.00 51.50 SOLV O HETATM 6114 O HOH G 313 10.491 -17.244 -29.110 1.00 44.23 SOLV O HETATM 6115 O HOH G 314 14.947 -8.072 8.196 1.00 53.11 SOLV O HETATM 6116 O HOH G 315 24.589 19.630 2.140 1.00 43.13 SOLV O HETATM 6117 O HOH G 316 5.934 -7.638 -34.790 1.00 46.26 SOLV O HETATM 6118 O HOH G 317 9.391 -3.074 -1.058 1.00 46.90 SOLV O HETATM 6119 O HOH G 318 51.854 -18.765 -45.934 1.00 54.35 SOLV O HETATM 6120 O HOH G 319 11.124 -11.195 -42.298 1.00 58.08 SOLV O HETATM 6121 O HOH G 320 19.190 -21.047 -51.660 1.00 42.34 SOLV O HETATM 6122 O HOH G 321 36.889 16.531 1.214 1.00 42.57 SOLV O HETATM 6123 O HOH G 322 8.118 22.224 3.488 1.00 55.80 SOLV O HETATM 6124 O HOH G 323 39.827 -5.915 -9.917 1.00 45.40 SOLV O HETATM 6125 O HOH G 324 31.998 3.517 20.229 1.00 34.87 SOLV O HETATM 6126 O HOH G 325 27.949 26.860 -9.386 1.00 57.74 SOLV O HETATM 6127 O HOH G 326 31.052 -9.759 6.961 1.00 46.67 SOLV O HETATM 6128 O HOH G 327 2.302 8.914 -6.583 1.00 48.95 SOLV O HETATM 6129 O HOH G 328 15.254 10.502 -13.325 1.00 56.62 SOLV O HETATM 6130 O HOH G 329 31.716 6.966 -11.103 1.00 37.17 SOLV O HETATM 6131 O HOH G 330 33.527 8.677 -10.957 1.00 40.28 SOLV O HETATM 6132 O HOH G 331 4.757 29.784 -11.421 1.00 56.44 SOLV O HETATM 6133 O HOH G 332 43.948 -28.191 -33.297 1.00 43.50 SOLV O HETATM 6134 O HOH G 333 36.505 -2.069 -32.165 1.00 43.52 SOLV O HETATM 6135 O HOH G 334 30.678 4.480 -32.816 1.00 42.05 SOLV O HETATM 6136 O HOH G 335 34.851 -25.906 -29.914 1.00 50.32 SOLV O HETATM 6137 O HOH G 336 33.683 -7.477 -51.422 1.00 43.96 SOLV O HETATM 6138 O HOH G 337 24.696 -17.160 -29.097 1.00 37.53 SOLV O HETATM 6139 O HOH G 338 21.375 -0.216 -19.401 1.00 45.82 SOLV O HETATM 6140 O HOH G 339 21.662 8.859 -19.831 1.00 47.42 SOLV O HETATM 6141 O HOH G 340 10.236 16.631 -19.072 1.00 49.50 SOLV O HETATM 6142 O HOH G 341 35.039 -16.167 -20.402 1.00 53.14 SOLV O HETATM 6143 O HOH G 342 27.337 -12.779 -26.495 1.00 42.98 SOLV O HETATM 6144 O HOH G 343 24.280 -16.323 -21.775 1.00 57.38 SOLV O HETATM 6145 O HOH G 344 38.226 -9.562 4.105 1.00 45.95 SOLV O HETATM 6146 O HOH G 345 20.827 0.186 -26.358 1.00 42.71 SOLV O HETATM 6147 O HOH G 346 7.947 2.403 12.728 1.00 44.28 SOLV O HETATM 6148 O HOH G 347 31.108 16.720 -43.136 1.00 53.39 SOLV O HETATM 6149 O HOH G 348 43.373 -6.738 -1.151 1.00 39.50 SOLV O HETATM 6150 O HOH G 349 16.132 12.402 -17.074 1.00 56.98 SOLV O HETATM 6151 O HOH G 350 12.045 -10.831 -39.092 1.00 44.90 SOLV O HETATM 6152 O HOH G 351 13.907 -9.060 -40.606 1.00 40.51 SOLV O HETATM 6153 O HOH G 352 3.909 -4.871 -39.395 1.00 48.48 SOLV O HETATM 6154 O HOH G 353 50.080 5.699 2.174 1.00 61.68 SOLV O HETATM 6155 O HOH G 354 40.382 6.607 -40.921 1.00 61.75 SOLV O HETATM 6156 O HOH G 355 15.033 1.957 -55.725 1.00 43.13 SOLV O HETATM 6157 O HOH G 356 34.801 -26.330 -42.107 1.00 69.53 SOLV O HETATM 6158 O HOH G 357 37.063 19.125 1.215 1.00 51.64 SOLV O HETATM 6159 O HOH G 358 4.692 5.651 -1.945 1.00 54.98 SOLV O HETATM 6160 O HOH G 359 36.005 13.311 -0.066 1.00 50.98 SOLV O HETATM 6161 O HOH G 360 19.608 25.413 0.222 1.00 52.33 SOLV O HETATM 6162 O HOH G 361 28.983 6.764 -20.895 1.00 66.32 SOLV O HETATM 6163 O HOH G 362 1.373 16.650 -4.110 1.00 52.37 SOLV O HETATM 6164 O HOH G 363 37.882 -10.888 -28.279 1.00 43.87 SOLV O HETATM 6165 O HOH G 364 30.449 1.673 19.614 1.00 49.89 SOLV O HETATM 6166 O HOH G 365 25.450 12.418 18.490 1.00 39.12 SOLV O HETATM 6167 O HOH G 366 30.592 -0.022 -31.345 1.00 19.85 SOLV O HETATM 6168 O HOH G 367 38.781 14.739 -42.833 1.00 50.94 SOLV O HETATM 6169 O HOH G 368 15.249 -16.742 -46.531 1.00 44.37 SOLV O HETATM 6170 O HOH G 369 17.366 17.350 -42.662 1.00 47.94 SOLV O HETATM 6171 O HOH G 370 22.185 11.294 -51.670 1.00 41.62 SOLV O HETATM 6172 O HOH G 371 12.831 0.434 -53.868 1.00 47.85 SOLV O HETATM 6173 O HOH G 372 13.015 1.008 17.615 1.00 40.38 SOLV O HETATM 6174 O HOH G 373 12.602 -11.651 6.601 1.00 51.34 SOLV O HETATM 6175 O HOH G 374 15.371 -14.109 -4.463 1.00 46.50 SOLV O HETATM 6176 O HOH G 375 8.480 -9.540 -5.323 1.00 62.77 SOLV O HETATM 6177 O HOH G 376 19.359 -22.056 -31.563 1.00 44.74 SOLV O HETATM 6178 O HOH G 377 6.522 -10.569 -11.971 1.00 47.00 SOLV O HETATM 6179 O HOH G 378 9.645 6.029 -13.041 1.00 47.89 SOLV O HETATM 6180 O HOH G 379 46.293 -19.772 -21.010 1.00 61.26 SOLV O HETATM 6181 O HOH G 380 13.260 -22.652 -37.789 1.00 49.95 SOLV O HETATM 6182 O HOH G 381 6.226 -10.512 -30.826 1.00 46.70 SOLV O HETATM 6183 O HOH G 382 23.384 -18.320 -16.960 1.00 44.54 SOLV O HETATM 6184 O HOH G 383 36.271 -3.045 13.063 1.00 55.33 SOLV O HETATM 6185 O HOH G 384 17.353 16.632 -14.925 1.00 55.26 SOLV O HETATM 6186 O HOH G 385 5.835 38.421 -2.696 1.00 61.58 SOLV O HETATM 6187 O HOH G 386 26.452 3.827 -15.752 1.00 45.25 SOLV O HETATM 6188 O HOH G 387 36.135 7.621 -11.372 1.00 64.15 SOLV O HETATM 6189 O HOH G 388 13.262 -10.806 -20.398 1.00 36.53 SOLV O HETATM 6190 O HOH G 389 -1.222 20.518 -4.231 1.00 54.27 SOLV O HETATM 6191 O HOH G 390 22.643 12.928 -13.720 1.00 51.22 SOLV O HETATM 6192 O HOH G 391 28.996 25.891 -5.847 1.00 66.99 SOLV O HETATM 6193 O HOH G 392 11.945 32.445 0.553 1.00 57.51 SOLV O HETATM 6194 O HOH G 393 54.023 -23.966 -42.638 1.00 63.07 SOLV O HETATM 6195 O HOH G 394 37.206 -2.943 -12.852 1.00 54.33 SOLV O HETATM 6196 O HOH G 395 18.382 -16.273 1.114 1.00 52.95 SOLV O HETATM 6197 O HOH G 396 7.294 2.271 -13.840 1.00 46.35 SOLV O HETATM 6198 O HOH G 397 12.211 -10.629 -0.023 1.00 51.48 SOLV O HETATM 6199 O HOH G 398 28.264 -9.634 7.343 1.00 53.85 SOLV O HETATM 6200 O HOH G 399 43.362 -6.870 1.602 1.00 56.77 SOLV O HETATM 6201 O HOH G 400 16.095 16.910 -45.525 1.00 57.20 SOLV O HETATM 6202 O HOH G 401 13.454 28.740 -13.914 1.00 57.46 SOLV O HETATM 6203 O HOH G 402 12.930 22.563 4.710 1.00 56.84 SOLV O HETATM 6204 O HOH G 403 12.192 -13.088 -18.809 1.00 57.08 SOLV O HETATM 6205 O HOH G 404 16.076 -2.339 -62.385 1.00 43.30 SOLV O HETATM 6206 O HOH G 405 40.037 5.194 7.990 1.00 52.02 SOLV O HETATM 6207 O HOH G 406 40.603 8.669 10.091 1.00 51.96 SOLV O HETATM 6208 O HOH G 407 39.945 10.739 13.182 1.00 53.68 SOLV O HETATM 6209 O HOH G 408 35.551 13.261 17.820 1.00 56.21 SOLV O HETATM 6210 O HOH G 409 33.206 10.611 24.541 1.00 54.18 SOLV O HETATM 6211 O HOH G 410 28.161 12.227 14.518 1.00 50.33 SOLV O HETATM 6212 O HOH G 411 31.317 5.492 22.425 1.00 43.36 SOLV O HETATM 6213 O HOH G 412 5.936 1.984 7.447 1.00 54.97 SOLV O HETATM 6214 O HOH G 413 40.479 7.204 -49.919 1.00 53.54 SOLV O HETATM 6215 O HOH G 414 25.198 -10.153 -60.922 1.00 50.25 SOLV O HETATM 6216 O HOH G 415 35.070 16.556 4.788 1.00 48.42 SOLV O HETATM 6217 O HOH G 416 27.285 1.005 -26.835 1.00 48.18 SOLV O HETATM 6218 O HOH G 417 26.211 13.162 -42.320 1.00 62.30 SOLV O HETATM 6219 O HOH G 418 9.298 -16.254 -25.611 1.00 46.85 SOLV O HETATM 6220 O HOH G 419 15.693 -13.548 -58.332 1.00 54.08 SOLV O END
【0057】
【配列表】 SEQUENCE LISTING <110> Mitsubishi Chemical Corporation <120> <130> J07040 <140> <141> <160> 1 <170> PatentIn Ver. 2.0 <210> 1 <211> 428 <212> PRT <213> Homo sapiens <400> 1 Met Ser Gly Arg Pro Arg Thr Thr Ser Phe Ala Glu Ser Cys Lys Pro 1 5 10 15 Val Gln Gln Pro Ser Ala Phe Gly Ser Met Lys Val Ser Arg Asp Lys 20 25 30 Asp Gly Ser Lys Val Thr Thr Val Val Ala Thr Pro Gly Gln Gly Pro 35 40 45 Asp Arg Pro Gln Glu Val Ser Tyr Thr Asp Thr Lys Val Ile Gly Asn 50 55 60 Gly Ser Phe Gly Val Val Tyr Gln Ala Lys Leu Cys Asp Ser Gly Glu 65 70 75 80 Leu Val Ala Ile Lys Lys Val Leu Gln Asp Lys Arg Phe Lys Asn Arg 85 90 95 Glu Leu Gln Ile Met Arg Lys Leu Asp His Cys Asn Ile Val Arg Leu 100 105 110 Arg Tyr Phe Phe Tyr Ser Ser Gly Glu Lys Lys Asp Glu Val Tyr Leu 115 120 125 Asn Leu Val Leu Asp Tyr Val Pro Glu Thr Val Tyr Arg Val Ala Arg 130 135 140 His Tyr Ser Arg Ala Lys Gln Thr Leu Pro Val Ile Tyr Val Lys Leu 145 150 155 160 Tyr Met Tyr Gln Leu Phe Arg Ser Leu Ala Tyr Ile His Ser Phe Gly 165 170 175 Ile Cys His Arg Asp Ile Lys Pro Gln Asn Leu Leu Leu Asp Pro Asp 180 185 190 Thr Ala Val Leu Lys Leu Cys Asp Phe Gly Ser Ala Lys Gln Leu Val 195 200 205 Arg Gly Glu Pro Asn Val Ser Tyr Ile Cys Ser Arg Tyr Tyr Arg Ala 210 215 220 Pro Glu Leu Ile Phe Gly Ala Thr Asp Tyr Thr Ser Ser Ile Asp Val 225 230 235 240 Trp Ser Ala Gly Cys Val Leu Ala Glu Leu Leu Leu Gly Gln Pro Ile 245 250 255 Phe Pro Gly Asp Ser Gly Val Asp Gln Leu Val Glu Ile Ile Lys Val 260 265 270 Leu Gly Thr Pro Thr Arg Glu Gln Ile Arg Glu Met Asn Pro Asn Tyr 275 280 285 Thr Glu Phe Lys Phe Pro Gln Ile Lys Ala His Pro Trp Thr Lys Val 290 295 300 Phe Arg Pro Arg Thr Pro Pro Glu Ala Ile Ala Leu Cys Ser Arg Leu 305 310 315 320 Leu Glu Tyr Thr Pro Thr Ala Arg Leu Thr Pro Leu Glu Ala Cys Ala 325 330 335 His Ser Phe Phe Asp Glu Leu Arg Asp Pro Asn Val Lys Leu Pro Asn 340 345 350 Gly Arg Asp Thr Pro Ala Leu Phe Asn Phe Thr Thr Gln Glu Leu Ser 355 360 365 Ser Asn Pro Pro Leu Ala Thr Ile Leu Ile Pro Pro His Ala Arg Ile 370 375 380 Gln Ala Ala Ala Ser Thr Pro Thr Asn Ala Thr Ala Ala Ser Asp Ala 385 390 395 400 Asn Thr Gly Asp Arg Gly Gln Thr Asn Asn Ala Ala Ser Ala Ser Ala 405 410 415 Ser Asn Ser Thr Leu Glu His His His His His His 420 425
【図1】 結晶中の非対称単位内にある、TPK IとADPと
の複合体(2分子)の構造について、主鎖をリボンモデ
ルで、ADPをボール&スティクモデルで示した図であ
る。
の複合体(2分子)の構造について、主鎖をリボンモデ
ルで、ADPをボール&スティクモデルで示した図であ
る。
【図2】 TPK IとADPとの複合体の構造について、主鎖
をリボンモデルで、ADP をボール&スティクモデルで示
した図である。
をリボンモデルで、ADP をボール&スティクモデルで示
した図である。
【図3】 TPK IとADPとの相互作用を特徴づけるアミノ
酸残基の空間的配置を、ボール&スティクモデルで示し
た図である。
酸残基の空間的配置を、ボール&スティクモデルで示し
た図である。
───────────────────────────────────────────────────── フロントページの続き (51)Int.Cl.7 識別記号 FI テーマコート゛(参考) G01N 1/28 G01N 23/20 4C084 23/20 33/15 Z 4G077 33/15 33/50 Z 33/50 1/28 K // C12N 15/09 ZNA C12N 15/00 ZNAA (72)発明者 青木 雅昭 東京都町田市南大谷11号 株式会社三菱化 学生命科学研究所内 (72)発明者 河野 俊之 東京都町田市南大谷11号 株式会社三菱化 学生命科学研究所内 Fターム(参考) 2G001 AA01 BA18 CA01 KA20 RA03 2G045 AA40 DA80 GC30 2G052 AA00 EB08 GA19 4B024 AA01 BA10 CA02 HA01 HA06 4B050 CC03 CC07 DD11 FF05 FF11 FF12 FF17 KK13 LL03 4C084 AA17 MA01 NA14 ZA022 ZA162 ZC202 4G077 AA01 AB07 BF05 CB01
Claims (28)
- 【請求項1】 タウ蛋白質リン酸化酵素Iの結晶。
- 【請求項2】 タウ蛋白質リン酸化酵素Iが、タウ蛋白
質リン酸化酵素IとATP類似化合物との複合体である請
求項1に記載の結晶。 - 【請求項3】 ATP類似化合物が、ADP又はAMPPNPである
請求項2に記載の結晶。 - 【請求項4】 結晶が斜方晶系の空間群対称 P212121
に属する請求項1〜3のいずれかに記載の結晶。 - 【請求項5】 結晶の単位格子が、a=83±10Å、b=
86±10Å、c=178±10Åの大きさを持つ請求項4に記
載の結晶。 - 【請求項6】 タウ蛋白質リン酸化酵素IとATP類似化
合物とが結合して複合体を形成しており、更にその複合
体が結晶学的な非対称単位中に2分子存在している請求
項2〜5のいずれかに記載の結晶。 - 【請求項7】 タウ蛋白質リン酸化酵素IとATP類似化
合物とが、配列番号1に示すヒト由来のタウ蛋白質リン
酸化酵素Iのアミノ酸配列において、Ile62、Gly65、Se
r66、Phe67、Gly68、Val70、Ala83、Lys85、Glu97、Val
110、Leu132、Asp133、Tyr134、Val135、Glu137、Thr13
8、Arg141、Asp181、Lys183、Gln185、Asn186、Leu18
8、Cys199、Asp200及びその近傍のアミノ酸残基の全て
又はその一部のアミノ酸残基と相互作用して複合体を形
成している請求項2〜6のいずれかに記載の結晶。 - 【請求項8】 精製タウ蛋白質リン酸化酵素IとATP類
似化合物とを沈殿剤の存在下に結晶化することを特徴と
するタウ蛋白質リン酸化酵素IとATP類似化合物との複
合体の結晶の作製方法。 - 【請求項9】 沈殿剤が、ポリエチレングリコールであ
る請求項8に記載の方法。 - 【請求項10】 請求項8又は9に記載の方法で得られ
た結晶を、多価アルコールを含有する結晶化溶液中で凍
結させ、凍結状態でX線回析データを収集することを特
徴とするX線回折像の測定方法。 - 【請求項11】 多価アルコールが、D−ソルビトー
ル、ショ糖またはグリセロールである請求項10に記載
の測定方法。 - 【請求項12】 請求項1〜7のいずれかに記載の結晶
のX線回折像より得られるタウ蛋白質リン酸化酵素Iの
3次元構造座標。 - 【請求項13】 請求項10又は11に記載の測定方法
により得られるタウ蛋白質リン酸化酵素Iの3次元構造
座標。 - 【請求項14】 3次元構造座標が、タウ蛋白質リン酸
化酵素IとATP類似化合物との複合体の構造座標である
請求項12又は13に記載の3次元構造座標。 - 【請求項15】 ATP類似化合物が、ADP又はAMPPNPであ
る請求項14に記載の3次元構造座標。 - 【請求項16】 表1に示されるタウ蛋白質リン酸化酵
素IとATPとの複合体の3次元構造座標。 - 【請求項17】 表3に示されるタウ蛋白質リン酸化酵
素IとAMPPNPとの複合体の3次元構造座標。 - 【請求項18】 請求項16または17に記載の3次元
構造座標について、各原子の相対的な配置を変化させず
に、3次元空間内で数学的な移動操作を行った結果とし
て得られる3次元構造座標。 - 【請求項19】 3次元構造が未知の蛋白質について、
請求項16または17に記載の3次元構造座標を元に、
蛋白質の3次元構造構築方法により求められたものであ
る蛋白質の3次元構造座標。 - 【請求項20】 3次元構造構築方法が、分子置換法又
はホモロジーモデリングである請求項19に記載の3次
元構造座標。 - 【請求項21】 3次元構造が未知の蛋白質が、ヒト由
来タウ蛋白質リン酸化酵素Iのアミノ酸配列に対して2
0%以上の相同性を持つ配列を有する蛋白質である請求
項19に記載の3次元構造座標。 - 【請求項22】 請求項12〜21のいずれかに記載の
3次元構造座標の全部又は一部を含む座標が記録された
データベース。 - 【請求項23】 請求項12〜21のいずれかに記載の
3次元構造座標の全部又は一部が記録されたコンピュー
タ読みとり可能な記録媒体。 - 【請求項24】 請求項12〜21のいずれかに記載の
3次元構造座標、又は請求項22に記載のデータベース
若しくは請求項23に記載の記録媒体に含まれる構造座
標と、薬物候補分子の3次元構造座標との相互作用に基
づいて、タウ蛋白質リン酸化酵素Iの拮抗薬を同定、検
索、評価または設計することを特徴とする薬物分子の設
計方法。 - 【請求項25】 タウ蛋白質リン酸化酵素Iの拮抗薬の
同定、検索、評価又は設計が、配列番号1に示すヒト由
来のタウ蛋白質リン酸化酵素Iのアミノ酸配列におい
て、Ile62、Gly65、Ser66、Phe67、Gly68、Val70、Ala8
3、Lys85、Glu97、Val110、Leu132、Asp133、Tyr134、V
al135、Glu137、Thr138、Arg141、Asp181、Lys183、Gln
185、Asn186、Leu188、Cys199、Asp200及びその近傍の
アミノ酸残基の全て又はその一部のアミノ酸残基の3次
元構造座標と薬物候補分子の3次元構造座標との相互作
用に基づいて行われる請求項24に記載の方法。 - 【請求項26】 請求項24又は25に記載の方法によ
り得られたタウ蛋白質リン酸化酵素Iの拮抗薬。 - 【請求項27】 請求項24又は25に記載の方法によ
り得られたタウ蛋白質リン酸化酵素Iの拮抗薬につい
て、所望の薬理学的又は生理学的性質を指標として医薬
としての活性を調べ、所望の活性を有する医薬候補分子
を選択することを特徴とする医薬分子のスクリーニング
方法。 - 【請求項28】 請求項24に記載の方法により得られ
た医薬分子と薬学的に許容され得る担体とを配合して製
剤化することを特徴とする医薬組成物の製造方法。
Priority Applications (1)
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JP2001131511A JP2002320474A (ja) | 2001-04-27 | 2001-04-27 | タウ蛋白質リン酸化酵素iの結晶、その3次元構造座標、及び3次元構造座標の使用 |
Applications Claiming Priority (1)
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JP2001131511A JP2002320474A (ja) | 2001-04-27 | 2001-04-27 | タウ蛋白質リン酸化酵素iの結晶、その3次元構造座標、及び3次元構造座標の使用 |
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