spacer
spacer

PDBsum entry 1m6v

Go to PDB code: 
Top Page protein ligands metals Protein-protein interface(s) links
Ligase PDB id
1m6v
Jmol
Contents
Protein chains
1059 a.a. *
375 a.a. *
Ligands
ADP ×8
PO4 ×4
ORN ×4
NET ×4
Metals
_CL ×28
_MN ×12
__K ×26
Waters ×3561
* Residue conservation analysis
HEADER    LIGASE                                  17-JUL-02   1M6V
TITLE     CRYSTAL STRUCTURE OF THE G359F (SMALL SUBUNIT) POINT MUTANT OF
TITLE    2 CARBAMOYL PHOSPHATE SYNTHETASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBAMOYL PHOSPHATE SYNTHETASE LARGE CHAIN;
COMPND   3 CHAIN: A, C, E, G;
COMPND   4 SYNONYM: CARBAMOYL-PHOSPHATE SYNTHETASE AMMONIA CHAIN;
COMPND   5 EC: 6.3.5.5;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: CARBAMOYL-PHOSPHATE SYNTHETASE SMALL CHAIN;
COMPND   9 CHAIN: B, D, F, H;
COMPND  10 SYNONYM: CARBAMOYL-PHOSPHATE SYNTHETASE GLUTAMINE CHAIN;
COMPND  11 EC: 6.3.5.5;
COMPND  12 ENGINEERED: YES;
COMPND  13 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: CARB;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 MOL_ID: 2;
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE  11 ORGANISM_TAXID: 562;
SOURCE  12 GENE: CARA;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    SUBSTRATE CHANNELING, TUNNEL, LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN
REVDAT   4   13-JUL-11 1M6V    1       VERSN
REVDAT   3   24-FEB-09 1M6V    1       VERSN
REVDAT   2   13-NOV-02 1M6V    1       JRNL
REVDAT   1   31-JUL-02 1M6V    0
JRNL        AUTH   J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN
JRNL        TITL   CARBAMOYL-PHOSPHATE SYNTHETASE. CREATION OF AN ESCAPE ROUTE
JRNL        TITL 2 FOR AMMONIA
JRNL        REF    J.BIOL.CHEM.                  V. 277 39722 2002
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   12130656
JRNL        DOI    10.1074/JBC.M206915200
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.4
REMARK   3   NUMBER OF REFLECTIONS             : 440901
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180
REMARK   3   R VALUE            (WORKING SET) : 0.174
REMARK   3   FREE R VALUE                     : 0.245
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 44271
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1800
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1740
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.245
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.00
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 44026
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 440901
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 44124
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 374
REMARK   3   SOLVENT ATOMS            : 3561
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : 0.012 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 2.330 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : ENGH & HUBER
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1M6V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-02.
REMARK 100 THE RCSB ID CODE IS RCSB016669.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-99
REMARK 200  TEMPERATURE           (KELVIN) : 110
REMARK 200  PH                             : 7.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 19-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.70004
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : SBC-2
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 445772
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.1
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07060
REMARK 200   FOR THE DATA SET  : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.24400
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: 1JDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 61.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-8000, MANGANESE CHLORIDE,
REMARK 280  POTASSIUM CHLORIDE, ADP, ORNITHINE, TETRAETHYLAMMONIUM CHLORIDE,
REMARK 280  HEPPS, PH 7.4, BATCH, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       75.75000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      165.75000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       82.10000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      165.75000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       75.75000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       82.10000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: BIOLOGICAL ASSEMBLY IS AN (AB)4 HETERO-TETRAMER:
REMARK 300 COMPRISED OF CHAINS A,B,C,D,E,F,G,H
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     TYR A   718
REMARK 465     VAL A   719
REMARK 465     LEU A   720
REMARK 465     GLY A   721
REMARK 465     GLY A   722
REMARK 465     ARG A   723
REMARK 465     VAL A   742
REMARK 465     SER A   743
REMARK 465     VAL A   744
REMARK 465     SER A   745
REMARK 465     ASN A   746
REMARK 465     ASP A   747
REMARK 465     ALA A   748
REMARK 465     PRO A   749
REMARK 465     MET B     1
REMARK 465     PHE B   359
REMARK 465     PRO B   360
REMARK 465     HIS B   361
REMARK 465     ASP B   362
REMARK 465     ALA B   381
REMARK 465     LYS B   382
REMARK 465     TYR C   718
REMARK 465     VAL C   719
REMARK 465     LEU C   720
REMARK 465     GLY C   721
REMARK 465     GLY C   722
REMARK 465     ARG C   723
REMARK 465     VAL C   742
REMARK 465     SER C   743
REMARK 465     VAL C   744
REMARK 465     SER C   745
REMARK 465     ASN C   746
REMARK 465     ASP C   747
REMARK 465     ALA C   748
REMARK 465     PRO C   749
REMARK 465     MET D     1
REMARK 465     PHE D   359
REMARK 465     PRO D   360
REMARK 465     HIS D   361
REMARK 465     ASP D   362
REMARK 465     ALA D   381
REMARK 465     LYS D   382
REMARK 465     TYR E   718
REMARK 465     VAL E   719
REMARK 465     LEU E   720
REMARK 465     GLY E   721
REMARK 465     GLY E   722
REMARK 465     ARG E   723
REMARK 465     VAL E   742
REMARK 465     SER E   743
REMARK 465     VAL E   744
REMARK 465     SER E   745
REMARK 465     ASN E   746
REMARK 465     ASP E   747
REMARK 465     ALA E   748
REMARK 465     PRO E   749
REMARK 465     MET F     1
REMARK 465     PHE F   359
REMARK 465     PRO F   360
REMARK 465     HIS F   361
REMARK 465     ASP F   362
REMARK 465     ALA F   381
REMARK 465     LYS F   382
REMARK 465     TYR G   718
REMARK 465     VAL G   719
REMARK 465     LEU G   720
REMARK 465     GLY G   721
REMARK 465     GLY G   722
REMARK 465     ARG G   723
REMARK 465     VAL G   742
REMARK 465     SER G   743
REMARK 465     VAL G   744
REMARK 465     SER G   745
REMARK 465     ASN G   746
REMARK 465     ASP G   747
REMARK 465     ALA G   748
REMARK 465     PRO G   749
REMARK 465     MET H     1
REMARK 465     PHE H   359
REMARK 465     PRO H   360
REMARK 465     HIS H   361
REMARK 465     ASP H   362
REMARK 465     ALA H   381
REMARK 465     LYS H   382
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     PRO A 716    CG   CD
REMARK 470     SER A 717    OG
REMARK 470     PRO C 716    CG   CD
REMARK 470     SER C 717    OG
REMARK 470     PRO E 716    CG   CD
REMARK 470     SER E 717    OG
REMARK 470     PRO G 716    CG   CD
REMARK 470     SER G 717    OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   K      K A  4009     O    HOH A  4434              1.26
REMARK 500   O    HOH A  4520     O    HOH A  4521              1.90
REMARK 500   O    HOH E  2600     O    HOH F  3294              2.01
REMARK 500   O    HOH G  4434     O    HOH G  4723              2.04
REMARK 500   O    HOH F  3308     O    HOH F  3309              2.08
REMARK 500   O    HOH A  4483     O    HOH A  4510              2.11
REMARK 500   O    HOH A  4197     O    HOH A  4562              2.13
REMARK 500   O    HOH F  3290     O    HOH F  3291              2.16
REMARK 500   OE1  GLU E    59     O    HOH E  1581              2.16
REMARK 500   O    HOH F  3244     O    HOH F  3245              2.19
REMARK 500   O    HOH A  4634     O    HOH A  4635              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A  25   CD    GLU A  25   OE2     0.071
REMARK 500    GLU A  59   CD    GLU A  59   OE2     0.071
REMARK 500    GLU A  81   CD    GLU A  81   OE2     0.070
REMARK 500    GLU A 103   CD    GLU A 103   OE2     0.072
REMARK 500    GLU A 109   CD    GLU A 109   OE2     0.080
REMARK 500    GLU A 110   CD    GLU A 110   OE2     0.069
REMARK 500    GLU A 153   CD    GLU A 153   OE2     0.068
REMARK 500    GLU A 186   CD    GLU A 186   OE2     0.074
REMARK 500    GLU A 203   CD    GLU A 203   OE2     0.067
REMARK 500    GLU A 208   CD    GLU A 208   OE2     0.071
REMARK 500    GLU A 217   CD    GLU A 217   OE2     0.082
REMARK 500    GLU A 260   CD    GLU A 260   OE2     0.069
REMARK 500    GLU A 299   CD    GLU A 299   OE2     0.076
REMARK 500    GLU A 334   CD    GLU A 334   OE2     0.070
REMARK 500    GLU A 365   CD    GLU A 365   OE2     0.076
REMARK 500    GLU A 383   CD    GLU A 383   OE2     0.074
REMARK 500    GLU A 419   CD    GLU A 419   OE2     0.068
REMARK 500    GLU A 427   CD    GLU A 427   OE2     0.075
REMARK 500    GLU A 467   CD    GLU A 467   OE2     0.067
REMARK 500    GLU A 468   CD    GLU A 468   OE2     0.072
REMARK 500    GLU A 473   CD    GLU A 473   OE2     0.081
REMARK 500    GLU A 478   CD    GLU A 478   OE2     0.073
REMARK 500    GLU A 512   CD    GLU A 512   OE2     0.070
REMARK 500    GLU A 549   CD    GLU A 549   OE2     0.067
REMARK 500    GLU A 577   CD    GLU A 577   OE2     0.071
REMARK 500    GLU A 633   CD    GLU A 633   OE2     0.073
REMARK 500    GLU A 655   CD    GLU A 655   OE2     0.066
REMARK 500    GLU A 683   CD    GLU A 683   OE2     0.102
REMARK 500    GLU A 699   CD    GLU A 699   OE2     0.079
REMARK 500    GLU A 703   CD    GLU A 703   OE2     0.069
REMARK 500    GLU A 707   CD    GLU A 707   OE2     0.081
REMARK 500    GLU A 726   CD    GLU A 726   OE2     0.071
REMARK 500    GLU A 731   CD    GLU A 731   OE2     0.079
REMARK 500    GLU A 761   CD    GLU A 761   OE2     0.071
REMARK 500    GLU A 783   CD    GLU A 783   OE2     0.076
REMARK 500    GLU A 836   CD    GLU A 836   OE2     0.070
REMARK 500    GLU A 876   CD    GLU A 876   OE2     0.088
REMARK 500    GLU A 910   CD    GLU A 910   OE2     0.077
REMARK 500    GLU A 951   CD    GLU A 951   OE2     0.066
REMARK 500    GLU A 955   CD    GLU A 955   OE2     0.088
REMARK 500    GLU A 970   CD    GLU A 970   OE2     0.070
REMARK 500    GLU A 983   CD    GLU A 983   OE2     0.067
REMARK 500    GLU A1009   CD    GLU A1009   OE2     0.072
REMARK 500    GLU A1024   CD    GLU A1024   OE2     0.070
REMARK 500    GLU A1060   CD    GLU A1060   OE2     0.076
REMARK 500    GLU B  71   CD    GLU B  71   OE2     0.066
REMARK 500    GLU B  96   CD    GLU B  96   OE2     0.070
REMARK 500    GLU B 145   CD    GLU B 145   OE2     0.078
REMARK 500    GLU B 166   CD    GLU B 166   OE2     0.085
REMARK 500    GLU B 187   CD    GLU B 187   OE2     0.079
REMARK 500
REMARK 500 THIS ENTRY HAS     193 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A   6   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ARG A  38   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG A  38   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ARG A  43   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    PRO A  58   C   -  N   -  CD  ANGL. DEV. = -15.1 DEGREES
REMARK 500    ASP A 121   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ASP A 128   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ASP A 133   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ASP A 161   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ARG A 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A 246   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP A 246   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    SER A 305   N   -  CA  -  CB  ANGL. DEV. =  -9.5 DEGREES
REMARK 500    ASP A 333   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 333   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ARG A 343   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ASP A 372   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES
REMARK 500    ASP A 410   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ASP A 416   CB  -  CG  -  OD2 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ASP A 434   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP A 459   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ARG A 460   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG A 460   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ASP A 487   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ASP A 499   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 514   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP A 521   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP A 579   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES
REMARK 500    ARG A 590   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ASP A 609   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A 609   CB  -  CG  -  OD2 ANGL. DEV. =  -7.3 DEGREES
REMARK 500    ASP A 611   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A 611   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ASP A 614   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ASP A 625   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP A 625   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    TYR A 642   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ASP A 667   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 667   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP A 670   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ASP A 670   CB  -  CG  -  OD2 ANGL. DEV. =  -7.7 DEGREES
REMARK 500    ARG A 671   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP A 674   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG A 736   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 736   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES
REMARK 500    ASP A 753   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP A 757   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 757   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     385 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    PRO A   2     -165.78    -75.14
REMARK 500    ALA A  23     -143.61   -113.16
REMARK 500    ASN A  48      119.78   -163.72
REMARK 500    PRO A  58      -38.28    -38.14
REMARK 500    ALA A 239     -179.28    -68.89
REMARK 500    THR A 279       56.32   -140.31
REMARK 500    ASN A 292       14.26   -148.73
REMARK 500    ARG A 303     -174.99    177.70
REMARK 500    THR A 340       38.88    -88.11
REMARK 500    THR A 375     -152.67   -145.47
REMARK 500    THR A 531      -13.45     68.23
REMARK 500    ALA A 541       76.24   -110.02
REMARK 500    CYS A 601       26.11   -140.74
REMARK 500    THR A 646      -71.88    -47.43
REMARK 500    THR A 696      -66.64    -92.79
REMARK 500    ILE A 698      -70.26    -53.59
REMARK 500    PRO A 716     -160.77    -61.65
REMARK 500    ASP A 758       58.53     35.49
REMARK 500    PRO A 905       58.64    -68.55
REMARK 500    HIS A 975      -71.68    -24.35
REMARK 500    ALA B 127      164.73    -45.61
REMARK 500    PRO B 138      130.98    -39.44
REMARK 500    GLU B 145      -75.39    -51.55
REMARK 500    ALA B 167      165.42    -40.32
REMARK 500    THR B 223      137.15    -38.76
REMARK 500    ASN B 232       86.39     46.83
REMARK 500    SER B 239      175.12    -58.99
REMARK 500    CYS B 248       48.44    -93.75
REMARK 500    CYS B 269     -112.36     60.76
REMARK 500    ALA B 281      173.30    -58.62
REMARK 500    ASN B 311       58.70   -150.96
REMARK 500    THR B 320       33.72    -79.32
REMARK 500    ASP B 334       13.15   -143.24
REMARK 500    THR B 336      161.64    -41.59
REMARK 500    LEU B 366      -72.78    -42.92
REMARK 500    GLN B 376      -40.21    -29.77
REMARK 500    PRO C   2     -157.03    -77.03
REMARK 500    ALA C  23     -152.23   -110.79
REMARK 500    ALA C  52       41.59    -89.69
REMARK 500    THR C 279       50.55   -140.88
REMARK 500    ASN C 292       12.05   -153.25
REMARK 500    PRO C 302       49.61    -69.05
REMARK 500    VAL C 328       31.42    -97.76
REMARK 500    THR C 340       37.15    -91.86
REMARK 500    ASN C 363       32.19   -141.80
REMARK 500    ASP C 530       -7.64   -142.50
REMARK 500    THR C 531      -15.08     83.13
REMARK 500    ALA C 541       75.23   -119.57
REMARK 500    GLU C 548     -158.54   -134.56
REMARK 500    CYS C 601       20.87   -144.85
REMARK 500
REMARK 500 THIS ENTRY HAS     147 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    MET A  55        23.7      L          L   OUTSIDE RANGE
REMARK 500    ILE A 139        22.9      L          L   OUTSIDE RANGE
REMARK 500    GLU A 142        23.1      L          L   OUTSIDE RANGE
REMARK 500    ILE A 339        22.1      L          L   OUTSIDE RANGE
REMARK 500    ARG A 343        24.8      L          L   OUTSIDE RANGE
REMARK 500    ALA A 651        22.8      L          L   OUTSIDE RANGE
REMARK 500    GLU A 726        20.9      L          L   OUTSIDE RANGE
REMARK 500    LYS A 954        22.8      L          L   OUTSIDE RANGE
REMARK 500    GLN A 967        24.6      L          L   OUTSIDE RANGE
REMARK 500    HIS A 975        19.2      L          L   OUTSIDE RANGE
REMARK 500    ASN A1007        22.4      L          L   OUTSIDE RANGE
REMARK 500    ILE B   2        23.0      L          L   OUTSIDE RANGE
REMARK 500    ASP B  11        24.4      L          L   OUTSIDE RANGE
REMARK 500    ASP B  69        23.9      L          L   OUTSIDE RANGE
REMARK 500    ALA B 127        15.6      L          L   OUTSIDE RANGE
REMARK 500    ASP B 136        24.7      L          L   OUTSIDE RANGE
REMARK 500    SER B 174        24.1      L          L   OUTSIDE RANGE
REMARK 500    ALA B 184        24.3      L          L   OUTSIDE RANGE
REMARK 500    GLU B 187        21.6      L          L   OUTSIDE RANGE
REMARK 500    ASN B 204        23.8      L          L   OUTSIDE RANGE
REMARK 500    THR B 336        20.8      L          L   OUTSIDE RANGE
REMARK 500    LYS C   3        24.4      L          L   OUTSIDE RANGE
REMARK 500    MET C  55        23.9      L          L   OUTSIDE RANGE
REMARK 500    ILE C 339        15.9      L          L   OUTSIDE RANGE
REMARK 500    ARG C 435        23.7      L          L   OUTSIDE RANGE
REMARK 500    GLU C 478        24.7      L          L   OUTSIDE RANGE
REMARK 500    ALA C 651        22.6      L          L   OUTSIDE RANGE
REMARK 500    GLU C 726        24.4      L          L   OUTSIDE RANGE
REMARK 500    ASP C 730        23.9      L          L   OUTSIDE RANGE
REMARK 500    LYS C 881        24.1      L          L   OUTSIDE RANGE
REMARK 500    LYS C 954        22.5      L          L   OUTSIDE RANGE
REMARK 500    ASN C1007        23.4      L          L   OUTSIDE RANGE
REMARK 500    ARG C1020        22.0      L          L   OUTSIDE RANGE
REMARK 500    TYR C1036        21.9      L          L   OUTSIDE RANGE
REMARK 500    ASP C1057        24.1      L          L   OUTSIDE RANGE
REMARK 500    ASP D 136        23.3      L          L   OUTSIDE RANGE
REMARK 500    GLU D 166        21.3      L          L   OUTSIDE RANGE
REMARK 500    ASN D 204        20.4      L          L   OUTSIDE RANGE
REMARK 500    SER D 239        24.2      L          L   OUTSIDE RANGE
REMARK 500    ALA D 323        22.1      L          L   OUTSIDE RANGE
REMARK 500    ASP D 334        24.6      L          L   OUTSIDE RANGE
REMARK 500    ASP D 368        21.2      L          L   OUTSIDE RANGE
REMARK 500    PHE E  26        23.1      L          L   OUTSIDE RANGE
REMARK 500    ILE E  69        24.3      L          L   OUTSIDE RANGE
REMARK 500    ILE E 339        19.7      L          L   OUTSIDE RANGE
REMARK 500    ALA E 420        22.9      L          L   OUTSIDE RANGE
REMARK 500    ARG E 435        20.9      L          L   OUTSIDE RANGE
REMARK 500    ASP E 674        23.6      L          L   OUTSIDE RANGE
REMARK 500    VAL E 773        17.7      L          L   OUTSIDE RANGE
REMARK 500    LYS E 954        19.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS      66 CHIRALITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH A4131        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH A4138        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A4345        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH A4595        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH A4599        DISTANCE =  7.13 ANGSTROMS
REMARK 525    HOH A4750        DISTANCE =  5.77 ANGSTROMS
REMARK 525    HOH A4752        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH A4756        DISTANCE =  6.42 ANGSTROMS
REMARK 525    HOH A4780        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A4812        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH B4145        DISTANCE =  7.53 ANGSTROMS
REMARK 525    HOH C4159        DISTANCE =  5.58 ANGSTROMS
REMARK 525    HOH C4559        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH C4562        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH C4617        DISTANCE =  5.70 ANGSTROMS
REMARK 525    HOH C4620        DISTANCE =  6.42 ANGSTROMS
REMARK 525    HOH C4627        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH C4641        DISTANCE =  5.19 ANGSTROMS
REMARK 525    HOH C4649        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH C4657        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH C4659        DISTANCE =  6.43 ANGSTROMS
REMARK 525    HOH C4661        DISTANCE =  5.46 ANGSTROMS
REMARK 525    HOH C4684        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH C4687        DISTANCE =  6.22 ANGSTROMS
REMARK 525    HOH C4694        DISTANCE =  6.80 ANGSTROMS
REMARK 525    HOH C4696        DISTANCE =  5.61 ANGSTROMS
REMARK 525    HOH C4702        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH C4705        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH C4712        DISTANCE =  6.24 ANGSTROMS
REMARK 525    HOH C4717        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH D2925        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH D3492        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH D3529        DISTANCE =  5.98 ANGSTROMS
REMARK 525    HOH D3531        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH D3539        DISTANCE =  7.10 ANGSTROMS
REMARK 525    HOH E1297        DISTANCE =  6.11 ANGSTROMS
REMARK 525    HOH E1314        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH E2281        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH E2282        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH E2556        DISTANCE =  5.46 ANGSTROMS
REMARK 525    HOH E2569        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH E2576        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH E2580        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH E2591        DISTANCE =  6.52 ANGSTROMS
REMARK 525    HOH E2626        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH E2632        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH E3548        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH E3582        DISTANCE =  6.89 ANGSTROMS
REMARK 525    HOH E3587        DISTANCE =  6.63 ANGSTROMS
REMARK 525    HOH E3599        DISTANCE =  5.83 ANGSTROMS
REMARK 525    HOH E3608        DISTANCE =  5.94 ANGSTROMS
REMARK 525    HOH F3213        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH F3245        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH F3304        DISTANCE =  6.55 ANGSTROMS
REMARK 525    HOH G4197        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH G4205        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH G4593        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH G4594        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH G4699        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH G4701        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH G4705        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH G4706        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH G4708        DISTANCE =  6.17 ANGSTROMS
REMARK 525    HOH G4710        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH G4715        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH G4718        DISTANCE =  5.77 ANGSTROMS
REMARK 525    HOH G4719        DISTANCE =  6.57 ANGSTROMS
REMARK 525    HOH G4722        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH G4724        DISTANCE =  6.28 ANGSTROMS
REMARK 525    HOH G4726        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH G4731        DISTANCE =  5.19 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A4013   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 112   O
REMARK 620 2 THR A 114   OG1 102.7
REMARK 620 3 HOH A4680   O    79.8 174.9
REMARK 620 4 HOH A4679   O    99.0  93.4  90.5
REMARK 620 5 HOH A4021   O   162.5  93.1  83.8  87.3
REMARK 620 6 ASP A  84   O    72.3  85.5  91.2 170.6 102.1
REMARK 620 7 THR A 114   N    64.6  49.4 129.7 127.8 123.7  45.8
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A4005   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 127   OE1
REMARK 620 2 GLU A 299   OE1 135.9
REMARK 620 3 MET A 300   O    93.3  95.7
REMARK 620 4 HOH A4112   O    75.1 100.1 164.2
REMARK 620 5 HOH A4113   O   134.8  88.4  69.5 111.0
REMARK 620 6 ALA A 126   O    85.3 138.2  86.5  81.9  53.3
REMARK 620 7 ASN A 301   OD1  80.2  61.7  73.2 114.4 128.8 154.2
REMARK 620 8 HOH A4111   O    70.8  68.2 123.3  63.5 153.5 141.7  51.0
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A4004   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 215   OE2
REMARK 620 2 ASP A 238   O   118.5
REMARK 620 3 ALA A 239   O    88.3  67.8
REMARK 620 4 ILE A 242   O    88.5 141.7  87.9
REMARK 620 5 SER A 247   OG  140.1  97.4 123.1  70.8
REMARK 620 6 ASN A 236   OD1  82.9  88.9 147.2 123.1  81.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A4003  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 285   OE1
REMARK 620 2 GLU A 299   OE2  78.6
REMARK 620 3 ADP A4001   O1B 173.3  95.6
REMARK 620 4 PO4 A4006   O3   82.5  81.6  93.4
REMARK 620 5 ADP A4001   O1A  93.5  84.7  89.2 166.3
REMARK 620 6 HOH A4537   O    85.4 161.7 100.8 105.2  87.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A4002  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 299   CD
REMARK 620 2 GLU A 299   OE1  28.4
REMARK 620 3 GLU A 299   OE2  31.1  59.2
REMARK 620 4 ASN A 301   OD1  89.5  88.7  95.8
REMARK 620 5 HOH A4111   O   118.1  90.2 149.2  78.5
REMARK 620 6 ADP A4001   O3B  84.6  77.8  88.3 161.4  88.7
REMARK 620 7 PO4 A4006   O1  127.1 155.4  96.3  92.5 114.1 105.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A4010   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 761   OE2
REMARK 620 2 HIS A 781   ND1  75.8
REMARK 620 3 GLU A 783   O   131.1  98.7
REMARK 620 4 GLN A 784   O    90.4 148.1  68.7
REMARK 620 5 VAL A 787   O    76.3 119.5 139.1  83.6
REMARK 620 6 SER A 792   OG  127.6  85.4  99.6 124.8  71.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A4008  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 829   OE1
REMARK 620 2 GLU A 841   OE2  86.3
REMARK 620 3 ADP A4007   O2A  94.2  95.6
REMARK 620 4 HOH A4590   O    92.8 176.5  87.8
REMARK 620 5 ADP A4007   O3B 176.9  91.0  87.7  89.8
REMARK 620 6 HOH A4638   O    96.3  80.8 168.7  96.0  81.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A4009   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 841   OE1
REMARK 620 2 GLU A 841   OE2  48.4
REMARK 620 3 ADP A4007   O2B  98.1 102.4
REMARK 620 4 ADP A4007   O3B  95.0  64.1  50.8
REMARK 620 5 HOH A4433   O    51.8  93.6  62.0  97.3
REMARK 620 6 ASN A 843   OD1  76.7  68.3 170.6 121.2 118.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K B4014   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  16   O
REMARK 620 2 ASP B 112   O    94.2
REMARK 620 3 HOH B4089   O    87.0  76.9
REMARK 620 4 HOH A4363   O   122.2  82.0 145.2
REMARK 620 5 HOH B4042   O    79.3 160.0 121.1  85.5
REMARK 620 6 HOH A4364   O   142.8 115.9  79.6  85.2  78.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C4033   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C  84   O
REMARK 620 2 THR C 114   OG1  81.9
REMARK 620 3 GLY C 112   O    79.3 107.9
REMARK 620 4 HOH C4043   O   122.2  67.1 155.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C4025   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 127   OE1
REMARK 620 2 GLU C 299   OE1 140.3
REMARK 620 3 MET C 300   O   100.1  96.0
REMARK 620 4 HOH C4135   O   134.8  84.8  63.7
REMARK 620 5 ALA C 126   O    83.2 135.1  82.5  54.1
REMARK 620 6  MN C4022  MN   102.1  38.3 106.3 122.7 168.4
REMARK 620 7 HOH C4133   O    71.6  69.9 128.3 152.3 142.4  35.2
REMARK 620 8 HOH C4134   O    65.0 102.8 161.2 117.5  84.1  88.8  60.3
REMARK 620 9 ASN C 301   OD1  89.7  58.8  77.5 123.3 157.3  34.1  52.2 112.4
REMARK 620 N                    1     2     3     4     5     6     7     8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C4034   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 143   OG1
REMARK 620 2 HOH C4143   O    71.8
REMARK 620 3 ALA C 144   O    81.0  60.9
REMARK 620 4 HOH C4144   O    81.1  69.7 130.5
REMARK 620 5 HOH C4145   O    80.3 142.2 139.2  81.5
REMARK 620 6 THR C 143   O    71.8 123.2  71.6 141.9  68.2
REMARK 620 7 HOH C4148   O   124.9  53.6  79.0  74.4 140.5 143.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C4024   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 215   OE2
REMARK 620 2 ASN C 236   OD1  88.0
REMARK 620 3 ASP C 238   O   119.2  96.1
REMARK 620 4 ALA C 239   O    83.6 154.4  67.7
REMARK 620 5 ILE C 242   O    84.6 113.7 143.1  89.6
REMARK 620 6 SER C 247   OG  140.5  78.4  99.1 122.4  68.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C4023  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 285   OE1
REMARK 620 2 GLU C 299   OE2  77.3
REMARK 620 3 ADP C4021   O1A  98.2  90.2
REMARK 620 4 HOH C4628   O    86.7 161.9  83.7
REMARK 620 5 PO4 C4026   O3   85.3  79.5 168.2 107.8
REMARK 620 6 ADP C4021   O1B 171.3  98.6  89.4  98.3  86.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C4022  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 299   CD
REMARK 620 2 GLU C 299   OE1  28.2
REMARK 620 3 GLU C 299   OE2  30.9  59.1
REMARK 620 4 ASN C 301   OD1  85.1  84.3  86.7
REMARK 620 5 ADP C4021   O3B  90.3  86.1  95.4 167.3
REMARK 620 6 PO4 C4026   O1  127.3 154.6  96.7  87.0 105.1
REMARK 620 7 HOH C4133   O   124.0  96.2 153.5  81.1  91.7 105.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C4030   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 761   OE2
REMARK 620 2 HIS C 781   ND1  76.0
REMARK 620 3 GLU C 783   O   128.8  94.5
REMARK 620 4 VAL C 787   O    83.2 120.5 139.1
REMARK 620 5 SER C 792   OG  127.1  81.0  99.6  68.8
REMARK 620 6 GLN C 784   O    94.6 153.3  71.6  82.2 123.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C4028  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 829   OE1
REMARK 620 2 GLU C 841   OE2  76.2
REMARK 620 3 ADP C4027   O3B 166.1  90.5
REMARK 620 4 HOH C4630   O    82.1  78.9  91.6
REMARK 620 5 HOH C4631   O    98.7 173.8  94.4  97.2
REMARK 620 6 ADP C4027   O2A 101.1 103.2  85.6 176.5  80.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C4029   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 841   OE1
REMARK 620 2 ADP C4027   O2B  83.1
REMARK 620 3 HOH C4440   O    74.1  89.5
REMARK 620 4 GLU C 841   OE2  37.8  81.0  36.7
REMARK 620 5 HOH C4441   O    64.8 144.4  95.8  82.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K D4035   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D  16   O
REMARK 620 2 ASP D 112   O    91.7
REMARK 620 3 HOH D1022   O    72.4 155.3
REMARK 620 4 HOH C4372   O   117.5  91.4  80.1
REMARK 620 5 HOH C4373   O   139.9 126.2  75.0  78.4
REMARK 620 6 HOH D2902   O    83.4  85.0 110.9 158.9  87.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E4056   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 112   O
REMARK 620 2 THR E 114   OG1  95.4
REMARK 620 3 ASP E  84   O    75.6  76.0
REMARK 620 4 HOH E1176   O   170.0  75.6 105.7
REMARK 620 5 HOH E2520   O    74.1  71.9 132.9  98.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E4048   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 127   OE1
REMARK 620 2 GLU E 299   OE1 130.8
REMARK 620 3 MET E 300   O    91.8  95.3
REMARK 620 4 HOH E1271   O    73.3  64.2 128.1
REMARK 620 5 HOH E1272   O    79.3  98.3 166.3  59.4
REMARK 620 6 ALA E 126   O    90.7 138.5  83.1 144.2  86.6
REMARK 620 7 HOH E1273   O   144.4  82.6  70.0 142.0 111.7  57.9
REMARK 620 8 ASN E 301   OD1  75.2  59.6  76.4  51.8 110.7 154.6 126.0
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E4057   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 143   O
REMARK 620 2 THR E 143   OG1  67.7
REMARK 620 3 HOH E1282   O    74.0  77.3
REMARK 620 4 HOH E1285   O   135.8 115.0 149.8
REMARK 620 5 ALA E 144   O    61.4  70.7 132.1  77.5
REMARK 620 6 HOH E1281   O   140.5  79.3  78.2  77.4 127.2
REMARK 620 7 HOH E1280   O   116.2  72.8 140.3  42.3  59.2  71.0
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E4047   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 215   OE2
REMARK 620 2 ASN E 236   OD1  83.2
REMARK 620 3 ASP E 238   O   119.2  93.9
REMARK 620 4 ALA E 239   O    86.9 154.0  70.2
REMARK 620 5 ILE E 242   O    87.7 118.1 141.2  85.3
REMARK 620 6 SER E 247   OG  141.1  80.5  97.1 120.8  69.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E4046  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 285   OE1
REMARK 620 2 GLU E 299   OE2  78.1
REMARK 620 3 HOH E2516   O    87.2 162.9
REMARK 620 4 ADP E4044   O1B 177.4  99.9  95.1
REMARK 620 5 PO4 E4049   O3   89.6  87.0 101.7  88.6
REMARK 620 6 ADP E4044   O1A  91.0  87.8  83.7  90.6 174.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E4045  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 299   CD
REMARK 620 2 GLU E 299   OE1  28.9
REMARK 620 3 GLU E 299   OE2  30.8  59.6
REMARK 620 4 ASN E 301   OD1  92.0  91.1  95.3
REMARK 620 5 ADP E4044   O3B  86.0  81.3  89.2 167.8
REMARK 620 6 HOH E1271   O   116.7  88.0 147.5  82.1  88.0
REMARK 620 7 PO4 E4049   O1  126.2 154.9  95.8  85.8 105.1 116.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E4053   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 761   OE2
REMARK 620 2 HIS E 781   ND1  81.3
REMARK 620 3 GLU E 783   O   128.5  93.9
REMARK 620 4 VAL E 787   O    76.5 121.0 141.6
REMARK 620 5 SER E 792   OG  127.0  78.8 101.5  73.0
REMARK 620 6 GLN E 784   O    91.2 148.1  66.8  86.6 128.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E4051  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 829   OE1
REMARK 620 2 GLU E 841   OE2  93.8
REMARK 620 3 ADP E4050   O2A  97.4  93.0
REMARK 620 4 HOH E2519   O    91.3 174.9  86.3
REMARK 620 5 ADP E4050   O3B 176.7  85.0  85.8  89.9
REMARK 620 6 HOH E2518   O    88.4  91.7 172.3  88.5  88.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E4052   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 841   OE1
REMARK 620 2 HOH E1603   O    58.1
REMARK 620 3 ADP E4050   O2B  94.0  66.7
REMARK 620 4 HOH E1604   O    88.8 131.9  84.0
REMARK 620 5 GLU E 841   OE2  40.0  84.3  77.3  51.4
REMARK 620 6 ASN E 843   OD1  63.8 118.2 138.2  62.0  62.8
REMARK 620 7 HOH E1605   O    57.5  81.8 146.2 110.6  88.2  49.0
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K F4058   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F  16   O
REMARK 620 2 ASP F 112   O    91.5
REMARK 620 3 HOH E2780   O    84.1  87.0
REMARK 620 4 HOH E1558   O    77.8 152.6 116.4
REMARK 620 5 HOH E1526   O   114.2  80.9 158.2  80.6
REMARK 620 6 HOH E1527   O   140.2 123.9  80.6  76.6  91.1
REMARK 620 7 HOH E2778   O    75.4 158.4  74.8  41.8 120.0  65.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G4078   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G  84   O
REMARK 620 2 GLY G 112   O    83.6
REMARK 620 3 THR G 114   OG1  85.1 104.3
REMARK 620 4 THR G 114   N    48.0  67.1  51.4
REMARK 620 5 HOH G4089   O   102.5 170.4  69.3 111.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G4079   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 143   OG1
REMARK 620 2 ALA G 144   O    72.7
REMARK 620 3 HOH G4190   O    76.1  65.0
REMARK 620 4 HOH G4195   O   131.7  76.5  57.3
REMARK 620 5 HOH G4544   O   174.5 102.6 104.7  47.9
REMARK 620 6 HOH G4192   O    86.2 135.2 147.3 140.5  95.6
REMARK 620 7 HOH G4191   O    78.7 128.2  66.8  92.7 106.6  83.1
REMARK 620 8 THR G 143   O    67.8  69.9 128.5 132.3 108.2  65.6 134.7
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G4069   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 215   OE2
REMARK 620 2 ASP G 238   O   120.7
REMARK 620 3 ALA G 239   O    87.6  71.5
REMARK 620 4 ILE G 242   O    89.8 142.3  89.9
REMARK 620 5 SER G 247   OG  138.6  96.6 123.4  66.1
REMARK 620 6 ASN G 236   OD1  87.2  89.5 154.0 115.6  75.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G4068  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 285   OE1
REMARK 620 2 GLU G 299   OE2  81.0
REMARK 620 3 PO4 G4071   O3   86.3  87.8
REMARK 620 4 HOH G4540   O    87.0 167.8  93.2
REMARK 620 5 ADP G4066   O1A  99.3  83.7 168.9  96.6
REMARK 620 6 ADP G4066   O1B 171.8  98.8  85.5  93.4  88.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G4067  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 299   CD
REMARK 620 2 GLU G 299   OE1  28.8
REMARK 620 3 GLU G 299   OE2  30.6  59.4
REMARK 620 4 ASN G 301   OD1  85.7  83.4  89.4
REMARK 620 5 HOH G4181   O   123.0  94.2 153.5  88.4
REMARK 620 6 PO4 G4071   O1  124.2 152.2  94.0  89.0 112.4
REMARK 620 7 ADP G4066   O3B  84.7  81.1  89.7 162.6  84.7 108.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G4070   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 299   OE1
REMARK 620 2 MET G 300   O    97.5
REMARK 620 3 HOH G4182   O   100.5 160.3
REMARK 620 4 HOH G4183   O    84.4  68.4 121.2
REMARK 620 5 ALA G 126   O   143.2  81.8  88.5  60.9
REMARK 620 6 HOH G4181   O    68.6 129.7  52.2 148.3 137.9
REMARK 620 7 ASN G 301   OD1  56.7  76.2 107.4 122.5 153.0  55.5
REMARK 620 8 GLU G 127   OE1 132.4  93.1  68.8 141.8  84.2  69.0  81.6
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G4075   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 761   OE2
REMARK 620 2 HIS G 781   ND1  80.6
REMARK 620 3 VAL G 787   O    80.4 127.7
REMARK 620 4 SER G 792   OG  129.2  80.8  74.8
REMARK 620 5 GLN G 784   O    91.6 144.0  84.6 128.4
REMARK 620 6 GLU G 783   O   130.4  92.1 135.9  97.0  66.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G4073  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 829   OE1
REMARK 620 2 GLU G 841   OE2  87.8
REMARK 620 3 HOH G4542   O   101.5  91.3
REMARK 620 4 ADP G4072   O3B 174.5  89.3  73.8
REMARK 620 5 HOH G4541   O    95.7 173.4  82.6  86.7
REMARK 620 6 ADP G4072   O2A  93.8  92.3 164.5  91.1  93.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G4074   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 841   OE1
REMARK 620 2 HOH G4464   O    83.3
REMARK 620 3 ADP G4072   O2B  89.9  74.5
REMARK 620 4 ASN G 843   OD1  58.3  62.0 127.3
REMARK 620 5 GLU G 841   OE2  38.0  48.1  68.9  60.2
REMARK 620 6 HOH G4465   O    52.6 116.4 135.8  56.4  87.0
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 4008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 4013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 4014
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4015
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4017
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4018
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 4019
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 4020
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4022
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4023
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4024
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4025
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 4028
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4029
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4030
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4033
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 4034
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 4035
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4036
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4037
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4038
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4039
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4040
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4041
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 4042
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 4043
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4045
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4046
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4047
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4048
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 4051
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4052
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4053
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4056
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 4057
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 4058
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4059
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4060
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4061
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4062
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4063
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 4064
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 4065
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4067
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4068
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4069
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4070
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 4073
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4074
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4075
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4078
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 4079
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4080
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4081
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4082
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4083
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4084
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 4085
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 4086
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 4006
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 4026
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 4049
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 4071
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 4007
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 4011
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 4012
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 4021
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 4027
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 4031
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 4032
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 4044
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 4050
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 4054
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 4055
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 4066
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 4072
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 4076
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 4077
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CLONE USED VARIED FROM THE SWISS-PROT
REMARK 999 ENTRY AT RESIDUE 46 OF CHAINS ACEG (SWS P00968)
REMARK 999 AND RESIDUE 183 OF CHAINS BDFH (SWS P00907).
DBREF  1M6V A    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1M6V C    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1M6V E    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1M6V G    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1M6V B    1   382  UNP    P00907   CARA_ECOLI       1    382
DBREF  1M6V D    1   382  UNP    P00907   CARA_ECOLI       1    382
DBREF  1M6V F    1   382  UNP    P00907   CARA_ECOLI       1    382
DBREF  1M6V H    1   382  UNP    P00907   CARA_ECOLI       1    382
SEQADV 1M6V ASN A   46  UNP  P00968    LEU    45 SEE REMARK 999
SEQADV 1M6V ASN C   46  UNP  P00968    LEU    45 SEE REMARK 999
SEQADV 1M6V ASN E   46  UNP  P00968    LEU    45 SEE REMARK 999
SEQADV 1M6V ASN G   46  UNP  P00968    LEU    45 SEE REMARK 999
SEQADV 1M6V GLN B  183  UNP  P00907    GLU   183 SEE REMARK 999
SEQADV 1M6V PHE B  359  UNP  P00907    GLY   359 ENGINEERED
SEQADV 1M6V GLN D  183  UNP  P00907    GLU   183 SEE REMARK 999
SEQADV 1M6V PHE D  359  UNP  P00907    GLY   359 ENGINEERED
SEQADV 1M6V GLN F  183  UNP  P00907    GLU   183 SEE REMARK 999
SEQADV 1M6V PHE F  359  UNP  P00907    GLY   359 ENGINEERED
SEQADV 1M6V GLN H  183  UNP  P00907    GLU   183 SEE REMARK 999
SEQADV 1M6V PHE H  359  UNP  P00907    GLY   359 ENGINEERED
SEQRES   1 A 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES   2 A 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES   3 A 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES   4 A 1073  GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES   5 A 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES   6 A 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES   7 A 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES   8 A 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES   9 A 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES  10 A 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES  11 A 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES  12 A 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES  13 A 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES  14 A 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES  15 A 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES  16 A 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES  17 A 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES  18 A 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES  19 A 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES  20 A 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES  21 A 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES  22 A 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES  23 A 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES  24 A 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES  25 A 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES  26 A 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES  27 A 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES  28 A 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES  29 A 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES  30 A 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES  31 A 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES  32 A 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES  33 A 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES  34 A 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES  35 A 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES  36 A 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES  37 A 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES  38 A 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES  39 A 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES  40 A 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES  41 A 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES  42 A 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES  43 A 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES  44 A 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES  45 A 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES  46 A 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES  47 A 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES  48 A 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES  49 A 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES  50 A 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES  51 A 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES  52 A 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES  53 A 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES  54 A 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES  55 A 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES  56 A 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES  57 A 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES  58 A 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES  59 A 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES  60 A 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES  61 A 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES  62 A 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES  63 A 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES  64 A 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES  65 A 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES  66 A 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES  67 A 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES  68 A 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES  69 A 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES  70 A 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES  71 A 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES  72 A 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES  73 A 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES  74 A 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES  75 A 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES  76 A 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES  77 A 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES  78 A 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES  79 A 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES  80 A 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES  81 A 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES  82 A 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES  83 A 1073  GLU MET HIS ALA GLN ILE LYS
SEQRES   1 B  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR
SEQRES   2 B  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA
SEQRES   3 B  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR
SEQRES   4 B  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE
SEQRES   5 B  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR
SEQRES   6 B  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN
SEQRES   7 B  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN
SEQRES   8 B  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG
SEQRES   9 B  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS
SEQRES  10 B  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY
SEQRES  11 B  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA
SEQRES  12 B  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET
SEQRES  13 B  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER
SEQRES  14 B  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO
SEQRES  15 B  382  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL
SEQRES  16 B  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET
SEQRES  17 B  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA
SEQRES  18 B  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP
SEQRES  19 B  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO
SEQRES  20 B  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU
SEQRES  21 B  382  THR ASP ILE PRO VAL PHE GLY ILE CYS LEU GLY HIS GLN
SEQRES  22 B  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET
SEQRES  23 B  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP
SEQRES  24 B  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS
SEQRES  25 B  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU
SEQRES  26 B  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN
SEQRES  27 B  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN
SEQRES  28 B  382  GLY HIS PRO GLU ALA SER PRO PHE PRO HIS ASP ALA ALA
SEQRES  29 B  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR
SEQRES  30 B  382  ARG LYS THR ALA LYS
SEQRES   1 C 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES   2 C 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES   3 C 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES   4 C 1073  GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES   5 C 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES   6 C 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES   7 C 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES   8 C 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES   9 C 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES  10 C 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES  11 C 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES  12 C 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES  13 C 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES  14 C 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES  15 C 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES  16 C 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES  17 C 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES  18 C 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES  19 C 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES  20 C 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES  21 C 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES  22 C 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES  23 C 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES  24 C 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES  25 C 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES  26 C 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES  27 C 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES  28 C 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES  29 C 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES  30 C 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES  31 C 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES  32 C 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES  33 C 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES  34 C 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES  35 C 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES  36 C 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES  37 C 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES  38 C 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES  39 C 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES  40 C 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES  41 C 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES  42 C 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES  43 C 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES  44 C 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES  45 C 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES  46 C 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES  47 C 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES  48 C 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES  49 C 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES  50 C 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES  51 C 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES  52 C 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES  53 C 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES  54 C 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES  55 C 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES  56 C 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES  57 C 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES  58 C 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES  59 C 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES  60 C 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES  61 C 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES  62 C 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES  63 C 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES  64 C 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES  65 C 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES  66 C 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES  67 C 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES  68 C 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES  69 C 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES  70 C 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES  71 C 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES  72 C 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES  73 C 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES  74 C 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES  75 C 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES  76 C 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES  77 C 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES  78 C 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES  79 C 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES  80 C 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES  81 C 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES  82 C 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES  83 C 1073  GLU MET HIS ALA GLN ILE LYS
SEQRES   1 D  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR
SEQRES   2 D  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA
SEQRES   3 D  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR
SEQRES   4 D  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE
SEQRES   5 D  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR
SEQRES   6 D  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN
SEQRES   7 D  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN
SEQRES   8 D  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG
SEQRES   9 D  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS
SEQRES  10 D  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY
SEQRES  11 D  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA
SEQRES  12 D  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET
SEQRES  13 D  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER
SEQRES  14 D  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO
SEQRES  15 D  382  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL
SEQRES  16 D  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET
SEQRES  17 D  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA
SEQRES  18 D  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP
SEQRES  19 D  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO
SEQRES  20 D  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU
SEQRES  21 D  382  THR ASP ILE PRO VAL PHE GLY ILE CYS LEU GLY HIS GLN
SEQRES  22 D  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET
SEQRES  23 D  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP
SEQRES  24 D  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS
SEQRES  25 D  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU
SEQRES  26 D  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN
SEQRES  27 D  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN
SEQRES  28 D  382  GLY HIS PRO GLU ALA SER PRO PHE PRO HIS ASP ALA ALA
SEQRES  29 D  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR
SEQRES  30 D  382  ARG LYS THR ALA LYS
SEQRES   1 E 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES   2 E 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES   3 E 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES   4 E 1073  GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES   5 E 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES   6 E 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES   7 E 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES   8 E 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES   9 E 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES  10 E 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES  11 E 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES  12 E 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES  13 E 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES  14 E 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES  15 E 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES  16 E 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES  17 E 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES  18 E 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES  19 E 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES  20 E 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES  21 E 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES  22 E 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES  23 E 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES  24 E 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES  25 E 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES  26 E 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES  27 E 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES  28 E 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES  29 E 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES  30 E 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES  31 E 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES  32 E 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES  33 E 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES  34 E 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES  35 E 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES  36 E 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES  37 E 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES  38 E 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES  39 E 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES  40 E 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES  41 E 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES  42 E 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES  43 E 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES  44 E 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES  45 E 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES  46 E 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES  47 E 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES  48 E 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES  49 E 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES  50 E 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES  51 E 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES  52 E 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES  53 E 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES  54 E 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES  55 E 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES  56 E 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES  57 E 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES  58 E 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES  59 E 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES  60 E 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES  61 E 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES  62 E 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES  63 E 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES  64 E 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES  65 E 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES  66 E 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES  67 E 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES  68 E 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES  69 E 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES  70 E 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES  71 E 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES  72 E 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES  73 E 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES  74 E 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES  75 E 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES  76 E 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES  77 E 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES  78 E 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES  79 E 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES  80 E 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES  81 E 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES  82 E 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES  83 E 1073  GLU MET HIS ALA GLN ILE LYS
SEQRES   1 F  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR
SEQRES   2 F  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA
SEQRES   3 F  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR
SEQRES   4 F  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE
SEQRES   5 F  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR
SEQRES   6 F  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN
SEQRES   7 F  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN
SEQRES   8 F  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG
SEQRES   9 F  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS
SEQRES  10 F  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY
SEQRES  11 F  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA
SEQRES  12 F  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET
SEQRES  13 F  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER
SEQRES  14 F  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO
SEQRES  15 F  382  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL
SEQRES  16 F  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET
SEQRES  17 F  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA
SEQRES  18 F  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP
SEQRES  19 F  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO
SEQRES  20 F  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU
SEQRES  21 F  382  THR ASP ILE PRO VAL PHE GLY ILE CYS LEU GLY HIS GLN
SEQRES  22 F  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET
SEQRES  23 F  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP
SEQRES  24 F  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS
SEQRES  25 F  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU
SEQRES  26 F  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN
SEQRES  27 F  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN
SEQRES  28 F  382  GLY HIS PRO GLU ALA SER PRO PHE PRO HIS ASP ALA ALA
SEQRES  29 F  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR
SEQRES  30 F  382  ARG LYS THR ALA LYS
SEQRES   1 G 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU
SEQRES   2 G 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE
SEQRES   3 G 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU
SEQRES   4 G 1073  GLU GLY TYR ARG VAL ILE ASN VAL ASN SER ASN PRO ALA
SEQRES   5 G 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR
SEQRES   6 G 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE
SEQRES   7 G 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY
SEQRES   8 G 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG
SEQRES   9 G 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY
SEQRES  10 G 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG
SEQRES  11 G 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR
SEQRES  12 G 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU
SEQRES  13 G 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG
SEQRES  14 G 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA
SEQRES  15 G 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY
SEQRES  16 G 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU
SEQRES  17 G 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL
SEQRES  18 G 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE
SEQRES  19 G 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER
SEQRES  20 G 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU
SEQRES  21 G 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG
SEQRES  22 G 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE
SEQRES  23 G 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU
SEQRES  24 G 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER
SEQRES  25 G 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS
SEQRES  26 G 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP
SEQRES  27 G 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER
SEQRES  28 G 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE
SEQRES  29 G 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN
SEQRES  30 G 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR
SEQRES  31 G 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU
SEQRES  32 G 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP
SEQRES  33 G 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS
SEQRES  34 G 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA
SEQRES  35 G 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU
SEQRES  36 G 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU
SEQRES  37 G 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE
SEQRES  38 G 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG
SEQRES  39 G 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY
SEQRES  40 G 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR
SEQRES  41 G 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA
SEQRES  42 G 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR
SEQRES  43 G 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG
SEQRES  44 G 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE
SEQRES  45 G 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA
SEQRES  46 G 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET
SEQRES  47 G 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP
SEQRES  48 G 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU
SEQRES  49 G 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY
SEQRES  50 G 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU
SEQRES  51 G 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY
SEQRES  52 G 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU
SEQRES  53 G 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN
SEQRES  54 G 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL
SEQRES  55 G 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG
SEQRES  56 G 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL
SEQRES  57 G 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA
SEQRES  58 G 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS
SEQRES  59 G 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE
SEQRES  60 G 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU
SEQRES  61 G 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA
SEQRES  62 G 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN
SEQRES  63 G 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU
SEQRES  64 G 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL
SEQRES  65 G 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG
SEQRES  66 G 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY
SEQRES  67 G 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY
SEQRES  68 G 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE
SEQRES  69 G 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE
SEQRES  70 G 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU
SEQRES  71 G 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR
SEQRES  72 G 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN
SEQRES  73 G 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL
SEQRES  74 G 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA
SEQRES  75 G 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS
SEQRES  76 G 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO
SEQRES  77 G 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE
SEQRES  78 G 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE
SEQRES  79 G 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG
SEQRES  80 G 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR
SEQRES  81 G 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA
SEQRES  82 G 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN
SEQRES  83 G 1073  GLU MET HIS ALA GLN ILE LYS
SEQRES   1 H  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR
SEQRES   2 H  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA
SEQRES   3 H  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR
SEQRES   4 H  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE
SEQRES   5 H  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR
SEQRES   6 H  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN
SEQRES   7 H  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN
SEQRES   8 H  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG
SEQRES   9 H  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS
SEQRES  10 H  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY
SEQRES  11 H  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA
SEQRES  12 H  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET
SEQRES  13 H  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER
SEQRES  14 H  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO
SEQRES  15 H  382  GLN ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL
SEQRES  16 H  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET
SEQRES  17 H  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA
SEQRES  18 H  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP
SEQRES  19 H  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO
SEQRES  20 H  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU
SEQRES  21 H  382  THR ASP ILE PRO VAL PHE GLY ILE CYS LEU GLY HIS GLN
SEQRES  22 H  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET
SEQRES  23 H  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP
SEQRES  24 H  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS
SEQRES  25 H  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU
SEQRES  26 H  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN
SEQRES  27 H  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN
SEQRES  28 H  382  GLY HIS PRO GLU ALA SER PRO PHE PRO HIS ASP ALA ALA
SEQRES  29 H  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR
SEQRES  30 H  382  ARG LYS THR ALA LYS
HET     MN  A4002       1
HET     MN  A4003       1
HET      K  A4004       1
HET      K  A4005       1
HET     MN  A4008       1
HET      K  A4009       1
HET      K  A4010       1
HET      K  A4013       1
HET      K  B4014       1
HET     CL  A4015       1
HET     CL  A4016       1
HET     CL  A4017       1
HET     CL  A4018       1
HET     CL  B4019       1
HET     CL  A4020       1
HET     MN  C4022       1
HET     MN  C4023       1
HET      K  C4024       1
HET      K  C4025       1
HET     MN  C4028       1
HET      K  C4029       1
HET      K  C4030       1
HET      K  C4033       1
HET      K  C4034       1
HET      K  D4035       1
HET     CL  C4036       1
HET     CL  C4037       1
HET     CL  C4038       1
HET     CL  C4039       1
HET     CL  C4040       1
HET     CL  C4041       1
HET     CL  C4042       1
HET     CL  D4043       1
HET     MN  E4045       1
HET     MN  E4046       1
HET      K  E4047       1
HET      K  E4048       1
HET     MN  E4051       1
HET      K  E4052       1
HET      K  E4053       1
HET      K  E4056       1
HET      K  E4057       1
HET      K  F4058       1
HET     CL  E4059       1
HET     CL  E4060       1
HET     CL  E4061       1
HET     CL  E4062       1
HET     CL  E4063       1
HET     CL  F4064       1
HET     CL  E4065       1
HET     MN  G4067       1
HET     MN  G4068       1
HET      K  G4069       1
HET      K  G4070       1
HET     MN  G4073       1
HET      K  G4074       1
HET      K  G4075       1
HET      K  G4078       1
HET      K  G4079       1
HET     CL  G4080       1
HET     CL  G4081       1
HET     CL  G4082       1
HET     CL  G4083       1
HET     CL  G4084       1
HET     CL  H4085       1
HET     CL  G4086       1
HET    PO4  A4006       5
HET    PO4  C4026       5
HET    PO4  E4049       5
HET    PO4  G4071       5
HET    ADP  A4001      27
HET    ADP  A4007      27
HET    ORN  A4011       9
HET    NET  A4012       9
HET    ADP  C4021      27
HET    ADP  C4027      27
HET    ORN  C4031       9
HET    NET  C4032       9
HET    ADP  E4044      27
HET    ADP  E4050      27
HET    ORN  E4054       9
HET    NET  E4055       9
HET    ADP  G4066      27
HET    ADP  G4072      27
HET    ORN  G4076       9
HET    NET  G4077       9
HETNAM      MN MANGANESE (II) ION
HETNAM       K POTASSIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     PO4 PHOSPHATE ION
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM     ORN L-ORNITHINE
HETNAM     NET TETRAETHYLAMMONIUM ION
FORMUL   9   MN    12(MN 2+)
FORMUL  11    K    26(K 1+)
FORMUL  18   CL    28(CL 1-)
FORMUL  75  PO4    4(O4 P 3-)
FORMUL  79  ADP    8(C10 H15 N5 O10 P2)
FORMUL  81  ORN    4(C5 H12 N2 O2)
FORMUL  82  NET    4(C8 H20 N 1+)
FORMUL  95  HOH   *3561(H2 O)
HELIX    1   1 CYS A   24  GLU A   39  1                                  16
HELIX    2   2 ASP A   57  ALA A   61  5                                   5
HELIX    3   3 HIS A   70  ARG A   82  1                                  13
HELIX    4   4 GLY A   91  GLN A  105  1                                  15
HELIX    5   5 GLY A  106  GLY A  112  1                                   7
HELIX    6   6 THR A  119  ASP A  128  1                                  10
HELIX    7   7 ASP A  128  ILE A  139  1                                  12
HELIX    8   8 THR A  151  GLY A  163  1                                  13
HELIX    9   9 ASN A  184  SER A  199  1                                  16
HELIX   10  10 HIS A  243  SER A  247  5                                   5
HELIX   11  11 THR A  257  GLY A  276  1                                  20
HELIX   12  12 SER A  305  GLY A  316  1                                  12
HELIX   13  13 PRO A  318  VAL A  328  1                                  11
HELIX   14  14 ASN A  363  PHE A  367  5                                   5
HELIX   15  15 THR A  390  LEU A  402  1                                  13
HELIX   16  16 GLU A  419  ASP A  430  1                                  12
HELIX   17  17 ASP A  434  ALA A  445  1                                  12
HELIX   18  18 SER A  448  ASN A  457  1                                  10
HELIX   19  19 ASP A  459  LEU A  484  1                                  26
HELIX   20  20 ASN A  485  LYS A  495  1                                  11
HELIX   21  21 ALA A  498  ALA A  506  1                                   9
HELIX   22  22 ARG A  509  ASP A  521  1                                  13
HELIX   23  23 GLY A  575  ASP A  592  1                                  18
HELIX   24  24 ASP A  609  SER A  613  5                                   5
HELIX   25  25 THR A  622  LYS A  634  1                                  13
HELIX   26  26 GLY A  644  ALA A  657  1                                  14
HELIX   27  27 SER A  665  ASP A  674  1                                  10
HELIX   28  28 ASP A  674  LEU A  685  1                                  12
HELIX   29  29 ALA A  697  GLY A  709  1                                  13
HELIX   30  30 ASP A  730  ALA A  741  1                                  12
HELIX   31  31 HIS A  788  SER A  792  5                                   5
HELIX   32  32 SER A  802  GLN A  821  1                                  20
HELIX   33  33 THR A  849  GLY A  858  1                                  10
HELIX   34  34 PRO A  860  GLY A  871  1                                  12
HELIX   35  35 SER A  873  GLY A  878  1                                   6
HELIX   36  36 LEU A  895  PHE A  900  5                                   6
HELIX   37  37 THR A  923  SER A  935  1                                  13
HELIX   38  38 ARG A  950  GLU A  955  5                                   6
HELIX   39  39 ARG A  956  GLN A  967  1                                  12
HELIX   40  40 THR A  974  ALA A  984  1                                  11
HELIX   41  41 HIS A 1000  GLY A 1008  1                                   9
HELIX   42  42 GLY A 1019  TYR A 1036  1                                  18
HELIX   43  43 THR A 1043  ASN A 1055  1                                  13
HELIX   44  44 SER A 1064  GLN A 1071  1                                   8
HELIX   45  45 GLY B   38  THR B   44  1                                   7
HELIX   46  46 ASP B   45  SER B   49  5                                   5
HELIX   47  47 ASN B   66  GLU B   70  5                                   5
HELIX   48  48 ASP B   97  HIS B  105  1                                   9
HELIX   49  49 ASP B  114  GLY B  126  1                                  13
HELIX   50  50 ASP B  139  PHE B  150  1                                  12
HELIX   51  51 LEU B  158  THR B  163  1                                   6
HELIX   52  52 LYS B  186  LEU B  190  5                                   5
HELIX   53  53 LYS B  202  ARG B  212  1                                  11
HELIX   54  54 SER B  224  LYS B  230  1                                   7
HELIX   55  55 CYS B  248  LEU B  259  1                                  12
HELIX   56  56 CYS B  269  SER B  279  1                                  11
HELIX   57  57 ALA B  363  LYS B  379  1                                  17
HELIX   58  58 CYS C   24  GLU C   40  1                                  17
HELIX   59  59 THR C   53  ALA C   61  5                                   9
HELIX   60  60 HIS C   70  ARG C   82  1                                  13
HELIX   61  61 GLY C   91  GLN C  105  1                                  15
HELIX   62  62 GLY C  106  GLY C  112  1                                   7
HELIX   63  63 THR C  119  ASP C  128  1                                  10
HELIX   64  64 ASP C  128  ILE C  139  1                                  12
HELIX   65  65 THR C  151  GLY C  163  1                                  13
HELIX   66  66 ASN C  184  SER C  199  1                                  16
HELIX   67  67 HIS C  243  SER C  247  5                                   5
HELIX   68  68 THR C  257  GLY C  276  1                                  20
HELIX   69  69 SER C  305  GLY C  316  1                                  12
HELIX   70  70 PRO C  318  VAL C  328  1                                  11
HELIX   71  71 THR C  331  LEU C  335  5                                   5
HELIX   72  72 ASN C  337  GLY C  341  5                                   5
HELIX   73  73 ASN C  363  PHE C  367  5                                   5
HELIX   74  74 THR C  390  LEU C  402  1                                  13
HELIX   75  75 GLU C  419  ASP C  430  1                                  12
HELIX   76  76 ASP C  434  ALA C  445  1                                  12
HELIX   77  77 SER C  448  ASN C  457  1                                  10
HELIX   78  78 ASP C  459  GLY C  480  1                                  22
HELIX   79  79 ASN C  485  LYS C  495  1                                  11
HELIX   80  80 ALA C  498  GLY C  507  1                                  10
HELIX   81  81 ARG C  509  ASP C  521  1                                  13
HELIX   82  82 GLY C  575  ASP C  592  1                                  18
HELIX   83  83 THR C  605  SER C  613  5                                   9
HELIX   84  84 THR C  622  LYS C  634  1                                  13
HELIX   85  85 GLY C  644  ALA C  657  1                                  14
HELIX   86  86 SER C  665  ASP C  674  1                                  10
HELIX   87  87 ASP C  674  LEU C  685  1                                  12
HELIX   88  88 ALA C  697  GLY C  709  1                                  13
HELIX   89  89 ASP C  730  ALA C  741  1                                  12
HELIX   90  90 HIS C  788  SER C  792  5                                   5
HELIX   91  91 SER C  802  GLN C  821  1                                  20
HELIX   92  92 THR C  849  GLY C  858  1                                  10
HELIX   93  93 PRO C  860  GLY C  871  1                                  12
HELIX   94  94 SER C  873  GLY C  878  1                                   6
HELIX   95  95 LEU C  895  PHE C  900  5                                   6
HELIX   96  96 THR C  923  SER C  935  1                                  13
HELIX   97  97 ARG C  950  GLU C  955  5                                   6
HELIX   98  98 ARG C  956  GLY C  968  1                                  13
HELIX   99  99 THR C  974  GLU C  983  1                                  10
HELIX  100 100 HIS C 1000  GLY C 1008  1                                   9
HELIX  101 101 GLY C 1019  LYS C 1037  1                                  19
HELIX  102 102 THR C 1043  LEU C 1054  1                                  12
HELIX  103 103 SER C 1064  GLN C 1071  1                                   8
HELIX  104 104 GLY D   38  THR D   44  1                                   7
HELIX  105 105 ASP D   45  SER D   49  5                                   5
HELIX  106 106 ASN D   66  GLU D   70  5                                   5
HELIX  107 107 ASP D   97  HIS D  105  1                                   9
HELIX  108 108 ASP D  114  GLY D  126  1                                  13
HELIX  109 109 ASP D  139  PHE D  150  1                                  12
HELIX  110 110 LEU D  158  THR D  163  1                                   6
HELIX  111 111 LYS D  186  LEU D  190  5                                   5
HELIX  112 112 LYS D  202  ARG D  212  1                                  11
HELIX  113 113 SER D  224  LYS D  230  1                                   7
HELIX  114 114 CYS D  248  LEU D  259  1                                  12
HELIX  115 115 CYS D  269  SER D  279  1                                  11
HELIX  116 116 GLU D  318  LEU D  321  5                                   4
HELIX  117 117 ALA D  364  THR D  380  1                                  17
HELIX  118 118 CYS E   24  GLU E   40  1                                  17
HELIX  119 119 THR E   53  ALA E   61  5                                   9
HELIX  120 120 HIS E   70  ARG E   82  1                                  13
HELIX  121 121 GLY E   91  GLN E  105  1                                  15
HELIX  122 122 GLY E  106  PHE E  111  1                                   6
HELIX  123 123 THR E  119  ASP E  128  1                                  10
HELIX  124 124 ASP E  128  GLY E  140  1                                  13
HELIX  125 125 THR E  151  GLY E  163  1                                  13
HELIX  126 126 ASN E  184  SER E  199  1                                  16
HELIX  127 127 HIS E  243  SER E  247  5                                   5
HELIX  128 128 THR E  257  GLY E  276  1                                  20
HELIX  129 129 SER E  305  GLY E  316  1                                  12
HELIX  130 130 PRO E  318  ALA E  327  1                                  10
HELIX  131 131 THR E  331  LEU E  335  5                                   5
HELIX  132 132 ASN E  337  GLY E  341  5                                   5
HELIX  133 133 ASN E  363  PHE E  367  5                                   5
HELIX  134 134 THR E  390  ARG E  400  1                                  11
HELIX  135 135 GLU E  419  ASP E  430  1                                  12
HELIX  136 136 ASP E  434  ALA E  445  1                                  12
HELIX  137 137 SER E  448  ASN E  457  1                                  10
HELIX  138 138 ASP E  459  GLY E  480  1                                  22
HELIX  139 139 ILE E  481  LEU E  484  5                                   4
HELIX  140 140 ASN E  485  LYS E  495  1                                  11
HELIX  141 141 ALA E  498  GLY E  507  1                                  10
HELIX  142 142 ARG E  509  TYR E  520  1                                  12
HELIX  143 143 GLY E  575  ASP E  592  1                                  18
HELIX  144 144 THR E  605  SER E  613  5                                   9
HELIX  145 145 THR E  622  LYS E  634  1                                  13
HELIX  146 146 GLY E  644  LYS E  649  1                                   6
HELIX  147 147 LEU E  650  ALA E  657  1                                   8
HELIX  148 148 SER E  665  ASP E  674  1                                  10
HELIX  149 149 ASP E  674  LEU E  685  1                                  12
HELIX  150 150 ALA E  697  GLY E  709  1                                  13
HELIX  151 151 ASP E  730  ALA E  741  1                                  12
HELIX  152 152 HIS E  788  SER E  792  5                                   5
HELIX  153 153 SER E  802  GLN E  821  1                                  20
HELIX  154 154 THR E  849  GLY E  858  1                                  10
HELIX  155 155 PRO E  860  GLY E  871  1                                  12
HELIX  156 156 SER E  873  GLY E  878  1                                   6
HELIX  157 157 PRO E  896  PHE E  900  5                                   5
HELIX  158 158 THR E  923  SER E  935  1                                  13
HELIX  159 159 ARG E  950  GLU E  955  5                                   6
HELIX  160 160 ARG E  956  GLY E  968  1                                  13
HELIX  161 161 HIS E  975  ALA E  984  1                                  10
HELIX  162 162 HIS E 1000  ASN E 1007  1                                   8
HELIX  163 163 GLY E 1019  TYR E 1036  1                                  18
HELIX  164 164 THR E 1043  LEU E 1054  1                                  12
HELIX  165 165 SER E 1064  ILE E 1072  1                                   9
HELIX  166 166 GLY F   38  THR F   44  1                                   7
HELIX  167 167 ASP F   45  SER F   49  5                                   5
HELIX  168 168 ASN F   66  GLU F   70  5                                   5
HELIX  169 169 ASP F   97  HIS F  105  1                                   9
HELIX  170 170 ASP F  114  GLY F  126  1                                  13
HELIX  171 171 ASP F  139  PHE F  150  1                                  12
HELIX  172 172 LEU F  158  THR F  163  1                                   6
HELIX  173 173 LYS F  186  LEU F  190  5                                   5
HELIX  174 174 LYS F  202  ASP F  211  1                                  10
HELIX  175 175 SER F  224  LYS F  230  1                                   7
HELIX  176 176 CYS F  248  LEU F  259  1                                  12
HELIX  177 177 CYS F  269  SER F  279  1                                  11
HELIX  178 178 ALA F  363  LYS F  379  1                                  17
HELIX  179 179 CYS G   24  GLU G   40  1                                  17
HELIX  180 180 THR G   53  ALA G   61  5                                   9
HELIX  181 181 HIS G   70  ARG G   82  1                                  13
HELIX  182 182 GLY G   91  GLN G  105  1                                  15
HELIX  183 183 GLY G  106  PHE G  111  1                                   6
HELIX  184 184 THR G  119  ASP G  128  1                                  10
HELIX  185 185 ASP G  128  ILE G  139  1                                  12
HELIX  186 186 THR G  151  GLY G  163  1                                  13
HELIX  187 187 ASN G  184  SER G  199  1                                  16
HELIX  188 188 HIS G  243  SER G  247  5                                   5
HELIX  189 189 THR G  257  GLY G  276  1                                  20
HELIX  190 190 SER G  305  GLY G  316  1                                  12
HELIX  191 191 PRO G  318  VAL G  328  1                                  11
HELIX  192 192 THR G  331  LEU G  335  5                                   5
HELIX  193 193 ASN G  337  GLY G  341  5                                   5
HELIX  194 194 ASN G  363  PHE G  367  5                                   5
HELIX  195 195 THR G  390  LEU G  402  1                                  13
HELIX  196 196 GLU G  419  ASP G  430  1                                  12
HELIX  197 197 ASP G  434  ALA G  445  1                                  12
HELIX  198 198 SER G  448  ASN G  457  1                                  10
HELIX  199 199 ASP G  459  LEU G  484  1                                  26
HELIX  200 200 ASN G  485  LYS G  495  1                                  11
HELIX  201 201 ALA G  498  GLY G  507  1                                  10
HELIX  202 202 ARG G  509  TYR G  520  1                                  12
HELIX  203 203 GLY G  575  GLY G  593  1                                  19
HELIX  204 204 THR G  605  ASP G  609  5                                   5
HELIX  205 205 THR G  622  LYS G  634  1                                  13
HELIX  206 206 GLY G  644  LYS G  649  1                                   6
HELIX  207 207 LEU G  650  ALA G  657  1                                   8
HELIX  208 208 SER G  665  ASP G  674  1                                  10
HELIX  209 209 ASP G  674  LYS G  686  1                                  13
HELIX  210 210 ALA G  697  GLY G  709  1                                  13
HELIX  211 211 ASP G  730  ALA G  741  1                                  12
HELIX  212 212 HIS G  788  SER G  792  5                                   5
HELIX  213 213 SER G  802  LEU G  820  1                                  19
HELIX  214 214 THR G  849  GLY G  858  1                                  10
HELIX  215 215 PRO G  860  GLY G  871  1                                  12
HELIX  216 216 SER G  873  GLY G  878  1                                   6
HELIX  217 217 LEU G  895  PHE G  900  5                                   6
HELIX  218 218 THR G  923  SER G  935  1                                  13
HELIX  219 219 ARG G  950  LYS G  954  5                                   5
HELIX  220 220 GLU G  955  GLU G  955  5                                   1
HELIX  221 221 ARG G  956  GLN G  967  1                                  12
HELIX  222 222 HIS G  975  GLU G  983  1                                   9
HELIX  223 223 LYS G  993  GLY G  997  5                                   5
HELIX  224 224 HIS G 1000  ASN G 1007  1                                   8
HELIX  225 225 GLY G 1019  LYS G 1037  1                                  19
HELIX  226 226 THR G 1043  LEU G 1054  1                                  12
HELIX  227 227 SER G 1064  GLN G 1071  1                                   8
HELIX  228 228 GLY H   38  THR H   44  1                                   7
HELIX  229 229 ASP H   45  SER H   49  5                                   5
HELIX  230 230 ASN H   66  GLU H   70  5                                   5
HELIX  231 231 ASP H   97  HIS H  105  1                                   9
HELIX  232 232 ASP H  114  GLY H  126  1                                  13
HELIX  233 233 ASP H  139  PHE H  150  1                                  12
HELIX  234 234 LEU H  158  THR H  163  1                                   6
HELIX  235 235 LYS H  186  LEU H  190  5                                   5
HELIX  236 236 LYS H  202  ASP H  211  1                                  10
HELIX  237 237 SER H  224  LYS H  230  1                                   7
HELIX  238 238 CYS H  248  LEU H  259  1                                  12
HELIX  239 239 CYS H  269  SER H  279  1                                  11
HELIX  240 240 ALA H  363  LYS H  379  1                                  17
SHEET    1   A 5 ALA A  63  TYR A  65  0
SHEET    2   A 5 ARG A  43  VAL A  47  1  N  ASN A  46   O  TYR A  65
SHEET    3   A 5 SER A   9  LEU A  13  1  N  ILE A  12   O  ILE A  45
SHEET    4   A 5 ALA A  85  LEU A  87  1  O  ALA A  85   N  LEU A  11
SHEET    5   A 5 THR A 114  MET A 115  1  O  THR A 114   N  VAL A  86
SHEET    1   B 4 SER A 146  ALA A 149  0
SHEET    2   B 4 LEU A 204  GLU A 208 -1  O  ILE A 206   N  GLY A 147
SHEET    3   B 4 CYS A 166  PRO A 170 -1  N  ARG A 169   O  LEU A 205
SHEET    4   B 4 GLY A 180  ALA A 182 -1  O  GLY A 180   N  ILE A 168
SHEET    1   C 7 LEU A 295  ASN A 301  0
SHEET    2   C 7 GLY A 280  VAL A 288 -1  N  GLN A 285   O  ILE A 298
SHEET    3   C 7 LYS A 214  ARG A 222 -1  N  TYR A 216   O  PHE A 286
SHEET    4   C 7 CYS A 228  ASN A 236 -1  O  VAL A 231   N  GLU A 219
SHEET    5   C 7 THR A 249  ALA A 251 -1  O  VAL A 250   N  GLU A 235
SHEET    6   C 7 VAL A 355  ARG A 361 -1  O  VAL A 356   N  ALA A 251
SHEET    7   C 7 GLY A 382  GLY A 388 -1  O  GLY A 388   N  VAL A 355
SHEET    1   D 6 VAL A 525  ARG A 528  0
SHEET    2   D 6 TYR A 542  THR A 546 -1  O  THR A 546   N  VAL A 525
SHEET    3   D 6 ARG A 615  PHE A 618  1  O  LEU A 616   N  MET A 543
SHEET    4   D 6 GLU A 595  ASN A 600  1  N  MET A 598   O  ARG A 615
SHEET    5   D 6 LYS A 561  LEU A 565  1  N  ILE A 562   O  ILE A 597
SHEET    6   D 6 GLY A 637  ILE A 639  1  O  ILE A 639   N  MET A 563
SHEET    1   E 4 ASN A 692  THR A 694  0
SHEET    2   E 4 LEU A 751  HIS A 754 -1  O  LEU A 752   N  ALA A 693
SHEET    3   E 4 LEU A 712  ARG A 715 -1  N  ARG A 715   O  LEU A 751
SHEET    4   E 4 GLU A 726  VAL A 728 -1  O  VAL A 728   N  LEU A 712
SHEET    1   F 7 VAL A 837  ASN A 843  0
SHEET    2   F 7 GLY A 824  VAL A 832 -1  N  GLN A 829   O  ILE A 840
SHEET    3   F 7 VAL A 760  CYS A 768 -1  N  VAL A 760   O  VAL A 832
SHEET    4   F 7 VAL A 773  HIS A 781 -1  O  LEU A 774   N  ILE A 767
SHEET    5   F 7 CYS A 794  LEU A 796 -1  O  SER A 795   N  GLU A 780
SHEET    6   F 7 TYR A 888  VAL A 894 -1  O  LYS A 891   N  CYS A 794
SHEET    7   F 7 GLY A 915  GLY A 921 -1  O  GLY A 919   N  VAL A 890
SHEET    1   G 5 ARG A 989  LEU A 990  0
SHEET    2   G 5 PHE A 969  ALA A 973  1  N  ALA A 973   O  ARG A 989
SHEET    3   G 5 GLY A 943  SER A 948  1  N  ALA A 945   O  GLU A 970
SHEET    4   G 5 TYR A1012  ASN A1015  1  O  ILE A1014   N  LEU A 946
SHEET    5   G 5 TYR A1040  ASP A1041  1  O  ASP A1041   N  ILE A1013
SHEET    1   H 8 SER B   4  LEU B   9  0
SHEET    2   H 8 GLN B  14  ALA B  19 -1  O  PHE B  15   N  LEU B   7
SHEET    3   H 8 VAL B 108  ALA B 111 -1  O  ALA B 111   N  ARG B  18
SHEET    4   H 8 ALA B  77  VAL B  81  1  N  LEU B  80   O  ILE B 110
SHEET    5   H 8 GLN B  51  LEU B  55  1  N  GLN B  51   O  GLN B  78
SHEET    6   H 8 GLY B  24  ASN B  33  1  N  GLU B  29   O  ILE B  52
SHEET    7   H 8 GLN B 128  ALA B 134 -1  O  GLN B 128   N  VAL B  30
SHEET    8   H 8 SER B   4  LEU B   9 -1  N  LEU B   6   O  ILE B 133
SHEET    1   I10 TYR B 168  TRP B 170  0
SHEET    2   I10 CYS B 214  VAL B 219 -1  O  ILE B 218   N  TYR B 168
SHEET    3   I10 PHE B 192  TYR B 197  1  N  ALA B 196   O  VAL B 219
SHEET    4   I10 GLY B 235  LEU B 238  1  O  PHE B 237   N  VAL B 195
SHEET    5   I10 VAL B 265  ILE B 268  1  O  ILE B 268   N  LEU B 238
SHEET    6   I10 ALA B 347  PHE B 350  1  O  PHE B 350   N  GLY B 267
SHEET    7   I10 LEU B 337  ARG B 342 -1  N  ILE B 340   O  SER B 349
SHEET    8   I10 LEU B 325  SER B 331 -1  N  HIS B 329   O  GLN B 338
SHEET    9   I10 THR B 283  ASP B 299 -1  N  LYS B 298   O  LYS B 330
SHEET   10   I10 VAL B 305  VAL B 316 -1  O  THR B 308   N  HIS B 295
SHEET    1   J 5 ALA C  63  TYR C  65  0
SHEET    2   J 5 ARG C  43  VAL C  47  1  N  ASN C  46   O  TYR C  65
SHEET    3   J 5 SER C   9  LEU C  13  1  N  ILE C  10   O  ILE C  45
SHEET    4   J 5 ALA C  85  LEU C  87  1  O  LEU C  87   N  LEU C  11
SHEET    5   J 5 THR C 114  MET C 115  1  O  THR C 114   N  VAL C  86
SHEET    1   K 4 SER C 146  ALA C 149  0
SHEET    2   K 4 LEU C 204  GLU C 208 -1  O  ILE C 206   N  GLY C 147
SHEET    3   K 4 CYS C 166  PRO C 170 -1  N  ARG C 169   O  LEU C 205
SHEET    4   K 4 GLY C 180  ALA C 182 -1  O  ALA C 182   N  CYS C 166
SHEET    1   L 7 LEU C 295  ASN C 301  0
SHEET    2   L 7 GLY C 280  VAL C 288 -1  N  ALA C 287   O  ILE C 296
SHEET    3   L 7 LYS C 214  ARG C 222 -1  N  LYS C 214   O  VAL C 288
SHEET    4   L 7 CYS C 228  ASN C 236 -1  O  VAL C 231   N  GLU C 219
SHEET    5   L 7 THR C 249  ALA C 251 -1  O  VAL C 250   N  GLU C 235
SHEET    6   L 7 VAL C 355  ARG C 361 -1  O  VAL C 356   N  ALA C 251
SHEET    7   L 7 GLY C 382  GLY C 388 -1  O  GLY C 388   N  VAL C 355
SHEET    1   M 7 VAL C 525  ARG C 528  0
SHEET    2   M 7 ALA C 541  THR C 546 -1  O  THR C 546   N  VAL C 525
SHEET    3   M 7 ARG C 615  PHE C 618  1  O  LEU C 616   N  ALA C 541
SHEET    4   M 7 GLU C 595  ASN C 600  1  N  MET C 598   O  TYR C 617
SHEET    5   M 7 LYS C 561  LEU C 565  1  N  ILE C 562   O  GLU C 595
SHEET    6   M 7 GLY C 637  ILE C 639  1  O  ILE C 639   N  MET C 563
SHEET    7   M 7 VAL C 661  ILE C 662  1  O  ILE C 662   N  VAL C 638
SHEET    1   N 4 ASN C 692  THR C 694  0
SHEET    2   N 4 LEU C 751  HIS C 754 -1  O  LEU C 752   N  ALA C 693
SHEET    3   N 4 LEU C 712  ARG C 715 -1  N  ARG C 715   O  LEU C 751
SHEET    4   N 4 GLU C 726  VAL C 728 -1  O  VAL C 728   N  LEU C 712
SHEET    1   O 7 GLU C 836  ASN C 843  0
SHEET    2   O 7 GLY C 824  LYS C 833 -1  N  ASN C 827   O  ASN C 843
SHEET    3   O 7 VAL C 760  CYS C 768 -1  N  VAL C 760   O  VAL C 832
SHEET    4   O 7 VAL C 773  HIS C 781 -1  O  LEU C 774   N  ILE C 767
SHEET    5   O 7 CYS C 794  LEU C 796 -1  O  SER C 795   N  GLU C 780
SHEET    6   O 7 TYR C 888  VAL C 894 -1  O  SER C 889   N  LEU C 796
SHEET    7   O 7 GLY C 915  GLY C 921 -1  O  GLY C 921   N  TYR C 888
SHEET    1   P 5 ARG C 989  LEU C 990  0
SHEET    2   P 5 GLU C 970  ALA C 973  1  N  ALA C 973   O  ARG C 989
SHEET    3   P 5 ARG C 944  SER C 948  1  N  ALA C 945   O  ASP C 972
SHEET    4   P 5 TYR C1012  ASN C1015  1  O  ILE C1014   N  LEU C 946
SHEET    5   P 5 TYR C1040  ASP C1041  1  O  ASP C1041   N  ILE C1013
SHEET    1   Q 8 SER D   4  LEU D   9  0
SHEET    2   Q 8 GLN D  14  ALA D  19 -1  O  GLY D  17   N  ALA D   5
SHEET    3   Q 8 VAL D 108  ALA D 111 -1  O  ALA D 111   N  ARG D  18
SHEET    4   Q 8 GLY D  79  VAL D  81  1  N  LEU D  80   O  ILE D 110
SHEET    5   Q 8 GLN D  51  LEU D  55  1  N  VAL D  53   O  VAL D  81
SHEET    6   Q 8 GLY D  24  ASN D  33  1  N  GLU D  29   O  ILE D  52
SHEET    7   Q 8 GLN D 128  ALA D 134 -1  O  ALA D 134   N  GLY D  24
SHEET    8   Q 8 SER D   4  LEU D   9 -1  N  LEU D   6   O  ILE D 133
SHEET    1   R10 TYR D 168  TRP D 170  0
SHEET    2   R10 CYS D 214  VAL D 219 -1  O  ILE D 218   N  TYR D 168
SHEET    3   R10 PHE D 192  TYR D 197  1  N  PHE D 192   O  ARG D 215
SHEET    4   R10 GLY D 235  LEU D 238  1  O  PHE D 237   N  VAL D 195
SHEET    5   R10 VAL D 265  ILE D 268  1  O  PHE D 266   N  ILE D 236
SHEET    6   R10 ALA D 347  PHE D 350  1  O  PHE D 350   N  GLY D 267
SHEET    7   R10 LEU D 337  ARG D 342 -1  N  ILE D 340   O  SER D 349
SHEET    8   R10 LEU D 325  SER D 331 -1  N  ARG D 326   O  HIS D 341
SHEET    9   R10 THR D 283  ASP D 299 -1  N  LYS D 298   O  LYS D 330
SHEET   10   R10 VAL D 304  VAL D 316 -1  O  ALA D 315   N  VAL D 284
SHEET    1   S 5 ALA E  63  TYR E  65  0
SHEET    2   S 5 ARG E  43  VAL E  47  1  N  ASN E  46   O  TYR E  65
SHEET    3   S 5 SER E   9  LEU E  13  1  N  ILE E  12   O  ILE E  45
SHEET    4   S 5 ALA E  85  LEU E  87  1  O  LEU E  87   N  LEU E  11
SHEET    5   S 5 THR E 114  MET E 115  1  O  THR E 114   N  VAL E  86
SHEET    1   T 4 SER E 146  ALA E 149  0
SHEET    2   T 4 LEU E 204  GLU E 208 -1  O  ILE E 206   N  GLY E 147
SHEET    3   T 4 CYS E 166  PRO E 170 -1  N  ARG E 169   O  LEU E 205
SHEET    4   T 4 GLY E 180  ALA E 182 -1  O  GLY E 180   N  ILE E 168
SHEET    1   U 7 LEU E 295  ASN E 301  0
SHEET    2   U 7 GLY E 280  VAL E 288 -1  N  GLN E 285   O  ILE E 298
SHEET    3   U 7 LYS E 214  ARG E 222 -1  N  VAL E 220   O  SER E 282
SHEET    4   U 7 CYS E 228  ASN E 236 -1  O  ILE E 229   N  VAL E 221
SHEET    5   U 7 THR E 249  ALA E 251 -1  O  VAL E 250   N  GLU E 235
SHEET    6   U 7 VAL E 355  ARG E 361 -1  O  LYS E 358   N  THR E 249
SHEET    7   U 7 GLY E 382  GLY E 388 -1  O  GLY E 388   N  VAL E 355
SHEET    1   V 6 VAL E 525  ARG E 528  0
SHEET    2   V 6 TYR E 542  THR E 546 -1  O  THR E 546   N  VAL E 525
SHEET    3   V 6 ARG E 615  PHE E 618  1  O  PHE E 618   N  MET E 543
SHEET    4   V 6 GLU E 595  ASN E 600  1  N  MET E 598   O  ARG E 615
SHEET    5   V 6 LYS E 561  LEU E 565  1  N  VAL E 564   O  ILE E 597
SHEET    6   V 6 GLY E 637  ILE E 639  1  O  ILE E 639   N  MET E 563
SHEET    1   W 4 ASN E 692  THR E 694  0
SHEET    2   W 4 LEU E 751  HIS E 754 -1  O  LEU E 752   N  ALA E 693
SHEET    3   W 4 LEU E 712  ARG E 715 -1  N  VAL E 713   O  ASP E 753
SHEET    4   W 4 GLU E 726  VAL E 728 -1  O  VAL E 728   N  LEU E 712
SHEET    1   X 7 GLU E 836  ASN E 843  0
SHEET    2   X 7 GLY E 824  LYS E 833 -1  N  ALA E 831   O  TYR E 838
SHEET    3   X 7 VAL E 760  CYS E 768 -1  N  VAL E 764   O  VAL E 828
SHEET    4   X 7 VAL E 773  GLN E 784 -1  O  LEU E 774   N  ILE E 767
SHEET    5   X 7 CYS E 794  LEU E 796 -1  O  SER E 795   N  GLU E 780
SHEET    6   X 7 TYR E 888  VAL E 894 -1  O  SER E 889   N  LEU E 796
SHEET    7   X 7 GLY E 915  GLY E 921 -1  O  GLY E 921   N  TYR E 888
SHEET    1   Y 5 ARG E 989  VAL E 991  0
SHEET    2   Y 5 GLU E 970  THR E 974  1  N  ALA E 973   O  VAL E 991
SHEET    3   Y 5 ARG E 944  SER E 948  1  N  ALA E 945   O  GLU E 970
SHEET    4   Y 5 TYR E1012  ASN E1015  1  O  ILE E1014   N  SER E 948
SHEET    5   Y 5 TYR E1040  ASP E1041  1  O  ASP E1041   N  ILE E1013
SHEET    1   Z 8 SER F   4  LEU F   9  0
SHEET    2   Z 8 GLN F  14  ALA F  19 -1  O  PHE F  15   N  LEU F   7
SHEET    3   Z 8 VAL F 108  ALA F 111 -1  O  ALA F 111   N  ARG F  18
SHEET    4   Z 8 GLY F  79  VAL F  81  1  N  LEU F  80   O  ILE F 110
SHEET    5   Z 8 GLN F  51  LEU F  55  1  N  VAL F  53   O  VAL F  81
SHEET    6   Z 8 GLY F  24  ASN F  33  1  N  VAL F  31   O  ILE F  52
SHEET    7   Z 8 GLN F 128  ALA F 134 -1  O  ALA F 134   N  GLY F  24
SHEET    8   Z 8 SER F   4  LEU F   9 -1  N  VAL F   8   O  CYS F 131
SHEET    1  AA10 TYR F 168  TRP F 170  0
SHEET    2  AA10 CYS F 214  PRO F 220 -1  O  LEU F 216   N  TRP F 170
SHEET    3  AA10 PHE F 192  ASP F 198  1  N  PHE F 192   O  ARG F 215
SHEET    4  AA10 GLY F 235  LEU F 238  1  O  PHE F 237   N  VAL F 195
SHEET    5  AA10 VAL F 265  ILE F 268  1  O  PHE F 266   N  LEU F 238
SHEET    6  AA10 ALA F 347  PHE F 350  1  O  PHE F 350   N  GLY F 267
SHEET    7  AA10 LEU F 337  ARG F 342 -1  N  ILE F 340   O  SER F 349
SHEET    8  AA10 LEU F 325  SER F 331 -1  N  ARG F 326   O  HIS F 341
SHEET    9  AA10 THR F 283  ASP F 299 -1  N  LYS F 298   O  LYS F 330
SHEET   10  AA10 VAL F 304  VAL F 316 -1  O  MET F 306   N  VAL F 297
SHEET    1  AB 5 ALA G  63  TYR G  65  0
SHEET    2  AB 5 ARG G  43  VAL G  47  1  N  ASN G  46   O  TYR G  65
SHEET    3  AB 5 SER G   9  LEU G  13  1  N  ILE G  10   O  ARG G  43
SHEET    4  AB 5 ALA G  85  LEU G  87  1  O  ALA G  85   N  LEU G  11
SHEET    5  AB 5 THR G 114  MET G 115  1  O  THR G 114   N  VAL G  86
SHEET    1  AC 4 SER G 146  ALA G 149  0
SHEET    2  AC 4 LEU G 204  GLU G 208 -1  O  LEU G 204   N  ALA G 149
SHEET    3  AC 4 CYS G 166  PRO G 170 -1  N  ARG G 169   O  LEU G 205
SHEET    4  AC 4 GLY G 180  ALA G 182 -1  O  GLY G 180   N  ILE G 168
SHEET    1  AD 7 LEU G 295  ASN G 301  0
SHEET    2  AD 7 GLY G 280  VAL G 288 -1  N  GLN G 285   O  ILE G 298
SHEET    3  AD 7 LYS G 214  ARG G 222 -1  N  VAL G 220   O  SER G 282
SHEET    4  AD 7 CYS G 228  ASN G 236 -1  O  CYS G 232   N  GLU G 219
SHEET    5  AD 7 THR G 249  ALA G 251 -1  O  VAL G 250   N  GLU G 235
SHEET    6  AD 7 VAL G 355  ARG G 361 -1  O  LYS G 358   N  THR G 249
SHEET    7  AD 7 GLY G 382  GLY G 388 -1  O  GLY G 388   N  VAL G 355
SHEET    1  AE 7 VAL G 525  ARG G 528  0
SHEET    2  AE 7 ALA G 541  THR G 546 -1  O  THR G 546   N  VAL G 525
SHEET    3  AE 7 ARG G 615  PHE G 618  1  O  LEU G 616   N  MET G 543
SHEET    4  AE 7 GLU G 595  ASN G 600  1  N  MET G 598   O  TYR G 617
SHEET    5  AE 7 LYS G 561  LEU G 565  1  N  VAL G 564   O  VAL G 599
SHEET    6  AE 7 GLY G 637  ILE G 639  1  O  GLY G 637   N  MET G 563
SHEET    7  AE 7 VAL G 661  ILE G 662  1  O  ILE G 662   N  VAL G 638
SHEET    1  AF 4 ASN G 692  THR G 694  0
SHEET    2  AF 4 LEU G 751  HIS G 754 -1  O  LEU G 752   N  ALA G 693
SHEET    3  AF 4 LEU G 712  ARG G 715 -1  N  VAL G 713   O  ASP G 753
SHEET    4  AF 4 GLU G 726  VAL G 728 -1  O  VAL G 728   N  LEU G 712
SHEET    1  AG 7 GLU G 836  ASN G 843  0
SHEET    2  AG 7 GLY G 824  LYS G 833 -1  N  ALA G 831   O  TYR G 838
SHEET    3  AG 7 VAL G 760  CYS G 768 -1  N  VAL G 760   O  VAL G 832
SHEET    4  AG 7 VAL G 773  HIS G 781 -1  O  MET G 779   N  ASP G 763
SHEET    5  AG 7 CYS G 794  LEU G 796 -1  O  SER G 795   N  GLU G 780
SHEET    6  AG 7 TYR G 888  VAL G 894 -1  O  SER G 889   N  LEU G 796
SHEET    7  AG 7 GLY G 915  GLY G 921 -1  O  GLY G 919   N  VAL G 890
SHEET    1  AH 5 ARG G 989  VAL G 991  0
SHEET    2  AH 5 PHE G 969  THR G 974  1  N  ALA G 973   O  ARG G 989
SHEET    3  AH 5 GLY G 943  SER G 948  1  N  ALA G 945   O  ASP G 972
SHEET    4  AH 5 TYR G1012  ASN G1015  1  O  ILE G1014   N  LEU G 946
SHEET    5  AH 5 HIS G1039  ASP G1041  1  O  ASP G1041   N  ILE G1013
SHEET    1  AI 8 SER H   4  LEU H   9  0
SHEET    2  AI 8 GLN H  14  ALA H  19 -1  O  PHE H  15   N  LEU H   7
SHEET    3  AI 8 VAL H 108  ALA H 111 -1  O  ALA H 111   N  ARG H  18
SHEET    4  AI 8 GLY H  79  VAL H  81  1  N  LEU H  80   O  ILE H 110
SHEET    5  AI 8 GLN H  51  LEU H  55  1  N  VAL H  53   O  VAL H  81
SHEET    6  AI 8 GLY H  24  ASN H  33  1  N  GLU H  29   O  ILE H  52
SHEET    7  AI 8 GLN H 128  ALA H 134 -1  O  ALA H 134   N  GLY H  24
SHEET    8  AI 8 SER H   4  LEU H   9 -1  N  VAL H   8   O  CYS H 131
SHEET    1  AJ10 TYR H 168  TRP H 170  0
SHEET    2  AJ10 CYS H 214  VAL H 219 -1  O  ILE H 218   N  TYR H 168
SHEET    3  AJ10 PHE H 192  TYR H 197  1  N  PHE H 192   O  ARG H 215
SHEET    4  AJ10 GLY H 235  LEU H 238  1  O  PHE H 237   N  VAL H 195
SHEET    5  AJ10 VAL H 265  ILE H 268  1  O  PHE H 266   N  ILE H 236
SHEET    6  AJ10 ALA H 347  PHE H 350  1  O  PHE H 350   N  GLY H 267
SHEET    7  AJ10 LEU H 337  ARG H 342 -1  N  ILE H 340   O  SER H 349
SHEET    8  AJ10 LEU H 325  SER H 331 -1  N  ARG H 326   O  HIS H 341
SHEET    9  AJ10 THR H 283  LYS H 298 -1  N  LYS H 298   O  LYS H 330
SHEET   10  AJ10 VAL H 305  VAL H 316 -1  O  THR H 308   N  HIS H 295
LINK         O   GLY A 112                 K     K A4013     1555   1555  2.60
LINK         OG1 THR A 114                 K     K A4013     1555   1555  2.83
LINK         OE1 GLU A 127                 K     K A4005     1555   1555  2.75
LINK         OE2 GLU A 215                 K     K A4004     1555   1555  2.78
LINK         O   ASP A 238                 K     K A4004     1555   1555  2.75
LINK         O   ALA A 239                 K     K A4004     1555   1555  2.79
LINK         O   ILE A 242                 K     K A4004     1555   1555  2.56
LINK         OG  SER A 247                 K     K A4004     1555   1555  2.64
LINK         OE1 GLN A 285                MN    MN A4003     1555   1555  1.89
LINK         CD  GLU A 299                MN    MN A4002     1555   1555  2.57
LINK         OE1 GLU A 299                MN    MN A4002     1555   1555  2.41
LINK         OE1 GLU A 299                 K     K A4005     1555   1555  2.84
LINK         OE2 GLU A 299                MN    MN A4002     1555   1555  2.21
LINK         OE2 GLU A 299                MN    MN A4003     1555   1555  2.22
LINK         O   MET A 300                 K     K A4005     1555   1555  2.53
LINK         OD1 ASN A 301                MN    MN A4002     1555   1555  2.05
LINK         OE2 GLU A 761                 K     K A4010     1555   1555  2.73
LINK         ND1 HIS A 781                 K     K A4010     1555   1555  2.68
LINK         O   GLU A 783                 K     K A4010     1555   1555  2.74
LINK         O   GLN A 784                 K     K A4010     1555   1555  2.84
LINK         O   VAL A 787                 K     K A4010     1555   1555  2.56
LINK         OG  SER A 792                 K     K A4010     1555   1555  2.67
LINK         OE1 GLN A 829                MN    MN A4008     1555   1555  2.21
LINK         OE1 GLU A 841                 K     K A4009     1555   1555  2.52
LINK         OE2 GLU A 841                MN    MN A4008     1555   1555  2.20
LINK         OE2 GLU A 841                 K     K A4009     1555   1555  2.82
LINK         O   HIS B  16                 K     K B4014     1555   1555  2.77
LINK         O   ASP B 112                 K     K B4014     1555   1555  2.74
LINK         O   ASP C  84                 K     K C4033     1555   1555  2.74
LINK         OG1 THR C 114                 K     K C4033     1555   1555  2.87
LINK         OE1 GLU C 127                 K     K C4025     1555   1555  2.60
LINK         OG1 THR C 143                 K     K C4034     1555   1555  2.76
LINK         OE2 GLU C 215                 K     K C4024     1555   1555  2.67
LINK         OD1 ASN C 236                 K     K C4024     1555   1555  2.88
LINK         O   ASP C 238                 K     K C4024     1555   1555  2.68
LINK         O   ALA C 239                 K     K C4024     1555   1555  2.91
LINK         O   ILE C 242                 K     K C4024     1555   1555  2.69
LINK         OG  SER C 247                 K     K C4024     1555   1555  2.72
LINK         OE1 GLN C 285                MN    MN C4023     1555   1555  2.25
LINK         CD  GLU C 299                MN    MN C4022     1555   1555  2.57
LINK         OE1 GLU C 299                 K     K C4025     1555   1555  2.74
LINK         OE1 GLU C 299                MN    MN C4022     1555   1555  2.31
LINK         OE2 GLU C 299                MN    MN C4023     1555   1555  2.27
LINK         OE2 GLU C 299                MN    MN C4022     1555   1555  2.21
LINK         O   MET C 300                 K     K C4025     1555   1555  2.78
LINK         OD1 ASN C 301                MN    MN C4022     1555   1555  2.09
LINK         OE2 GLU C 761                 K     K C4030     1555   1555  2.41
LINK         ND1 HIS C 781                 K     K C4030     1555   1555  2.80
LINK         O   GLU C 783                 K     K C4030     1555   1555  2.76
LINK         O   VAL C 787                 K     K C4030     1555   1555  2.50
LINK         OG  SER C 792                 K     K C4030     1555   1555  2.76
LINK         OE1 GLN C 829                MN    MN C4028     1555   1555  2.19
LINK         OE1 GLU C 841                 K     K C4029     1555   1555  2.64
LINK         OE2 GLU C 841                MN    MN C4028     1555   1555  2.16
LINK         O   HIS D  16                 K     K D4035     1555   1555  2.80
LINK         O   ASP D 112                 K     K D4035     1555   1555  2.70
LINK         O   GLY E 112                 K     K E4056     1555   1555  2.91
LINK         OG1 THR E 114                 K     K E4056     1555   1555  2.86
LINK         OE1 GLU E 127                 K     K E4048     1555   1555  2.75
LINK         O   THR E 143                 K     K E4057     1555   1555  2.71
LINK         OG1 THR E 143                 K     K E4057     1555   1555  2.68
LINK         OE2 GLU E 215                 K     K E4047     1555   1555  2.42
LINK         OD1 ASN E 236                 K     K E4047     1555   1555  2.61
LINK         O   ASP E 238                 K     K E4047     1555   1555  2.69
LINK         O   ALA E 239                 K     K E4047     1555   1555  2.89
LINK         O   ILE E 242                 K     K E4047     1555   1555  2.60
LINK         OG  SER E 247                 K     K E4047     1555   1555  2.71
LINK         OE1 GLN E 285                MN    MN E4046     1555   1555  2.07
LINK         CD  GLU E 299                MN    MN E4045     1555   1555  2.55
LINK         OE1 GLU E 299                MN    MN E4045     1555   1555  2.23
LINK         OE1 GLU E 299                 K     K E4048     1555   1555  2.74
LINK         OE2 GLU E 299                MN    MN E4045     1555   1555  2.27
LINK         OE2 GLU E 299                MN    MN E4046     1555   1555  2.19
LINK         O   MET E 300                 K     K E4048     1555   1555  2.77
LINK         OD1 ASN E 301                MN    MN E4045     1555   1555  2.14
LINK         OE2 GLU E 761                 K     K E4053     1555   1555  2.54
LINK         ND1 HIS E 781                 K     K E4053     1555   1555  2.63
LINK         O   GLU E 783                 K     K E4053     1555   1555  2.88
LINK         O   VAL E 787                 K     K E4053     1555   1555  2.47
LINK         OG  SER E 792                 K     K E4053     1555   1555  2.69
LINK         OE1 GLN E 829                MN    MN E4051     1555   1555  2.30
LINK         OE1 GLU E 841                 K     K E4052     1555   1555  2.70
LINK         OE2 GLU E 841                MN    MN E4051     1555   1555  1.98
LINK         O   HIS F  16                 K     K F4058     1555   1555  2.83
LINK         O   ASP F 112                 K     K F4058     1555   1555  2.79
LINK         O   ASP G  84                 K     K G4078     1555   1555  2.93
LINK         O   GLY G 112                 K     K G4078     1555   1555  2.49
LINK         OG1 THR G 114                 K     K G4078     1555   1555  2.77
LINK         OG1 THR G 143                 K     K G4079     1555   1555  2.70
LINK         O   ALA G 144                 K     K G4079     1555   1555  2.92
LINK         OE2 GLU G 215                 K     K G4069     1555   1555  2.37
LINK         O   ASP G 238                 K     K G4069     1555   1555  2.75
LINK         O   ALA G 239                 K     K G4069     1555   1555  2.68
LINK         O   ILE G 242                 K     K G4069     1555   1555  2.57
LINK         OG  SER G 247                 K     K G4069     1555   1555  2.79
LINK         OE1 GLN G 285                MN    MN G4068     1555   1555  2.03
LINK         CD  GLU G 299                MN    MN G4067     1555   1555  2.57
LINK         OE1 GLU G 299                 K     K G4070     1555   1555  2.63
LINK         OE1 GLU G 299                MN    MN G4067     1555   1555  2.28
LINK         OE2 GLU G 299                MN    MN G4068     1555   1555  2.14
LINK         OE2 GLU G 299                MN    MN G4067     1555   1555  2.29
LINK         O   MET G 300                 K     K G4070     1555   1555  2.68
LINK         OD1 ASN G 301                MN    MN G4067     1555   1555  2.12
LINK         OE2 GLU G 761                 K     K G4075     1555   1555  2.36
LINK         ND1 HIS G 781                 K     K G4075     1555   1555  2.68
LINK         O   VAL G 787                 K     K G4075     1555   1555  2.54
LINK         OG  SER G 792                 K     K G4075     1555   1555  2.58
LINK         OE1 GLN G 829                MN    MN G4073     1555   1555  2.03
LINK         OE1 GLU G 841                 K     K G4074     1555   1555  2.56
LINK         OE2 GLU G 841                MN    MN G4073     1555   1555  1.89
LINK        MN    MN A4002                 O   HOH A4111     1555   1555  2.16
LINK        MN    MN A4002                 O3B ADP A4001     1555   1555  1.97
LINK        MN    MN A4002                 O1  PO4 A4006     1555   1555  2.03
LINK        MN    MN A4003                 O1B ADP A4001     1555   1555  2.02
LINK        MN    MN A4003                 O3  PO4 A4006     1555   1555  2.14
LINK        MN    MN A4003                 O1A ADP A4001     1555   1555  2.10
LINK        MN    MN A4003                 O   HOH A4537     1555   1555  2.17
LINK         K     K A4005                 O   HOH A4112     1555   1555  2.75
LINK         K     K A4005                 O   HOH A4113     1555   1555  2.90
LINK        MN    MN A4008                 O2A ADP A4007     1555   1555  1.89
LINK        MN    MN A4008                 O   HOH A4590     1555   1555  2.35
LINK        MN    MN A4008                 O3B ADP A4007     1555   1555  2.23
LINK        MN    MN A4008                 O   HOH A4638     1555   1555  2.30
LINK         K     K A4009                 O2B ADP A4007     1555   1555  2.47
LINK         K     K A4013                 O   HOH A4680     1555   1555  2.86
LINK         K     K A4013                 O   HOH A4679     1555   1555  2.93
LINK         K     K A4013                 O   HOH A4021     1555   1555  2.73
LINK         K     K B4014                 O   HOH B4089     1555   1555  2.84
LINK         K     K B4014                 O   HOH A4363     1555   1555  2.84
LINK         K     K B4014                 O   HOH B4042     1555   1555  2.59
LINK        MN    MN C4022                 O3B ADP C4021     1555   1555  1.91
LINK        MN    MN C4022                 O1  PO4 C4026     1555   1555  2.07
LINK        MN    MN C4022                 O   HOH C4133     1555   1555  2.14
LINK        MN    MN C4023                 O1A ADP C4021     1555   1555  2.16
LINK        MN    MN C4023                 O   HOH C4628     1555   1555  2.11
LINK        MN    MN C4023                 O3  PO4 C4026     1555   1555  2.09
LINK        MN    MN C4023                 O1B ADP C4021     1555   1555  2.26
LINK         K     K C4025                 O   HOH C4135     1555   1555  2.84
LINK        MN    MN C4028                 O3B ADP C4027     1555   1555  1.99
LINK        MN    MN C4028                 O   HOH C4630     1555   1555  2.18
LINK        MN    MN C4028                 O   HOH C4631     1555   1555  2.20
LINK        MN    MN C4028                 O2A ADP C4027     1555   1555  2.24
LINK         K     K C4029                 O2B ADP C4027     1555   1555  2.50
LINK         K     K C4029                 O   HOH C4440     1555   1555  1.85
LINK         K     K C4034                 O   HOH C4143     1555   1555  2.36
LINK         K     K D4035                 O   HOH D1022     1555   1555  2.78
LINK         K     K D4035                 O   HOH C4372     1555   1555  2.88
LINK        MN    MN E4045                 O3B ADP E4044     1555   1555  1.95
LINK        MN    MN E4045                 O   HOH E1271     1555   1555  2.15
LINK        MN    MN E4045                 O1  PO4 E4049     1555   1555  1.99
LINK        MN    MN E4046                 O   HOH E2516     1555   1555  2.03
LINK        MN    MN E4046                 O1B ADP E4044     1555   1555  2.05
LINK        MN    MN E4046                 O3  PO4 E4049     1555   1555  2.24
LINK        MN    MN E4046                 O1A ADP E4044     1555   1555  2.03
LINK        MN    MN E4051                 O2A ADP E4050     1555   1555  1.91
LINK        MN    MN E4051                 O   HOH E2519     1555   1555  2.36
LINK        MN    MN E4051                 O3B ADP E4050     1555   1555  2.05
LINK        MN    MN E4051                 O   HOH E2518     1555   1555  2.34
LINK         K     K E4052                 O   HOH E1603     1555   1555  2.82
LINK         K     K E4052                 O2B ADP E4050     1555   1555  2.38
LINK         K     K E4052                 O   HOH E1604     1555   1555  1.76
LINK         K     K E4057                 O   HOH E1282     1555   1555  2.90
LINK         K     K F4058                 O   HOH E2780     1555   1555  2.78
LINK         K     K F4058                 O   HOH E1558     1555   1555  2.79
LINK         K     K F4058                 O   HOH E1526     1555   1555  2.66
LINK        MN    MN G4067                 O   HOH G4181     1555   1555  2.29
LINK        MN    MN G4067                 O1  PO4 G4071     1555   1555  2.00
LINK        MN    MN G4067                 O3B ADP G4066     1555   1555  2.15
LINK        MN    MN G4068                 O3  PO4 G4071     1555   1555  2.06
LINK        MN    MN G4068                 O   HOH G4540     1555   1555  2.13
LINK        MN    MN G4068                 O1A ADP G4066     1555   1555  2.05
LINK        MN    MN G4068                 O1B ADP G4066     1555   1555  2.18
LINK        MN    MN G4073                 O   HOH G4542     1555   1555  2.32
LINK        MN    MN G4073                 O3B ADP G4072     1555   1555  2.21
LINK        MN    MN G4073                 O   HOH G4541     1555   1555  2.29
LINK        MN    MN G4073                 O2A ADP G4072     1555   1555  1.93
LINK         K     K G4074                 O   HOH G4464     1555   1555  2.32
LINK         K     K G4074                 O2B ADP G4072     1555   1555  2.72
LINK         K     K G4079                 O   HOH G4190     1555   1555  2.40
LINK         K     K A4004                 OD1 ASN A 236     1555   1555  2.94
LINK         K     K A4005                 O   ALA A 126     1555   1555  3.25
LINK         K     K A4005                 OD1 ASN A 301     1555   1555  3.23
LINK         K     K A4005                 O   HOH A4111     1555   1555  2.93
LINK         K     K A4009                 O3B ADP A4007     1555   1555  3.11
LINK         K     K A4009                 O   HOH A4433     1555   1555  3.51
LINK         K     K A4009                 OD1 ASN A 843     1555   1555  3.11
LINK         K     K A4013                 O   ASP A  84     1555   1555  3.04
LINK         K     K A4013                 N   THR A 114     1555   1555  3.72
LINK         K     K B4014                 O   HOH A4364     1555   1555  3.19
LINK         K     K C4025                 O   ALA C 126     1555   1555  3.44
LINK         K     K C4025                MN    MN C4022     1555   1555  3.71
LINK         K     K C4025                 O   HOH C4133     1555   1555  3.02
LINK         K     K C4025                 O   HOH C4134     1555   1555  3.29
LINK         K     K C4025                 OD1 ASN C 301     1555   1555  3.21
LINK         K     K C4029                 OE2 GLU C 841     1555   1555  3.59
LINK         K     K C4029                 O   HOH C4441     1555   1555  3.67
LINK         K     K C4030                 O   GLN C 784     1555   1555  3.07
LINK         K     K C4033                 O   GLY C 112     1555   1555  3.13
LINK         K     K C4033                 O   HOH C4043     1555   1555  3.64
LINK         K     K C4034                 O   ALA C 144     1555   1555  2.97
LINK         K     K C4034                 O   HOH C4144     1555   1555  3.13
LINK         K     K C4034                 O   HOH C4145     1555   1555  3.10
LINK         K     K C4034                 O   THR C 143     1555   1555  2.96
LINK         K     K C4034                 O   HOH C4148     1555   1555  3.67
LINK         K     K D4035                 O   HOH C4373     1555   1555  3.44
LINK         K     K D4035                 O   HOH D2902     1555   1555  3.15
LINK         K     K E4048                 O   HOH E1271     1555   1555  2.96
LINK         K     K E4048                 O   HOH E1272     1555   1555  3.18
LINK         K     K E4048                 O   ALA E 126     1555   1555  3.21
LINK         K     K E4048                 O   HOH E1273     1555   1555  3.07
LINK         K     K E4048                 OD1 ASN E 301     1555   1555  3.42
LINK         K     K E4052                 OE2 GLU E 841     1555   1555  3.48
LINK         K     K E4052                 OD1 ASN E 843     1555   1555  3.55
LINK         K     K E4052                 O   HOH E1605     1555   1555  3.60
LINK         K     K E4053                 O   GLN E 784     1555   1555  2.93
LINK         K     K E4056                 O   ASP E  84     1555   1555  2.98
LINK         K     K E4056                 O   HOH E1176     1555   1555  3.09
LINK         K     K E4056                 O   HOH E2520     1555   1555  3.09
LINK         K     K E4057                 O   HOH E1285     1555   1555  3.66
LINK         K     K E4057                 O   ALA E 144     1555   1555  2.96
LINK         K     K E4057                 O   HOH E1281     1555   1555  3.59
LINK         K     K E4057                 O   HOH E1280     1555   1555  3.10
LINK         K     K F4058                 O   HOH E1527     1555   1555  3.57
LINK         K     K F4058                 O   HOH E2778     1555   1555  3.49
LINK         K     K G4069                 OD1 ASN G 236     1555   1555  3.10
LINK         K     K G4070                 O   HOH G4182     1555   1555  3.70
LINK         K     K G4070                 O   HOH G4183     1555   1555  3.06
LINK         K     K G4070                 O   ALA G 126     1555   1555  3.04
LINK         K     K G4070                 O   HOH G4181     1555   1555  3.24
LINK         K     K G4070                 OD1 ASN G 301     1555   1555  3.37
LINK         K     K G4070                 OE1 GLU G 127     1555   1555  3.09
LINK         K     K G4074                 OD1 ASN G 843     1555   1555  3.44
LINK         K     K G4074                 OE2 GLU G 841     1555   1555  3.59
LINK         K     K G4074                 O   HOH G4465     1555   1555  3.41
LINK         K     K G4075                 O   GLN G 784     1555   1555  2.95
LINK         K     K G4075                 O   GLU G 783     1555   1555  3.14
LINK         K     K G4078                 N   THR G 114     1555   1555  3.67
LINK         K     K G4078                 O   HOH G4089     1555   1555  3.39
LINK         K     K G4079                 O   HOH G4195     1555   1555  3.45
LINK         K     K G4079                 O   HOH G4544     1555   1555  3.21
LINK         K     K G4079                 O   HOH G4192     1555   1555  3.04
LINK         K     K G4079                 O   HOH G4191     1555   1555  3.11
LINK         K     K G4079                 O   THR G 143     1555   1555  3.08
CISPEP   1 PHE A  164    PRO A  165          0        -2.75
CISPEP   2 ALA A  251    PRO A  252          0         0.59
CISPEP   3 TYR A  710    PRO A  711          0         0.45
CISPEP   4 LEU A  796    PRO A  797          0         2.62
CISPEP   5 ARG A  998    PRO A  999          0        -3.03
CISPEP   6 SER B  357    PRO B  358          0         0.32
CISPEP   7 PHE C  164    PRO C  165          0        -1.60
CISPEP   8 ALA C  251    PRO C  252          0         2.10
CISPEP   9 TYR C  710    PRO C  711          0         1.86
CISPEP  10 LEU C  796    PRO C  797          0         3.86
CISPEP  11 ARG C  998    PRO C  999          0        -1.54
CISPEP  12 SER D  357    PRO D  358          0        -0.91
CISPEP  13 PHE E  164    PRO E  165          0        -0.34
CISPEP  14 ALA E  251    PRO E  252          0        -1.98
CISPEP  15 TYR E  710    PRO E  711          0         0.34
CISPEP  16 LEU E  796    PRO E  797          0         4.98
CISPEP  17 ARG E  998    PRO E  999          0        -1.98
CISPEP  18 SER F  357    PRO F  358          0         1.77
CISPEP  19 PHE G  164    PRO G  165          0        -0.99
CISPEP  20 ALA G  251    PRO G  252          0         0.04
CISPEP  21 TYR G  710    PRO G  711          0        -0.70
CISPEP  22 LEU G  796    PRO G  797          0         3.05
CISPEP  23 ARG G  998    PRO G  999          0         3.87
CISPEP  24 SER H  357    PRO H  358          0         4.70
SITE     1 AC1  6 GLU A 299  ASN A 301  ADP A4001   MN A4003
SITE     2 AC1  6 PO4 A4006  HOH A4111
SITE     1 AC2  6 GLN A 285  GLU A 299  ADP A4001   MN A4002
SITE     2 AC2  6 PO4 A4006  HOH A4537
SITE     1 AC3  6 GLU A 215  ASN A 236  ASP A 238  ALA A 239
SITE     2 AC3  6 ILE A 242  SER A 247
SITE     1 AC4  8 ALA A 126  GLU A 127  GLU A 299  MET A 300
SITE     2 AC4  8 ASN A 301  HOH A4111  HOH A4112  HOH A4113
SITE     1 AC5  5 GLN A 829  GLU A 841  ADP A4007  HOH A4590
SITE     2 AC5  5 HOH A4638
SITE     1 AC6  4 GLU A 841  ASN A 843  ADP A4007  HOH A4434
SITE     1 AC7  6 GLU A 761  HIS A 781  GLU A 783  GLN A 784
SITE     2 AC7  6 VAL A 787  SER A 792
SITE     1 AC8  6 ASP A  84  GLY A 112  THR A 114  HOH A4021
SITE     2 AC8  6 HOH A4679  HOH A4680
SITE     1 AC9  5 HOH A4363  HIS B  16  ASP B 112  HOH B4042
SITE     2 AC9  5 HOH B4089
SITE     1 BC1  4 THR A 173  MET A 174  HOH A4048  HOH A4093
SITE     1 BC2  3 ASN A 289  ASN A 292  ARG A 294
SITE     1 BC3  6 ALA A 370  ASN A 371  PHE A 900  PRO A 901
SITE     2 BC3  6 GLY A 902  HOH A4167
SITE     1 BC4  2 LYS A 475  ASN A 485
SITE     1 BC5  4 HOH A4363  ILE B 113  ASP B 114  HOH B4041
SITE     1 BC6  3 PHE A 578  ALA A 847  ARG A 848
SITE     1 BC7  6 GLU C 299  ASN C 301  ADP C4021   MN C4023
SITE     2 BC7  6 PO4 C4026  HOH C4133
SITE     1 BC8  6 GLN C 285  GLU C 299  ADP C4021   MN C4022
SITE     2 BC8  6 PO4 C4026  HOH C4628
SITE     1 BC9  6 GLU C 215  ASN C 236  ASP C 238  ALA C 239
SITE     2 BC9  6 ILE C 242  SER C 247
SITE     1 CC1  7 ALA C 126  GLU C 127  GLU C 299  MET C 300
SITE     2 CC1  7 ASN C 301  HOH C4133  HOH C4135
SITE     1 CC2  5 GLN C 829  GLU C 841  ADP C4027  HOH C4630
SITE     2 CC2  5 HOH C4631
SITE     1 CC3  3 GLU C 841  ADP C4027  HOH C4440
SITE     1 CC4  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784
SITE     2 CC4  6 VAL C 787  SER C 792
SITE     1 CC5  3 ASP C  84  GLY C 112  THR C 114
SITE     1 CC6  4 THR C 143  ALA C 144  HOH C4143  HOH C4145
SITE     1 CC7  4 HOH C4372  HIS D  16  ASP D 112  HOH D1022
SITE     1 CC8  4 MET C 174  NET C4032  HOH C4070  HOH C4115
SITE     1 CC9  1 TRP C  71
SITE     1 DC1  3 ASN C 289  ASN C 292  ARG C 294
SITE     1 DC2  5 ALA C 370  ASN C 371  PHE C 900  PRO C 901
SITE     2 DC2  5 GLY C 902
SITE     1 DC3  3 LYS C 475  ASN C 485  HOH C4567
SITE     1 DC4  4 GLU C 549  ILE D 113  ASP D 114  HOH D1021
SITE     1 DC5  2 ALA C 847  ARG C 848
SITE     1 DC6  3 SER D 169  TRP D 170  THR D 171
SITE     1 DC7  6 GLU E 299  ASN E 301  HOH E1271  ADP E4044
SITE     2 DC7  6  MN E4046  PO4 E4049
SITE     1 DC8  7 HIS E 243  GLN E 285  GLU E 299  HOH E2516
SITE     2 DC8  7 ADP E4044   MN E4045  PO4 E4049
SITE     1 DC9  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239
SITE     2 DC9  6 ILE E 242  SER E 247
SITE     1 EC1  7 ALA E 126  GLU E 127  GLU E 299  MET E 300
SITE     2 EC1  7 ASN E 301  HOH E1271  HOH E1273
SITE     1 EC2  5 GLN E 829  GLU E 841  HOH E2518  HOH E2519
SITE     2 EC2  5 ADP E4050
SITE     1 EC3  5 GLU E 841  ASN E 843  HOH E1603  HOH E1604
SITE     2 EC3  5 ADP E4050
SITE     1 EC4  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784
SITE     2 EC4  6 VAL E 787  SER E 792
SITE     1 EC5  5 ASP E  84  GLY E 112  THR E 114  HOH E1176
SITE     2 EC5  5 HOH E2520
SITE     1 EC6  4 THR E 143  ALA E 144  HOH E1280  HOH E1282
SITE     1 EC7  5 HOH E1526  HOH E1558  HOH E2780  HIS F  16
SITE     2 EC7  5 ASP F 112
SITE     1 EC8  5 GLN E  93  THR E 173  MET E 174  HOH E1203
SITE     2 EC8  5 HOH E1252
SITE     1 EC9  1 TRP E  71
SITE     1 FC1  3 ASN E 289  ASN E 292  ARG E 294
SITE     1 FC2  5 ALA E 370  ASN E 371  PHE E 900  PRO E 901
SITE     2 FC2  5 GLY E 902
SITE     1 FC3  3 LYS E 475  ASN E 485  HOH E2644
SITE     1 FC4  2 PHE F  15  ASP F 114
SITE     1 FC5  3 ARG E 845  ALA E 847  ARG E 848
SITE     1 FC6  6 GLU G 299  ASN G 301  ADP G4066   MN G4068
SITE     2 FC6  6 PO4 G4071  HOH G4181
SITE     1 FC7  6 GLN G 285  GLU G 299  ADP G4066   MN G4067
SITE     2 FC7  6 PO4 G4071  HOH G4540
SITE     1 FC8  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239
SITE     2 FC8  6 ILE G 242  SER G 247
SITE     1 FC9  6 ALA G 126  GLU G 127  GLU G 299  MET G 300
SITE     2 FC9  6 ASN G 301  HOH G4183
SITE     1 GC1  5 GLN G 829  GLU G 841  ADP G4072  HOH G4541
SITE     2 GC1  5 HOH G4542
SITE     1 GC2  4 GLU G 841  ASN G 843  ADP G4072  HOH G4464
SITE     1 GC3  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784
SITE     2 GC3  6 VAL G 787  SER G 792
SITE     1 GC4  3 ASP G  84  GLY G 112  THR G 114
SITE     1 GC5  4 THR G 143  ALA G 144  HOH G4190  HOH G4192
SITE     1 GC6  4 GLN G  93  THR G 173  MET G 174  HOH G4161
SITE     1 GC7  1 TRP G  71
SITE     1 GC8  3 ASN G 289  ASN G 292  ARG G 294
SITE     1 GC9  5 ALA G 370  ASN G 371  PHE G 900  PRO G 901
SITE     2 GC9  5 GLY G 902
SITE     1 HC1  2 LYS G 475  ASN G 485
SITE     1 HC2  3 PHE H  15  ASP H 114  HOH H2082
SITE     1 HC3  3 ARG G 845  ALA G 847  ARG G 848
SITE     1 HC4 14 MET A 174  GLY A 175  HIS A 243  GLN A 285
SITE     2 HC4 14 GLU A 299  ASN A 301  ARG A 303  ARG A 306
SITE     3 HC4 14 ADP A4001   MN A4002   MN A4003  HOH A4055
SITE     4 HC4 14 HOH A4214  HOH A4215
SITE     1 HC5 14 MET C 174  GLY C 175  HIS C 243  GLN C 285
SITE     2 HC5 14 GLU C 299  ASN C 301  ARG C 303  ARG C 306
SITE     3 HC5 14 ADP C4021   MN C4022   MN C4023  HOH C4077
SITE     4 HC5 14 HOH C4231  HOH C4232
SITE     1 HC6 14 MET E 174  GLY E 175  HIS E 243  GLN E 285
SITE     2 HC6 14 GLU E 299  ASN E 301  ARG E 303  ARG E 306
SITE     3 HC6 14 HOH E1210  HOH E1371  HOH E1372  ADP E4044
SITE     4 HC6 14  MN E4045   MN E4046
SITE     1 HC7 15 MET G 174  GLY G 175  HIS G 243  GLN G 285
SITE     2 HC7 15 GLU G 299  ASN G 301  ARG G 303  ARG G 306
SITE     3 HC7 15 ADP G4066   MN G4067   MN G4068  HOH G4123
SITE     4 HC7 15 HOH G4275  HOH G4276  HOH G4540
SITE     1 HC8 26 ARG A 129  ILE A 167  ARG A 169  MET A 174
SITE     2 HC8 26 GLY A 175  GLY A 176  ASP A 207  GLU A 208
SITE     3 HC8 26 LEU A 210  ILE A 211  GLU A 215  MET A 240
SITE     4 HC8 26 GLY A 241  ILE A 242  HIS A 243  THR A 244
SITE     5 HC8 26 GLN A 285  GLU A 299  THR A 376   MN A4002
SITE     6 HC8 26  MN A4003  PO4 A4006  HOH A4111  HOH A4144
SITE     7 HC8 26 HOH A4157  HOH A4537
SITE     1 HC9 20 ARG A 715  MET A 725  HIS A 754  PHE A 755
SITE     2 HC9 20 LEU A 756  GLU A 761  ALA A 785  GLY A 786
SITE     3 HC9 20 VAL A 787  HIS A 788  SER A 789  GLN A 829
SITE     4 HC9 20 GLU A 841  PRO A 909   MN A4008    K A4009
SITE     5 HC9 20 HOH A4432  HOH A4434  HOH A4590  HOH A4638
SITE     1 IC1 13 GLU A 783  ASP A 791  ALA A 793  GLU A 892
SITE     2 IC1 13 VAL A 893  LEU A 907  TYR A1040  ASP A1041
SITE     3 IC1 13 THR A1042  HOH A4448  HOH A4468  HOH A4473
SITE     4 IC1 13 HOH A4639
SITE     1 IC2  3 GLN A  22  THR A  94  ASN A 936
SITE     1 IC3 28 ARG C 129  ILE C 167  ARG C 169  THR C 173
SITE     2 IC3 28 MET C 174  GLY C 175  GLY C 176  ASP C 207
SITE     3 IC3 28 GLU C 208  SER C 209  LEU C 210  ILE C 211
SITE     4 IC3 28 GLU C 215  MET C 240  GLY C 241  ILE C 242
SITE     5 IC3 28 HIS C 243  THR C 244  GLN C 285  ILE C 298
SITE     6 IC3 28 GLU C 299  THR C 376   MN C4022   MN C4023
SITE     7 IC3 28 PO4 C4026  HOH C4133  HOH C4175  HOH C4628
SITE     1 IC4 20 PRO C 690  ARG C 715  MET C 725  HIS C 754
SITE     2 IC4 20 PHE C 755  LEU C 756  GLU C 761  ALA C 785
SITE     3 IC4 20 GLY C 786  VAL C 787  HIS C 788  SER C 789
SITE     4 IC4 20 GLN C 829  GLU C 841   MN C4028    K C4029
SITE     5 IC4 20 HOH C4439  HOH C4440  HOH C4630  HOH C4631
SITE     1 IC5 11 GLU C 783  ASP C 791  ALA C 793  GLU C 892
SITE     2 IC5 11 VAL C 893  LEU C 907  TYR C1040  ASP C1041
SITE     3 IC5 11 THR C1042  HOH C4452  HOH C4476
SITE     1 IC6  2 THR C  94   CL C4036
SITE     1 IC7 25 ARG E 129  ILE E 167  ARG E 169  MET E 174
SITE     2 IC7 25 GLY E 175  GLY E 176  GLU E 208  LEU E 210
SITE     3 IC7 25 ILE E 211  GLU E 215  MET E 240  GLY E 241
SITE     4 IC7 25 ILE E 242  HIS E 243  THR E 244  GLN E 285
SITE     5 IC7 25 GLU E 299  THR E 376  HOH E1271  HOH E1303
SITE     6 IC7 25 HOH E1315  HOH E2516   MN E4045   MN E4046
SITE     7 IC7 25 PO4 E4049
SITE     1 IC8 21 ARG E 715  MET E 725  HIS E 754  PHE E 755
SITE     2 IC8 21 LEU E 756  GLU E 761  ALA E 785  GLY E 786
SITE     3 IC8 21 VAL E 787  HIS E 788  SER E 789  GLN E 829
SITE     4 IC8 21 GLU E 841  HOH E1577  HOH E1603  HOH E1604
SITE     5 IC8 21 HOH E2517  HOH E2518  HOH E2519   MN E4051
SITE     6 IC8 21   K E4052
SITE     1 IC9 10 GLU E 783  ASP E 791  GLU E 892  LEU E 907
SITE     2 IC9 10 TYR E1040  ASP E1041  THR E1042  HOH E1617
SITE     3 IC9 10 HOH E1618  HOH E1644
SITE     1 JC1  3 THR E  94  ASN E 936  HOH E1188
SITE     1 JC2 28 ARG G 129  ILE G 167  ARG G 169  THR G 173
SITE     2 JC2 28 MET G 174  GLY G 175  GLY G 176  ASP G 207
SITE     3 JC2 28 GLU G 208  LEU G 210  ILE G 211  GLU G 215
SITE     4 JC2 28 MET G 240  GLY G 241  ILE G 242  HIS G 243
SITE     5 JC2 28 THR G 244  GLN G 285  ILE G 298  GLU G 299
SITE     6 JC2 28 THR G 376   MN G4067   MN G4068  PO4 G4071
SITE     7 JC2 28 HOH G4181  HOH G4211  HOH G4222  HOH G4540
SITE     1 JC3 19 ARG G 715  HIS G 754  PHE G 755  LEU G 756
SITE     2 JC3 19 GLU G 761  ALA G 785  GLY G 786  VAL G 787
SITE     3 JC3 19 HIS G 788  SER G 789  GLN G 829  GLU G 841
SITE     4 JC3 19  MN G4073    K G4074  HOH G4444  HOH G4463
SITE     5 JC3 19 HOH G4464  HOH G4541  HOH G4542
SITE     1 JC4 10 GLU G 783  ASP G 791  GLU G 892  LEU G 907
SITE     2 JC4 10 TYR G1040  ASP G1041  THR G1042  HOH G4476
SITE     3 JC4 10 HOH G4501  HOH G4511
SITE     1 JC5  3 GLN G  22  THR G  94  ASN G  97
CRYST1  151.500  164.200  331.500  90.00  90.00  90.00 P 21 21 21   16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.006601  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006090  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003017        0.00000
      
PROCHECK
Go to PROCHECK summary
 References