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PDBsum entry 1ce8

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Top Page protein ligands metals Protein-protein interface(s) links
Ligase imp PDB id
1ce8
Jmol
Contents
Protein chains
1058 a.a. *
379 a.a. *
Ligands
ADP ×8
PO4 ×4
ORN ×8
IMP ×4
NET ×4
Metals
__K ×28
_MN ×12
_CL ×12
Waters ×4037
* Residue conservation analysis
HEADER    LIGASE IMP                              18-MAR-99   1CE8
TITLE     CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIS COLI WITH COMPLEXED
TITLE    2 WITH THE ALLOSTERIC LIGAND IMP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN (CARBAMOYL-PHOSPHATE SYNTHASE);
COMPND   3 CHAIN: A, C, E, G;
COMPND   4 EC: 6.3.5.5;
COMPND   5 ENGINEERED: YES;
COMPND   6 OTHER_DETAILS: LONG CHAIN;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: PROTEIN (CARBAMOYL-PHOSPHATE SYNTHASE);
COMPND   9 CHAIN: B, D, F, H;
COMPND  10 EC: 6.3.5.5;
COMPND  11 ENGINEERED: YES;
COMPND  12 OTHER_DETAILS: SHORT CHAIN
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   8 ORGANISM_TAXID: 562;
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    IMP, ALLOSTERIC LIGAND, LIGASE IMP
EXPDTA    X-RAY DIFFRACTION
AUTHOR    J.B.THODEN,F.M.RAUSHEL,H.M.HOLDEN
REVDAT   4   13-JUL-11 1CE8    1       VERSN
REVDAT   3   24-FEB-09 1CE8    1       VERSN
REVDAT   2   01-APR-03 1CE8    1       JRNL
REVDAT   1   26-JUL-99 1CE8    0
JRNL        AUTH   J.B.THODEN,F.M.RAUSHEL,G.WESENBERG,H.M.HOLDEN
JRNL        TITL   THE BINDING OF INOSINE MONOPHOSPHATE TO ESCHERICHIA COLI
JRNL        TITL 2 CARBAMOYL PHOSPHATE SYNTHETASE.
JRNL        REF    J.BIOL.CHEM.                  V. 274 22502 1999
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   10428826
JRNL        DOI    10.1074/JBC.274.32.22502
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT V. 5-D
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        (%) : 93.0
REMARK   3   NUMBER OF REFLECTIONS             : 445013
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.250
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2225
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1930
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1920
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.257
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.00
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 22250
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 445013
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 44220
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 488
REMARK   3   SOLVENT ATOMS            : 4037
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) : 0.013 ; 7.500 ; 45563
REMARK   3   BOND ANGLES            (DEGREES) : 2.300 ; 13.000; 61446
REMARK   3   TORSION ANGLES         (DEGREES) : 17.899; 0.000 ; 27456
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : 0.005 ; 40.000; 1224
REMARK   3   GENERAL PLANES               (A) : 0.009 ; 65.000; 6605
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : 0.040 ; NULL  ; 796
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : TNT
REMARK   3   KSOL        : 0.88
REMARK   3   BSOL        : 403.80
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : TNT PROTGEO
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  MISSING RESIDUES
REMARK   3  THR: LAST TWO RESIDUES, 381ALA AND 382LYS ARE NOT VISIBLE IN
REMARK   3  ELECTRON DENSITY MAP
REMARK   3  THR: LAST TWO RESIDUES, 381ALA AND 382LYS ARE NOT VISIBLE IN
REMARK   3  ELECTRON DENSITY MAP
REMARK   3  THR: LAST TWO RESIDUES, 381ALA AND 382LYS ARE NOT VISIBLE IN
REMARK   3  ELECTRON DENSITY MAP
REMARK   3  THR: LAST TWO RESIDUES, 381ALA AND 382LYS ARE NOT VISIBLE IN
REMARK   3  ELECTRON DENSITY MAP
REMARK   4
REMARK   4 1CE8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-99.
REMARK 100 THE RCSB ID CODE IS RCSB000678.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : FEB-98
REMARK 200  TEMPERATURE           (KELVIN) : 130
REMARK 200  PH                             : 7.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL7-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 445013
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     (%) : 93.0
REMARK 200  DATA REDUNDANCY                : 4.000
REMARK 200  R MERGE                    (I) : 0.05000
REMARK 200  R SYM                      (I) : 0.05000
REMARK 200   FOR THE DATA SET  : 30.3000
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     (%) : 81.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30
REMARK 200  R MERGE FOR SHELL          (I) : 0.22100
REMARK 200  R SYM FOR SHELL            (I) : 0.22100
REMARK 200   FOR SHELL         : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1A9X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.4
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       76.05000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      165.60000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.95000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      165.60000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.05000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.95000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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     SER A   717
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     ALA B   381
REMARK 465     LYS B   382
REMARK 465     SER C   717
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     ALA D   381
REMARK 465     LYS D   382
REMARK 465     SER E   717
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     ALA F   381
REMARK 465     LYS F   382
REMARK 465     SER G   717
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     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     PRO C 716    CG   CD
REMARK 470     PRO E 716    CG   CD
REMARK 470     PRO G 716    CG   CD
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   O    HOH E  5316     O    HOH E  5868              2.09
REMARK 500   O    HOH G  5374     O    HOH G  5375              2.09
REMARK 500   O    HOH C  5389     O    HOH C  5589              2.10
REMARK 500   O    HOH A  5698     O    HOH A  5699              2.13
REMARK 500   O    HOH C  5247     O    HOH C  5248              2.14
REMARK 500   O    HOH H  3628     O    HOH H  4000              2.15
REMARK 500   OD2  ASP F   157     O    HOH F  3087              2.17
REMARK 500   O    GLU E    79     NH1  ARG E    82              2.18
REMARK 500   OG1  THR G   344     O    HOH G  5810              2.19
REMARK 500   O    HOH E  5635     O    HOH E  5923              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   NH1  ARG A   130     O    HOH F  3079     3545     1.65
REMARK 500   OE1  GLU F    10     O    HOH A  5434     3555     2.15
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  39   CD    GLU A  39   OE1     0.072
REMARK 500    GLU A  72   CD    GLU A  72   OE2     0.078
REMARK 500    GLU A  79   CD    GLU A  79   OE2     0.073
REMARK 500    GLU A 109   CD    GLU A 109   OE1     0.081
REMARK 500    GLU A 110   CD    GLU A 110   OE2     0.077
REMARK 500    GLU A 154   CD    GLU A 154   OE1     0.072
REMARK 500    GLU A 187   CD    GLU A 187   OE2     0.081
REMARK 500    GLU A 217   CD    GLU A 217   OE2     0.078
REMARK 500    GLU A 235   CD    GLU A 235   OE1     0.070
REMARK 500    GLU A 260   CD    GLU A 260   OE1     0.070
REMARK 500    GLU A 334   CD    GLU A 334   OE2     0.069
REMARK 500    GLU A 365   CD    GLU A 365   OE1     0.070
REMARK 500    GLU A 468   CD    GLU A 468   OE1     0.067
REMARK 500    GLU A 473   CD    GLU A 473   OE1     0.071
REMARK 500    GLU A 474   CD    GLU A 474   OE1     0.079
REMARK 500    GLU A 478   CD    GLU A 478   OE2     0.067
REMARK 500    GLU A 512   CD    GLU A 512   OE1     0.077
REMARK 500    GLU A 535   CD    GLU A 535   OE1     0.067
REMARK 500    GLU A 560   CD    GLU A 560   OE2     0.067
REMARK 500    GLU A 577   CD    GLU A 577   OE1     0.076
REMARK 500    GLU A 591   CD    GLU A 591   OE1     0.071
REMARK 500    GLU A 676   CD    GLU A 676   OE1     0.077
REMARK 500    GLU A 683   CD    GLU A 683   OE2     0.078
REMARK 500    GLU A 703   CD    GLU A 703   OE1     0.086
REMARK 500    GLU A 707   CD    GLU A 707   OE1     0.072
REMARK 500    GLU A 731   CD    GLU A 731   OE1     0.068
REMARK 500    GLU A 771   CD    GLU A 771   OE2     0.066
REMARK 500    GLU A 804   CD    GLU A 804   OE1     0.066
REMARK 500    GLU A 819   CD    GLU A 819   OE1     0.066
REMARK 500    GLU A 836   CD    GLU A 836   OE1     0.075
REMARK 500    GLU A 841   CD    GLU A 841   OE1    -0.147
REMARK 500    GLU A 841   CD    GLU A 841   OE2     0.075
REMARK 500    GLU A 892   CD    GLU A 892   OE2     0.067
REMARK 500    GLU A 955   CD    GLU A 955   OE1     0.069
REMARK 500    GLU A 970   CD    GLU A 970   OE1     0.068
REMARK 500    GLU A 996   CD    GLU A 996   OE2     0.068
REMARK 500    GLU A1024   CD    GLU A1024   OE1     0.069
REMARK 500    GLU B  10   CD    GLU B  10   OE1     0.075
REMARK 500    GLU B 145   CD    GLU B 145   OE1     0.073
REMARK 500    GLU B 161   CD    GLU B 161   OE2     0.071
REMARK 500    GLU B 166   CD    GLU B 166   OE1     0.077
REMARK 500    GLU B 226   CD    GLU B 226   OE1     0.085
REMARK 500    GLU B 260   CD    GLU B 260   OE2     0.068
REMARK 500    GLU B 318   CD    GLU B 318   OE2     0.076
REMARK 500    GLU B 372   CD    GLU B 372   OE2     0.092
REMARK 500    GLU C  25   CD    GLU C  25   OE1     0.069
REMARK 500    GLU C  59   CD    GLU C  59   OE1     0.082
REMARK 500    GLU C  67   CD    GLU C  67   OE1     0.077
REMARK 500    GLU C  72   CD    GLU C  72   OE2     0.067
REMARK 500    GLU C  81   CD    GLU C  81   OE1     0.067
REMARK 500
REMARK 500 THIS ENTRY HAS     189 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  27   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG A  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ASP A  62   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A  84   CB  -  CG  -  OD1 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ASP A 124   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ASP A 124   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A 128   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 128   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ASP A 133   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    ARG A 194   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ASP A 226   CB  -  CG  -  OD1 ANGL. DEV. =  -8.0 DEGREES
REMARK 500    ARG A 303   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 343   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES
REMARK 500    ARG A 361   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ASP A 372   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES
REMARK 500    ASP A 410   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ASP A 410   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP A 416   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ARG A 425   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ASP A 430   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    TYR A 438   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    ARG A 444   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ASP A 518   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    ASP A 521   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES
REMARK 500    ASP A 539   CB  -  CG  -  OD1 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    ASP A 558   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG A 571   CD  -  NE  -  CZ  ANGL. DEV. =  -9.0 DEGREES
REMARK 500    ARG A 571   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES
REMARK 500    ASP A 579   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP A 579   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 592   CB  -  CG  -  OD1 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    ASP A 592   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES
REMARK 500    ASP A 614   CB  -  CG  -  OD1 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP A 614   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ARG A 615   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ASP A 625   CB  -  CG  -  OD1 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ASP A 625   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES
REMARK 500    ASP A 670   CB  -  CG  -  OD1 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ASP A 674   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 674   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A 677   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES
REMARK 500    ARG A 677   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    PRO A 716   N   -  CA  -  CB  ANGL. DEV. =   7.5 DEGREES
REMARK 500    ASP A 733   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ASP A 733   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ARG A 736   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     400 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     -161.15    -68.92
REMARK 500    LYS A   8      -50.11   -120.24
REMARK 500    ALA A  23     -148.52   -115.96
REMARK 500    ALA A  52       39.16    -85.88
REMARK 500    ASP A 226       10.29     81.13
REMARK 500    THR A 279       55.17   -140.53
REMARK 500    ASN A 292        7.53   -151.66
REMARK 500    PRO A 302       58.62    -69.72
REMARK 500    ARG A 303     -173.39   -179.86
REMARK 500    VAL A 328       33.25    -96.16
REMARK 500    ASP A 353       46.52   -106.85
REMARK 500    ASN A 363       29.13   -143.92
REMARK 500    THR A 375     -158.64   -144.79
REMARK 500    ASP A 530       -6.06   -143.98
REMARK 500    THR A 531      -14.21     77.31
REMARK 500    ALA A 541       71.88   -106.41
REMARK 500    GLU A 549      -70.06    -80.16
REMARK 500    ASN A 554       48.54     38.97
REMARK 500    GLN A 679      -30.60    -35.35
REMARK 500    LYS A 686       30.56     71.41
REMARK 500    ALA A 693      138.09   -170.49
REMARK 500    THR A 800      -21.68   -141.04
REMARK 500    GLN A 821       37.62     70.13
REMARK 500    PRO A 844       46.94    -67.66
REMARK 500    SER A 948       89.56   -152.44
REMARK 500    HIS A 975      -71.65    -29.28
REMARK 500    ARG A1027      -39.59    -32.87
REMARK 500    LYS B   3       72.11   -114.00
REMARK 500    ASP B 114       82.65    -69.72
REMARK 500    SER B 239      174.31    -57.66
REMARK 500    CYS B 269     -103.84     62.38
REMARK 500    ASN B 311       82.70   -161.74
REMARK 500    ALA B 356     -111.22     52.84
REMARK 500    SER B 357      -64.62    112.29
REMARK 500    PRO B 365       -9.90    -58.48
REMARK 500    PRO C   2     -152.98    -64.11
REMARK 500    ALA C  23     -148.55   -112.91
REMARK 500    ASN C  48      112.24   -165.26
REMARK 500    ALA C  52       34.49    -83.01
REMARK 500    ALA C 239     -179.11    -66.36
REMARK 500    THR C 279       57.16   -141.38
REMARK 500    ASN C 292        9.78   -153.80
REMARK 500    PRO C 302       48.11    -68.28
REMARK 500    ARG C 303     -179.47   -172.02
REMARK 500    THR C 340       35.14    -96.03
REMARK 500    ASP C 353       46.01   -109.50
REMARK 500    ASN C 363       42.09   -151.25
REMARK 500    ALA C 368      -87.54    -34.31
REMARK 500    ASP C 416       32.06    -94.94
REMARK 500    ASP C 530       -3.26   -144.57
REMARK 500
REMARK 500 THIS ENTRY HAS     135 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 SER B  357     PRO B  358                  144.81
REMARK 500 SER H  357     PRO H  358                  149.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR H 250         0.06    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    PHE B 314         12.77
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   1        24.2      L          L   OUTSIDE RANGE
REMARK 500    GLU A 127        24.1      L          L   OUTSIDE RANGE
REMARK 500    ILE A 339        23.4      L          L   OUTSIDE RANGE
REMARK 500    ARG A 435        19.2      L          L   OUTSIDE RANGE
REMARK 500    ALA A 534        23.9      L          L   OUTSIDE RANGE
REMARK 500    THR A 612        24.9      L          L   OUTSIDE RANGE
REMARK 500    ASP A 758        23.7      L          L   OUTSIDE RANGE
REMARK 500    LEU A 801        23.7      L          L   OUTSIDE RANGE
REMARK 500    LYS A 954        25.0      L          L   OUTSIDE RANGE
REMARK 500    ILE B   2        24.5      L          L   OUTSIDE RANGE
REMARK 500    SER B  35        23.7      L          L   OUTSIDE RANGE
REMARK 500    ASP B  69        23.8      L          L   OUTSIDE RANGE
REMARK 500    LEU B  98        24.1      L          L   OUTSIDE RANGE
REMARK 500    ASP B 112        24.7      L          L   OUTSIDE RANGE
REMARK 500    ASP B 249        23.7      L          L   OUTSIDE RANGE
REMARK 500    THR B 328        23.3      L          L   OUTSIDE RANGE
REMARK 500    ALA B 364        24.1      L          L   OUTSIDE RANGE
REMARK 500    PHE C  26        24.7      L          L   OUTSIDE RANGE
REMARK 500    VAL C  44        24.0      L          L   OUTSIDE RANGE
REMARK 500    TRP C  71        24.3      L          L   OUTSIDE RANGE
REMARK 500    PHE C 172        21.0      L          L   OUTSIDE RANGE
REMARK 500    ILE C 339        13.5      L          L   OUTSIDE RANGE
REMARK 500    TYR C1036        22.7      L          L   OUTSIDE RANGE
REMARK 500    TYR D  39        21.4      L          L   OUTSIDE RANGE
REMARK 500    THR D  44        24.9      L          L   OUTSIDE RANGE
REMARK 500    ARG D  50        21.0      L          L   OUTSIDE RANGE
REMARK 500    PRO D  58        24.2      L          L   OUTSIDE RANGE
REMARK 500    ASP D 112        24.8      L          L   OUTSIDE RANGE
REMARK 500    ARG D 212        24.3      L          L   OUTSIDE RANGE
REMARK 500    SER D 239        20.4      L          L   OUTSIDE RANGE
REMARK 500    ASP D 362        24.1      L          L   OUTSIDE RANGE
REMARK 500    THR E   5        23.5      L          L   OUTSIDE RANGE
REMARK 500    PHE E  26        22.4      L          L   OUTSIDE RANGE
REMARK 500    THR E  56        23.5      L          L   OUTSIDE RANGE
REMARK 500    ILE E  69        23.8      L          L   OUTSIDE RANGE
REMARK 500    ARG E  82        22.9      L          L   OUTSIDE RANGE
REMARK 500    ASP E 133        24.5      L          L   OUTSIDE RANGE
REMARK 500    PHE E 172        18.8      L          L   OUTSIDE RANGE
REMARK 500    ILE E 339        16.9      L          L   OUTSIDE RANGE
REMARK 500    ARG E 435        24.8      L          L   OUTSIDE RANGE
REMARK 500    GLU E 548        22.5      L          L   OUTSIDE RANGE
REMARK 500    VAL E 750        18.9      L          L   OUTSIDE RANGE
REMARK 500    LEU E 801        23.8      L          L   OUTSIDE RANGE
REMARK 500    VAL E 850        24.6      L          L   OUTSIDE RANGE
REMARK 500    PHE E 897        24.8      L          L   OUTSIDE RANGE
REMARK 500    ASN E 936        24.3      L          L   OUTSIDE RANGE
REMARK 500    VAL E 957        24.4      L          L   OUTSIDE RANGE
REMARK 500    LEU E 971        24.4      L          L   OUTSIDE RANGE
REMARK 500    ARG E 998        24.3      L          L   OUTSIDE RANGE
REMARK 500    ILE F   2        24.9      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS      78 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 A5214        DISTANCE =  6.38 ANGSTROMS
REMARK 525    HOH A5306        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH A5370        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH A5385        DISTANCE =  5.82 ANGSTROMS
REMARK 525    HOH A5387        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH A5428        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH A5442        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH A5443        DISTANCE =  6.48 ANGSTROMS
REMARK 525    HOH A5512        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH A5520        DISTANCE =  5.55 ANGSTROMS
REMARK 525    HOH A5598        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH A5602        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH A5642        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A5643        DISTANCE =  5.77 ANGSTROMS
REMARK 525    HOH A5673        DISTANCE =  5.97 ANGSTROMS
REMARK 525    HOH A5719        DISTANCE =  5.92 ANGSTROMS
REMARK 525    HOH A5736        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH A5743        DISTANCE =  5.86 ANGSTROMS
REMARK 525    HOH A5801        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH A5802        DISTANCE =  7.70 ANGSTROMS
REMARK 525    HOH A5835        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH A5842        DISTANCE =  6.32 ANGSTROMS
REMARK 525    HOH A5856        DISTANCE =  7.26 ANGSTROMS
REMARK 525    HOH A5858        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH B5101        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH B5113        DISTANCE =  6.92 ANGSTROMS
REMARK 525    HOH B5170        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH C5140        DISTANCE =  5.52 ANGSTROMS
REMARK 525    HOH C5142        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH C5162        DISTANCE =  6.00 ANGSTROMS
REMARK 525    HOH C5233        DISTANCE =  6.60 ANGSTROMS
REMARK 525    HOH C5242        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH C5388        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH C5409        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH C5445        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH C5459        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH C5466        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH C5470        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH C5471        DISTANCE =  5.66 ANGSTROMS
REMARK 525    HOH C5479        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH C5480        DISTANCE =  7.46 ANGSTROMS
REMARK 525    HOH C5507        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH C5581        DISTANCE =  6.03 ANGSTROMS
REMARK 525    HOH C5618        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH C5622        DISTANCE =  5.88 ANGSTROMS
REMARK 525    HOH D1591        DISTANCE =  6.08 ANGSTROMS
REMARK 525    HOH D1844        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH D1953        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH E5158        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH E5182        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH E5258        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH E5338        DISTANCE =  6.09 ANGSTROMS
REMARK 525    HOH E5410        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH E5446        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH E5450        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH E5496        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH E5501        DISTANCE =  5.81 ANGSTROMS
REMARK 525    HOH E5510        DISTANCE =  6.81 ANGSTROMS
REMARK 525    HOH E5516        DISTANCE =  6.86 ANGSTROMS
REMARK 525    HOH E5517        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH E5554        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH E5581        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH E5589        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH E5671        DISTANCE =  6.80 ANGSTROMS
REMARK 525    HOH E5731        DISTANCE =  7.52 ANGSTROMS
REMARK 525    HOH E5737        DISTANCE =  5.79 ANGSTROMS
REMARK 525    HOH E5743        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH E5767        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH E5770        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH E5790        DISTANCE =  7.89 ANGSTROMS
REMARK 525    HOH E5806        DISTANCE =  7.11 ANGSTROMS
REMARK 525    HOH E5807        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH E5809        DISTANCE =  5.84 ANGSTROMS
REMARK 525    HOH E5814        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH E5840        DISTANCE =  5.46 ANGSTROMS
REMARK 525    HOH E5843        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH E5851        DISTANCE =  5.50 ANGSTROMS
REMARK 525    HOH E5871        DISTANCE =  6.07 ANGSTROMS
REMARK 525    HOH E5875        DISTANCE =  6.90 ANGSTROMS
REMARK 525    HOH E5877        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH E5968        DISTANCE =  5.67 ANGSTROMS
REMARK 525    HOH E5971        DISTANCE =  5.37 ANGSTROMS
REMARK 525    HOH E5987        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH E5994        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH F2181        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH F2258        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH F2553        DISTANCE =  6.18 ANGSTROMS
REMARK 525    HOH F2554        DISTANCE =  7.95 ANGSTROMS
REMARK 525    HOH F2900        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH F2960        DISTANCE =  6.33 ANGSTROMS
REMARK 525    HOH F3070        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH F3108        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH G5221        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH G5227        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH G5287        DISTANCE =  6.85 ANGSTROMS
REMARK 525    HOH G5361        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH G5362        DISTANCE =  8.43 ANGSTROMS
REMARK 525    HOH G5373        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH G5393        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH G5399        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH G5451        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH G5494        DISTANCE =  6.11 ANGSTROMS
REMARK 525    HOH G5509        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH G5525        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH G5526        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH G5532        DISTANCE =  5.04 ANGSTROMS
REMARK 525    HOH G5542        DISTANCE =  6.36 ANGSTROMS
REMARK 525    HOH G5568        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH G5594        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH G5602        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH G5610        DISTANCE =  5.77 ANGSTROMS
REMARK 525    HOH G5679        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH G5680        DISTANCE =  5.87 ANGSTROMS
REMARK 525    HOH G5684        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH G5695        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH G5711        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH G5723        DISTANCE =  5.59 ANGSTROMS
REMARK 525    HOH G5742        DISTANCE =  6.35 ANGSTROMS
REMARK 525    HOH G5743        DISTANCE =  7.14 ANGSTROMS
REMARK 525    HOH G5746        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH G5793        DISTANCE =  6.99 ANGSTROMS
REMARK 525    HOH G5800        DISTANCE =  5.05 ANGSTROMS
REMARK 525    HOH G5801        DISTANCE =  6.80 ANGSTROMS
REMARK 525    HOH G5815        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH H3695        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH H3753        DISTANCE =  7.08 ANGSTROMS
REMARK 525    HOH H3944        DISTANCE =  6.27 ANGSTROMS
REMARK 525    HOH H3945        DISTANCE =  5.87 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 A5015   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 112   O
REMARK 620 2 ASP A  84   O    71.8
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A5004   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 127   OE2
REMARK 620 2 GLU A 299   OE1 129.4
REMARK 620 3 MET A 300   O    92.4 102.6
REMARK 620 4 HOH A5108   O   145.5  84.6  71.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A5003   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 215   OE1
REMARK 620 2 ASN A 236   OD1  82.8
REMARK 620 3 ASP A 238   O   124.2  91.0
REMARK 620 4 ILE A 242   O    81.8 119.2 143.9
REMARK 620 5 SER A 247   OG  133.3  80.6  99.5  69.4
REMARK 620 6 ALA A 239   O    92.5 152.8  69.5  86.2 120.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A5005   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 217   OE1
REMARK 620 2 PO4 A5006   O3  174.6
REMARK 620 3 HOH A5225   O    92.6  86.9
REMARK 620 4 GLN A 285   OE1 118.5  63.3 146.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A5002  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 285   OE1
REMARK 620 2 GLU A 299   OE2  76.4
REMARK 620 3 ADP A5000   O1B 176.6 105.1
REMARK 620 4 ADP A5000   O1A  91.6  88.5  85.4
REMARK 620 5 HOH A5611   O    85.0 161.1  93.3  88.7
REMARK 620 6 PO4 A5006   O3   95.5  87.3  87.7 170.7  97.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A5001  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 299   CD
REMARK 620 2 GLU A 299   OE1  28.3
REMARK 620 3 GLU A 299   OE2  30.1  58.3
REMARK 620 4 ASN A 301   OD1  95.3 101.6  89.5
REMARK 620 5 ADP A5000   O3B  84.8  75.4  93.8 173.4
REMARK 620 6 PO4 A5006   O1  127.0 155.0  96.9  79.6 105.6
REMARK 620 7 HOH A5623   O   127.7 100.4 156.4  84.9  89.8 104.5
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A5010   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 761   OE1
REMARK 620 2 HIS A 781   ND1  80.8
REMARK 620 3 GLU A 783   O   130.4  93.0
REMARK 620 4 GLN A 784   O    91.3 147.0  68.0
REMARK 620 5 VAL A 787   O    76.9 125.7 138.2  82.6
REMARK 620 6 SER A 792   OG  127.5  83.7 100.1 124.9  72.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A5008  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 829   OE1
REMARK 620 2 GLU A 841   OE2  99.5
REMARK 620 3 ADP A5007   O2A  91.1  87.0
REMARK 620 4 ADP A5007   O3B 175.2  77.5  85.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A5009   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 841   OE1
REMARK 620 2 GLU A 841   OE2  46.1
REMARK 620 3 ADP A5007   O2B  90.9  91.3
REMARK 620 4 ADP A5007   O3B  94.2  59.7  51.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K B5019   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  16   O
REMARK 620 2 ASP B 112   O   103.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5035   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C  84   O
REMARK 620 2 GLY C 112   O    74.9
REMARK 620 3 THR C 114   OG1  83.8 116.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5024   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 127   OE2
REMARK 620 2 GLU C 299   OE1 127.8
REMARK 620 3 MET C 300   O    99.1  96.5
REMARK 620 4 HOH C5128   O   141.5  90.4  69.4
REMARK 620 5 HOH C5663   O    94.5 100.7 144.5  79.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5023   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 215   OE1
REMARK 620 2 ASN C 236   OD1  83.1
REMARK 620 3 ASP C 238   O   126.9  97.8
REMARK 620 4 ALA C 239   O    88.0 155.5  69.6
REMARK 620 5 ILE C 242   O    76.3 114.7 143.1  85.0
REMARK 620 6 SER C 247   OG  134.4  79.1  97.1 122.3  73.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5025   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 285   OE1
REMARK 620 2 GLU C 217   OE1 120.0
REMARK 620 3 PO4 C5026   O3   64.9 172.1
REMARK 620 4 HOH C5244   O   145.0  92.2  84.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C5022  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 285   OE1
REMARK 620 2 GLU C 299   OE2  78.0
REMARK 620 3 HOH C5629   O    88.3 164.7
REMARK 620 4 ADP C5020   O1A 100.7  86.6  89.2
REMARK 620 5 ADP C5020   O1B 172.8  98.5  95.8  85.4
REMARK 620 6 PO4 C5026   O3   89.2  86.5 100.4 166.5  84.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C5021  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 299   CD
REMARK 620 2 GLU C 299   OE1  28.0
REMARK 620 3 GLU C 299   OE2  30.4  58.4
REMARK 620 4 ASN C 301   OD1  86.2  85.1  89.1
REMARK 620 5 ADP C5020   O3B  92.0  86.5  96.7 165.3
REMARK 620 6 PO4 C5026   O1  125.1 152.6  95.2  87.6 105.2
REMARK 620 7 HOH C5662   O   121.7  93.7 151.9  84.6  83.9 111.8
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5030   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 761   OE1
REMARK 620 2 HIS C 781   ND1  76.1
REMARK 620 3 GLU C 783   O   131.7  94.3
REMARK 620 4 GLN C 784   O    95.9 150.0  69.3
REMARK 620 5 VAL C 787   O    75.1 123.7 140.1  80.3
REMARK 620 6 SER C 792   OG  123.1  81.2 101.1 125.5  75.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C5028  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 829   OE1
REMARK 620 2 GLU C 841   OE2  96.7
REMARK 620 3 ADP C5027   O3B 163.5  79.8
REMARK 620 4 ADP C5027   O2A  85.8  85.3  77.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5029   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 841   OE2
REMARK 620 2 ADP C5027   O2B  92.4
REMARK 620 3 GLU C 841   OE1  47.2  80.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K D5039   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D  16   O
REMARK 620 2 ASP D 112   O    87.5
REMARK 620 3 HOH C5319   O   111.5  89.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5055   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E  84   O
REMARK 620 2 GLY E 112   O    79.4
REMARK 620 3 THR E 114   OG1  84.7 101.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5044   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 127   OE2
REMARK 620 2 GLU E 299   OE1 130.8
REMARK 620 3 MET E 300   O    94.5  94.0
REMARK 620 4 HOH E5153   O   143.6  85.3  75.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5043   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 215   OE1
REMARK 620 2 ASN E 236   OD1  80.2
REMARK 620 3 ASP E 238   O   125.5  91.6
REMARK 620 4 ALA E 239   O    94.6 150.5  67.7
REMARK 620 5 ILE E 242   O    85.4 119.0 141.3  89.2
REMARK 620 6 SER E 247   OG  136.1  79.2  93.4 121.1  71.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5045   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 217   OE1
REMARK 620 2 GLN E 285   OE1 119.6
REMARK 620 3 PO4 E5046   O3  171.3  63.5
REMARK 620 4 HOH E5269   O    90.3 147.0  89.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E5042  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 285   OE1
REMARK 620 2 GLU E 299   OE2  76.9
REMARK 620 3 ADP E5040   O1B 169.6  95.1
REMARK 620 4 HOH E5681   O    84.2 160.1 104.4
REMARK 620 5 ADP E5040   O1A  94.9  81.5  90.3  94.2
REMARK 620 6 PO4 E5046   O3   89.8  86.9  83.2  99.3 166.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E5041  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 299   CD
REMARK 620 2 GLU E 299   OE1  27.4
REMARK 620 3 GLU E 299   OE2  29.9  57.2
REMARK 620 4 ASN E 301   OD1  84.7  85.6  86.7
REMARK 620 5 ADP E5040   O3B  90.0  86.4  92.2 171.1
REMARK 620 6 HOH E5686   O   118.7  91.4 148.5  88.3  87.9
REMARK 620 7 PO4 E5046   O1  125.6 151.1  97.1  79.5 109.4 112.5
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5050   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 761   OE1
REMARK 620 2 HIS E 781   ND1  81.2
REMARK 620 3 GLN E 784   O    88.2 147.8
REMARK 620 4 VAL E 787   O    73.9 121.1  84.2
REMARK 620 5 SER E 792   OG  130.4  82.8 125.8  75.2
REMARK 620 6 GLU E 783   O   126.0  92.1  69.8 145.1 101.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E5048  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 829   OE1
REMARK 620 2 GLU E 841   OE2  80.5
REMARK 620 3 ADP E5047   O2A 100.7  95.1
REMARK 620 4 ADP E5047   O3B 160.6  80.2  83.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5049   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 841   OE1
REMARK 620 2 ADP E5047   O2B  93.1
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K F5059   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F  16   O
REMARK 620 2 ASP F 112   O    89.1
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5075   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G  84   O
REMARK 620 2 GLY G 112   O    77.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5064   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 127   OE2
REMARK 620 2 GLU G 299   OE1 132.0
REMARK 620 3 MET G 300   O    97.1  93.2
REMARK 620 4 HOH G5182   O   144.4  82.6  68.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5063   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 215   OE1
REMARK 620 2 ASN G 236   OD1  80.0
REMARK 620 3 ASP G 238   O   118.1  92.1
REMARK 620 4 ALA G 239   O    87.2 150.2  70.5
REMARK 620 5 ILE G 242   O    87.6 119.2 143.5  86.7
REMARK 620 6 SER G 247   OG  139.7  83.2  98.7 122.2  69.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5065   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 285   OE1
REMARK 620 2 HOH G5298   O   152.2
REMARK 620 3 PO4 G5066   O3   64.9  90.0
REMARK 620 4 ASN G 283   OD1  84.4  93.3 109.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G5062  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 285   OE1
REMARK 620 2 GLU G 299   OE2  81.9
REMARK 620 3 PO4 G5066   O3   87.9  93.5
REMARK 620 4 HOH G5694   O    84.4 166.2  87.3
REMARK 620 5 ADP G5060   O1A 101.0  84.2 170.4  97.2
REMARK 620 6 ADP G5060   O1B 174.3 100.7  86.8  93.1  84.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G5061  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 299   CD
REMARK 620 2 GLU G 299   OE1  27.3
REMARK 620 3 GLU G 299   OE2  29.3  56.4
REMARK 620 4 ASN G 301   OD1  83.0  84.0  87.1
REMARK 620 5 HOH G5704   O   124.8  97.5 153.7  94.2
REMARK 620 6 PO4 G5066   O1  121.4 148.7  92.3  93.0 113.8
REMARK 620 7 ADP G5060   O3B  84.3  78.5  88.4 161.4  82.0 105.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5070   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 761   OE1
REMARK 620 2 HIS G 781   ND1  80.7
REMARK 620 3 GLU G 783   O   136.4  88.1
REMARK 620 4 GLN G 784   O    95.1 148.9  73.7
REMARK 620 5 VAL G 787   O    86.0 122.7 133.7  87.4
REMARK 620 6 SER G 792   OG  123.1  73.5  92.9 131.1  68.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G5068  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 829   OE1
REMARK 620 2 GLU G 841   OE2  83.1
REMARK 620 3 ADP G5067   O3B 169.5 104.9
REMARK 620 4 ADP G5067   O2A  93.3  84.8  94.1
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5069   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 841   OE1
REMARK 620 2 ASN G 843   OD1  88.9
REMARK 620 3 ADP G5067   O2B  78.9 160.6
REMARK 620 N                    1     2
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 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5015
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5017
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5018
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 5019
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5021
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5022
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5023
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5024
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5025
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5028
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5029
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5030
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5035
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5036
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5037
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5038
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 5039
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5041
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5042
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5043
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5044
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5045
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5048
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5049
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5050
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5055
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5056
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5057
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5058
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 5059
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 5061
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 5062
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5063
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5064
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5065
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 5068
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5069
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5070
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5075
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5076
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5077
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5078
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 5079
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 5006
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 5026
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 5046
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 5066
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 5000
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 5007
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 5011
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMP A 5012
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 5013
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 5014
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 5020
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 5027
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 5031
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMP C 5032
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 5033
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 5034
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 5040
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 5047
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 5051
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMP E 5052
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 5053
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 5054
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 5060
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 5067
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 5071
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMP G 5072
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 5073
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 5074
DBREF  1CE8 A    1  1073  UNP    P00968   CARB_ECOLI       1   1073
DBREF  1CE8 B    2   380  UNP    P0A6F1   CARA_ECOLI       1    382
DBREF  1CE8 C    1  1073  UNP    P00968   CARB_ECOLI       1   1073
DBREF  1CE8 D    2   380  UNP    P0A6F1   CARA_ECOLI       1    382
DBREF  1CE8 E    1  1073  UNP    P00968   CARB_ECOLI       1   1073
DBREF  1CE8 F    2   380  UNP    P0A6F1   CARA_ECOLI       1    382
DBREF  1CE8 G    1  1073  UNP    P00968   CARB_ECOLI       1   1073
DBREF  1CE8 H    2   380  UNP    P0A6F1   CARA_ECOLI       1    382
SEQADV 1CE8 ASN A   46  UNP  P00968    LEU    46 SEQUENCE CONFLICT
SEQADV 1CE8 GLN B  183  UNP  P0A6F1    GLU   183 SEQUENCE CONFLICT
SEQADV 1CE8 ASN C   46  UNP  P00968    LEU    46 SEQUENCE CONFLICT
SEQADV 1CE8 GLN D  183  UNP  P0A6F1    GLU   183 SEQUENCE CONFLICT
SEQADV 1CE8 ASN E   46  UNP  P00968    LEU    46 SEQUENCE CONFLICT
SEQADV 1CE8 GLN F  183  UNP  P0A6F1    GLU   183 SEQUENCE CONFLICT
SEQADV 1CE8 ASN G   46  UNP  P00968    LEU    46 SEQUENCE CONFLICT8
SEQADV 1CE8 GLN H  183  UNP  P0A6F1    GLU   183 SEQUENCE CONFLICT8
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 GLY 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 GLY 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 GLY 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 GLY 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  A5001       1
HET     MN  A5002       1
HET      K  A5003       1
HET      K  A5004       1
HET      K  A5005       1
HET     MN  A5008       1
HET      K  A5009       1
HET      K  A5010       1
HET      K  A5015       1
HET     CL  A5016       1
HET     CL  A5017       1
HET     CL  A5018       1
HET      K  B5019       1
HET     MN  C5021       1
HET     MN  C5022       1
HET      K  C5023       1
HET      K  C5024       1
HET      K  C5025       1
HET     MN  C5028       1
HET      K  C5029       1
HET      K  C5030       1
HET      K  C5035       1
HET     CL  C5036       1
HET     CL  C5037       1
HET     CL  C5038       1
HET      K  D5039       1
HET     MN  E5041       1
HET     MN  E5042       1
HET      K  E5043       1
HET      K  E5044       1
HET      K  E5045       1
HET     MN  E5048       1
HET      K  E5049       1
HET      K  E5050       1
HET      K  E5055       1
HET     CL  E5056       1
HET     CL  E5057       1
HET     CL  E5058       1
HET      K  F5059       1
HET     MN  G5061       1
HET     MN  G5062       1
HET      K  G5063       1
HET      K  G5064       1
HET      K  G5065       1
HET     MN  G5068       1
HET      K  G5069       1
HET      K  G5070       1
HET      K  G5075       1
HET     CL  G5076       1
HET     CL  G5077       1
HET     CL  G5078       1
HET      K  H5079       1
HET    PO4  A5006       5
HET    PO4  C5026       5
HET    PO4  E5046       5
HET    PO4  G5066       5
HET    ADP  A5000      27
HET    ADP  A5007      27
HET    ORN  A5011       9
HET    IMP  A5012      23
HET    NET  A5013       9
HET    ORN  A5014       9
HET    ADP  C5020      27
HET    ADP  C5027      27
HET    ORN  C5031       9
HET    IMP  C5032      23
HET    NET  C5033       9
HET    ORN  C5034       9
HET    ADP  E5040      27
HET    ADP  E5047      27
HET    ORN  E5051       9
HET    IMP  E5052      23
HET    NET  E5053       9
HET    ORN  E5054       9
HET    ADP  G5060      27
HET    ADP  G5067      27
HET    ORN  G5071       9
HET    IMP  G5072      23
HET    NET  G5073       9
HET    ORN  G5074       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     IMP INOSINIC ACID
HETNAM     NET TETRAETHYLAMMONIUM ION
FORMUL   9   MN    12(MN 2+)
FORMUL  11    K    28(K 1+)
FORMUL  18   CL    12(CL 1-)
FORMUL  61  PO4    4(O4 P 3-)
FORMUL  65  ADP    8(C10 H15 N5 O10 P2)
FORMUL  67  ORN    8(C5 H12 N2 O2)
FORMUL  68  IMP    4(C10 H13 N4 O8 P)
FORMUL  69  NET    4(C8 H20 N 1+)
FORMUL  89  HOH   *4037(H2 O)
HELIX    1   1 CYS A   24  GLU A   39  5                                  16
HELIX    2   2 PRO A   58  MET A   60  5                                   3
HELIX    3   3 TRP A   71  GLU A   81  1                                  11
HELIX    4   4 GLY A   92  ARG A  104  1                                  13
HELIX    5   5 VAL A  107  PHE A  111  1                                   5
HELIX    6   6 ALA A  120  GLU A  127  1                                   8
HELIX    7   7 ARG A  129  LYS A  138  1                                  10
HELIX    8   8 MET A  152  VAL A  162  1                                  11
HELIX    9   9 ARG A  185  LEU A  198  1                                  14
HELIX   10  10 ASP A  258  ILE A  275  1                                  18
HELIX   11  11 ARG A  306  THR A  315  1                                  10
HELIX   12  12 ILE A  319  VAL A  328  1                                  10
HELIX   13  13 LEU A  332  GLU A  334  5                                   3
HELIX   14  14 ASP A  338  THR A  340  5                                   3
HELIX   15  15 PHE A  364  LYS A  366  5                                   3
HELIX   16  16 GLN A  391  GLY A  401  1                                  11
HELIX   17  17 ALA A  420  LYS A  429  1                                  10
HELIX   18  18 ARG A  435  ARG A  444  1                                  10
HELIX   19  19 VAL A  449  THR A  456  1                                   8
HELIX   20  20 ARG A  460  VAL A  479  1                                  20
HELIX   21  21 ILE A  481  GLY A  483  5                                   3
HELIX   22  22 ALA A  486  LYS A  495  1                                  10
HELIX   23  23 ASP A  499  LEU A  505  1                                   7
HELIX   24  24 GLU A  510  GLN A  519  1                                  10
HELIX   25  25 ILE A  576  GLU A  591  1                                  16
HELIX   26  26 TYR A  610  THR A  612  5                                   3
HELIX   27  27 LEU A  623  GLU A  633  1                                  11
HELIX   28  28 GLN A  645  ALA A  656  1                                  12
HELIX   29  29 PRO A  666  GLU A  673  1                                   8
HELIX   30  30 ARG A  675  LEU A  685  1                                  11
HELIX   31  31 ILE A  698  ILE A  708  1                                  11
HELIX   32  32 GLU A  731  THR A  740  1                                  10
HELIX   33  33 SER A  789  ASP A  791  5                                   3
HELIX   34  34 GLN A  803  LEU A  820  1                                  18
HELIX   35  35 VAL A  850  THR A  857  1                                   8
HELIX   36  36 LEU A  861  MET A  869  1                                   9
HELIX   37  37 LEU A  874  GLN A  877  1                                   4
HELIX   38  38 PRO A  896  LYS A  899  5                                   4
HELIX   39  39 PHE A  924  GLY A  934  1                                  11
HELIX   40  40 GLU A  951  LYS A  966  5                                  16
HELIX   41  41 HIS A  975  ALA A  984  1                                  10
HELIX   42  42 VAL A  994  GLU A  996  5                                   3
HELIX   43  43 ILE A 1001  LYS A 1006  1                                   6
HELIX   44  44 ARG A 1020  GLN A 1035  1                                  16
HELIX   45  45 LEU A 1044  ASN A 1055  1                                  12
HELIX   46  46 VAL A 1065  GLN A 1071  1                                   7
HELIX   47  47 TYR B   39  LEU B   43  1                                   5
HELIX   48  48 PRO B   46  TYR B   48  5                                   3
HELIX   49  49 ASP B   67  ASP B   69  5                                   3
HELIX   50  50 LEU B   98  ARG B  104  1                                   7
HELIX   51  51 THR B  115  LYS B  125  1                                  11
HELIX   52  52 ALA B  140  ALA B  149  1                                  10
HELIX   53  53 ALA B  159  VAL B  162  1                                   4
HELIX   54  54 GLU B  187  GLU B  189  5                                   3
HELIX   55  55 ARG B  203  ARG B  212  1                                  10
HELIX   56  56 ALA B  225  MET B  231  1                                   7
HELIX   57  57 ASP B  249  GLU B  260  1                                  12
HELIX   58  58 LEU B  270  SER B  279  1                                  10
HELIX   59  59 GLU B  318  THR B  320  5                                   3
HELIX   60  60 ALA B  364  ARG B  378  5                                  15
HELIX   61  61 CYS C   24  GLU C   39  5                                  16
HELIX   62  62 PRO C   58  MET C   60  5                                   3
HELIX   63  63 TRP C   71  GLU C   81  1                                  11
HELIX   64  64 GLY C   92  GLN C  105  1                                  14
HELIX   65  65 VAL C  107  GLU C  110  1                                   4
HELIX   66  66 ALA C  120  GLU C  127  1                                   8
HELIX   67  67 ARG C  129  LYS C  138  1                                  10
HELIX   68  68 MET C  152  VAL C  162  1                                  11
HELIX   69  69 ARG C  185  LEU C  198  1                                  14
HELIX   70  70 THR C  244  ASP C  246  5                                   3
HELIX   71  71 ASP C  258  ILE C  275  1                                  18
HELIX   72  72 ARG C  306  THR C  315  1                                  10
HELIX   73  73 ILE C  319  VAL C  328  1                                  10
HELIX   74  74 LEU C  332  GLU C  334  5                                   3
HELIX   75  75 PHE C  364  LYS C  366  5                                   3
HELIX   76  76 GLN C  391  GLY C  401  1                                  11
HELIX   77  77 ALA C  420  LYS C  429  1                                  10
HELIX   78  78 ARG C  435  ARG C  444  1                                  10
HELIX   79  79 VAL C  449  THR C  456  1                                   8
HELIX   80  80 ARG C  460  THR C  482  1                                  23
HELIX   81  81 ALA C  486  LYS C  495  1                                  10
HELIX   82  82 ASP C  499  ALA C  506  1                                   8
HELIX   83  83 GLU C  510  TYR C  520  1                                  11
HELIX   84  84 ILE C  576  GLU C  591  1                                  16
HELIX   85  85 TYR C  610  THR C  612  5                                   3
HELIX   86  86 LEU C  623  GLU C  633  1                                  11
HELIX   87  87 GLN C  645  ALA C  656  1                                  12
HELIX   88  88 PRO C  666  GLU C  673  1                                   8
HELIX   89  89 ARG C  675  ARG C  684  1                                  10
HELIX   90  90 ILE C  698  ILE C  708  1                                  11
HELIX   91  91 GLU C  731  THR C  740  1                                  10
HELIX   92  92 SER C  789  ASP C  791  5                                   3
HELIX   93  93 GLN C  803  LEU C  820  1                                  18
HELIX   94  94 VAL C  850  THR C  857  1                                   8
HELIX   95  95 LEU C  861  MET C  869  1                                   9
HELIX   96  96 LEU C  874  GLN C  877  1                                   4
HELIX   97  97 PRO C  896  LYS C  899  5                                   4
HELIX   98  98 PHE C  924  GLY C  934  1                                  11
HELIX   99  99 GLU C  951  LYS C  954  1                                   4
HELIX  100 100 ARG C  956  LYS C  966  5                                  11
HELIX  101 101 HIS C  975  ALA C  984  1                                  10
HELIX  102 102 VAL C  994  GLU C  996  5                                   3
HELIX  103 103 ILE C 1001  LYS C 1006  1                                   6
HELIX  104 104 ARG C 1020  TYR C 1036  1                                  17
HELIX  105 105 LEU C 1044  ASN C 1055  1                                  12
HELIX  106 106 VAL C 1065  GLN C 1071  1                                   7
HELIX  107 107 TYR D   39  LEU D   43  1                                   5
HELIX  108 108 PRO D   46  TYR D   48  5                                   3
HELIX  109 109 ASP D   67  ASP D   69  5                                   3
HELIX  110 110 LEU D   98  ARG D  104  1                                   7
HELIX  111 111 THR D  115  LYS D  125  1                                  11
HELIX  112 112 ALA D  140  ALA D  149  1                                  10
HELIX  113 113 ALA D  159  VAL D  162  1                                   4
HELIX  114 114 GLU D  187  GLU D  189  5                                   3
HELIX  115 115 ARG D  203  ASP D  211  1                                   9
HELIX  116 116 ALA D  225  MET D  231  1                                   7
HELIX  117 117 ASP D  249  PHE D  258  1                                  10
HELIX  118 118 LEU D  270  ALA D  278  1                                   9
HELIX  119 119 GLU D  318  THR D  320  5                                   3
HELIX  120 120 HIS D  361  ARG D  378  5                                  18
HELIX  121 121 CYS E   24  GLU E   39  5                                  16
HELIX  122 122 ILE E   54  THR E   56  5                                   3
HELIX  123 123 PRO E   58  MET E   60  5                                   3
HELIX  124 124 TRP E   71  GLU E   81  1                                  11
HELIX  125 125 GLY E   92  ARG E  104  1                                  13
HELIX  126 126 VAL E  107  PHE E  111  1                                   5
HELIX  127 127 ALA E  120  GLU E  127  1                                   8
HELIX  128 128 ARG E  129  LYS E  138  1                                  10
HELIX  129 129 MET E  152  VAL E  162  1                                  11
HELIX  130 130 ARG E  185  LEU E  198  1                                  14
HELIX  131 131 THR E  244  ASP E  246  5                                   3
HELIX  132 132 ASP E  258  ILE E  275  1                                  18
HELIX  133 133 ARG E  306  THR E  315  1                                  10
HELIX  134 134 ILE E  319  VAL E  328  1                                  10
HELIX  135 135 ASP E  338  THR E  340  5                                   3
HELIX  136 136 PHE E  364  LYS E  366  5                                   3
HELIX  137 137 GLN E  391  GLY E  401  1                                  11
HELIX  138 138 ALA E  420  LYS E  429  1                                  10
HELIX  139 139 ARG E  435  ARG E  444  1                                  10
HELIX  140 140 VAL E  449  THR E  456  1                                   8
HELIX  141 141 ARG E  460  VAL E  479  1                                  20
HELIX  142 142 ILE E  481  GLY E  483  5                                   3
HELIX  143 143 ALA E  486  ARG E  494  1                                   9
HELIX  144 144 ASP E  499  ALA E  506  1                                   8
HELIX  145 145 GLU E  510  GLN E  519  1                                  10
HELIX  146 146 ILE E  576  ASP E  592  1                                  17
HELIX  147 147 VAL E  606  THR E  608  5                                   3
HELIX  148 148 TYR E  610  THR E  612  5                                   3
HELIX  149 149 LEU E  623  GLU E  633  1                                  11
HELIX  150 150 GLN E  645  ALA E  656  1                                  12
HELIX  151 151 PRO E  666  GLU E  673  1                                   8
HELIX  152 152 ARG E  675  LEU E  685  1                                  11
HELIX  153 153 ALA E  701  ILE E  708  1                                   8
HELIX  154 154 GLU E  731  THR E  740  1                                  10
HELIX  155 155 SER E  789  ASP E  791  5                                   3
HELIX  156 156 GLN E  803  LEU E  820  1                                  18
HELIX  157 157 VAL E  850  THR E  857  1                                   8
HELIX  158 158 LEU E  861  MET E  869  1                                   9
HELIX  159 159 LEU E  874  GLN E  877  1                                   4
HELIX  160 160 PRO E  896  PHE E  900  5                                   5
HELIX  161 161 PHE E  924  GLY E  934  1                                  11
HELIX  162 162 GLU E  951  ASP E  953  5                                   3
HELIX  163 163 ARG E  956  LYS E  966  5                                  11
HELIX  164 164 HIS E  975  ALA E  984  1                                  10
HELIX  165 165 VAL E  994  GLU E  996  5                                   3
HELIX  166 166 ILE E 1001  LYS E 1006  1                                   6
HELIX  167 167 ARG E 1020  GLN E 1035  1                                  16
HELIX  168 168 LEU E 1044  ASN E 1055  1                                  12
HELIX  169 169 VAL E 1065  GLN E 1071  1                                   7
HELIX  170 170 TYR F   39  LEU F   43  1                                   5
HELIX  171 171 PRO F   46  TYR F   48  5                                   3
HELIX  172 172 ASP F   67  ASP F   69  5                                   3
HELIX  173 173 LEU F   98  HIS F  105  1                                   8
HELIX  174 174 THR F  115  LYS F  125  1                                  11
HELIX  175 175 ALA F  140  ALA F  149  1                                  10
HELIX  176 176 ALA F  159  VAL F  162  1                                   4
HELIX  177 177 GLU F  187  GLU F  189  5                                   3
HELIX  178 178 ARG F  203  ARG F  212  1                                  10
HELIX  179 179 ALA F  225  MET F  231  1                                   7
HELIX  180 180 ASP F  249  PHE F  258  1                                  10
HELIX  181 181 LEU F  270  ALA F  278  1                                   9
HELIX  182 182 GLU F  318  THR F  320  5                                   3
HELIX  183 183 ALA F  364  ARG F  378  5                                  15
HELIX  184 184 CYS G   24  GLU G   39  5                                  16
HELIX  185 185 PRO G   58  MET G   60  5                                   3
HELIX  186 186 TRP G   71  GLU G   81  1                                  11
HELIX  187 187 GLY G   92  ARG G  104  1                                  13
HELIX  188 188 VAL G  107  PHE G  111  1                                   5
HELIX  189 189 ALA G  120  GLU G  127  1                                   8
HELIX  190 190 ARG G  129  LYS G  138  1                                  10
HELIX  191 191 MET G  152  VAL G  162  1                                  11
HELIX  192 192 ARG G  185  LEU G  198  1                                  14
HELIX  193 193 THR G  244  ASP G  246  5                                   3
HELIX  194 194 ASP G  258  ILE G  275  1                                  18
HELIX  195 195 ARG G  306  THR G  315  1                                  10
HELIX  196 196 ILE G  319  VAL G  328  1                                  10
HELIX  197 197 ASP G  338  THR G  340  5                                   3
HELIX  198 198 PHE G  364  LYS G  366  5                                   3
HELIX  199 199 GLN G  391  GLY G  401  1                                  11
HELIX  200 200 ALA G  420  LYS G  429  1                                  10
HELIX  201 201 ARG G  435  ARG G  444  1                                  10
HELIX  202 202 VAL G  449  THR G  456  1                                   8
HELIX  203 203 ARG G  460  VAL G  479  1                                  20
HELIX  204 204 ALA G  486  ARG G  494  1                                   9
HELIX  205 205 ASP G  499  ALA G  506  1                                   8
HELIX  206 206 GLU G  510  TYR G  520  1                                  11
HELIX  207 207 ILE G  576  ASP G  592  1                                  17
HELIX  208 208 VAL G  606  THR G  608  5                                   3
HELIX  209 209 TYR G  610  THR G  612  5                                   3
HELIX  210 210 LEU G  623  GLU G  633  1                                  11
HELIX  211 211 GLN G  645  LYS G  649  1                                   5
HELIX  212 212 ALA G  651  ALA G  657  1                                   7
HELIX  213 213 PRO G  666  GLU G  673  1                                   8
HELIX  214 214 ARG G  675  LEU G  685  1                                  11
HELIX  215 215 ILE G  698  ILE G  708  1                                  11
HELIX  216 216 GLU G  731  THR G  740  1                                  10
HELIX  217 217 SER G  789  ASP G  791  5                                   3
HELIX  218 218 GLN G  803  LEU G  820  1                                  18
HELIX  219 219 VAL G  850  THR G  857  1                                   8
HELIX  220 220 LEU G  861  ALA G  870  1                                  10
HELIX  221 221 LEU G  874  GLN G  877  1                                   4
HELIX  222 222 PRO G  896  LYS G  899  5                                   4
HELIX  223 223 PHE G  924  GLY G  934  1                                  11
HELIX  224 224 GLU G  951  ASP G  953  5                                   3
HELIX  225 225 ARG G  956  LYS G  966  5                                  11
HELIX  226 226 HIS G  975  ALA G  984  1                                  10
HELIX  227 227 VAL G  994  GLU G  996  5                                   3
HELIX  228 228 ILE G 1001  LYS G 1006  1                                   6
HELIX  229 229 ARG G 1020  GLN G 1035  1                                  16
HELIX  230 230 LEU G 1044  ASN G 1055  1                                  12
HELIX  231 231 VAL G 1065  ALA G 1070  1                                   6
HELIX  232 232 TYR H   39  LEU H   43  1                                   5
HELIX  233 233 PRO H   46  TYR H   48  5                                   3
HELIX  234 234 ASP H   67  ASP H   69  5                                   3
HELIX  235 235 LEU H   98  ARG H  104  1                                   7
HELIX  236 236 THR H  115  LYS H  125  1                                  11
HELIX  237 237 ALA H  140  ALA H  149  1                                  10
HELIX  238 238 ALA H  159  VAL H  162  1                                   4
HELIX  239 239 GLU H  187  GLU H  189  5                                   3
HELIX  240 240 ARG H  203  ARG H  212  1                                  10
HELIX  241 241 LEU H  229  MET H  231  5                                   3
HELIX  242 242 ASP H  249  GLU H  260  1                                  12
HELIX  243 243 LEU H  270  SER H  279  1                                  10
HELIX  244 244 GLU H  318  THR H  320  5                                   3
HELIX  245 245 HIS H  361  ARG H  378  5                                  18
SHEET    1   A 5 THR A 114  ILE A 116  0
SHEET    2   A 5 ALA A  85  LEU A  87  1  N  VAL A  86   O  THR A 114
SHEET    3   A 5 SER A   9  LEU A  13  1  N  LEU A  11   O  ALA A  85
SHEET    4   A 5 ARG A  43  VAL A  47  1  N  ARG A  43   O  ILE A  10
SHEET    5   A 5 ALA A  63  TYR A  65  1  N  ALA A  63   O  ASN A  46
SHEET    1   B 4 SER A 146  ALA A 149  0
SHEET    2   B 4 LEU A 204  GLU A 208 -1  N  ILE A 206   O  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  N  ALA A 182   O  CYS A 166
SHEET    1   C 4 CYS A 228  GLU A 235  0
SHEET    2   C 4 LYS A 214  ARG A 222 -1  N  VAL A 221   O  ILE A 229
SHEET    3   C 4 GLY A 280  ASN A 289 -1  N  VAL A 288   O  LYS A 214
SHEET    4   C 4 ARG A 294  ASN A 301 -1  N  ASN A 301   O  ASN A 283
SHEET    1   D 3 THR A 249  ALA A 251  0
SHEET    2   D 3 VAL A 355  ARG A 361 -1  N  LYS A 358   O  THR A 249
SHEET    3   D 3 GLY A 382  GLY A 388 -1  N  GLY A 388   O  VAL A 355
SHEET    1   E 2 VAL A 525  ARG A 528  0
SHEET    2   E 2 MET A 543  THR A 546 -1  N  THR A 546   O  VAL A 525
SHEET    1   F 4 GLY A 637  ILE A 639  0
SHEET    2   F 4 LYS A 561  LEU A 565  1  N  MET A 563   O  GLY A 637
SHEET    3   F 4 GLU A 595  ASN A 600  1  N  GLU A 595   O  ILE A 562
SHEET    4   F 4 ARG A 615  PHE A 618  1  N  ARG A 615   O  MET A 598
SHEET    1   G 4 ASN A 692  THR A 694  0
SHEET    2   G 4 LEU A 751  HIS A 754 -1  N  LEU A 752   O  ALA A 693
SHEET    3   G 4 LEU A 712  ARG A 715 -1  N  ARG A 715   O  LEU A 751
SHEET    4   G 4 GLU A 726  VAL A 728 -1  N  VAL A 728   O  LEU A 712
SHEET    1   H 4 VAL A 773  GLU A 780  0
SHEET    2   H 4 VAL A 760  CYS A 768 -1  N  ILE A 767   O  LEU A 774
SHEET    3   H 4 GLY A 824  VAL A 832 -1  N  VAL A 832   O  VAL A 760
SHEET    4   H 4 VAL A 837  ASN A 843 -1  N  ASN A 843   O  ASN A 827
SHEET    1   I 3 CYS A 794  LEU A 796  0
SHEET    2   I 3 TYR A 888  LEU A 895 -1  N  LYS A 891   O  CYS A 794
SHEET    3   I 3 SER A 913  GLY A 921 -1  N  GLY A 921   O  TYR A 888
SHEET    1   J 5 HIS A1039  ASP A1041  0
SHEET    2   J 5 TYR A1012  ASN A1015  1  N  ILE A1013   O  HIS A1039
SHEET    3   J 5 ARG A 944  SER A 948  1  N  LEU A 946   O  TYR A1012
SHEET    4   J 5 GLU A 970  THR A 974  1  N  GLU A 970   O  ALA A 945
SHEET    5   J 5 ARG A 989  VAL A 991  1  N  ARG A 989   O  ALA A 973
SHEET    1   K 7 GLN B  14  ARG B  18  0
SHEET    2   K 7 SER B   4  LEU B   9 -1  N  LEU B   7   O  PHE B  15
SHEET    3   K 7 GLN B 128  ALA B 134 -1  N  ILE B 133   O  LEU B   6
SHEET    4   K 7 GLY B  24  ASN B  33 -1  N  VAL B  30   O  GLN B 128
SHEET    5   K 7 GLN B  51  LEU B  55  1  N  ILE B  52   O  GLU B  29
SHEET    6   K 7 GLY B  79  VAL B  81  1  N  GLY B  79   O  VAL B  53
SHEET    7   K 7 VAL B 108  ILE B 110  1  N  VAL B 108   O  LEU B  80
SHEET    1   L10 TYR B 168  TRP B 170  0
SHEET    2   L10 CYS B 214  VAL B 219 -1  N  ILE B 218   O  TYR B 168
SHEET    3   L10 PHE B 192  TYR B 197  1  N  PHE B 192   O  ARG B 215
SHEET    4   L10 GLY B 235  LEU B 238  1  N  GLY B 235   O  VAL B 195
SHEET    5   L10 VAL B 265  ILE B 268  1  N  PHE B 266   O  ILE B 236
SHEET    6   L10 ALA B 347  PHE B 350  1  N  PHE B 348   O  VAL B 265
SHEET    7   L10 GLY B 339  ARG B 342 -1  N  ILE B 340   O  SER B 349
SHEET    8   L10 LEU B 325  SER B 331 -1  N  HIS B 329   O  GLY B 339
SHEET    9   L10 HIS B 295  ASP B 299 -1  N  LYS B 298   O  LYS B 330
SHEET   10   L10 VAL B 304  THR B 308 -1  N  THR B 308   O  HIS B 295
SHEET    1   M 2 THR B 283  LYS B 285  0
SHEET    2   M 2 PHE B 314  VAL B 316 -1  N  ALA B 315   O  VAL B 284
SHEET    1   N 2 HIS B 290  GLY B 292  0
SHEET    2   N 2 GLN B 310  HIS B 312 -1  N  HIS B 312   O  HIS B 290
SHEET    1   O 5 THR C 114  ILE C 116  0
SHEET    2   O 5 ALA C  85  LEU C  87  1  N  VAL C  86   O  THR C 114
SHEET    3   O 5 SER C   9  LEU C  13  1  N  LEU C  11   O  ALA C  85
SHEET    4   O 5 ARG C  43  VAL C  47  1  N  ARG C  43   O  ILE C  10
SHEET    5   O 5 ALA C  63  TYR C  65  1  N  ALA C  63   O  ASN C  46
SHEET    1   P 4 SER C 146  ALA C 149  0
SHEET    2   P 4 LEU C 204  GLU C 208 -1  N  ILE C 206   O  GLY C 147
SHEET    3   P 4 CYS C 166  PRO C 170 -1  N  ARG C 169   O  LEU C 205
SHEET    4   P 4 GLY C 180  ALA C 182 -1  N  ALA C 182   O  CYS C 166
SHEET    1   Q 4 CYS C 228  GLU C 235  0
SHEET    2   Q 4 LYS C 214  ARG C 222 -1  N  VAL C 221   O  ILE C 229
SHEET    3   Q 4 GLY C 280  ASN C 289 -1  N  VAL C 288   O  LYS C 214
SHEET    4   Q 4 ARG C 294  ASN C 301 -1  N  ASN C 301   O  ASN C 283
SHEET    1   R 3 THR C 249  ALA C 251  0
SHEET    2   R 3 VAL C 355  ARG C 361 -1  N  LYS C 358   O  THR C 249
SHEET    3   R 3 GLY C 382  GLY C 388 -1  N  GLY C 388   O  VAL C 355
SHEET    1   S 2 VAL C 525  ARG C 528  0
SHEET    2   S 2 MET C 543  THR C 546 -1  N  THR C 546   O  VAL C 525
SHEET    1   T 4 GLY C 637  ILE C 639  0
SHEET    2   T 4 LYS C 561  LEU C 565  1  N  MET C 563   O  GLY C 637
SHEET    3   T 4 GLU C 595  VAL C 599  1  N  GLU C 595   O  ILE C 562
SHEET    4   T 4 ARG C 615  TYR C 617  1  N  ARG C 615   O  MET C 598
SHEET    1   U 4 ASN C 692  VAL C 695  0
SHEET    2   U 4 VAL C 750  HIS C 754 -1  N  LEU C 752   O  ALA C 693
SHEET    3   U 4 LEU C 712  ARG C 715 -1  N  ARG C 715   O  LEU C 751
SHEET    4   U 4 GLU C 726  VAL C 728 -1  N  VAL C 728   O  LEU C 712
SHEET    1   V 4 VAL C 773  GLU C 780  0
SHEET    2   V 4 VAL C 760  CYS C 768 -1  N  ILE C 767   O  LEU C 774
SHEET    3   V 4 GLY C 824  LYS C 833 -1  N  VAL C 832   O  VAL C 760
SHEET    4   V 4 GLU C 836  ASN C 843 -1  N  ASN C 843   O  ASN C 827
SHEET    1   W 3 CYS C 794  LEU C 796  0
SHEET    2   W 3 TYR C 888  LEU C 895 -1  N  LYS C 891   O  CYS C 794
SHEET    3   W 3 SER C 913  GLY C 921 -1  N  GLY C 921   O  TYR C 888
SHEET    1   X 5 HIS C1039  ASP C1041  0
SHEET    2   X 5 TYR C1012  ASN C1015  1  N  ILE C1013   O  HIS C1039
SHEET    3   X 5 ARG C 944  SER C 948  1  N  LEU C 946   O  TYR C1012
SHEET    4   X 5 GLU C 970  THR C 974  1  N  GLU C 970   O  ALA C 945
SHEET    5   X 5 ARG C 989  VAL C 991  1  N  ARG C 989   O  ALA C 973
SHEET    1   Y 7 GLN D  14  ARG D  18  0
SHEET    2   Y 7 SER D   4  LEU D   9 -1  N  LEU D   7   O  PHE D  15
SHEET    3   Y 7 GLN D 128  ALA D 134 -1  N  ILE D 133   O  LEU D   6
SHEET    4   Y 7 GLY D  24  ASN D  33 -1  N  VAL D  30   O  GLN D 128
SHEET    5   Y 7 GLN D  51  LEU D  55  1  N  ILE D  52   O  GLU D  29
SHEET    6   Y 7 GLY D  79  VAL D  81  1  N  GLY D  79   O  VAL D  53
SHEET    7   Y 7 VAL D 108  ILE D 110  1  N  VAL D 108   O  LEU D  80
SHEET    1   Z10 TYR D 168  TRP D 170  0
SHEET    2   Z10 CYS D 214  PRO D 220 -1  N  ILE D 218   O  TYR D 168
SHEET    3   Z10 PHE D 192  ASP D 198  1  N  PHE D 192   O  ARG D 215
SHEET    4   Z10 GLY D 235  LEU D 238  1  N  GLY D 235   O  VAL D 195
SHEET    5   Z10 VAL D 265  ILE D 268  1  N  PHE D 266   O  ILE D 236
SHEET    6   Z10 ALA D 347  PHE D 350  1  N  PHE D 348   O  VAL D 265
SHEET    7   Z10 GLY D 339  ARG D 342 -1  N  ILE D 340   O  SER D 349
SHEET    8   Z10 LEU D 325  SER D 331 -1  N  HIS D 329   O  GLY D 339
SHEET    9   Z10 HIS D 295  ASP D 299 -1  N  LYS D 298   O  LYS D 330
SHEET   10   Z10 VAL D 304  THR D 308 -1  N  THR D 308   O  HIS D 295
SHEET    1  AA 2 THR D 283  LYS D 285  0
SHEET    2  AA 2 PHE D 314  VAL D 316 -1  N  ALA D 315   O  VAL D 284
SHEET    1  AB 2 HIS D 290  GLY D 292  0
SHEET    2  AB 2 GLN D 310  HIS D 312 -1  N  HIS D 312   O  HIS D 290
SHEET    1  AC 5 THR E 114  ILE E 116  0
SHEET    2  AC 5 ALA E  85  LEU E  87  1  N  VAL E  86   O  THR E 114
SHEET    3  AC 5 SER E   9  LEU E  13  1  N  LEU E  11   O  ALA E  85
SHEET    4  AC 5 ARG E  43  VAL E  47  1  N  ARG E  43   O  ILE E  10
SHEET    5  AC 5 ALA E  63  TYR E  65  1  N  ALA E  63   O  ASN E  46
SHEET    1  AD 4 SER E 146  ALA E 149  0
SHEET    2  AD 4 LEU E 204  GLU E 208 -1  N  ILE E 206   O  GLY E 147
SHEET    3  AD 4 CYS E 166  PRO E 170 -1  N  ARG E 169   O  LEU E 205
SHEET    4  AD 4 GLY E 180  ALA E 182 -1  N  ALA E 182   O  CYS E 166
SHEET    1  AE 4 CYS E 228  GLU E 235  0
SHEET    2  AE 4 LYS E 214  ARG E 222 -1  N  VAL E 221   O  ILE E 229
SHEET    3  AE 4 GLY E 280  ASN E 289 -1  N  VAL E 288   O  LYS E 214
SHEET    4  AE 4 ARG E 294  ASN E 301 -1  N  ASN E 301   O  ASN E 283
SHEET    1  AF 3 THR E 249  ALA E 251  0
SHEET    2  AF 3 VAL E 355  ARG E 361 -1  N  LYS E 358   O  THR E 249
SHEET    3  AF 3 GLY E 382  GLY E 388 -1  N  GLY E 388   O  VAL E 355
SHEET    1  AG 2 VAL E 525  ARG E 528  0
SHEET    2  AG 2 MET E 543  THR E 546 -1  N  THR E 546   O  VAL E 525
SHEET    1  AH 4 GLY E 637  ILE E 639  0
SHEET    2  AH 4 LYS E 561  LEU E 565  1  N  MET E 563   O  GLY E 637
SHEET    3  AH 4 GLU E 595  ASN E 600  1  N  GLU E 595   O  ILE E 562
SHEET    4  AH 4 ARG E 615  PHE E 618  1  N  ARG E 615   O  MET E 598
SHEET    1  AI 4 ASN E 692  VAL E 695  0
SHEET    2  AI 4 VAL E 750  HIS E 754 -1  N  LEU E 752   O  ALA E 693
SHEET    3  AI 4 LEU E 712  ARG E 715 -1  N  ARG E 715   O  LEU E 751
SHEET    4  AI 4 GLU E 726  VAL E 728 -1  N  VAL E 728   O  LEU E 712
SHEET    1  AJ 4 VAL E 773  GLU E 780  0
SHEET    2  AJ 4 VAL E 760  CYS E 768 -1  N  ILE E 767   O  LEU E 774
SHEET    3  AJ 4 GLY E 824  VAL E 832 -1  N  VAL E 832   O  VAL E 760
SHEET    4  AJ 4 VAL E 837  ASN E 843 -1  N  ASN E 843   O  ASN E 827
SHEET    1  AK 3 CYS E 794  LEU E 796  0
SHEET    2  AK 3 TYR E 888  LEU E 895 -1  N  LYS E 891   O  CYS E 794
SHEET    3  AK 3 SER E 913  GLY E 921 -1  N  GLY E 921   O  TYR E 888
SHEET    1  AL 4 GLU E 970  ALA E 973  0
SHEET    2  AL 4 ARG E 944  SER E 948  1  N  ALA E 945   O  GLU E 970
SHEET    3  AL 4 TYR E1012  ASN E1015  1  N  TYR E1012   O  LEU E 946
SHEET    4  AL 4 HIS E1039  ASP E1041  1  N  HIS E1039   O  ILE E1013
SHEET    1  AM 7 GLN F  14  ARG F  18  0
SHEET    2  AM 7 SER F   4  LEU F   9 -1  N  LEU F   7   O  PHE F  15
SHEET    3  AM 7 GLN F 128  ALA F 134 -1  N  ILE F 133   O  LEU F   6
SHEET    4  AM 7 GLY F  24  ASN F  33 -1  N  VAL F  30   O  GLN F 128
SHEET    5  AM 7 GLN F  51  LEU F  55  1  N  ILE F  52   O  GLU F  29
SHEET    6  AM 7 GLY F  79  VAL F  81  1  N  GLY F  79   O  VAL F  53
SHEET    7  AM 7 VAL F 108  ILE F 110  1  N  VAL F 108   O  LEU F  80
SHEET    1  AN10 TYR F 168  TRP F 170  0
SHEET    2  AN10 CYS F 214  PRO F 220 -1  N  ILE F 218   O  TYR F 168
SHEET    3  AN10 PHE F 192  ASP F 198  1  N  PHE F 192   O  ARG F 215
SHEET    4  AN10 GLY F 235  LEU F 238  1  N  GLY F 235   O  VAL F 195
SHEET    5  AN10 VAL F 265  ILE F 268  1  N  PHE F 266   O  ILE F 236
SHEET    6  AN10 ALA F 347  PHE F 350  1  N  PHE F 348   O  VAL F 265
SHEET    7  AN10 GLY F 339  ARG F 342 -1  N  ILE F 340   O  SER F 349
SHEET    8  AN10 LEU F 325  SER F 331 -1  N  HIS F 329   O  GLY F 339
SHEET    9  AN10 HIS F 295  ASP F 299 -1  N  LYS F 298   O  LYS F 330
SHEET   10  AN10 VAL F 304  THR F 308 -1  N  THR F 308   O  HIS F 295
SHEET    1  AO 2 THR F 283  LYS F 285  0
SHEET    2  AO 2 PHE F 314  VAL F 316 -1  N  ALA F 315   O  VAL F 284
SHEET    1  AP 2 HIS F 290  GLY F 292  0
SHEET    2  AP 2 GLN F 310  HIS F 312 -1  N  HIS F 312   O  HIS F 290
SHEET    1  AQ 5 THR G 114  ILE G 116  0
SHEET    2  AQ 5 ALA G  85  LEU G  87  1  N  VAL G  86   O  THR G 114
SHEET    3  AQ 5 SER G   9  LEU G  13  1  N  LEU G  11   O  ALA G  85
SHEET    4  AQ 5 ARG G  43  VAL G  47  1  N  ARG G  43   O  ILE G  10
SHEET    5  AQ 5 ALA G  63  TYR G  65  1  N  ALA G  63   O  ASN G  46
SHEET    1  AR 4 SER G 146  ALA G 149  0
SHEET    2  AR 4 LEU G 204  GLU G 208 -1  N  ILE G 206   O  GLY G 147
SHEET    3  AR 4 CYS G 166  PRO G 170 -1  N  ARG G 169   O  LEU G 205
SHEET    4  AR 4 GLY G 180  ALA G 182 -1  N  ALA G 182   O  CYS G 166
SHEET    1  AS 4 CYS G 228  GLU G 235  0
SHEET    2  AS 4 LYS G 214  ARG G 222 -1  N  VAL G 221   O  ILE G 229
SHEET    3  AS 4 GLY G 281  ASN G 289 -1  N  VAL G 288   O  LYS G 214
SHEET    4  AS 4 ARG G 294  ASN G 301 -1  N  ASN G 301   O  ASN G 283
SHEET    1  AT 3 THR G 249  ALA G 251  0
SHEET    2  AT 3 VAL G 355  ARG G 361 -1  N  LYS G 358   O  THR G 249
SHEET    3  AT 3 GLY G 382  GLY G 388 -1  N  GLY G 388   O  VAL G 355
SHEET    1  AU 2 VAL G 525  ARG G 528  0
SHEET    2  AU 2 MET G 543  THR G 546 -1  N  THR G 546   O  VAL G 525
SHEET    1  AV 4 GLY G 637  ILE G 639  0
SHEET    2  AV 4 LYS G 561  LEU G 565  1  N  MET G 563   O  GLY G 637
SHEET    3  AV 4 GLU G 595  ASN G 600  1  N  GLU G 595   O  ILE G 562
SHEET    4  AV 4 ARG G 615  PHE G 618  1  N  ARG G 615   O  MET G 598
SHEET    1  AW 3 GLU G 726  VAL G 728  0
SHEET    2  AW 3 LEU G 712  ARG G 715 -1  N  VAL G 714   O  GLU G 726
SHEET    3  AW 3 LEU G 751  HIS G 754 -1  N  ASP G 753   O  VAL G 713
SHEET    1  AX 4 VAL G 773  GLU G 780  0
SHEET    2  AX 4 VAL G 760  CYS G 768 -1  N  ILE G 767   O  LEU G 774
SHEET    3  AX 4 GLY G 824  VAL G 832 -1  N  VAL G 832   O  VAL G 760
SHEET    4  AX 4 VAL G 837  ASN G 843 -1  N  ASN G 843   O  ASN G 827
SHEET    1  AY 3 CYS G 794  LEU G 796  0
SHEET    2  AY 3 TYR G 888  LEU G 895 -1  N  LYS G 891   O  CYS G 794
SHEET    3  AY 3 SER G 913  GLY G 921 -1  N  GLY G 921   O  TYR G 888
SHEET    1  AZ 5 HIS G1039  ASP G1041  0
SHEET    2  AZ 5 TYR G1012  ASN G1015  1  N  ILE G1013   O  HIS G1039
SHEET    3  AZ 5 ARG G 944  SER G 948  1  N  LEU G 946   O  TYR G1012
SHEET    4  AZ 5 GLU G 970  THR G 974  1  N  GLU G 970   O  ALA G 945
SHEET    5  AZ 5 ARG G 989  VAL G 991  1  N  ARG G 989   O  ALA G 973
SHEET    1  BA 6 GLN H  14  ARG H  18  0
SHEET    2  BA 6 SER H   4  LEU H   9 -1  N  LEU H   7   O  PHE H  15
SHEET    3  BA 6 GLN H 128  GLY H 135 -1  N  GLY H 135   O  SER H   4
SHEET    4  BA 6 GLY H  24  ASN H  33 -1  N  VAL H  30   O  GLN H 128
SHEET    5  BA 6 GLN H  51  LEU H  55  1  N  ILE H  52   O  GLU H  29
SHEET    6  BA 6 GLY H  79  VAL H  81  1  N  GLY H  79   O  VAL H  53
SHEET    1  BB10 TYR H 168  TRP H 170  0
SHEET    2  BB10 CYS H 214  VAL H 219 -1  N  ILE H 218   O  TYR H 168
SHEET    3  BB10 PHE H 192  TYR H 197  1  N  PHE H 192   O  ARG H 215
SHEET    4  BB10 GLY H 235  LEU H 238  1  N  GLY H 235   O  VAL H 195
SHEET    5  BB10 VAL H 265  ILE H 268  1  N  PHE H 266   O  ILE H 236
SHEET    6  BB10 ALA H 347  PHE H 350  1  N  PHE H 348   O  VAL H 265
SHEET    7  BB10 GLY H 339  ARG H 342 -1  N  ILE H 340   O  SER H 349
SHEET    8  BB10 LEU H 325  SER H 331 -1  N  HIS H 329   O  GLY H 339
SHEET    9  BB10 HIS H 295  ASP H 299 -1  N  LYS H 298   O  LYS H 330
SHEET   10  BB10 VAL H 304  THR H 308 -1  N  THR H 308   O  HIS H 295
SHEET    1  BC 2 THR H 283  LYS H 285  0
SHEET    2  BC 2 PHE H 314  VAL H 316 -1  N  ALA H 315   O  VAL H 284
SHEET    1  BD 2 HIS H 290  GLY H 292  0
SHEET    2  BD 2 GLN H 310  HIS H 312 -1  N  HIS H 312   O  HIS H 290
LINK         O   GLY A 112                 K     K A5015     1555   1555  2.93
LINK         OE2 GLU A 127                 K     K A5004     1555   1555  2.92
LINK         OE1 GLU A 215                 K     K A5003     1555   1555  2.45
LINK         OE1 GLU A 217                 K     K A5005     1555   1555  2.87
LINK         OD1 ASN A 236                 K     K A5003     1555   1555  2.83
LINK         O   ASP A 238                 K     K A5003     1555   1555  2.81
LINK         O   ILE A 242                 K     K A5003     1555   1555  2.63
LINK         OG  SER A 247                 K     K A5003     1555   1555  2.68
LINK         OE1 GLN A 285                MN    MN A5002     1555   1555  2.06
LINK         CD  GLU A 299                MN    MN A5001     1555   1555  2.57
LINK         OE1 GLU A 299                 K     K A5004     1555   1555  2.89
LINK         OE1 GLU A 299                MN    MN A5001     1555   1555  2.26
LINK         OE2 GLU A 299                MN    MN A5002     1555   1555  2.42
LINK         OE2 GLU A 299                MN    MN A5001     1555   1555  2.30
LINK         O   MET A 300                 K     K A5004     1555   1555  2.57
LINK         OD1 ASN A 301                MN    MN A5001     1555   1555  1.94
LINK         OE1 GLU A 761                 K     K A5010     1555   1555  2.55
LINK         ND1 HIS A 781                 K     K A5010     1555   1555  2.68
LINK         O   GLU A 783                 K     K A5010     1555   1555  2.79
LINK         O   GLN A 784                 K     K A5010     1555   1555  2.84
LINK         O   VAL A 787                 K     K A5010     1555   1555  2.67
LINK         OG  SER A 792                 K     K A5010     1555   1555  2.70
LINK         OE1 GLN A 829                MN    MN A5008     1555   1555  2.12
LINK         OE1 GLU A 841                 K     K A5009     1555   1555  2.90
LINK         OE2 GLU A 841                MN    MN A5008     1555   1555  2.28
LINK         OE2 GLU A 841                 K     K A5009     1555   1555  2.51
LINK         O   HIS B  16                 K     K B5019     1555   1555  2.85
LINK         O   ASP B 112                 K     K B5019     1555   1555  2.64
LINK         O   ASP C  84                 K     K C5035     1555   1555  2.85
LINK         O   GLY C 112                 K     K C5035     1555   1555  2.82
LINK         OG1 THR C 114                 K     K C5035     1555   1555  2.64
LINK         OE2 GLU C 127                 K     K C5024     1555   1555  2.77
LINK         OE1 GLU C 215                 K     K C5023     1555   1555  2.79
LINK         OD1 ASN C 236                 K     K C5023     1555   1555  2.87
LINK         O   ASP C 238                 K     K C5023     1555   1555  2.45
LINK         O   ALA C 239                 K     K C5023     1555   1555  2.83
LINK         O   ILE C 242                 K     K C5023     1555   1555  2.69
LINK         OG  SER C 247                 K     K C5023     1555   1555  2.59
LINK         OE1 GLN C 285                 K     K C5025     1555   1555  2.53
LINK         OE1 GLN C 285                MN    MN C5022     1555   1555  2.23
LINK         CD  GLU C 299                MN    MN C5021     1555   1555  2.53
LINK         OE1 GLU C 299                MN    MN C5021     1555   1555  2.10
LINK         OE1 GLU C 299                 K     K C5024     1555   1555  2.77
LINK         OE2 GLU C 299                MN    MN C5022     1555   1555  2.24
LINK         OE2 GLU C 299                MN    MN C5021     1555   1555  2.37
LINK         O   MET C 300                 K     K C5024     1555   1555  2.63
LINK         OD1 ASN C 301                MN    MN C5021     1555   1555  2.12
LINK         OE1 GLU C 761                 K     K C5030     1555   1555  2.57
LINK         ND1 HIS C 781                 K     K C5030     1555   1555  2.71
LINK         O   GLU C 783                 K     K C5030     1555   1555  2.77
LINK         O   GLN C 784                 K     K C5030     1555   1555  2.80
LINK         O   VAL C 787                 K     K C5030     1555   1555  2.81
LINK         OG  SER C 792                 K     K C5030     1555   1555  2.87
LINK         OE1 GLN C 829                MN    MN C5028     1555   1555  2.04
LINK         OE2 GLU C 841                 K     K C5029     1555   1555  2.64
LINK         OE2 GLU C 841                MN    MN C5028     1555   1555  2.40
LINK         O   HIS D  16                 K     K D5039     1555   1555  2.81
LINK         O   ASP D 112                 K     K D5039     1555   1555  2.76
LINK         O   ASP E  84                 K     K E5055     1555   1555  2.73
LINK         O   GLY E 112                 K     K E5055     1555   1555  2.88
LINK         OG1 THR E 114                 K     K E5055     1555   1555  2.83
LINK         OE2 GLU E 127                 K     K E5044     1555   1555  2.72
LINK         OE1 GLU E 215                 K     K E5043     1555   1555  2.39
LINK         OE1 GLU E 217                 K     K E5045     1555   1555  2.74
LINK         OD1 ASN E 236                 K     K E5043     1555   1555  2.74
LINK         O   ASP E 238                 K     K E5043     1555   1555  2.79
LINK         O   ALA E 239                 K     K E5043     1555   1555  2.74
LINK         O   ILE E 242                 K     K E5043     1555   1555  2.53
LINK         OG  SER E 247                 K     K E5043     1555   1555  2.71
LINK         OE1 GLN E 285                MN    MN E5042     1555   1555  2.15
LINK         OE1 GLN E 285                 K     K E5045     1555   1555  2.63
LINK         CD  GLU E 299                MN    MN E5041     1555   1555  2.63
LINK         OE1 GLU E 299                 K     K E5044     1555   1555  2.69
LINK         OE1 GLU E 299                MN    MN E5041     1555   1555  2.28
LINK         OE2 GLU E 299                MN    MN E5042     1555   1555  2.25
LINK         OE2 GLU E 299                MN    MN E5041     1555   1555  2.35
LINK         O   MET E 300                 K     K E5044     1555   1555  2.64
LINK         OD1 ASN E 301                MN    MN E5041     1555   1555  2.28
LINK         OE1 GLU E 761                 K     K E5050     1555   1555  2.71
LINK         ND1 HIS E 781                 K     K E5050     1555   1555  2.77
LINK         O   GLN E 784                 K     K E5050     1555   1555  2.92
LINK         O   VAL E 787                 K     K E5050     1555   1555  2.58
LINK         OG  SER E 792                 K     K E5050     1555   1555  2.68
LINK         OE1 GLN E 829                MN    MN E5048     1555   1555  2.05
LINK         OE1 GLU E 841                 K     K E5049     1555   1555  2.76
LINK         OE2 GLU E 841                MN    MN E5048     1555   1555  2.02
LINK         O   HIS F  16                 K     K F5059     1555   1555  2.83
LINK         O   ASP F 112                 K     K F5059     1555   1555  2.92
LINK         O   ASP G  84                 K     K G5075     1555   1555  2.93
LINK         O   GLY G 112                 K     K G5075     1555   1555  2.66
LINK         OE2 GLU G 127                 K     K G5064     1555   1555  2.76
LINK         OE1 GLU G 215                 K     K G5063     1555   1555  2.45
LINK         OD1 ASN G 236                 K     K G5063     1555   1555  2.93
LINK         O   ASP G 238                 K     K G5063     1555   1555  2.84
LINK         O   ALA G 239                 K     K G5063     1555   1555  2.69
LINK         O   ILE G 242                 K     K G5063     1555   1555  2.58
LINK         OG  SER G 247                 K     K G5063     1555   1555  2.63
LINK         OE1 GLN G 285                 K     K G5065     1555   1555  2.53
LINK         OE1 GLN G 285                MN    MN G5062     1555   1555  2.20
LINK         CD  GLU G 299                MN    MN G5061     1555   1555  2.66
LINK         OE1 GLU G 299                 K     K G5064     1555   1555  2.91
LINK         OE1 GLU G 299                MN    MN G5061     1555   1555  2.34
LINK         OE2 GLU G 299                MN    MN G5062     1555   1555  2.21
LINK         OE2 GLU G 299                MN    MN G5061     1555   1555  2.34
LINK         O   MET G 300                 K     K G5064     1555   1555  2.84
LINK         OD1 ASN G 301                MN    MN G5061     1555   1555  2.06
LINK         OE1 GLU G 761                 K     K G5070     1555   1555  2.42
LINK         ND1 HIS G 781                 K     K G5070     1555   1555  2.92
LINK         O   GLU G 783                 K     K G5070     1555   1555  2.78
LINK         O   GLN G 784                 K     K G5070     1555   1555  2.80
LINK         O   VAL G 787                 K     K G5070     1555   1555  2.58
LINK         OG  SER G 792                 K     K G5070     1555   1555  2.87
LINK         OE1 GLN G 829                MN    MN G5068     1555   1555  2.54
LINK         OE1 GLU G 841                 K     K G5069     1555   1555  2.59
LINK         OE2 GLU G 841                MN    MN G5068     1555   1555  1.78
LINK         OD1 ASN G 843                 K     K G5069     1555   1555  2.77
LINK         O   ASP H 112                 K     K H5079     1555   1555  2.84
LINK        MN    MN A5001                 O3B ADP A5000     1555   1555  2.11
LINK        MN    MN A5001                 O1  PO4 A5006     1555   1555  2.07
LINK        MN    MN A5001                 O   HOH A5623     1555   1555  1.92
LINK        MN    MN A5002                 O1B ADP A5000     1555   1555  2.13
LINK        MN    MN A5002                 O1A ADP A5000     1555   1555  2.05
LINK        MN    MN A5002                 O   HOH A5611     1555   1555  2.08
LINK        MN    MN A5002                 O3  PO4 A5006     1555   1555  2.05
LINK         K     K A5004                 O   HOH A5108     1555   1555  2.71
LINK         K     K A5005                 O3  PO4 A5006     1555   1555  2.86
LINK         K     K A5005                 O   HOH A5225     1555   1555  2.76
LINK        MN    MN A5008                 O2A ADP A5007     1555   1555  2.05
LINK        MN    MN A5008                 O3B ADP A5007     1555   1555  2.09
LINK         K     K A5009                 O2B ADP A5007     1555   1555  2.59
LINK        MN    MN C5021                 O3B ADP C5020     1555   1555  2.06
LINK        MN    MN C5021                 O1  PO4 C5026     1555   1555  2.04
LINK        MN    MN C5021                 O   HOH C5662     1555   1555  1.94
LINK        MN    MN C5022                 O   HOH C5629     1555   1555  2.22
LINK        MN    MN C5022                 O1A ADP C5020     1555   1555  2.09
LINK        MN    MN C5022                 O1B ADP C5020     1555   1555  2.22
LINK        MN    MN C5022                 O3  PO4 C5026     1555   1555  1.97
LINK         K     K C5024                 O   HOH C5128     1555   1555  2.86
LINK         K     K C5024                 O   HOH C5663     1555   1555  2.74
LINK        MN    MN C5028                 O3B ADP C5027     1555   1555  2.16
LINK        MN    MN C5028                 O2A ADP C5027     1555   1555  2.14
LINK         K     K C5029                 O2B ADP C5027     1555   1555  2.89
LINK        MN    MN E5041                 O3B ADP E5040     1555   1555  2.11
LINK        MN    MN E5041                 O   HOH E5686     1555   1555  2.01
LINK        MN    MN E5041                 O1  PO4 E5046     1555   1555  1.96
LINK        MN    MN E5042                 O1B ADP E5040     1555   1555  2.11
LINK        MN    MN E5042                 O   HOH E5681     1555   1555  2.34
LINK        MN    MN E5042                 O1A ADP E5040     1555   1555  2.11
LINK        MN    MN E5042                 O3  PO4 E5046     1555   1555  2.00
LINK         K     K E5045                 O3  PO4 E5046     1555   1555  2.92
LINK        MN    MN E5048                 O2A ADP E5047     1555   1555  2.11
LINK        MN    MN E5048                 O3B ADP E5047     1555   1555  2.20
LINK         K     K E5049                 O2B ADP E5047     1555   1555  2.66
LINK        MN    MN G5061                 O   HOH G5704     1555   1555  2.18
LINK        MN    MN G5061                 O1  PO4 G5066     1555   1555  1.91
LINK        MN    MN G5061                 O3B ADP G5060     1555   1555  2.07
LINK        MN    MN G5062                 O3  PO4 G5066     1555   1555  1.96
LINK        MN    MN G5062                 O   HOH G5694     1555   1555  2.07
LINK        MN    MN G5062                 O1A ADP G5060     1555   1555  2.00
LINK        MN    MN G5062                 O1B ADP G5060     1555   1555  2.10
LINK         K     K G5064                 O   HOH G5182     1555   1555  2.91
LINK         K     K G5065                 O   HOH G5298     1555   1555  2.79
LINK         K     K G5065                 O3  PO4 G5066     1555   1555  2.83
LINK        MN    MN G5068                 O3B ADP G5067     1555   1555  2.35
LINK        MN    MN G5068                 O2A ADP G5067     1555   1555  2.09
LINK         K     K G5069                 O2B ADP G5067     1555   1555  2.74
LINK         O   ASP A  84                 K     K A5015     1555   1555  2.95
LINK         O   ALA A 239                 K     K A5003     1555   1555  2.93
LINK         OE1 GLN A 285                 K     K A5005     1555   1555  2.94
LINK         OE1 GLU C 217                 K     K C5025     1555   1555  2.96
LINK         OE1 GLU C 841                 K     K C5029     1555   1555  2.97
LINK         O   GLU E 783                 K     K E5050     1555   1555  2.98
LINK         OD1 ASN G 283                 K     K G5065     1555   1555  2.95
LINK         K     K A5009                 O3B ADP A5007     1555   1555  2.94
LINK         K     K C5025                 O3  PO4 C5026     1555   1555  2.94
LINK         K     K C5025                 O   HOH C5244     1555   1555  2.96
LINK         K     K D5039                 O   HOH C5319     1555   1555  2.96
LINK         K     K E5044                 O   HOH E5153     1555   1555  2.97
LINK         K     K E5045                 O   HOH E5269     1555   1555  2.97
CISPEP   1 PHE A  164    PRO A  165          0        -3.29
CISPEP   2 ALA A  251    PRO A  252          0         0.63
CISPEP   3 TYR A  710    PRO A  711          0         0.52
CISPEP   4 LEU A  796    PRO A  797          0         0.31
CISPEP   5 ARG A  998    PRO A  999          0         4.45
CISPEP   6 PHE C  164    PRO C  165          0        -1.35
CISPEP   7 ALA C  251    PRO C  252          0         1.55
CISPEP   8 TYR C  710    PRO C  711          0        -1.61
CISPEP   9 LEU C  796    PRO C  797          0         1.51
CISPEP  10 ARG C  998    PRO C  999          0        -5.21
CISPEP  11 SER D  357    PRO D  358          0         1.75
CISPEP  12 PHE E  164    PRO E  165          0         0.66
CISPEP  13 ALA E  251    PRO E  252          0        -0.94
CISPEP  14 TYR E  710    PRO E  711          0         1.89
CISPEP  15 LEU E  796    PRO E  797          0         1.55
CISPEP  16 ARG E  998    PRO E  999          0       -10.68
CISPEP  17 PHE G  164    PRO G  165          0        -0.83
CISPEP  18 ALA G  251    PRO G  252          0         2.83
CISPEP  19 TYR G  710    PRO G  711          0        -0.79
CISPEP  20 LEU G  796    PRO G  797          0        -5.24
CISPEP  21 ARG G  998    PRO G  999          0        -3.33
SITE     1 AC1  6 GLU A 299  ASN A 301  ADP A5000   MN A5002
SITE     2 AC1  6 PO4 A5006  HOH A5623
SITE     1 AC2  6 GLN A 285  GLU A 299  ADP A5000   MN A5001
SITE     2 AC2  6 PO4 A5006  HOH A5611
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  6 ALA A 126  GLU A 127  GLU A 299  MET A 300
SITE     2 AC4  6 ASN A 301  HOH A5108
SITE     1 AC5  6 GLU A 217  THR A 244  ASN A 283  GLN A 285
SITE     2 AC5  6 PO4 A5006  HOH A5225
SITE     1 AC6  3 GLN A 829  GLU A 841  ADP A5007
SITE     1 AC7  3 GLU A 841  ASN A 843  ADP A5007
SITE     1 AC8  6 GLU A 761  HIS A 781  GLU A 783  GLN A 784
SITE     2 AC8  6 VAL A 787  SER A 792
SITE     1 AC9  3 ASP A  84  GLY A 112  THR A 114
SITE     1 BC1  4 GLN A  93  THR A 173  MET A 174  HOH A5073
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 A5582
SITE     1 BC4  2 HIS B  16  ASP B 112
SITE     1 BC5  6 GLU C 299  ASN C 301  ADP C5020   MN C5022
SITE     2 BC5  6 PO4 C5026  HOH C5662
SITE     1 BC6  7 GLN C 285  GLU C 299  ADP C5020   MN C5021
SITE     2 BC6  7   K C5025  PO4 C5026  HOH C5629
SITE     1 BC7  6 GLU C 215  ASN C 236  ASP C 238  ALA C 239
SITE     2 BC7  6 ILE C 242  SER C 247
SITE     1 BC8  7 ALA C 126  GLU C 127  GLU C 299  MET C 300
SITE     2 BC8  7 ASN C 301  HOH C5128  HOH C5663
SITE     1 BC9  7 GLU C 217  THR C 244  ASN C 283  GLN C 285
SITE     2 BC9  7  MN C5022  PO4 C5026  HOH C5244
SITE     1 CC1  3 GLN C 829  GLU C 841  ADP C5027
SITE     1 CC2  3 GLU C 841  ASN C 843  ADP C5027
SITE     1 CC3  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784
SITE     2 CC3  6 VAL C 787  SER C 792
SITE     1 CC4  4 ASP C  84  GLY C 112  THR C 114  HOH C5043
SITE     1 CC5  1 MET C 174
SITE     1 CC6  3 ASN C 289  ASN C 292  ARG C 294
SITE     1 CC7  5 ALA C 370  ASN C 371  PHE C 900  PRO C 901
SITE     2 CC7  5 GLY C 902
SITE     1 CC8  4 HOH C5319  HIS D  16  ASP D 112  HOH D1873
SITE     1 CC9  6 GLU E 299  ASN E 301  ADP E5040   MN E5042
SITE     2 CC9  6 PO4 E5046  HOH E5686
SITE     1 DC1  7 GLN E 285  GLU E 299  ADP E5040   MN E5041
SITE     2 DC1  7   K E5045  PO4 E5046  HOH E5681
SITE     1 DC2  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239
SITE     2 DC2  6 ILE E 242  SER E 247
SITE     1 DC3  7 ALA E 126  GLU E 127  GLU E 299  MET E 300
SITE     2 DC3  7 ASN E 301  HOH E5153  HOH E5686
SITE     1 DC4  7 GLU E 217  THR E 244  ASN E 283  GLN E 285
SITE     2 DC4  7  MN E5042  PO4 E5046  HOH E5269
SITE     1 DC5  4 SER E 789  GLN E 829  GLU E 841  ADP E5047
SITE     1 DC6  3 GLU E 841  ASN E 843  ADP E5047
SITE     1 DC7  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784
SITE     2 DC7  6 VAL E 787  SER E 792
SITE     1 DC8  3 ASP E  84  GLY E 112  THR E 114
SITE     1 DC9  5 GLN E  93  THR E 173  MET E 174  HOH E5098
SITE     2 DC9  5 HOH E5118
SITE     1 EC1  3 ASN E 289  ASN E 292  ARG E 294
SITE     1 EC2  5 ALA E 370  ASN E 371  PHE E 900  PRO E 901
SITE     2 EC2  5 GLY E 902
SITE     1 EC3  5 ARG E 490  HOH E5341  HIS F  16  ASP F 112
SITE     2 EC3  5 HOH F2962
SITE     1 EC4  6 GLU G 299  ASN G 301  ADP G5060   MN G5062
SITE     2 EC4  6 PO4 G5066  HOH G5704
SITE     1 EC5  7 HIS G 243  GLN G 285  GLU G 299  ADP G5060
SITE     2 EC5  7  MN G5061  PO4 G5066  HOH G5694
SITE     1 EC6  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239
SITE     2 EC6  6 ILE G 242  SER G 247
SITE     1 EC7  6 ALA G 126  GLU G 127  GLU G 299  MET G 300
SITE     2 EC7  6 ASN G 301  HOH G5182
SITE     1 EC8  6 GLU G 217  THR G 244  ASN G 283  GLN G 285
SITE     2 EC8  6 PO4 G5066  HOH G5298
SITE     1 EC9  3 GLN G 829  GLU G 841  ADP G5067
SITE     1 FC1  3 GLU G 841  ASN G 843  ADP G5067
SITE     1 FC2  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784
SITE     2 FC2  6 VAL G 787  SER G 792
SITE     1 FC3  4 ASP G  84  GLY G 112  THR G 114  HOH G5713
SITE     1 FC4  3 GLN G  93  THR G 173  MET G 174
SITE     1 FC5  3 ASN G 289  ASN G 292  ARG G 294
SITE     1 FC6  5 ALA G 370  ASN G 371  PHE G 900  PRO G 901
SITE     2 FC6  5 GLY G 902
SITE     1 FC7  3 HIS H  16  ASP H 112  HOH H3446
SITE     1 FC8 14 MET A 174  GLY A 175  HIS A 243  GLN A 285
SITE     2 FC8 14 GLU A 299  ASN A 301  ARG A 303  ARG A 306
SITE     3 FC8 14 ADP A5000   MN A5001   MN A5002    K A5005
SITE     4 FC8 14 HOH A5056  HOH A5225
SITE     1 FC9 14 MET C 174  GLY C 175  HIS C 243  GLN C 285
SITE     2 FC9 14 GLU C 299  ASN C 301  ARG C 303  ARG C 306
SITE     3 FC9 14 ADP C5020   MN C5021   MN C5022    K C5025
SITE     4 FC9 14 HOH C5076  HOH C5244
SITE     1 GC1 12 MET E 174  GLY E 175  HIS E 243  GLN E 285
SITE     2 GC1 12 GLU E 299  ASN E 301  ARG E 303  ARG E 306
SITE     3 GC1 12 ADP E5040   MN E5041   MN E5042    K E5045
SITE     1 GC2 15 MET G 174  GLY G 175  HIS G 243  GLN G 285
SITE     2 GC2 15 GLU G 299  ASN G 301  ARG G 303  ARG G 306
SITE     3 GC2 15 ADP G5060   MN G5061   MN G5062    K G5065
SITE     4 GC2 15 HOH G5130  HOH G5298  HOH G5694
SITE     1 GC3 25 ARG A 129  ILE A 167  ARG A 169  MET A 174
SITE     2 GC3 25 GLY A 175  GLY A 176  GLU A 208  LEU A 210
SITE     3 GC3 25 ILE A 211  GLU A 215  MET A 240  GLY A 241
SITE     4 GC3 25 ILE A 242  HIS A 243  THR A 244  GLN A 285
SITE     5 GC3 25 ILE A 298  GLU A 299  THR A 376   MN A5001
SITE     6 GC3 25  MN A5002  PO4 A5006  HOH A5445  HOH A5611
SITE     7 GC3 25 HOH A5623
SITE     1 GC4 17 PRO A 690  ARG A 715  HIS A 754  PHE A 755
SITE     2 GC4 17 LEU A 756  GLU A 761  ALA A 785  GLY A 786
SITE     3 GC4 17 VAL A 787  HIS A 788  SER A 789  GLN A 829
SITE     4 GC4 17 GLU A 841   MN A5008    K A5009  HOH A5627
SITE     5 GC4 17 HOH A5628
SITE     1 GC5  9 GLU A 783  ASP A 791  GLU A 892  LEU A 907
SITE     2 GC5  9 TYR A1040  ASP A1041  THR A1042  HOH A5097
SITE     3 GC5  9 HOH A5321
SITE     1 GC6 16 SER A 948  VAL A 949  LYS A 954  THR A 974
SITE     2 GC6 16 GLY A 976  THR A 977  LYS A 993  VAL A 994
SITE     3 GC6 16 ILE A1001  ASN A1015  THR A1016  THR A1017
SITE     4 GC6 16 ASP A1025  SER A1026  VAL A1028  HOH A5379
SITE     1 GC7  2 GLN A  22  THR A  94
SITE     1 GC8  8 ARG A 528  ALA A 537  THR A 538  GLU A 552
SITE     2 GC8  8 ASN A 554  HOH A5294  ARG B 120  ARG B 123
SITE     1 GC9 27 ARG C 129  ILE C 167  ARG C 169  THR C 173
SITE     2 GC9 27 MET C 174  GLY C 175  GLY C 176  GLU C 208
SITE     3 GC9 27 LEU C 210  ILE C 211  GLU C 215  MET C 240
SITE     4 GC9 27 GLY C 241  ILE C 242  HIS C 243  THR C 244
SITE     5 GC9 27 GLN C 285  ILE C 298  GLU C 299  THR C 376
SITE     6 GC9 27  MN C5021   MN C5022  PO4 C5026  HOH C5462
SITE     7 GC9 27 HOH C5629  HOH C5662  HOH C5762
SITE     1 HC1 14 ARG C 715  HIS C 754  PHE C 755  LEU C 756
SITE     2 HC1 14 GLU C 761  ALA C 785  GLY C 786  VAL C 787
SITE     3 HC1 14 HIS C 788  SER C 789  GLN C 829  GLU C 841
SITE     4 HC1 14  MN C5028    K C5029
SITE     1 HC2 10 GLU C 783  ASP C 791  GLU C 892  VAL C 893
SITE     2 HC2 10 LEU C 907  TYR C1040  ASP C1041  THR C1042
SITE     3 HC2 10 HOH C5117  HOH C5339
SITE     1 HC3 16 SER C 948  VAL C 949  LYS C 954  THR C 974
SITE     2 HC3 16 GLY C 976  THR C 977  LYS C 993  VAL C 994
SITE     3 HC3 16 ILE C1001  ASN C1015  THR C1016  THR C1017
SITE     4 HC3 16 ASP C1025  SER C1026  VAL C1028  HOH C5398
SITE     1 HC4  4 THR C  94  ASN C  97  ASN C 936  HOH C5070
SITE     1 HC5 10 ARG C 528  ALA C 537  THR C 538  GLU C 552
SITE     2 HC5 10 ASN C 554  HOH C5689  HOH C5713  ARG D 120
SITE     3 HC5 10 ARG D 123  HOH D1337
SITE     1 HC6 27 ARG E 129  ILE E 167  ARG E 169  THR E 173
SITE     2 HC6 27 MET E 174  GLY E 175  GLY E 176  GLU E 208
SITE     3 HC6 27 LEU E 210  ILE E 211  GLU E 215  MET E 240
SITE     4 HC6 27 GLY E 241  ILE E 242  HIS E 243  THR E 244
SITE     5 HC6 27 GLN E 285  ILE E 298  GLU E 299  THR E 376
SITE     6 HC6 27  MN E5041   MN E5042  PO4 E5046  HOH E5505
SITE     7 HC6 27 HOH E5681  HOH E5686  HOH E5687
SITE     1 HC7 15 ARG E 715  HIS E 754  PHE E 755  LEU E 756
SITE     2 HC7 15 GLU E 761  ALA E 785  GLY E 786  VAL E 787
SITE     3 HC7 15 HIS E 788  SER E 789  GLN E 829  GLU E 841
SITE     4 HC7 15 PRO E 909   MN E5048    K E5049
SITE     1 HC8 11 GLU E 783  ASP E 791  GLU E 892  VAL E 893
SITE     2 HC8 11 LEU E 907  TYR E1040  ASP E1041  THR E1042
SITE     3 HC8 11 HOH E5142  HOH E5361  HOH E5697
SITE     1 HC9 17 SER E 948  LYS E 954  THR E 974  GLY E 976
SITE     2 HC9 17 THR E 977  LYS E 993  VAL E 994  ILE E1001
SITE     3 HC9 17 ASN E1015  THR E1016  THR E1017  ASP E1025
SITE     4 HC9 17 SER E1026  VAL E1028  HOH E5420  HOH E5702
SITE     5 HC9 17 HOH E5703
SITE     1 IC1  4 GLN E  22  GLN E  93  THR E  94  ASN E 936
SITE     1 IC2 11 ARG E 528  ALA E 537  THR E 538  GLU E 552
SITE     2 IC2 11 ASN E 554  HOH E5333  HOH E5785  HOH E5789
SITE     3 IC2 11 HOH E5880  ARG F 120  ARG F 123
SITE     1 IC3 26 ARG G 129  ILE G 167  ARG G 169  THR G 173
SITE     2 IC3 26 MET G 174  GLY G 175  GLY G 176  GLU G 208
SITE     3 IC3 26 LEU G 210  ILE G 211  GLU G 215  MET G 240
SITE     4 IC3 26 GLY G 241  ILE G 242  HIS G 243  THR G 244
SITE     5 IC3 26 GLN G 285  ILE G 298  GLU G 299  THR G 376
SITE     6 IC3 26  MN G5061   MN G5062  PO4 G5066  HOH G5513
SITE     7 IC3 26 HOH G5694  HOH G5704
SITE     1 IC4 15 ARG G 715  HIS G 754  PHE G 755  LEU G 756
SITE     2 IC4 15 GLU G 761  ALA G 785  GLY G 786  VAL G 787
SITE     3 IC4 15 HIS G 788  SER G 789  GLN G 829  GLU G 841
SITE     4 IC4 15  MN G5068    K G5069  HOH G5707
SITE     1 IC5 12 GLU G 783  ASP G 791  ALA G 793  GLU G 892
SITE     2 IC5 12 VAL G 893  LEU G 895  LEU G 907  TYR G1040
SITE     3 IC5 12 ASP G1041  THR G1042  HOH G5171  HOH G5391
SITE     1 IC6 15 SER G 948  VAL G 949  LYS G 954  THR G 974
SITE     2 IC6 15 GLY G 976  THR G 977  LYS G 993  VAL G 994
SITE     3 IC6 15 ILE G1001  ASN G1015  THR G1016  THR G1017
SITE     4 IC6 15 ASP G1025  SER G1026  HOH G5446
SITE     1 IC7  5 GLN G  22  GLN G  93  THR G  94  ASN G  97
SITE     2 IC7  5 HOH G5125
SITE     1 IC8  7 ARG G 528  ALA G 537  THR G 538  GLU G 552
SITE     2 IC8  7 ASN G 554  ARG H 120  ARG H 123
CRYST1  152.100  163.900  331.200  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      0.006575  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006101  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003019        0.00000
      
PROCHECK
Go to PROCHECK summary
 References