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PDBsum entry 1kee

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Top Page protein ligands metals Protein-protein interface(s) links
Ligase PDB id
1kee
Jmol
Contents
Protein chains
1058 a.a. *
379 a.a. *
Ligands
ADP ×8
PO4 ×4
ORN ×4
NET ×4
Metals
_CL ×22
_MN ×12
__K ×32
Waters ×4176
* Residue conservation analysis
HEADER    LIGASE                                  15-NOV-01   1KEE
TITLE     INACTIVATION OF THE AMIDOTRANSFERASE ACTIVITY OF CARBAMOYL PHOSPHATE
TITLE    2 SYNTHETASE BY THE ANTIBIOTIC ACIVICIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBAMOYL-PHOSPHATE SYNTHETASE LARGE CHAIN;
COMPND   3 CHAIN: A, C, E, G;
COMPND   4 SYNONYM: CARBAMOYL-PHOSPHATE SYNTHETASE AMMONIA CHAIN;
COMPND   5 EC: 6.3.5.5;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: CARBAMOYL-PHOSPHATE SYNTHETASE SMALL CHAIN;
COMPND   9 CHAIN: B, D, F, H;
COMPND  10 SYNONYM: CARBAMOYL-PHOSPHATE SYNTHETASE GLUTAMINE CHAIN;
COMPND  11 EC: 6.3.5.5;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE   3 ORGANISM_TAXID: 562;
SOURCE   4 GENE: CARB;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21DE3(PLYSS);
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 MOL_ID: 2;
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE  11 ORGANISM_TAXID: 562;
SOURCE  12 GENE: CARA;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21DE3(PYSS)LYSS);
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS    ATP GRASP, CHANNELING, ANTIBIOTIC, LIGASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.W.MILES,J.B.THODEN,H.M.HOLDEN,F.M.RAUSHEL
REVDAT   4   13-JUL-11 1KEE    1       VERSN
REVDAT   3   24-FEB-09 1KEE    1       VERSN
REVDAT   2   03-APR-02 1KEE    1       JRNL   REMARK
REVDAT   1   21-DEC-01 1KEE    0
JRNL        AUTH   B.W.MILES,J.B.THODEN,H.M.HOLDEN,F.M.RAUSHEL
JRNL        TITL   INACTIVATION OF THE AMIDOTRANSFERASE ACTIVITY OF CARBAMOYL
JRNL        TITL 2 PHOSPHATE SYNTHETASE BY THE ANTIBIOTIC ACIVICIN.
JRNL        REF    J.BIOL.CHEM.                  V. 277  4368 2002
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   11729189
JRNL        DOI    10.1074/JBC.M108582200
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.9
REMARK   3   NUMBER OF REFLECTIONS             : 429957
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) : 0.187
REMARK   3   R VALUE            (WORKING SET) : 0.186
REMARK   3   FREE R VALUE                     : 0.211
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 42997
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1870
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 429957
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 44260
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 374
REMARK   3   SOLVENT ATOMS            : 4176
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) : 0.010 ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : 2.120 ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : 17.700; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : ENGH & HUBER
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : ISOTROPIC
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1KEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-01.
REMARK 100 THE RCSB ID CODE IS RCSB014865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 31-JUL-98
REMARK 200  TEMPERATURE           (KELVIN) : 100
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) : 0.908
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 : MAR
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 429957
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     (%) : 88.9
REMARK 200  DATA REDUNDANCY                : 4.400
REMARK 200  R MERGE                    (I) : 0.04400
REMARK 200  R SYM                      (I) : 0.04400
REMARK 200   FOR THE DATA SET  : 37.9000
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     (%) : 72.7
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.17900
REMARK 200  R SYM FOR SHELL            (I) : 0.17900
REMARK 200   FOR SHELL         : 5.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: PDB ENTRY 1JDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, HEPES, POTASSIUM CHLORIDE,
REMARK 280  MANGANESE CHLORIDE, ORNITHINE, TETRAETHYLAMMONIUM CHLORIDE,
REMARK 280  HEPPS, PH 7.4, BATCH, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       76.20000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      166.60000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       82.20000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      166.60000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.20000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       82.20000
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN OCTAMER
REMARK 300 COMPRISED OF CHAINS A,B,C,D,E,F,G, AND H
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 8210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 47070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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 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    LEU B   325     O    HOH B  5179              2.06
REMARK 500   OE2  GLU C   110     O    HOH C  5132              2.14
REMARK 500   O    HOH A  5719     O    HOH A  5849              2.17
REMARK 500   O    SER D   100     O    HOH D  1835              2.18
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  72   CD    GLU A  72   OE2     0.083
REMARK 500    GLU A 109   CD    GLU A 109   OE2     0.073
REMARK 500    GLU A 153   CD    GLU A 153   OE2     0.075
REMARK 500    GLU A 186   CD    GLU A 186   OE2     0.071
REMARK 500    GLU A 187   CD    GLU A 187   OE2     0.067
REMARK 500    GLU A 217   CD    GLU A 217   OE2     0.077
REMARK 500    GLU A 219   CD    GLU A 219   OE2     0.068
REMARK 500    GLU A 365   CD    GLU A 365   OE2     0.070
REMARK 500    GLU A 427   CD    GLU A 427   OE2     0.066
REMARK 500    GLU A 468   CD    GLU A 468   OE2     0.067
REMARK 500    GLU A 474   CD    GLU A 474   OE2     0.069
REMARK 500    GLU A 478   CD    GLU A 478   OE2     0.074
REMARK 500    GLU A 512   CD    GLU A 512   OE2     0.077
REMARK 500    GLU A 549   CD    GLU A 549   OE2     0.070
REMARK 500    GLU A 550   CD    GLU A 550   OE2     0.071
REMARK 500    GLU A 577   CD    GLU A 577   OE2     0.075
REMARK 500    GLU A 595   CD    GLU A 595   OE2     0.068
REMARK 500    GLU A 604   CD    GLU A 604   OE2     0.068
REMARK 500    GLU A 655   CD    GLU A 655   OE2     0.072
REMARK 500    GLU A 673   CD    GLU A 673   OE2     0.070
REMARK 500    GLU A 676   CD    GLU A 676   OE2     0.066
REMARK 500    GLU A 683   CD    GLU A 683   OE2     0.078
REMARK 500    GLU A 699   CD    GLU A 699   OE2     0.069
REMARK 500    GLU A 703   CD    GLU A 703   OE2     0.075
REMARK 500    GLU A 707   CD    GLU A 707   OE2     0.067
REMARK 500    GLU A 731   CD    GLU A 731   OE2     0.072
REMARK 500    GLU A 771   CD    GLU A 771   OE2     0.072
REMARK 500    GLU A 780   CD    GLU A 780   OE2     0.075
REMARK 500    GLU A 804   CD    GLU A 804   OE2     0.069
REMARK 500    GLU A 836   CD    GLU A 836   OE2     0.075
REMARK 500    GLU A 951   CD    GLU A 951   OE2     0.076
REMARK 500    GLU A 955   CD    GLU A 955   OE2     0.075
REMARK 500    GLU A1009   CD    GLU A1009   OE2     0.068
REMARK 500    GLU A1024   CD    GLU A1024   OE2     0.074
REMARK 500    GLU B  41   CD    GLU B  41   OE2     0.070
REMARK 500    GLU B  70   CD    GLU B  70   OE2     0.069
REMARK 500    GLU B  71   CD    GLU B  71   OE2     0.071
REMARK 500    GLU B 124   CD    GLU B 124   OE2     0.075
REMARK 500    GLU B 166   CD    GLU B 166   OE2     0.069
REMARK 500    GLU B 183   CD    GLU B 183   OE2     0.087
REMARK 500    GLU B 226   CD    GLU B 226   OE2     0.069
REMARK 500    GLU B 372   CD    GLU B 372   OE2     0.082
REMARK 500    GLU C  59   CD    GLU C  59   OE2     0.086
REMARK 500    GLU C 109   CD    GLU C 109   OE2     0.068
REMARK 500    GLU C 110   CD    GLU C 110   OE2     0.090
REMARK 500    GLU C 153   CD    GLU C 153   OE2     0.073
REMARK 500    GLU C 186   CD    GLU C 186   OE2     0.073
REMARK 500    GLU C 187   CD    GLU C 187   OE2     0.072
REMARK 500    GLU C 203   CD    GLU C 203   OE2     0.073
REMARK 500    GLU C 219   CD    GLU C 219   OE2     0.067
REMARK 500
REMARK 500 THIS ENTRY HAS     163 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A   6   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES
REMARK 500    ASP A   6   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    TYR A  42   CB  -  CG  -  CD1 ANGL. DEV. =  -3.6 DEGREES
REMARK 500    ASP A  57   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ASP A  62   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A  84   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES
REMARK 500    ASP A 128   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ASP A 128   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES
REMARK 500    ASP A 226   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES
REMARK 500    ASP A 246   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ASP A 246   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP A 333   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ASP A 338   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    ASP A 372   CB  -  CG  -  OD2 ANGL. DEV. =  -7.1 DEGREES
REMARK 500    ARG A 373   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ASP A 410   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES
REMARK 500    ASP A 410   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP A 416   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES
REMARK 500    ASP A 416   CB  -  CG  -  OD2 ANGL. DEV. =  -8.7 DEGREES
REMARK 500    ASP A 459   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP A 487   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ARG A 514   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A 514   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    ASP A 521   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 521   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES
REMARK 500    ASP A 530   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES
REMARK 500    ASP A 539   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ASP A 558   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES
REMARK 500    ASP A 579   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ASP A 579   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES
REMARK 500    ASP A 609   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES
REMARK 500    ASP A 609   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES
REMARK 500    TYR A 610   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    TYR A 610   CB  -  CG  -  CD1 ANGL. DEV. =   4.6 DEGREES
REMARK 500    ASP A 611   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES
REMARK 500    ASP A 611   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ASP A 625   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES
REMARK 500    TYR A 642   CB  -  CG  -  CD2 ANGL. DEV. =  -6.7 DEGREES
REMARK 500    TYR A 642   CB  -  CG  -  CD1 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ASP A 670   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES
REMARK 500    ARG A 671   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG A 671   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 677   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    PRO A 716   N   -  CA  -  CB  ANGL. DEV. =   7.3 DEGREES
REMARK 500    ARG A 736   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES
REMARK 500    ASP A 757   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP A 807   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     325 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    ALA A  23     -153.09   -105.70
REMARK 500    ALA A  52       30.98    -82.24
REMARK 500    GLN A 105        1.63    -62.93
REMARK 500    PHE A 172       30.33     74.08
REMARK 500    ASN A 292       11.71   -147.75
REMARK 500    ARG A 303     -173.01   -172.90
REMARK 500    ASP A 353       41.72   -102.94
REMARK 500    ASN A 363       35.86   -153.60
REMARK 500    THR A 375     -157.34   -143.79
REMARK 500    ASP A 416       30.39    -94.19
REMARK 500    THR A 531      -11.03     67.60
REMARK 500    ALA A 541       77.74   -116.03
REMARK 500    ASP A 558      -84.12    -50.59
REMARK 500    CYS A 601       21.70   -140.91
REMARK 500    THR A 646      -77.61    -40.73
REMARK 500    ASP A 758       54.14     36.52
REMARK 500    HIS A 788      132.82    -38.55
REMARK 500    GLN A 821       41.25     70.80
REMARK 500    PRO A 844       48.78    -68.72
REMARK 500    PRO A 905       47.28    -65.36
REMARK 500    LYS A 954      -18.17    -49.46
REMARK 500    HIS A 975      -82.44    -27.45
REMARK 500    GLU B  96      133.51   -172.35
REMARK 500    ASP B 114       81.05    -67.16
REMARK 500    ALA B 127      154.77    -49.42
REMARK 500    143 B 269      -99.52     55.22
REMARK 500    ASN B 311       74.44   -168.63
REMARK 500    ALA B 356     -131.57     44.97
REMARK 500    SER B 357       71.83     63.57
REMARK 500    PRO C   2     -159.28    -74.71
REMARK 500    ALA C  23     -153.58   -108.06
REMARK 500    ALA C  52       34.74    -84.65
REMARK 500    ALA C 239     -179.89    -63.66
REMARK 500    ILE C 298      -60.20   -100.03
REMARK 500    PRO C 302       35.74    -72.28
REMARK 500    ASP C 338      -70.27    -36.73
REMARK 500    ASN C 363       35.41   -149.20
REMARK 500    THR C 375     -159.03   -142.29
REMARK 500    ASP C 530       -3.92   -142.66
REMARK 500    THR C 531       -9.32     75.02
REMARK 500    ALA C 541       72.17   -112.35
REMARK 500    TYR C 547       79.80   -104.01
REMARK 500    GLU C 548     -160.13   -125.00
REMARK 500    CYS C 601       20.64   -140.03
REMARK 500    PRO C 660       67.78    -68.48
REMARK 500    ILE C 698      -70.16    -48.55
REMARK 500    GLN C 739      -76.90    -62.69
REMARK 500    ASP C 758       45.80     39.61
REMARK 500    GLN C 821       46.50     72.79
REMARK 500    SER C 948       89.47   -156.61
REMARK 500
REMARK 500 THIS ENTRY HAS     117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    LYS A   3        23.8      L          L   OUTSIDE RANGE
REMARK 500    GLU A 127        24.4      L          L   OUTSIDE RANGE
REMARK 500    ILE A 139        24.7      L          L   OUTSIDE RANGE
REMARK 500    ILE A 339        21.7      L          L   OUTSIDE RANGE
REMARK 500    ARG A 435        24.8      L          L   OUTSIDE RANGE
REMARK 500    ILE A 481        24.7      L          L   OUTSIDE RANGE
REMARK 500    GLU A 726        24.8      L          L   OUTSIDE RANGE
REMARK 500    TYR A 729        23.8      L          L   OUTSIDE RANGE
REMARK 500    HIS A 975        24.1      L          L   OUTSIDE RANGE
REMARK 500    VAL B  53        24.6      L          L   OUTSIDE RANGE
REMARK 500    THR B 336        23.9      L          L   OUTSIDE RANGE
REMARK 500    PHE C  26        23.3      L          L   OUTSIDE RANGE
REMARK 500    TRP C  71        24.8      L          L   OUTSIDE RANGE
REMARK 500    ILE C 139        23.3      L          L   OUTSIDE RANGE
REMARK 500    PHE C 172        20.7      L          L   OUTSIDE RANGE
REMARK 500    VAL C 328        24.5      L          L   OUTSIDE RANGE
REMARK 500    ILE C 339        18.4      L          L   OUTSIDE RANGE
REMARK 500    ARG C 435        23.4      L          L   OUTSIDE RANGE
REMARK 500    TYR D  39        24.3      L          L   OUTSIDE RANGE
REMARK 500    ASP D  69        24.7      L          L   OUTSIDE RANGE
REMARK 500    ASP D 112        24.6      L          L   OUTSIDE RANGE
REMARK 500    ASN D 232        23.2      L          L   OUTSIDE RANGE
REMARK 500    ARG E   4        24.7      L          L   OUTSIDE RANGE
REMARK 500    ALA E  23        24.6      L          L   OUTSIDE RANGE
REMARK 500    THR E  56        24.9      L          L   OUTSIDE RANGE
REMARK 500    ILE E 139        24.7      L          L   OUTSIDE RANGE
REMARK 500    ILE E 339        12.2      L          L   OUTSIDE RANGE
REMARK 500    ARG E 435        22.1      L          L   OUTSIDE RANGE
REMARK 500    VAL E 994        24.5      L          L   OUTSIDE RANGE
REMARK 500    THR F 163        23.8      L          L   OUTSIDE RANGE
REMARK 500    PHE F 192        23.4      L          L   OUTSIDE RANGE
REMARK 500    LYS G   3        24.5      L          L   OUTSIDE RANGE
REMARK 500    ILE G 339        16.7      L          L   OUTSIDE RANGE
REMARK 500    TYR G 729        24.2      L          L   OUTSIDE RANGE
REMARK 500    VAL G 750        24.8      L          L   OUTSIDE RANGE
REMARK 500    ASP G 758        23.9      L          L   OUTSIDE RANGE
REMARK 500    PHE G 897        24.9      L          L   OUTSIDE RANGE
REMARK 500    HIS G 975        24.6      L          L   OUTSIDE RANGE
REMARK 500    ASN H 204        23.1      L          L   OUTSIDE RANGE
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 A5078        DISTANCE =  5.24 ANGSTROMS
REMARK 525    HOH A5154        DISTANCE =  6.11 ANGSTROMS
REMARK 525    HOH A5159        DISTANCE =  6.39 ANGSTROMS
REMARK 525    HOH A5162        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH A5176        DISTANCE =  6.75 ANGSTROMS
REMARK 525    HOH A5178        DISTANCE =  5.42 ANGSTROMS
REMARK 525    HOH A5181        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH A5276        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH A5358        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH A5377        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH A5566        DISTANCE =  6.11 ANGSTROMS
REMARK 525    HOH A5620        DISTANCE =  6.21 ANGSTROMS
REMARK 525    HOH A5645        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH A5671        DISTANCE =  5.28 ANGSTROMS
REMARK 525    HOH A5672        DISTANCE =  7.31 ANGSTROMS
REMARK 525    HOH A5673        DISTANCE =  7.96 ANGSTROMS
REMARK 525    HOH A5682        DISTANCE =  5.54 ANGSTROMS
REMARK 525    HOH A5686        DISTANCE =  7.09 ANGSTROMS
REMARK 525    HOH A5690        DISTANCE =  5.48 ANGSTROMS
REMARK 525    HOH A5707        DISTANCE =  7.33 ANGSTROMS
REMARK 525    HOH A5722        DISTANCE =  5.93 ANGSTROMS
REMARK 525    HOH A5746        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH A5779        DISTANCE =  6.55 ANGSTROMS
REMARK 525    HOH A5805        DISTANCE =  7.05 ANGSTROMS
REMARK 525    HOH A5806        DISTANCE =  5.12 ANGSTROMS
REMARK 525    HOH A5845        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH A5861        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH B5205        DISTANCE =  6.39 ANGSTROMS
REMARK 525    HOH B5224        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH B5237        DISTANCE =  5.41 ANGSTROMS
REMARK 525    HOH C5170        DISTANCE =  7.10 ANGSTROMS
REMARK 525    HOH C5176        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH C5180        DISTANCE =  6.48 ANGSTROMS
REMARK 525    HOH C5201        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH C5360        DISTANCE =  5.01 ANGSTROMS
REMARK 525    HOH C5370        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH C5390        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH C5566        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH C5568        DISTANCE =  5.17 ANGSTROMS
REMARK 525    HOH C5569        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH C5584        DISTANCE =  5.56 ANGSTROMS
REMARK 525    HOH C5633        DISTANCE =  6.69 ANGSTROMS
REMARK 525    HOH C5635        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH C5700        DISTANCE =  5.06 ANGSTROMS
REMARK 525    HOH C5721        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH C5753        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH C5798        DISTANCE =  5.36 ANGSTROMS
REMARK 525    HOH D1823        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH D2066        DISTANCE =  5.08 ANGSTROMS
REMARK 525    HOH D2088        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH D2122        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH D2123        DISTANCE =  6.04 ANGSTROMS
REMARK 525    HOH D2199        DISTANCE =  5.09 ANGSTROMS
REMARK 525    HOH D2217        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH D2219        DISTANCE =  5.43 ANGSTROMS
REMARK 525    HOH E5171        DISTANCE =  5.32 ANGSTROMS
REMARK 525    HOH E5202        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH E5206        DISTANCE =  6.52 ANGSTROMS
REMARK 525    HOH E5210        DISTANCE =  5.49 ANGSTROMS
REMARK 525    HOH E5245        DISTANCE =  5.60 ANGSTROMS
REMARK 525    HOH E5397        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH E5609        DISTANCE =  6.20 ANGSTROMS
REMARK 525    HOH E5692        DISTANCE =  5.59 ANGSTROMS
REMARK 525    HOH E5694        DISTANCE =  8.10 ANGSTROMS
REMARK 525    HOH E5695        DISTANCE =  7.30 ANGSTROMS
REMARK 525    HOH E5704        DISTANCE =  6.06 ANGSTROMS
REMARK 525    HOH E5712        DISTANCE =  6.16 ANGSTROMS
REMARK 525    HOH E5714        DISTANCE =  5.51 ANGSTROMS
REMARK 525    HOH E5724        DISTANCE =  5.20 ANGSTROMS
REMARK 525    HOH E5758        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH E5762        DISTANCE =  7.17 ANGSTROMS
REMARK 525    HOH E5777        DISTANCE =  7.25 ANGSTROMS
REMARK 525    HOH E5778        DISTANCE =  7.32 ANGSTROMS
REMARK 525    HOH E5810        DISTANCE =  5.26 ANGSTROMS
REMARK 525    HOH E5862        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH E5866        DISTANCE =  7.83 ANGSTROMS
REMARK 525    HOH E5867        DISTANCE =  7.40 ANGSTROMS
REMARK 525    HOH E5877        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH E5894        DISTANCE =  5.34 ANGSTROMS
REMARK 525    HOH E5895        DISTANCE =  7.11 ANGSTROMS
REMARK 525    HOH E5897        DISTANCE =  6.34 ANGSTROMS
REMARK 525    HOH E5898        DISTANCE =  7.21 ANGSTROMS
REMARK 525    HOH E5908        DISTANCE =  5.68 ANGSTROMS
REMARK 525    HOH E5912        DISTANCE =  5.40 ANGSTROMS
REMARK 525    HOH F2510        DISTANCE =  5.27 ANGSTROMS
REMARK 525    HOH F2888        DISTANCE =  5.75 ANGSTROMS
REMARK 525    HOH F3154        DISTANCE =  6.15 ANGSTROMS
REMARK 525    HOH F3165        DISTANCE =  5.13 ANGSTROMS
REMARK 525    HOH F3169        DISTANCE =  6.86 ANGSTROMS
REMARK 525    HOH F3288        DISTANCE =  6.47 ANGSTROMS
REMARK 525    HOH F3298        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH F3387        DISTANCE =  7.58 ANGSTROMS
REMARK 525    HOH G3504        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH G3525        DISTANCE =  6.01 ANGSTROMS
REMARK 525    HOH G3529        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH G3530        DISTANCE =  6.64 ANGSTROMS
REMARK 525    HOH G3741        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH G3756        DISTANCE =  5.74 ANGSTROMS
REMARK 525    HOH G3774        DISTANCE =  5.25 ANGSTROMS
REMARK 525    HOH G3778        DISTANCE =  5.72 ANGSTROMS
REMARK 525    HOH G3802        DISTANCE =  6.18 ANGSTROMS
REMARK 525    HOH G4136        DISTANCE =  6.75 ANGSTROMS
REMARK 525    HOH G4148        DISTANCE =  5.21 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 HOH A5026   O   163.1
REMARK 620 3 ASP A  84   O    74.8 107.8
REMARK 620 4 THR A 114   OG1 103.5  93.4  80.6
REMARK 620 N                    1     2     3
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 127   OE1
REMARK 620 2 GLU A 299   OE1 125.3
REMARK 620 3 MET A 300   O    96.4  94.0
REMARK 620 4 HOH A5128   O   145.2  88.8  71.9
REMARK 620 5 HOH A5129   O    63.7  65.0 120.8 150.4
REMARK 620 6 ALA A 126   O    90.3 143.4  89.7  57.9 140.4
REMARK 620 7 ASN A 301   OD1  77.8  54.2  73.9 126.6  48.3 158.3
REMARK 620 N                    1     2     3     4     5     6
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 215   OE2
REMARK 620 2 ASN A 236   OD1  85.7
REMARK 620 3 ASP A 238   O   122.5  90.7
REMARK 620 4 ALA A 239   O    89.5 152.7  69.4
REMARK 620 5 ILE A 242   O    87.3 120.2 139.9  86.4
REMARK 620 6 SER A 247   OG  139.9  79.5  94.9 119.4  69.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A2003  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 285   OE1
REMARK 620 2 GLU A 299   OE2  75.0
REMARK 620 3 ADP A2001   O1B 174.0 100.1
REMARK 620 4 ADP A2001   O1A  97.8  92.5  85.8
REMARK 620 5 HOH A5185   O    94.0 168.1  90.5  93.6
REMARK 620 6 PO4 A2006   O3   90.3  86.1  85.8 171.1  89.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A2002  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 299   CD
REMARK 620 2 GLU A 299   OE1  26.9
REMARK 620 3 GLU A 299   OE2  29.2  56.1
REMARK 620 4 ASN A 301   OD1  85.8  88.1  84.6
REMARK 620 5 ADP A2001   O3B  92.1  88.1  95.8 175.0
REMARK 620 6 PO4 A2006   O1  117.0 143.8  87.7  89.5  95.5
REMARK 620 7 HOH A5129   O   120.4  93.9 148.9  86.4  90.8 122.0
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A5014   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 383   N
REMARK 620 2 ASN A 570   OD1 143.8
REMARK 620 3 GLU A 604   OE2 110.8  62.6
REMARK 620 4 GLU A 383   O    55.6 154.4 135.8
REMARK 620 5 ASN A 602   OD1 126.9  89.3  89.1  75.5
REMARK 620 6 ASN A 602   ND2 149.9  59.6  97.3  96.7  40.3
REMARK 620 7 ASN A 570   N    95.7  71.0 130.2  94.1 108.1  72.7
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   OE2
REMARK 620 2 HIS A 781   ND1  81.2
REMARK 620 3 GLU A 783   O   134.0  95.9
REMARK 620 4 GLN A 784   O    96.2 148.6  63.5
REMARK 620 5 VAL A 787   O    78.4 124.9 133.9  84.5
REMARK 620 6 SER A 792   OG  127.8  82.2  96.7 121.6  71.7
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  88.1
REMARK 620 3 ADP A2007   O2A  95.7  94.1
REMARK 620 4 HOH A5502   O    89.9 178.0  86.1
REMARK 620 5 ADP A2007   O3B 175.4  93.1  79.7  89.0
REMARK 620 6 HOH A5501   O   107.9  86.9 156.4  93.7  76.7
REMARK 620 N                    1     2     3     4     5
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   OE2
REMARK 620 2 ASN A 843   OD1  65.8
REMARK 620 3 ADP A2007   O2B  94.3 156.3
REMARK 620 4 ADP A2007   O3B  64.4 125.4  46.3
REMARK 620 5 HOH A5501   O    57.6  89.0  90.7  45.2
REMARK 620 6 HOH A5504   O    97.1 123.6  42.8  83.7 128.0
REMARK 620 7 HOH A5666   O   158.6 132.4  65.1 101.4 124.7  64.2
REMARK 620 8 GLU A 841   OE1  45.6  73.6  83.3  87.0 101.9  59.6 121.8
REMARK 620 N                    1     2     3     4     5     6     7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K B5016   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B  16   O
REMARK 620 2 ASP B 112   O    94.0
REMARK 620 3 HOH B5068   O    73.4 154.3
REMARK 620 4 HOH A5421   O   116.3  82.6  83.3
REMARK 620 5 HOH A5422   O   146.9 117.3  81.1  80.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5037   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 114   OG1
REMARK 620 2 HOH C5047   O   155.2
REMARK 620 3 ASP C  84   O    81.5  74.5
REMARK 620 4 HOH C5048   O    86.3  88.5  93.2
REMARK 620 5 GLY C 112   O   113.9  64.2  70.7 150.9
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5026   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 215   OE2
REMARK 620 2 ASN C 236   OD1  85.8
REMARK 620 3 ASP C 238   O   126.4  93.5
REMARK 620 4 ALA C 239   O    91.4 153.6  67.3
REMARK 620 5 ILE C 242   O    81.2 119.4 140.1  85.9
REMARK 620 6 SER C 247   OG  137.7  78.3  93.7 119.2  73.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C2025  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 285   OE1
REMARK 620 2 GLU C 299   OE2  76.6
REMARK 620 3 HOH C5205   O    86.7 162.6
REMARK 620 4 ADP C2023   O1A 101.8  89.7  89.0
REMARK 620 5 ADP C2023   O1B 171.5  99.1  98.1  85.3
REMARK 620 6 PO4 C2028   O3   89.6  86.5  98.3 166.8  82.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C2024  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 299   CD
REMARK 620 2 GLU C 299   OE1  27.1
REMARK 620 3 GLU C 299   OE2  29.4  56.5
REMARK 620 4 ASN C 301   OD1  84.9  85.5  84.8
REMARK 620 5 ADP C2023   O3B  90.0  87.5  93.5 172.6
REMARK 620 6 PO4 C2028   O1  122.9 150.0  93.5  91.8  95.5
REMARK 620 7 HOH C5151   O   126.2  99.2 155.2  88.5  90.1 110.7
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5027   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 299   OE1
REMARK 620 2 MET C 300   O    94.6
REMARK 620 3 HOH C5150   O    90.9  70.7
REMARK 620 4 ALA C 126   O   142.2  85.3  53.5
REMARK 620 5 GLU C 127   OE1 131.5  92.7 136.4  86.1
REMARK 620 6  MN C2024  MN    37.3 104.1 128.1 170.5  94.5
REMARK 620 7 HOH C5151   O    69.1 124.7 154.5 139.2  67.4  34.8
REMARK 620 8 HOH C5618   O   102.3 161.6 101.6  76.9  81.5  93.8  69.2
REMARK 620 9 ASN C 301   OD1  56.1  74.6 129.2 155.0  80.2  33.5  52.0 121.0
REMARK 620 N                    1     2     3     4     5     6     7     8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5036   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 383   N
REMARK 620 2 ASN C 602   OD1 121.0
REMARK 620 3 ASN C 602   ND2 154.3  42.0
REMARK 620 4 GLU C 383   O    57.8  69.4  96.8
REMARK 620 5 GLU C 604   OE2 107.7  85.8  91.7 129.7
REMARK 620 6 ASN C 570   N   101.6 112.1  76.8  99.9 130.3
REMARK 620 7 ASN C 570   OD1 145.0  91.7  59.9 156.6  59.1  73.8
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5032   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 761   OE2
REMARK 620 2 HIS C 781   ND1  76.8
REMARK 620 3 GLU C 783   O   125.4  94.7
REMARK 620 4 VAL C 787   O    76.1 125.3 139.4
REMARK 620 5 SER C 792   OG  132.1  92.1 101.6  73.3
REMARK 620 6 GLN C 784   O    87.9 146.3  69.9  78.0 119.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN C2030  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 829   CD
REMARK 620 2 GLN C 829   OE1  18.6
REMARK 620 3 GLU C 841   OE2  95.5  90.3
REMARK 620 4 ADP C2029   O3B 165.9 173.4  92.3
REMARK 620 5 HOH C5518   O    86.2 103.9  88.0  82.3
REMARK 620 6 ADP C2029   O2A 108.3  91.4  97.0  82.3 164.0
REMARK 620 7 HOH C5519   O    79.7  83.9 173.7  93.3  95.7  80.8
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K C5031   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 841   OE1
REMARK 620 2 ADP C2029   O2B  89.1
REMARK 620 3 GLU C 841   OE2  45.3  98.7
REMARK 620 4 ASN C 843   OD1  72.9 155.2  56.5
REMARK 620 5 ADP C2029   O3B  82.3  47.6  60.7 111.5
REMARK 620 6 HOH C5522   O    53.6  57.6  95.2 118.6  90.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K D5038   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D  16   O
REMARK 620 2 ASP D 112   O    91.5
REMARK 620 3 HOH C5439   O   108.1  82.2
REMARK 620 4 HOH C5440   O   145.6 122.5  84.1
REMARK 620 5 HOH D1762   O    77.4 151.5  76.6  74.3
REMARK 620 6 HOH D2137   O    84.5  81.9 159.9  94.3 122.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5059   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E  84   O
REMARK 620 2 GLY E 112   O    81.2
REMARK 620 3 THR E 114   OG1  76.2 105.5
REMARK 620 4 HOH E5073   O    95.0  89.7 160.8
REMARK 620 5 THR E 114   N    45.0  66.5  47.9 134.2
REMARK 620 6 HOH E5074   O    99.1 175.8  78.6  86.1 116.6
REMARK 620 N                    1     2     3     4     5
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 127   OE1
REMARK 620 2 GLU E 299   OE1 130.0
REMARK 620 3 MET E 300   O    97.0  87.5
REMARK 620 4 HOH E5177   O   133.4  96.6  82.0
REMARK 620 5 HOH E5178   O    67.2  68.7 122.7 148.9
REMARK 620 6 ASN E 301   OD1  81.0  54.6  68.0 137.8  55.5
REMARK 620 7 ALA E 126   O    84.6 145.2  92.7  49.2 135.9 154.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5057   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 143   O
REMARK 620 2 THR E 143   OG1  64.6
REMARK 620 3 ALA E 144   O    71.1  77.3
REMARK 620 4 HOH E5188   O   142.0 101.6  71.4
REMARK 620 5 HOH E5189   O    65.0  75.8 135.0 149.4
REMARK 620 6 HOH E5690   O   120.5 153.1 129.6  88.3  83.1
REMARK 620 7 HOH E5183   O   130.7  76.5 129.4  72.6  77.3  82.8
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E2048   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 215   OE2
REMARK 620 2 ASN E 236   OD1  78.6
REMARK 620 3 ASP E 238   O   126.7  94.1
REMARK 620 4 ALA E 239   O    96.5 155.1  69.1
REMARK 620 5 ILE E 242   O    82.8 116.9 142.1  86.2
REMARK 620 6 SER E 247   OG  130.1  77.3  98.1 121.9  70.5
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E2047  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 285   OE1
REMARK 620 2 GLU E 299   OE2  76.4
REMARK 620 3 ADP E2045   O1B 165.4  98.5
REMARK 620 4 HOH E5232   O    96.6 168.0  90.5
REMARK 620 5 ADP E2045   O1A  99.3  82.8  93.6  88.8
REMARK 620 6 PO4 E2050   O3   84.4  92.0  82.1  97.0 172.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E2046  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 299   CD
REMARK 620 2 GLU E 299   OE1  27.0
REMARK 620 3 GLU E 299   OE2  29.6  56.6
REMARK 620 4 ASN E 301   OD1  88.5  84.8  94.3
REMARK 620 5 ADP E2045   O3B  88.2  88.1  87.4 170.3
REMARK 620 6 HOH E5178   O   116.8  89.8 146.1  86.9  86.4
REMARK 620 7 PO4 E2050   O1  122.7 147.8  94.7  83.0 106.4 119.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5058   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 570   OD1
REMARK 620 2 ASN E 602   OD1  84.9
REMARK 620 3 GLU E 383   N   150.2 124.6
REMARK 620 4 GLU E 604   OE2  68.7  86.8 112.5
REMARK 620 5 ASN E 570   N    69.8 110.3  93.5 133.2
REMARK 620 6 GLU E 383   O   146.8  73.4  55.1 132.7  94.1
REMARK 620 7 ASN E 602   ND2  51.7  43.7 147.6  97.9  72.0  96.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5054   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 761   OE2
REMARK 620 2 HIS E 781   ND1  81.4
REMARK 620 3 GLN E 784   O    90.8 147.2
REMARK 620 4 VAL E 787   O    78.7 120.7  88.3
REMARK 620 5 SER E 792   OG  133.6  81.0 124.8  74.3
REMARK 620 6 GLU E 783   O   124.0  93.9  64.4 142.5  99.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN E2052  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN E 829   OE1
REMARK 620 2 GLU E 841   OE2  84.2
REMARK 620 3 ADP E2051   O2A  93.8  94.5
REMARK 620 4 HOH E5544   O    82.3 166.4  86.9
REMARK 620 5 ADP E2051   O3B 176.4  93.8  83.4  99.8
REMARK 620 6 HOH E5543   O    90.1  94.3 170.7  85.2  93.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K E5053   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 841   OE1
REMARK 620 2 HOH E5547   O    61.3
REMARK 620 3 ADP E2051   O2B  90.3  63.0
REMARK 620 4 HOH E5816   O    90.9 145.4  99.9
REMARK 620 5 GLU E 841   OE2  40.9  96.5  88.4  51.1
REMARK 620 6 ASN E 843   OD1  66.8 121.6 142.4  53.7  54.6
REMARK 620 7 ADP E2051   O3B  79.3  94.0  43.3  58.7  53.5 101.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K F5060   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F  16   O
REMARK 620 2 ASP F 112   O    89.9
REMARK 620 3 HOH F2843   O    78.9 152.1
REMARK 620 4 HOH E5466   O   148.6 118.9  79.7
REMARK 620 5 HOH E5465   O   115.0  82.6  79.3  82.9
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5080   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 112   O
REMARK 620 2 THR G 114   OG1 103.0
REMARK 620 3 HOH G4115   O   158.7  80.0
REMARK 620 4 HOH G3396   O    88.3 160.6  95.2
REMARK 620 5 ASP G  84   O    76.7  80.8 124.4  86.7
REMARK 620 6 HOH G3397   O   160.6  81.3  40.2  83.0  85.5
REMARK 620 N                    1     2     3     4     5
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 127   OE1
REMARK 620 2 GLU G 299   OE1 130.0
REMARK 620 3 MET G 300   O    93.4  96.8
REMARK 620 4 HOH G3500   O   139.2  90.4  74.0
REMARK 620 5 HOH G3501   O    63.7  72.7 130.5 150.8
REMARK 620 6 ALA G 126   O    89.9 139.4  86.5  51.5 132.9
REMARK 620 7 ASN G 301   OD1  77.1  58.6  75.7 133.0  57.3 157.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G2069   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 215   OE2
REMARK 620 2 ASP G 238   O   123.7
REMARK 620 3 ALA G 239   O    94.6  69.9
REMARK 620 4 ILE G 242   O    82.4 144.6  85.9
REMARK 620 5 SER G 247   OG  134.9  96.5 120.1  73.2
REMARK 620 6 ASN G 236   OD1  79.6  92.2 154.1 117.9  79.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G2068  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 285   CD
REMARK 620 2 GLN G 285   OE1  18.5
REMARK 620 3 GLU G 299   OE2  78.4  76.4
REMARK 620 4 PO4 G2071   O3  108.0  89.5  88.8
REMARK 620 5 HOH G3558   O    90.2  92.2 168.4  93.1
REMARK 620 6 ADP G2066   O1A  84.6 102.8  86.9 165.6  93.9
REMARK 620 7 ADP G2066   O1B 172.6 168.3 100.3  79.2  91.3  88.1
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G2067  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 299   CD
REMARK 620 2 GLU G 299   OE1  25.6
REMARK 620 3 GLU G 299   OE2  27.7  53.2
REMARK 620 4 ASN G 301   OD1  89.3  89.1  92.6
REMARK 620 5 HOH G3501   O   115.1  89.7 142.8  83.9
REMARK 620 6 PO4 G2071   O1  123.0 148.3  95.9  85.3 120.6
REMARK 620 7 ADP G2066   O3B  91.4  85.5  94.6 165.9  83.0 105.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5079   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN G 602   OD1
REMARK 620 2 GLU G 604   OE2  87.8
REMARK 620 3 ASN G 570   OD1  86.0  62.6
REMARK 620 4 ASN G 602   ND2  43.4  92.3  51.3
REMARK 620 5 ASN G 570   N   112.9 124.4  68.0  75.0
REMARK 620 6 GLU G 383   O    77.8 137.8 152.2 103.0  97.7
REMARK 620 7 GLU G 383   N   129.3 110.4 144.6 156.7  95.3  56.6
REMARK 620 N                    1     2     3     4     5     6
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 GLU G 761   OE2
REMARK 620 2 HIS G 781   ND1  74.8
REMARK 620 3 GLU G 783   O   131.4  97.2
REMARK 620 4 GLN G 784   O    92.7 147.3  68.3
REMARK 620 5 VAL G 787   O    78.4 122.2 137.6  83.1
REMARK 620 6 SER G 792   OG  123.3  82.6 102.2 128.1  71.1
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN G2073  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 HOH G3912   O   106.7  91.4
REMARK 620 4 ADP G2072   O3B 167.9  85.2  76.5
REMARK 620 5 HOH G3913   O    90.4 170.4  83.7 101.6
REMARK 620 6 ADP G2072   O2A  92.9  85.0 159.5  83.1 102.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5074   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 841   OE1
REMARK 620 2 HOH G3879   O   108.4
REMARK 620 3 ADP G2072   O2B 101.1  97.4
REMARK 620 4 HOH G3916   O    66.5 149.5  56.7
REMARK 620 5 GLU G 841   OE2  45.6  64.9  93.6  98.2
REMARK 620 6 ADP G2072   O3B  90.3  59.8  44.7  89.8  57.3
REMARK 620 7 ASN G 843   OD1  69.4  64.1 153.0 131.9  61.3 108.7
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K H5081   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 112   O
REMARK 620 2 HIS H  16   O    84.1
REMARK 620 3 HOH G3832   O   133.6 141.7
REMARK 620 4 HOH H3992   O   146.3  75.5  73.3
REMARK 620 5 HOH H3831   O    80.5 109.4  87.2  81.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K A5013   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A5134   O
REMARK 620 2 HOH A5139   O    72.4
REMARK 620 3 HOH A5820   O   128.5  56.1
REMARK 620 4 ALA A 144   O    58.8  89.5 117.9
REMARK 620 5 THR A 143   OG1  64.3 136.5 165.8  72.7
REMARK 620 6 THR A 143   O   111.1 141.0 110.0  63.9  64.8
REMARK 620 7 HOH A5140   O   130.1 142.2  94.3 127.5  71.6  66.5
REMARK 620 N                    1     2     3     4     5     6
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 HOH C5156   O
REMARK 620 2 HOH C5161   O    61.8
REMARK 620 3 HOH C5162   O   130.1 144.6
REMARK 620 4 THR C 143   O   109.9 152.1  62.2
REMARK 620 5 HOH C5620   O    67.2  70.9  83.8 133.1
REMARK 620 6 THR C 143   OG1  57.6 117.3  75.9  68.3  72.9
REMARK 620 7 ALA C 144   O    53.7  85.6 129.3  70.0 120.7  71.6
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                               K G5078   K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G3511   O
REMARK 620 2 HOH G3506   O   135.1
REMARK 620 3 ALA G 144   O   129.0  63.5
REMARK 620 4 THR G 143   OG1  77.1  69.0  68.9
REMARK 620 5 THR G 143   O    65.2 122.2  66.9  66.9
REMARK 620 N                    1     2     3     4
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 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5014
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5015
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 5016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5017
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5018
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5019
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5020
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 5021
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 2024
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 2025
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5026
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5027
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 2030
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5031
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5032
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5035
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5036
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5037
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 5038
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5039
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5040
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5041
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5042
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 5043
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5044
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 2046
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 2047
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 2048
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5049
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 2052
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5053
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5054
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5057
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5058
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5059
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 5060
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5061
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5062
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5063
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5064
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 5065
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 2067
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 2068
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 2069
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5070
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 2073
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5074
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5075
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5078
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5079
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5080
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 5081
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5082
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5083
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5084
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5085
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 5086
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 2028
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 2050
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 2071
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 5011
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 5012
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 2023
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 2029
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 5033
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 5034
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 2045
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 2051
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 5055
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 5056
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 2066
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 2072
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 5076
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 5077
DBREF  1KEE A    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1KEE C    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1KEE E    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1KEE G    1  1073  UNP    P00968   CARB_ECOLI       0   1072
DBREF  1KEE B    1   382  UNP    P00907   CARA_ECOLI       1    382
DBREF  1KEE D    1   382  UNP    P00907   CARA_ECOLI       1    382
DBREF  1KEE F    1   382  UNP    P00907   CARA_ECOLI       1    382
DBREF  1KEE H    1   382  UNP    P00907   CARA_ECOLI       1    382
SEQADV 1KEE 143 B  269  UNP  P00907    CYS   269 MODIFIED RESIDUE
SEQADV 1KEE 143 D  269  UNP  P00907    CYS   269 MODIFIED RESIDUE
SEQADV 1KEE 143 F  269  UNP  P00907    CYS   269 MODIFIED RESIDUE
SEQADV 1KEE 143 H  269  UNP  P00907    CYS   269 MODIFIED RESIDUE
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 LEU 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  GLU 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 143 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 LEU 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  GLU 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 143 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 LEU 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  GLU 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 143 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 LEU 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  GLU 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 143 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
MODRES 1KEE 143 B  269  CYS
MODRES 1KEE 143 D  269  CYS
MODRES 1KEE 143 F  269  CYS
MODRES 1KEE 143 H  269  CYS
HET    143  B 269      16
HET    143  D 269      16
HET    143  F 269      16
HET    143  H 269      16
HET     MN  A2002       1
HET     MN  A2003       1
HET      K  A5004       1
HET      K  A5005       1
HET     MN  A5008       1
HET      K  A5009       1
HET      K  A5010       1
HET      K  A5013       1
HET      K  A5014       1
HET      K  A5015       1
HET      K  B5016       1
HET     CL  A5017       1
HET     CL  A5018       1
HET     CL  A5019       1
HET     CL  A5020       1
HET     CL  B5021       1
HET     CL  A5022       1
HET     MN  C2024       1
HET     MN  C2025       1
HET      K  C5026       1
HET      K  C5027       1
HET     MN  C2030       1
HET      K  C5031       1
HET      K  C5032       1
HET      K  C5035       1
HET      K  C5036       1
HET      K  C5037       1
HET      K  D5038       1
HET     CL  C5039       1
HET     CL  C5040       1
HET     CL  C5041       1
HET     CL  C5042       1
HET     CL  D5043       1
HET     CL  C5044       1
HET     MN  E2046       1
HET     MN  E2047       1
HET      K  E2048       1
HET      K  E5049       1
HET     MN  E2052       1
HET      K  E5053       1
HET      K  E5054       1
HET      K  E5057       1
HET      K  E5058       1
HET      K  E5059       1
HET      K  F5060       1
HET     CL  E5061       1
HET     CL  E5062       1
HET     CL  E5063       1
HET     CL  E5064       1
HET     CL  F5065       1
HET     MN  G2067       1
HET     MN  G2068       1
HET      K  G2069       1
HET      K  G5070       1
HET     MN  G2073       1
HET      K  G5074       1
HET      K  G5075       1
HET      K  G5078       1
HET      K  G5079       1
HET      K  G5080       1
HET      K  H5081       1
HET     CL  G5082       1
HET     CL  G5083       1
HET     CL  G5084       1
HET     CL  G5085       1
HET     CL  H5086       1
HET    PO4  A2006       5
HET    PO4  C2028       5
HET    PO4  E2050       5
HET    PO4  G2071       5
HET    ADP  A2001      27
HET    ADP  A2007      27
HET    ORN  A5011       9
HET    NET  A5012       9
HET    ADP  C2023      27
HET    ADP  C2029      27
HET    ORN  C5033       9
HET    NET  C5034       9
HET    ADP  E2045      27
HET    ADP  E2051      27
HET    ORN  E5055       9
HET    NET  E5056       9
HET    ADP  G2066      27
HET    ADP  G2072      27
HET    ORN  G5076       9
HET    NET  G5077       9
HETNAM     143 S-2,3-DIHYDRO-5-GLYCIN-2-YL-ISOXAZOL-3-YL-CYSTEINE
HETNAM      MN MANGANESE (II) ION
HETNAM       K POTASSIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     PO4 PHOSPHATE ION
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM     ORN L-ORNITHINE
HETNAM     NET TETRAETHYLAMMONIUM ION
HETSYN     143 2-AMINO-3-[5-(AMINO-CARBOXY-METHYL)-2,3-DIHYDRO-
HETSYN   2 143  ISOXAZOL-3-YLSULFANYL]-PROPIONIC ACID
FORMUL   2  143    4(C8 H13 N3 O5 S)
FORMUL   9   MN    12(MN 2+)
FORMUL  11    K    32(K 1+)
FORMUL  20   CL    22(CL 1-)
FORMUL  75  PO4    4(O4 P 3-)
FORMUL  79  ADP    8(C10 H15 N5 O10 P2)
FORMUL  81  ORN    4(C5 H12 N2 O2)
FORMUL  82  NET    4(C8 H20 N 1+)
FORMUL  95  HOH   *4176(H2 O)
HELIX    1   1 CYS A   24  GLU A   40  1                                  17
HELIX    2   2 THR A   53  ASP A   57  5                                   5
HELIX    3   3 HIS A   70  ARG A   82  1                                  13
HELIX    4   4 GLY A   91  GLN A  105  1                                  15
HELIX    5   5 GLY A  106  GLY A  112  1                                   7
HELIX    6   6 THR A  119  ASP A  128  1                                  10
HELIX    7   7 ASP A  128  ILE A  139  1                                  12
HELIX    8   8 THR A  151  GLY A  163  1                                  13
HELIX    9   9 ASN A  184  SER A  199  1                                  16
HELIX   10  10 HIS A  243  SER A  247  5                                   5
HELIX   11  11 THR A  257  GLY A  276  1                                  20
HELIX   12  12 SER A  305  GLY A  316  1                                  12
HELIX   13  13 PRO A  318  VAL A  328  1                                  11
HELIX   14  14 THR A  331  LEU A  335  5                                   5
HELIX   15  15 ASN A  363  PHE A  367  5                                   5
HELIX   16  16 THR A  390  LEU A  402  1                                  13
HELIX   17  17 GLU A  419  ASP A  430  1                                  12
HELIX   18  18 ASP A  434  ALA A  445  1                                  12
HELIX   19  19 SER A  448  ASN A  457  1                                  10
HELIX   20  20 ASP A  459  GLY A  480  1                                  22
HELIX   21  21 ILE A  481  LEU A  484  5                                   4
HELIX   22  22 ASN A  485  LYS A  495  1                                  11
HELIX   23  23 ALA A  498  GLY A  507  1                                  10
HELIX   24  24 ARG A  509  ASP A  521  1                                  13
HELIX   25  25 GLY A  575  ASP A  592  1                                  18
HELIX   26  26 THR A  622  LYS A  634  1                                  13
HELIX   27  27 GLY A  644  ALA A  657  1                                  14
HELIX   28  28 SER A  665  ASP A  674  1                                  10
HELIX   29  29 ASP A  674  LYS A  686  1                                  13
HELIX   30  30 ALA A  697  GLY A  709  1                                  13
HELIX   31  31 ASP A  730  ALA A  741  1                                  12
HELIX   32  32 HIS A  788  SER A  792  5                                   5
HELIX   33  33 SER A  802  GLN A  821  1                                  20
HELIX   34  34 THR A  849  GLY A  858  1                                  10
HELIX   35  35 PRO A  860  GLY A  871  1                                  12
HELIX   36  36 SER A  873  GLY A  878  1                                   6
HELIX   37  37 PRO A  896  PHE A  900  5                                   5
HELIX   38  38 THR A  923  SER A  935  1                                  13
HELIX   39  39 ARG A  950  LYS A  954  5                                   5
HELIX   40  40 ARG A  956  GLY A  968  1                                  13
HELIX   41  41 THR A  974  ALA A  984  1                                  11
HELIX   42  42 HIS A 1000  ASN A 1007  1                                   8
HELIX   43  43 GLY A 1019  TYR A 1036  1                                  18
HELIX   44  44 THR A 1043  LEU A 1054  1                                  12
HELIX   45  45 SER A 1064  ILE A 1072  1                                   9
HELIX   46  46 GLY B   38  THR B   44  1                                   7
HELIX   47  47 ASP B   45  SER B   49  5                                   5
HELIX   48  48 ASN B   66  GLU B   70  5                                   5
HELIX   49  49 ASP B   97  HIS B  105  1                                   9
HELIX   50  50 ASP B  114  GLY B  126  1                                  13
HELIX   51  51 ASP B  139  ALA B  149  1                                  11
HELIX   52  52 LEU B  158  THR B  163  1                                   6
HELIX   53  53 LYS B  186  LEU B  190  5                                   5
HELIX   54  54 LYS B  202  ARG B  212  1                                  11
HELIX   55  55 SER B  224  LYS B  230  1                                   7
HELIX   56  56 CYS B  248  GLU B  260  1                                  13
HELIX   57  57 143 B  269  SER B  279  1                                  11
HELIX   58  58 GLU B  318  LEU B  321  5                                   4
HELIX   59  59 ALA B  364  THR B  380  1                                  17
HELIX   60  60 CYS C   24  GLU C   40  1                                  17
HELIX   61  61 THR C   53  ALA C   61  5                                   9
HELIX   62  62 HIS C   70  ARG C   82  1                                  13
HELIX   63  63 GLY C   91  GLN C  105  1                                  15
HELIX   64  64 GLY C  106  PHE C  111  1                                   6
HELIX   65  65 THR C  119  ASP C  128  1                                  10
HELIX   66  66 ASP C  128  ILE C  139  1                                  12
HELIX   67  67 THR C  151  GLY C  163  1                                  13
HELIX   68  68 ASN C  184  SER C  199  1                                  16
HELIX   69  69 HIS C  243  SER C  247  5                                   5
HELIX   70  70 THR C  257  GLY C  276  1                                  20
HELIX   71  71 SER C  305  GLY C  316  1                                  12
HELIX   72  72 PRO C  318  ALA C  327  1                                  10
HELIX   73  73 THR C  331  LEU C  335  5                                   5
HELIX   74  74 ASN C  337  GLY C  341  5                                   5
HELIX   75  75 ASN C  363  PHE C  367  5                                   5
HELIX   76  76 THR C  390  LEU C  402  1                                  13
HELIX   77  77 GLU C  419  ASP C  430  1                                  12
HELIX   78  78 ASP C  434  ALA C  445  1                                  12
HELIX   79  79 SER C  448  ASN C  457  1                                  10
HELIX   80  80 ASP C  459  GLY C  480  1                                  22
HELIX   81  81 ASN C  485  LYS C  495  1                                  11
HELIX   82  82 ALA C  498  GLY C  507  1                                  10
HELIX   83  83 ARG C  509  ASP C  521  1                                  13
HELIX   84  84 GLY C  575  ASP C  592  1                                  18
HELIX   85  85 ASP C  609  SER C  613  5                                   5
HELIX   86  86 THR C  622  LYS C  634  1                                  13
HELIX   87  87 GLY C  644  ALA C  657  1                                  14
HELIX   88  88 SER C  665  ASP C  674  1                                  10
HELIX   89  89 ASP C  674  LEU C  685  1                                  12
HELIX   90  90 ALA C  697  GLY C  709  1                                  13
HELIX   91  91 ASP C  730  ALA C  741  1                                  12
HELIX   92  92 HIS C  788  SER C  792  5                                   5
HELIX   93  93 SER C  802  GLN C  821  1                                  20
HELIX   94  94 THR C  849  GLY C  858  1                                  10
HELIX   95  95 PRO C  860  ALA C  870  1                                  11
HELIX   96  96 SER C  873  GLY C  878  1                                   6
HELIX   97  97 PRO C  896  PHE C  900  5                                   5
HELIX   98  98 THR C  923  SER C  935  1                                  13
HELIX   99  99 ARG C  950  LYS C  954  5                                   5
HELIX  100 100 GLU C  955  GLU C  955  5                                   1
HELIX  101 101 ARG C  956  GLN C  967  1                                  12
HELIX  102 102 THR C  974  ALA C  984  1                                  11
HELIX  103 103 HIS C 1000  GLY C 1008  1                                   9
HELIX  104 104 GLY C 1019  LYS C 1037  1                                  19
HELIX  105 105 THR C 1043  LEU C 1054  1                                  12
HELIX  106 106 SER C 1064  GLN C 1071  1                                   8
HELIX  107 107 GLY D   38  THR D   44  1                                   7
HELIX  108 108 ASP D   45  SER D   49  5                                   5
HELIX  109 109 ASN D   66  GLU D   70  5                                   5
HELIX  110 110 ASP D   97  HIS D  105  1                                   9
HELIX  111 111 ASP D  114  GLY D  126  1                                  13
HELIX  112 112 ASP D  139  PHE D  150  1                                  12
HELIX  113 113 LEU D  158  THR D  163  1                                   6
HELIX  114 114 LYS D  186  LEU D  190  5                                   5
HELIX  115 115 LYS D  202  ARG D  212  1                                  11
HELIX  116 116 SER D  224  LYS D  230  1                                   7
HELIX  117 117 CYS D  248  LEU D  259  1                                  12
HELIX  118 118 143 D  269  SER D  279  1                                  11
HELIX  119 119 GLU D  318  LEU D  321  5                                   4
HELIX  120 120 ALA D  364  THR D  380  1                                  17
HELIX  121 121 CYS E   24  GLU E   40  1                                  17
HELIX  122 122 THR E   53  ALA E   61  5                                   9
HELIX  123 123 HIS E   70  ARG E   82  1                                  13
HELIX  124 124 GLY E   91  GLN E  105  1                                  15
HELIX  125 125 GLY E  106  PHE E  111  1                                   6
HELIX  126 126 THR E  119  ASP E  128  1                                  10
HELIX  127 127 ASP E  128  GLY E  140  1                                  13
HELIX  128 128 THR E  151  GLY E  163  1                                  13
HELIX  129 129 ASN E  184  SER E  199  1                                  16
HELIX  130 130 HIS E  243  SER E  247  5                                   5
HELIX  131 131 THR E  257  GLY E  276  1                                  20
HELIX  132 132 SER E  305  GLY E  316  1                                  12
HELIX  133 133 PRO E  318  ALA E  327  1                                  10
HELIX  134 134 ASN E  337  GLY E  341  5                                   5
HELIX  135 135 ASN E  363  ALA E  368  5                                   6
HELIX  136 136 THR E  390  GLY E  401  1                                  12
HELIX  137 137 GLU E  419  ASP E  430  1                                  12
HELIX  138 138 ASP E  434  ALA E  445  1                                  12
HELIX  139 139 SER E  448  ASN E  457  1                                  10
HELIX  140 140 ASP E  459  GLY E  480  1                                  22
HELIX  141 141 ILE E  481  LEU E  484  5                                   4
HELIX  142 142 ASN E  485  LYS E  495  1                                  11
HELIX  143 143 ALA E  498  GLY E  507  1                                  10
HELIX  144 144 ARG E  509  ASP E  521  1                                  13
HELIX  145 145 GLY E  575  GLY E  593  1                                  19
HELIX  146 146 THR E  605  SER E  613  5                                   9
HELIX  147 147 THR E  622  LYS E  634  1                                  13
HELIX  148 148 GLY E  644  LYS E  649  1                                   6
HELIX  149 149 LEU E  650  ALA E  657  1                                   8
HELIX  150 150 SER E  665  ASP E  674  1                                  10
HELIX  151 151 ASP E  674  LYS E  686  1                                  13
HELIX  152 152 ALA E  697  GLY E  709  1                                  13
HELIX  153 153 ASP E  730  ALA E  741  1                                  12
HELIX  154 154 HIS E  788  SER E  792  5                                   5
HELIX  155 155 SER E  802  GLN E  821  1                                  20
HELIX  156 156 THR E  849  GLY E  858  1                                  10
HELIX  157 157 PRO E  860  GLY E  871  1                                  12
HELIX  158 158 SER E  873  GLY E  878  1                                   6
HELIX  159 159 PRO E  896  PHE E  900  5                                   5
HELIX  160 160 THR E  923  SER E  935  1                                  13
HELIX  161 161 ARG E  956  GLY E  968  1                                  13
HELIX  162 162 THR E  974  GLU E  983  1                                  10
HELIX  163 163 LYS E  993  GLY E  997  5                                   5
HELIX  164 164 HIS E 1000  ASN E 1007  1                                   8
HELIX  165 165 GLY E 1019  TYR E 1036  1                                  18
HELIX  166 166 THR E 1043  LEU E 1054  1                                  12
HELIX  167 167 SER E 1064  GLN E 1071  1                                   8
HELIX  168 168 GLY F   38  THR F   44  1                                   7
HELIX  169 169 ASP F   45  SER F   49  5                                   5
HELIX  170 170 ASN F   66  GLU F   70  5                                   5
HELIX  171 171 ASP F   97  HIS F  105  1                                   9
HELIX  172 172 ASP F  114  GLY F  126  1                                  13
HELIX  173 173 ASP F  139  PHE F  150  1                                  12
HELIX  174 174 LEU F  158  THR F  163  1                                   6
HELIX  175 175 LYS F  186  LEU F  190  5                                   5
HELIX  176 176 LYS F  202  ARG F  212  1                                  11
HELIX  177 177 SER F  224  LYS F  230  1                                   7
HELIX  178 178 CYS F  248  LEU F  259  1                                  12
HELIX  179 179 143 F  269  SER F  279  1                                  11
HELIX  180 180 ALA F  364  THR F  380  1                                  17
HELIX  181 181 CYS G   24  GLU G   40  1                                  17
HELIX  182 182 THR G   53  ALA G   61  5                                   9
HELIX  183 183 HIS G   70  ARG G   82  1                                  13
HELIX  184 184 GLY G   91  GLN G  105  1                                  15
HELIX  185 185 GLY G  106  PHE G  111  1                                   6
HELIX  186 186 THR G  119  ASP G  128  1                                  10
HELIX  187 187 ASP G  128  ILE G  139  1                                  12
HELIX  188 188 THR G  151  GLY G  163  1                                  13
HELIX  189 189 ASN G  184  SER G  199  1                                  16
HELIX  190 190 HIS G  243  SER G  247  5                                   5
HELIX  191 191 THR G  257  GLY G  276  1                                  20
HELIX  192 192 SER G  305  GLY G  316  1                                  12
HELIX  193 193 PRO G  318  VAL G  328  1                                  11
HELIX  194 194 THR G  331  LEU G  335  5                                   5
HELIX  195 195 ASN G  337  GLY G  341  5                                   5
HELIX  196 196 ASN G  363  PHE G  367  5                                   5
HELIX  197 197 THR G  390  LEU G  402  1                                  13
HELIX  198 198 GLU G  419  ASP G  430  1                                  12
HELIX  199 199 ASP G  434  ALA G  445  1                                  12
HELIX  200 200 SER G  448  ASN G  457  1                                  10
HELIX  201 201 ASP G  459  GLY G  480  1                                  22
HELIX  202 202 ASN G  485  LYS G  495  1                                  11
HELIX  203 203 ALA G  498  GLY G  507  1                                  10
HELIX  204 204 ARG G  509  ASP G  521  1                                  13
HELIX  205 205 GLY G  575  ASP G  592  1                                  18
HELIX  206 206 ASP G  609  SER G  613  5                                   5
HELIX  207 207 THR G  622  LYS G  634  1                                  13
HELIX  208 208 GLY G  644  LYS G  649  1                                   6
HELIX  209 209 LEU G  650  ALA G  657  1                                   8
HELIX  210 210 SER G  665  ASP G  674  1                                  10
HELIX  211 211 ASP G  674  LEU G  685  1                                  12
HELIX  212 212 ALA G  697  GLY G  709  1                                  13
HELIX  213 213 ASP G  730  ALA G  741  1                                  12
HELIX  214 214 HIS G  788  SER G  792  5                                   5
HELIX  215 215 SER G  802  GLN G  821  1                                  20
HELIX  216 216 THR G  849  GLY G  858  1                                  10
HELIX  217 217 PRO G  860  ALA G  870  1                                  11
HELIX  218 218 SER G  873  GLY G  878  1                                   6
HELIX  219 219 LEU G  895  PHE G  900  5                                   6
HELIX  220 220 THR G  923  SER G  935  1                                  13
HELIX  221 221 ARG G  950  GLU G  955  1                                   6
HELIX  222 222 ARG G  956  GLN G  967  1                                  12
HELIX  223 223 THR G  974  ALA G  984  1                                  11
HELIX  224 224 HIS G 1000  ASN G 1007  1                                   8
HELIX  225 225 GLY G 1019  TYR G 1036  1                                  18
HELIX  226 226 THR G 1043  ASN G 1055  1                                  13
HELIX  227 227 SER G 1064  ALA G 1070  1                                   7
HELIX  228 228 GLY H   38  THR H   44  1                                   7
HELIX  229 229 ASP H   45  SER H   49  5                                   5
HELIX  230 230 ASN H   66  GLU H   70  5                                   5
HELIX  231 231 ASP H   97  HIS H  105  1                                   9
HELIX  232 232 ASP H  114  GLY H  126  1                                  13
HELIX  233 233 ASP H  139  PHE H  150  1                                  12
HELIX  234 234 LEU H  158  THR H  163  1                                   6
HELIX  235 235 LYS H  186  LEU H  190  5                                   5
HELIX  236 236 LYS H  202  ARG H  212  1                                  11
HELIX  237 237 SER H  224  LYS H  230  1                                   7
HELIX  238 238 CYS H  248  LEU H  259  1                                  12
HELIX  239 239 143 H  269  GLY H  280  1                                  12
HELIX  240 240 GLU H  318  LEU H  321  5                                   4
HELIX  241 241 PRO H  360  ALA H  363  5                                   4
HELIX  242 242 ALA H  364  THR H  380  1                                  17
SHEET    1   A 5 ALA A  63  TYR A  65  0
SHEET    2   A 5 ARG A  43  VAL A  47  1  N  LEU A  46   O  TYR A  65
SHEET    3   A 5 SER A   9  LEU A  13  1  N  ILE A  12   O  ILE A  45
SHEET    4   A 5 ALA A  85  LEU A  87  1  O  LEU A  87   N  LEU A  11
SHEET    5   A 5 THR A 114  MET A 115  1  O  THR A 114   N  VAL A  86
SHEET    1   B 4 SER A 146  ALA A 149  0
SHEET    2   B 4 LEU A 204  GLU A 208 -1  O  ILE A 206   N  GLY A 147
SHEET    3   B 4 CYS A 166  PRO A 170 -1  N  ARG A 169   O  LEU A 205
SHEET    4   B 4 GLY A 180  ALA A 182 -1  O  ALA A 182   N  CYS A 166
SHEET    1   C 7 LEU A 295  ASN A 301  0
SHEET    2   C 7 GLY A 280  VAL A 288 -1  N  GLN A 285   O  GLU A 299
SHEET    3   C 7 LYS A 214  ARG A 222 -1  N  VAL A 220   O  SER A 282
SHEET    4   C 7 CYS A 228  ASN A 236 -1  O  VAL A 231   N  GLU A 219
SHEET    5   C 7 THR A 249  ALA A 251 -1  O  VAL A 250   N  GLU A 235
SHEET    6   C 7 VAL A 355  ARG A 361 -1  O  LYS A 358   N  THR A 249
SHEET    7   C 7 GLY A 382  GLY A 388 -1  O  GLY A 388   N  VAL A 355
SHEET    1   D 6 VAL A 525  ARG A 528  0
SHEET    2   D 6 TYR A 542  THR A 546 -1  O  THR A 546   N  VAL A 525
SHEET    3   D 6 ARG A 615  PHE A 618  1  O  LEU A 616   N  MET A 543
SHEET    4   D 6 GLU A 595  ASN A 600  1  N  MET A 598   O  TYR A 617
SHEET    5   D 6 LYS A 561  LEU A 565  1  N  ILE A 562   O  GLU A 595
SHEET    6   D 6 GLY A 637  ILE A 639  1  O  ILE A 639   N  MET A 563
SHEET    1   E 2 ASN A 692  THR A 694  0
SHEET    2   E 2 LEU A 751  ASP A 753 -1  O  LEU A 752   N  ALA A 693
SHEET    1   F 7 GLU A 836  ASN A 843  0
SHEET    2   F 7 GLY A 824  LYS A 833 -1  N  ASN A 827   O  ASN A 843
SHEET    3   F 7 VAL A 760  CYS A 768 -1  N  ALA A 766   O  MET A 826
SHEET    4   F 7 VAL A 773  HIS A 781 -1  O  LEU A 774   N  ILE A 767
SHEET    5   F 7 CYS A 794  LEU A 796 -1  O  SER A 795   N  GLU A 780
SHEET    6   F 7 TYR A 888  VAL A 894 -1  O  LYS A 891   N  CYS A 794
SHEET    7   F 7 GLY A 915  GLY A 921 -1  O  GLY A 919   N  VAL A 890
SHEET    1   G 5 ARG A 989  LEU A 990  0
SHEET    2   G 5 PHE A 969  ALA A 973  1  N  ALA A 973   O  ARG A 989
SHEET    3   G 5 GLY A 943  SER A 948  1  N  ALA A 945   O  GLU A 970
SHEET    4   G 5 TYR A1012  ASN A1015  1  O  ILE A1014   N  LEU A 946
SHEET    5   G 5 HIS A1039  ASP A1041  1  O  HIS A1039   N  ILE A1013
SHEET    1   H 8 SER B   4  LEU B   9  0
SHEET    2   H 8 GLN B  14  ALA B  19 -1  O  PHE B  15   N  LEU B   7
SHEET    3   H 8 VAL B 108  ALA B 111 -1  O  ALA B 111   N  ARG B  18
SHEET    4   H 8 GLY B  79  VAL B  81  1  N  LEU B  80   O  ILE B 110
SHEET    5   H 8 GLN B  51  LEU B  55  1  N  VAL B  53   O  VAL B  81
SHEET    6   H 8 GLY B  24  ASN B  33  1  N  GLU B  29   O  ILE B  52
SHEET    7   H 8 GLN B 128  ALA B 134 -1  O  GLN B 128   N  VAL B  30
SHEET    8   H 8 SER B   4  LEU B   9 -1  N  VAL B   8   O  CYS B 131
SHEET    1   I10 TYR B 168  TRP B 170  0
SHEET    2   I10 CYS B 214  PRO B 220 -1  O  ILE B 218   N  TYR B 168
SHEET    3   I10 PHE B 192  ASP B 198  1  N  ALA B 196   O  VAL B 219
SHEET    4   I10 GLY B 235  LEU B 238  1  O  PHE B 237   N  VAL B 195
SHEET    5   I10 VAL B 265  ILE B 268  1  O  PHE B 266   N  LEU B 238
SHEET    6   I10 ALA B 347  PHE B 350  1  O  PHE B 348   N  VAL B 265
SHEET    7   I10 LEU B 337  ARG B 342 -1  N  ILE B 340   O  SER B 349
SHEET    8   I10 LEU B 325  SER B 331 -1  N  HIS B 329   O  GLN B 338
SHEET    9   I10 THR B 283  ASP B 299 -1  N  LYS B 298   O  LYS B 330
SHEET   10   I10 VAL B 304  VAL B 316 -1  O  ALA B 315   N  VAL B 284
SHEET    1   J 5 ALA C  63  TYR C  65  0
SHEET    2   J 5 ARG C  43  VAL C  47  1  N  LEU C  46   O  TYR C  65
SHEET    3   J 5 SER C   9  LEU C  13  1  N  ILE C  12   O  ILE C  45
SHEET    4   J 5 ALA C  85  LEU C  87  1  O  ALA C  85   N  LEU C  11
SHEET    5   J 5 THR C 114  MET C 115  1  O  THR C 114   N  VAL C  86
SHEET    1   K 4 SER C 146  ALA C 149  0
SHEET    2   K 4 LEU C 204  GLU C 208 -1  O  ILE C 206   N  GLY C 147
SHEET    3   K 4 CYS C 166  PRO C 170 -1  N  ARG C 169   O  LEU C 205
SHEET    4   K 4 GLY C 180  ALA C 182 -1  O  ALA C 182   N  CYS C 166
SHEET    1   L 7 LEU C 295  ASN C 301  0
SHEET    2   L 7 GLY C 280  VAL C 288 -1  N  GLN C 285   O  ILE C 298
SHEET    3   L 7 LYS C 214  ARG C 222 -1  N  ARG C 222   O  GLY C 280
SHEET    4   L 7 CYS C 228  ASN C 236 -1  O  ILE C 229   N  VAL C 221
SHEET    5   L 7 THR C 249  ALA C 251 -1  O  VAL C 250   N  GLU C 235
SHEET    6   L 7 VAL C 355  ARG C 361 -1  O  LYS C 358   N  THR C 249
SHEET    7   L 7 GLY C 382  GLY C 388 -1  O  GLY C 382   N  ARG C 361
SHEET    1   M 6 VAL C 525  ARG C 528  0
SHEET    2   M 6 ALA C 541  THR C 546 -1  O  THR C 546   N  VAL C 525
SHEET    3   M 6 ARG C 615  TYR C 617  1  O  LEU C 616   N  ALA C 541
SHEET    4   M 6 GLU C 595  VAL C 599  1  N  MET C 598   O  TYR C 617
SHEET    5   M 6 LYS C 561  LEU C 565  1  N  ILE C 562   O  GLU C 595
SHEET    6   M 6 GLY C 637  ILE C 639  1  O  ILE C 639   N  MET C 563
SHEET    1   N 2 ASN C 692  THR C 694  0
SHEET    2   N 2 LEU C 751  ASP C 753 -1  O  LEU C 752   N  ALA C 693
SHEET    1   O 2 LEU C 712  VAL C 714  0
SHEET    2   O 2 GLU C 726  VAL C 728 -1  O  VAL C 728   N  LEU C 712
SHEET    1   P 7 GLU C 836  ASN C 843  0
SHEET    2   P 7 GLY C 824  LYS C 833 -1  N  ASN C 827   O  ASN C 843
SHEET    3   P 7 VAL C 760  CYS C 768 -1  N  VAL C 762   O  PHE C 830
SHEET    4   P 7 VAL C 773  HIS C 781 -1  O  LEU C 774   N  ILE C 767
SHEET    5   P 7 CYS C 794  LEU C 796 -1  O  SER C 795   N  GLU C 780
SHEET    6   P 7 TYR C 888  VAL C 894 -1  O  SER C 889   N  LEU C 796
SHEET    7   P 7 GLY C 915  GLY C 921 -1  O  GLY C 921   N  TYR C 888
SHEET    1   Q 5 ARG C 989  LEU C 990  0
SHEET    2   Q 5 PHE C 969  ALA C 973  1  N  ALA C 973   O  ARG C 989
SHEET    3   Q 5 GLY C 943  SER C 948  1  N  ALA C 945   O  GLU C 970
SHEET    4   Q 5 TYR C1012  ASN C1015  1  O  ILE C1014   N  LEU C 946
SHEET    5   Q 5 HIS C1039  ASP C1041  1  O  ASP C1041   N  ILE C1013
SHEET    1   R 8 SER D   4  LEU D   9  0
SHEET    2   R 8 GLN D  14  ALA D  19 -1  O  PHE D  15   N  LEU D   7
SHEET    3   R 8 VAL D 108  ALA D 111 -1  O  ALA D 111   N  ARG D  18
SHEET    4   R 8 GLY D  79  VAL D  81  1  N  LEU D  80   O  ILE D 110
SHEET    5   R 8 GLN D  51  LEU D  55  1  N  VAL D  53   O  VAL D  81
SHEET    6   R 8 GLY D  24  ASN D  33  1  N  GLU D  29   O  ILE D  52
SHEET    7   R 8 GLN D 128  ALA D 134 -1  O  ALA D 134   N  GLY D  24
SHEET    8   R 8 SER D   4  LEU D   9 -1  N  LEU D   6   O  ILE D 133
SHEET    1   S10 TYR D 168  TRP D 170  0
SHEET    2   S10 CYS D 214  PRO D 220 -1  O  ILE D 218   N  TYR D 168
SHEET    3   S10 PHE D 192  ASP D 198  1  N  PHE D 192   O  ARG D 215
SHEET    4   S10 GLY D 235  LEU D 238  1  O  PHE D 237   N  TYR D 197
SHEET    5   S10 VAL D 265  ILE D 268  1  O  PHE D 266   N  ILE D 236
SHEET    6   S10 ALA D 347  PHE D 350  1  O  PHE D 348   N  VAL D 265
SHEET    7   S10 LEU D 337  ARG D 342 -1  N  ILE D 340   O  SER D 349
SHEET    8   S10 LEU D 325  SER D 331 -1  N  ARG D 326   O  HIS D 341
SHEET    9   S10 THR D 283  ASP D 299 -1  N  LYS D 298   O  LYS D 330
SHEET   10   S10 VAL D 304  VAL D 316 -1  O  ALA D 315   N  VAL D 284
SHEET    1   T 5 ALA E  63  TYR E  65  0
SHEET    2   T 5 ARG E  43  VAL E  47  1  N  LEU E  46   O  TYR E  65
SHEET    3   T 5 SER E   9  LEU E  13  1  N  ILE E  12   O  ILE E  45
SHEET    4   T 5 ALA E  85  LEU E  87  1  O  ALA E  85   N  LEU E  11
SHEET    5   T 5 THR E 114  MET E 115  1  O  THR E 114   N  VAL E  86
SHEET    1   U 4 SER E 146  ALA E 149  0
SHEET    2   U 4 LEU E 204  GLU E 208 -1  O  LEU E 204   N  ALA E 149
SHEET    3   U 4 CYS E 166  PRO E 170 -1  N  ILE E 167   O  ASP E 207
SHEET    4   U 4 GLY E 180  ALA E 182 -1  O  ALA E 182   N  CYS E 166
SHEET    1   V 7 LEU E 295  ASN E 301  0
SHEET    2   V 7 GLY E 280  VAL E 288 -1  N  GLN E 285   O  GLU E 299
SHEET    3   V 7 LYS E 214  ARG E 222 -1  N  LYS E 214   O  VAL E 288
SHEET    4   V 7 CYS E 228  ASN E 236 -1  O  ILE E 234   N  GLU E 217
SHEET    5   V 7 THR E 249  ALA E 251 -1  O  VAL E 250   N  GLU E 235
SHEET    6   V 7 VAL E 355  ARG E 361 -1  O  LYS E 358   N  THR E 249
SHEET    7   V 7 GLY E 382  GLY E 388 -1  O  GLY E 382   N  ARG E 361
SHEET    1   W 6 VAL E 525  ARG E 528  0
SHEET    2   W 6 TYR E 542  THR E 546 -1  O  THR E 546   N  VAL E 525
SHEET    3   W 6 ARG E 615  PHE E 618  1  O  PHE E 618   N  MET E 543
SHEET    4   W 6 GLU E 595  ASN E 600  1  N  MET E 598   O  TYR E 617
SHEET    5   W 6 LYS E 561  LEU E 565  1  N  VAL E 564   O  ILE E 597
SHEET    6   W 6 GLY E 637  ILE E 639  1  O  ILE E 639   N  MET E 563
SHEET    1   X 4 ASN E 692  THR E 694  0
SHEET    2   X 4 LEU E 751  HIS E 754 -1  O  LEU E 752   N  ALA E 693
SHEET    3   X 4 LEU E 712  ARG E 715 -1  N  VAL E 713   O  ASP E 753
SHEET    4   X 4 GLU E 726  VAL E 728 -1  O  VAL E 728   N  LEU E 712
SHEET    1   Y 7 GLU E 836  ASN E 843  0
SHEET    2   Y 7 ARG E 823  LYS E 833 -1  N  ALA E 831   O  TYR E 838
SHEET    3   Y 7 VAL E 760  ASP E 769 -1  N  VAL E 764   O  VAL E 828
SHEET    4   Y 7 VAL E 773  GLN E 784 -1  O  LEU E 774   N  ILE E 767
SHEET    5   Y 7 CYS E 794  LEU E 796 -1  O  SER E 795   N  GLU E 780
SHEET    6   Y 7 TYR E 888  VAL E 894 -1  O  LYS E 891   N  CYS E 794
SHEET    7   Y 7 GLY E 915  GLY E 921 -1  O  VAL E 917   N  GLU E 892
SHEET    1   Z 5 ARG E 989  LEU E 990  0
SHEET    2   Z 5 PHE E 969  ALA E 973  1  N  ALA E 973   O  ARG E 989
SHEET    3   Z 5 GLY E 943  SER E 948  1  N  ALA E 945   O  GLU E 970
SHEET    4   Z 5 TYR E1012  ASN E1015  1  O  ILE E1014   N  LEU E 946
SHEET    5   Z 5 HIS E1039  ASP E1041  1  O  ASP E1041   N  ILE E1013
SHEET    1  AA 8 SER F   4  LEU F   9  0
SHEET    2  AA 8 GLN F  14  ALA F  19 -1  O  PHE F  15   N  LEU F   7
SHEET    3  AA 8 VAL F 108  ALA F 111 -1  O  ALA F 111   N  ARG F  18
SHEET    4  AA 8 GLY F  79  VAL F  81  1  N  LEU F  80   O  ILE F 110
SHEET    5  AA 8 GLN F  51  LEU F  55  1  N  VAL F  53   O  VAL F  81
SHEET    6  AA 8 GLY F  24  ASN F  33  1  N  GLU F  29   O  ILE F  52
SHEET    7  AA 8 GLN F 128  ALA F 134 -1  O  GLN F 128   N  VAL F  30
SHEET    8  AA 8 SER F   4  LEU F   9 -1  N  VAL F   8   O  CYS F 131
SHEET    1  AB10 TYR F 168  TRP F 170  0
SHEET    2  AB10 CYS F 214  PRO F 220 -1  O  LEU F 216   N  TRP F 170
SHEET    3  AB10 PHE F 192  ASP F 198  1  N  PHE F 192   O  ARG F 215
SHEET    4  AB10 GLY F 235  LEU F 238  1  O  GLY F 235   N  VAL F 195
SHEET    5  AB10 VAL F 265  ILE F 268  1  O  PHE F 266   N  LEU F 238
SHEET    6  AB10 ALA F 347  PHE F 350  1  O  PHE F 348   N  VAL F 265
SHEET    7  AB10 LEU F 337  ARG F 342 -1  N  ILE F 340   O  SER F 349
SHEET    8  AB10 LEU F 325  SER F 331 -1  N  HIS F 329   O  GLN F 338
SHEET    9  AB10 THR F 283  ASP F 299 -1  N  LYS F 298   O  LYS F 330
SHEET   10  AB10 VAL F 304  VAL F 316 -1  O  MET F 306   N  VAL F 297
SHEET    1  AC 5 ALA G  63  TYR G  65  0
SHEET    2  AC 5 ARG G  43  VAL G  47  1  N  LEU G  46   O  TYR G  65
SHEET    3  AC 5 SER G   9  LEU G  13  1  N  ILE G  10   O  ARG G  43
SHEET    4  AC 5 ALA G  85  LEU G  87  1  O  ALA G  85   N  LEU G  11
SHEET    5  AC 5 THR G 114  MET G 115  1  O  THR G 114   N  VAL G  86
SHEET    1  AD 4 SER G 146  ALA G 149  0
SHEET    2  AD 4 LEU G 204  GLU G 208 -1  O  LEU G 204   N  ALA G 149
SHEET    3  AD 4 CYS G 166  ILE G 168 -1  N  ILE G 167   O  ASP G 207
SHEET    4  AD 4 GLY G 180  ALA G 182 -1  O  GLY G 180   N  ILE G 168
SHEET    1  AE 7 LEU G 295  ASN G 301  0
SHEET    2  AE 7 GLY G 280  VAL G 288 -1  N  GLN G 285   O  ILE G 298
SHEET    3  AE 7 LYS G 214  ARG G 222 -1  N  VAL G 220   O  SER G 282
SHEET    4  AE 7 CYS G 228  ASN G 236 -1  O  CYS G 232   N  GLU G 219
SHEET    5  AE 7 THR G 249  ALA G 251 -1  O  VAL G 250   N  GLU G 235
SHEET    6  AE 7 VAL G 355  ARG G 361 -1  O  LYS G 358   N  THR G 249
SHEET    7  AE 7 GLY G 382  GLY G 388 -1  O  GLY G 388   N  VAL G 355
SHEET    1  AF 6 VAL G 525  ARG G 528  0
SHEET    2  AF 6 ALA G 541  THR G 546 -1  O  THR G 546   N  VAL G 525
SHEET    3  AF 6 ARG G 615  TYR G 617  1  O  LEU G 616   N  MET G 543
SHEET    4  AF 6 GLU G 595  VAL G 599  1  N  MET G 598   O  TYR G 617
SHEET    5  AF 6 LYS G 561  LEU G 565  1  N  ILE G 562   O  ILE G 597
SHEET    6  AF 6 GLY G 637  ILE G 639  1  O  ILE G 639   N  MET G 563
SHEET    1  AG 2 ASN G 692  THR G 694  0
SHEET    2  AG 2 LEU G 751  ASP G 753 -1  O  LEU G 752   N  ALA G 693
SHEET    1  AH 2 LEU G 712  VAL G 714  0
SHEET    2  AH 2 GLU G 726  VAL G 728 -1  O  VAL G 728   N  LEU G 712
SHEET    1  AI 7 GLU G 836  ASN G 843  0
SHEET    2  AI 7 GLY G 824  LYS G 833 -1  N  ASN G 827   O  ASN G 843
SHEET    3  AI 7 VAL G 760  CYS G 768 -1  N  VAL G 764   O  VAL G 828
SHEET    4  AI 7 VAL G 773  GLN G 784 -1  O  LEU G 774   N  ILE G 767
SHEET    5  AI 7 CYS G 794  LEU G 796 -1  O  SER G 795   N  GLU G 780
SHEET    6  AI 7 TYR G 888  VAL G 894 -1  O  SER G 889   N  LEU G 796
SHEET    7  AI 7 GLY G 915  GLY G 921 -1  O  GLY G 921   N  TYR G 888
SHEET    1  AJ 5 ARG G 989  LEU G 990  0
SHEET    2  AJ 5 GLU G 970  ALA G 973  1  N  ALA G 973   O  ARG G 989
SHEET    3  AJ 5 ARG G 944  SER G 948  1  N  ALA G 945   O  GLU G 970
SHEET    4  AJ 5 TYR G1012  ASN G1015  1  O  ILE G1014   N  LEU G 946
SHEET    5  AJ 5 HIS G1039  ASP G1041  1  O  ASP G1041   N  ILE G1013
SHEET    1  AK 8 SER H   4  LEU H   9  0
SHEET    2  AK 8 GLN H  14  ALA H  19 -1  O  PHE H  15   N  LEU H   7
SHEET    3  AK 8 VAL H 108  ALA H 111 -1  O  ALA H 111   N  ARG H  18
SHEET    4  AK 8 GLY H  79  VAL H  81  1  N  LEU H  80   O  ILE H 110
SHEET    5  AK 8 GLN H  51  LEU H  55  1  N  VAL H  53   O  VAL H  81
SHEET    6  AK 8 GLY H  24  ASN H  33  1  N  GLU H  29   O  ILE H  52
SHEET    7  AK 8 GLN H 128  ALA H 134 -1  O  ALA H 134   N  GLY H  24
SHEET    8  AK 8 SER H   4  LEU H   9 -1  N  LEU H   6   O  ILE H 133
SHEET    1  AL10 TYR H 168  TRP H 170  0
SHEET    2  AL10 CYS H 214  VAL H 219 -1  O  ILE H 218   N  TYR H 168
SHEET    3  AL10 PHE H 192  TYR H 197  1  N  VAL H 194   O  ARG H 215
SHEET    4  AL10 GLY H 235  LEU H 238  1  O  PHE H 237   N  VAL H 195
SHEET    5  AL10 VAL H 265  ILE H 268  1  O  PHE H 266   N  LEU H 238
SHEET    6  AL10 ALA H 347  PHE H 350  1  O  PHE H 350   N  GLY H 267
SHEET    7  AL10 LEU H 337  ARG H 342 -1  N  ILE H 340   O  SER H 349
SHEET    8  AL10 LEU H 325  SER H 331 -1  N  HIS H 329   O  GLN H 338
SHEET    9  AL10 THR H 283  ASP H 299 -1  N  LYS H 298   O  LYS H 330
SHEET   10  AL10 VAL H 304  VAL H 316 -1  O  ALA H 315   N  VAL H 284
LINK         O   GLY A 112                 K     K A5015     1555   1555  2.68
LINK         OE1 GLU A 127                 K     K A5005     1555   1555  2.93
LINK         OE2 GLU A 215                 K     K A5004     1555   1555  2.76
LINK         OD1 ASN A 236                 K     K A5004     1555   1555  2.92
LINK         O   ASP A 238                 K     K A5004     1555   1555  2.82
LINK         O   ALA A 239                 K     K A5004     1555   1555  2.93
LINK         O   ILE A 242                 K     K A5004     1555   1555  2.61
LINK         OG  SER A 247                 K     K A5004     1555   1555  2.78
LINK         OE1 GLN A 285                MN    MN A2003     1555   1555  2.01
LINK         CD  GLU A 299                MN    MN A2002     1555   1555  2.65
LINK         OE1 GLU A 299                 K     K A5005     1555   1555  2.80
LINK         OE1 GLU A 299                MN    MN A2002     1555   1555  2.27
LINK         OE2 GLU A 299                MN    MN A2003     1555   1555  2.34
LINK         OE2 GLU A 299                MN    MN A2002     1555   1555  2.40
LINK         O   MET A 300                 K     K A5005     1555   1555  2.64
LINK         OD1 ASN A 301                MN    MN A2002     1555   1555  1.92
LINK         N   GLU A 383                 K     K A5014     1555   1555  2.93
LINK         OE2 GLU A 761                 K     K A5010     1555   1555  2.58
LINK         ND1 HIS A 781                 K     K A5010     1555   1555  2.69
LINK         O   GLU A 783                 K     K A5010     1555   1555  2.80
LINK         O   GLN A 784                 K     K A5010     1555   1555  2.85
LINK         O   VAL A 787                 K     K A5010     1555   1555  2.60
LINK         OG  SER A 792                 K     K A5010     1555   1555  2.86
LINK         OE1 GLN A 829                MN    MN A5008     1555   1555  2.00
LINK         OE2 GLU A 841                MN    MN A5008     1555   1555  2.34
LINK         OE2 GLU A 841                 K     K A5009     1555   1555  2.66
LINK         OD1 ASN A 843                 K     K A5009     1555   1555  2.48
LINK         O   HIS B  16                 K     K B5016     1555   1555  2.75
LINK         O   ASP B 112                 K     K B5016     1555   1555  2.77
LINK         OG1 THR C 114                 K     K C5037     1555   1555  2.61
LINK         OE2 GLU C 215                 K     K C5026     1555   1555  2.56
LINK         OD1 ASN C 236                 K     K C5026     1555   1555  2.86
LINK         O   ASP C 238                 K     K C5026     1555   1555  2.63
LINK         O   ALA C 239                 K     K C5026     1555   1555  2.79
LINK         O   ILE C 242                 K     K C5026     1555   1555  2.70
LINK         OG  SER C 247                 K     K C5026     1555   1555  2.83
LINK         OE1 GLN C 285                MN    MN C2025     1555   1555  2.06
LINK         CD  GLU C 299                MN    MN C2024     1555   1555  2.65
LINK         OE1 GLU C 299                MN    MN C2024     1555   1555  2.27
LINK         OE1 GLU C 299                 K     K C5027     1555   1555  2.63
LINK         OE2 GLU C 299                MN    MN C2025     1555   1555  2.32
LINK         OE2 GLU C 299                MN    MN C2024     1555   1555  2.40
LINK         O   MET C 300                 K     K C5027     1555   1555  2.74
LINK         OD1 ASN C 301                MN    MN C2024     1555   1555  2.08
LINK         N   GLU C 383                 K     K C5036     1555   1555  2.89
LINK         OD1 ASN C 602                 K     K C5036     1555   1555  2.92
LINK         OE2 GLU C 761                 K     K C5032     1555   1555  2.57
LINK         ND1 HIS C 781                 K     K C5032     1555   1555  2.74
LINK         O   GLU C 783                 K     K C5032     1555   1555  2.81
LINK         O   VAL C 787                 K     K C5032     1555   1555  2.86
LINK         OG  SER C 792                 K     K C5032     1555   1555  2.77
LINK         CD  GLN C 829                MN    MN C2030     1555   1555  2.90
LINK         OE1 GLN C 829                MN    MN C2030     1555   1555  1.90
LINK         OE1 GLU C 841                 K     K C5031     1555   1555  2.87
LINK         OE2 GLU C 841                MN    MN C2030     1555   1555  2.36
LINK         O   HIS D  16                 K     K D5038     1555   1555  2.70
LINK         O   ASP D 112                 K     K D5038     1555   1555  2.79
LINK         O   ASP E  84                 K     K E5059     1555   1555  2.85
LINK         O   GLY E 112                 K     K E5059     1555   1555  2.76
LINK         OG1 THR E 114                 K     K E5059     1555   1555  2.55
LINK         OE1 GLU E 127                 K     K E5049     1555   1555  2.85
LINK         O   THR E 143                 K     K E5057     1555   1555  2.87
LINK         OG1 THR E 143                 K     K E5057     1555   1555  2.89
LINK         O   ALA E 144                 K     K E5057     1555   1555  2.75
LINK         OE2 GLU E 215                 K     K E2048     1555   1555  2.36
LINK         OD1 ASN E 236                 K     K E2048     1555   1555  2.75
LINK         O   ASP E 238                 K     K E2048     1555   1555  2.69
LINK         O   ALA E 239                 K     K E2048     1555   1555  2.90
LINK         O   ILE E 242                 K     K E2048     1555   1555  2.64
LINK         OG  SER E 247                 K     K E2048     1555   1555  2.81
LINK         OE1 GLN E 285                MN    MN E2047     1555   1555  2.01
LINK         CD  GLU E 299                MN    MN E2046     1555   1555  2.64
LINK         OE1 GLU E 299                 K     K E5049     1555   1555  2.70
LINK         OE1 GLU E 299                MN    MN E2046     1555   1555  2.23
LINK         OE2 GLU E 299                MN    MN E2047     1555   1555  2.09
LINK         OE2 GLU E 299                MN    MN E2046     1555   1555  2.44
LINK         O   MET E 300                 K     K E5049     1555   1555  2.67
LINK         OD1 ASN E 301                MN    MN E2046     1555   1555  2.23
LINK         OD1 ASN E 570                 K     K E5058     1555   1555  2.66
LINK         OD1 ASN E 602                 K     K E5058     1555   1555  2.85
LINK         OE2 GLU E 761                 K     K E5054     1555   1555  2.77
LINK         ND1 HIS E 781                 K     K E5054     1555   1555  2.82
LINK         O   GLN E 784                 K     K E5054     1555   1555  2.89
LINK         O   VAL E 787                 K     K E5054     1555   1555  2.55
LINK         OG  SER E 792                 K     K E5054     1555   1555  2.78
LINK         OE1 GLN E 829                MN    MN E2052     1555   1555  2.11
LINK         OE1 GLU E 841                 K     K E5053     1555   1555  2.80
LINK         OE2 GLU E 841                MN    MN E2052     1555   1555  2.13
LINK         O   HIS F  16                 K     K F5060     1555   1555  2.80
LINK         O   ASP F 112                 K     K F5060     1555   1555  2.84
LINK         O   GLY G 112                 K     K G5080     1555   1555  2.77
LINK         OE1 GLU G 127                 K     K G5070     1555   1555  2.92
LINK         OE2 GLU G 215                 K     K G2069     1555   1555  2.24
LINK         O   ASP G 238                 K     K G2069     1555   1555  2.85
LINK         O   ALA G 239                 K     K G2069     1555   1555  2.66
LINK         O   ILE G 242                 K     K G2069     1555   1555  2.63
LINK         OG  SER G 247                 K     K G2069     1555   1555  2.88
LINK         CD  GLN G 285                MN    MN G2068     1555   1555  2.90
LINK         OE1 GLN G 285                MN    MN G2068     1555   1555  1.92
LINK         CD  GLU G 299                MN    MN G2067     1555   1555  2.79
LINK         OE1 GLU G 299                 K     K G5070     1555   1555  2.86
LINK         OE1 GLU G 299                MN    MN G2067     1555   1555  2.35
LINK         OE2 GLU G 299                MN    MN G2068     1555   1555  2.10
LINK         OE2 GLU G 299                MN    MN G2067     1555   1555  2.60
LINK         O   MET G 300                 K     K G5070     1555   1555  2.83
LINK         OD1 ASN G 301                MN    MN G2067     1555   1555  2.22
LINK         OD1 ASN G 602                 K     K G5079     1555   1555  2.76
LINK         OE2 GLU G 761                 K     K G5075     1555   1555  2.54
LINK         ND1 HIS G 781                 K     K G5075     1555   1555  2.71
LINK         O   GLU G 783                 K     K G5075     1555   1555  2.89
LINK         O   GLN G 784                 K     K G5075     1555   1555  2.68
LINK         O   VAL G 787                 K     K G5075     1555   1555  2.73
LINK         OG  SER G 792                 K     K G5075     1555   1555  2.66
LINK         OE1 GLN G 829                MN    MN G2073     1555   1555  2.08
LINK         OE1 GLU G 841                 K     K G5074     1555   1555  2.53
LINK         OE2 GLU G 841                MN    MN G2073     1555   1555  2.35
LINK         O   ASP H 112                 K     K H5081     1555   1555  2.60
LINK        MN    MN A2002                 O3B ADP A2001     1555   1555  2.16
LINK        MN    MN A2002                 O1  PO4 A2006     1555   1555  2.06
LINK        MN    MN A2002                 O   HOH A5129     1555   1555  2.01
LINK        MN    MN A2003                 O1B ADP A2001     1555   1555  2.19
LINK        MN    MN A2003                 O1A ADP A2001     1555   1555  2.06
LINK        MN    MN A2003                 O   HOH A5185     1555   1555  2.06
LINK        MN    MN A2003                 O3  PO4 A2006     1555   1555  2.25
LINK         K     K A5005                 O   HOH A5128     1555   1555  2.87
LINK        MN    MN A5008                 O2A ADP A2007     1555   1555  2.11
LINK        MN    MN A5008                 O   HOH A5502     1555   1555  2.12
LINK        MN    MN A5008                 O3B ADP A2007     1555   1555  2.05
LINK        MN    MN A5008                 O   HOH A5501     1555   1555  2.28
LINK         K     K A5009                 O2B ADP A2007     1555   1555  2.30
LINK         K     K A5013                 O   HOH A5134     1555   1555  2.50
LINK         K     K A5015                 O   HOH A5026     1555   1555  2.80
LINK         K     K B5016                 O   HOH B5068     1555   1555  2.88
LINK        MN    MN C2024                 O3B ADP C2023     1555   1555  2.03
LINK        MN    MN C2024                 O1  PO4 C2028     1555   1555  2.28
LINK        MN    MN C2024                 O   HOH C5151     1555   1555  2.12
LINK        MN    MN C2025                 O   HOH C5205     1555   1555  2.19
LINK        MN    MN C2025                 O1A ADP C2023     1555   1555  2.08
LINK        MN    MN C2025                 O1B ADP C2023     1555   1555  2.19
LINK        MN    MN C2025                 O3  PO4 C2028     1555   1555  2.04
LINK         K     K C5027                 O   HOH C5150     1555   1555  2.76
LINK        MN    MN C2030                 O3B ADP C2029     1555   1555  2.09
LINK        MN    MN C2030                 O   HOH C5518     1555   1555  2.43
LINK        MN    MN C2030                 O2A ADP C2029     1555   1555  2.08
LINK        MN    MN C2030                 O   HOH C5519     1555   1555  2.23
LINK         K     K C5031                 O2B ADP C2029     1555   1555  2.57
LINK         K     K C5035                 O   HOH C5156     1555   1555  2.63
LINK         K     K C5037                 O   HOH C5047     1555   1555  2.27
LINK         K     K D5038                 O   HOH C5439     1555   1555  2.91
LINK        MN    MN E2046                 O3B ADP E2045     1555   1555  2.15
LINK        MN    MN E2046                 O   HOH E5178     1555   1555  2.30
LINK        MN    MN E2046                 O1  PO4 E2050     1555   1555  2.04
LINK        MN    MN E2047                 O1B ADP E2045     1555   1555  2.20
LINK        MN    MN E2047                 O   HOH E5232     1555   1555  2.06
LINK        MN    MN E2047                 O1A ADP E2045     1555   1555  2.10
LINK        MN    MN E2047                 O3  PO4 E2050     1555   1555  2.26
LINK         K     K E5049                 O   HOH E5177     1555   1555  2.53
LINK        MN    MN E2052                 O2A ADP E2051     1555   1555  2.07
LINK        MN    MN E2052                 O   HOH E5544     1555   1555  2.36
LINK        MN    MN E2052                 O3B ADP E2051     1555   1555  2.16
LINK        MN    MN E2052                 O   HOH E5543     1555   1555  2.14
LINK         K     K E5053                 O   HOH E5547     1555   1555  2.81
LINK         K     K E5053                 O2B ADP E2051     1555   1555  2.31
LINK         K     K E5053                 O   HOH E5816     1555   1555  1.94
LINK         K     K E5057                 O   HOH E5188     1555   1555  2.88
LINK         K     K E5059                 O   HOH E5073     1555   1555  2.84
LINK         K     K F5060                 O   HOH F2843     1555   1555  2.84
LINK        MN    MN G2067                 O   HOH G3501     1555   1555  2.51
LINK        MN    MN G2067                 O1  PO4 G2071     1555   1555  1.89
LINK        MN    MN G2067                 O3B ADP G2066     1555   1555  2.40
LINK        MN    MN G2068                 O3  PO4 G2071     1555   1555  2.30
LINK        MN    MN G2068                 O   HOH G3558     1555   1555  2.16
LINK        MN    MN G2068                 O1A ADP G2066     1555   1555  1.94
LINK        MN    MN G2068                 O1B ADP G2066     1555   1555  2.24
LINK         K     K G5070                 O   HOH G3500     1555   1555  2.84
LINK         K     K G5070                 O   HOH G3501     1555   1555  2.92
LINK        MN    MN G2073                 O   HOH G3912     1555   1555  2.67
LINK        MN    MN G2073                 O3B ADP G2072     1555   1555  2.29
LINK        MN    MN G2073                 O   HOH G3913     1555   1555  2.11
LINK        MN    MN G2073                 O2A ADP G2072     1555   1555  2.14
LINK         K     K G5074                 O   HOH G3879     1555   1555  2.11
LINK         K     K G5074                 O2B ADP G2072     1555   1555  2.48
LINK         K     K G5074                 O   HOH G3916     1555   1555  2.89
LINK         K     K G5078                 O   HOH G3511     1555   1555  2.71
LINK         K     K G5078                 O   HOH G3506     1555   1555  2.86
LINK         K     K A5005                 O   HOH A5129     1555   1555  3.02
LINK         K     K A5005                 O   ALA A 126     1555   1555  3.27
LINK         K     K A5005                 OD1 ASN A 301     1555   1555  3.48
LINK         K     K A5009                 O3B ADP A2007     1555   1555  3.25
LINK         K     K A5009                 O   HOH A5501     1555   1555  3.68
LINK         K     K A5009                 O   HOH A5504     1555   1555  3.46
LINK         K     K A5009                 O   HOH A5666     1555   1555  3.39
LINK         K     K A5009                 OE1 GLU A 841     1555   1555  2.96
LINK         K     K A5013                 O   HOH A5139     1555   1555  3.55
LINK         K     K A5013                 O   HOH A5820     1555   1555  3.33
LINK         K     K A5013                 O   ALA A 144     1555   1555  3.14
LINK         K     K A5013                 OG1 THR A 143     1555   1555  2.99
LINK         K     K A5013                 O   THR A 143     1555   1555  3.13
LINK         K     K A5013                 O   HOH A5140     1555   1555  3.38
LINK         K     K A5014                 OD1 ASN A 570     1555   1555  3.25
LINK         K     K A5014                 OE2 GLU A 604     1555   1555  3.20
LINK         K     K A5014                 O   GLU A 383     1555   1555  3.17
LINK         K     K A5014                 OD1 ASN A 602     1555   1555  3.10
LINK         K     K A5014                 ND2 ASN A 602     1555   1555  3.38
LINK         K     K A5014                 N   ASN A 570     1555   1555  3.22
LINK         K     K A5015                 O   ASP A  84     1555   1555  2.97
LINK         K     K A5015                 OG1 THR A 114     1555   1555  2.99
LINK         C   ILE B 268                 N   143 B 269     1555   1555  1.33
LINK         C   143 B 269                 N   LEU B 270     1555   1555  1.34
LINK         K     K B5016                 O   HOH A5421     1555   1555  2.99
LINK         K     K B5016                 O   HOH A5422     1555   1555  3.29
LINK         K     K C5027                 O   ALA C 126     1555   1555  3.37
LINK         K     K C5027                 OE1 GLU C 127     1555   1555  2.95
LINK         K     K C5027                MN    MN C2024     1555   1555  3.71
LINK         K     K C5027                 O   HOH C5151     1555   1555  3.21
LINK         K     K C5027                 O   HOH C5618     1555   1555  2.98
LINK         K     K C5027                 OD1 ASN C 301     1555   1555  3.47
LINK         K     K C5031                 OE2 GLU C 841     1555   1555  2.96
LINK         K     K C5031                 OD1 ASN C 843     1555   1555  3.06
LINK         K     K C5031                 O3B ADP C2029     1555   1555  3.36
LINK         K     K C5031                 O   HOH C5522     1555   1555  3.13
LINK         K     K C5032                 O   GLN C 784     1555   1555  2.97
LINK         K     K C5035                 O   HOH C5161     1555   1555  3.65
LINK         K     K C5035                 O   HOH C5162     1555   1555  3.15
LINK         K     K C5035                 O   THR C 143     1555   1555  3.06
LINK         K     K C5035                 O   HOH C5620     1555   1555  3.34
LINK         K     K C5035                 OG1 THR C 143     1555   1555  3.30
LINK         K     K C5035                 O   ALA C 144     1555   1555  3.06
LINK         K     K C5036                 ND2 ASN C 602     1555   1555  3.25
LINK         K     K C5036                 O   GLU C 383     1555   1555  3.07
LINK         K     K C5036                 OE2 GLU C 604     1555   1555  3.52
LINK         K     K C5036                 N   ASN C 570     1555   1555  2.95
LINK         K     K C5036                 OD1 ASN C 570     1555   1555  3.13
LINK         K     K C5037                 O   ASP C  84     1555   1555  3.10
LINK         K     K C5037                 O   HOH C5048     1555   1555  3.16
LINK         K     K C5037                 O   GLY C 112     1555   1555  3.05
LINK         C   ILE D 268                 N   143 D 269     1555   1555  1.34
LINK         C   143 D 269                 N   LEU D 270     1555   1555  1.34
LINK         K     K D5038                 O   HOH C5440     1555   1555  3.64
LINK         K     K D5038                 O   HOH D1762     1555   1555  3.23
LINK         K     K D5038                 O   HOH D2137     1555   1555  3.27
LINK         K     K E5049                 O   HOH E5178     1555   1555  2.96
LINK         K     K E5049                 OD1 ASN E 301     1555   1555  3.61
LINK         K     K E5049                 O   ALA E 126     1555   1555  3.42
LINK         K     K E5053                 OE2 GLU E 841     1555   1555  3.43
LINK         K     K E5053                 OD1 ASN E 843     1555   1555  3.50
LINK         K     K E5053                 O3B ADP E2051     1555   1555  3.52
LINK         K     K E5054                 O   GLU E 783     1555   1555  2.97
LINK         K     K E5057                 O   HOH E5189     1555   1555  3.13
LINK         K     K E5057                 O   HOH E5690     1555   1555  3.23
LINK         K     K E5057                 O   HOH E5183     1555   1555  3.02
LINK         K     K E5058                 N   GLU E 383     1555   1555  3.04
LINK         K     K E5058                 OE2 GLU E 604     1555   1555  3.41
LINK         K     K E5058                 N   ASN E 570     1555   1555  3.22
LINK         K     K E5058                 O   GLU E 383     1555   1555  3.22
LINK         K     K E5058                 ND2 ASN E 602     1555   1555  3.28
LINK         K     K E5059                 N   THR E 114     1555   1555  3.70
LINK         K     K E5059                 O   HOH E5074     1555   1555  3.07
LINK         C   ILE F 268                 N   143 F 269     1555   1555  1.33
LINK         C   143 F 269                 N   LEU F 270     1555   1555  1.34
LINK         K     K F5060                 O   HOH E5466     1555   1555  3.53
LINK         K     K F5060                 O   HOH E5465     1555   1555  2.93
LINK         K     K G2069                 OD1 ASN G 236     1555   1555  3.09
LINK         K     K G5070                 O   ALA G 126     1555   1555  3.45
LINK         K     K G5070                 OD1 ASN G 301     1555   1555  3.58
LINK         K     K G5074                 OE2 GLU G 841     1555   1555  3.08
LINK         K     K G5074                 O3B ADP G2072     1555   1555  3.44
LINK         K     K G5074                 OD1 ASN G 843     1555   1555  3.50
LINK         K     K G5078                 O   ALA G 144     1555   1555  3.41
LINK         K     K G5078                 OG1 THR G 143     1555   1555  2.94
LINK         K     K G5078                 O   THR G 143     1555   1555  3.04
LINK         K     K G5079                 OE2 GLU G 604     1555   1555  3.28
LINK         K     K G5079                 OD1 ASN G 570     1555   1555  3.22
LINK         K     K G5079                 ND2 ASN G 602     1555   1555  3.25
LINK         K     K G5079                 N   ASN G 570     1555   1555  3.20
LINK         K     K G5079                 O   GLU G 383     1555   1555  3.06
LINK         K     K G5079                 N   GLU G 383     1555   1555  3.01
LINK         K     K G5080                 OG1 THR G 114     1555   1555  2.98
LINK         K     K G5080                 O   HOH G4115     1555   1555  3.42
LINK         K     K G5080                 O   HOH G3396     1555   1555  2.95
LINK         K     K G5080                 O   ASP G  84     1555   1555  3.15
LINK         K     K G5080                 O   HOH G3397     1555   1555  3.26
LINK         C   ILE H 268                 N   143 H 269     1555   1555  1.33
LINK         C   143 H 269                 N   LEU H 270     1555   1555  1.34
LINK         K     K H5081                 O   HIS H  16     1555   1555  3.03
LINK         K     K H5081                 O   HOH G3832     1555   1555  3.42
LINK         K     K H5081                 O   HOH H3992     1555   1555  3.44
LINK         K     K H5081                 O   HOH H3831     1555   1555  3.20
CISPEP   1 PHE A  164    PRO A  165          0         1.14
CISPEP   2 ALA A  251    PRO A  252          0        -1.79
CISPEP   3 TYR A  710    PRO A  711          0         2.37
CISPEP   4 LEU A  796    PRO A  797          0         2.95
CISPEP   5 ARG A  998    PRO A  999          0        -3.51
CISPEP   6 SER B  357    PRO B  358          0         1.82
CISPEP   7 PHE C  164    PRO C  165          0        -0.32
CISPEP   8 ALA C  251    PRO C  252          0        -0.01
CISPEP   9 TYR C  710    PRO C  711          0         2.70
CISPEP  10 LEU C  796    PRO C  797          0         3.06
CISPEP  11 ARG C  998    PRO C  999          0        -3.81
CISPEP  12 SER D  357    PRO D  358          0         4.99
CISPEP  13 PHE E  164    PRO E  165          0         1.79
CISPEP  14 ALA E  251    PRO E  252          0        -1.41
CISPEP  15 TYR E  710    PRO E  711          0         2.23
CISPEP  16 LEU E  796    PRO E  797          0         1.65
CISPEP  17 ARG E  998    PRO E  999          0        -1.43
CISPEP  18 SER F  357    PRO F  358          0         2.45
CISPEP  19 PHE G  164    PRO G  165          0         1.18
CISPEP  20 ALA G  251    PRO G  252          0         1.37
CISPEP  21 TYR G  710    PRO G  711          0         2.51
CISPEP  22 LEU G  796    PRO G  797          0         0.83
CISPEP  23 ARG G  998    PRO G  999          0         0.31
CISPEP  24 SER H  357    PRO H  358          0         2.11
SITE     1 AC1  5 GLU A 299  ASN A 301  ADP A2001  PO4 A2006
SITE     2 AC1  5 HOH A5129
SITE     1 AC2  5 GLN A 285  GLU A 299  ADP A2001  PO4 A2006
SITE     2 AC2  5 HOH A5185
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  7 ALA A 126  GLU A 127  GLU A 299  MET A 300
SITE     2 AC4  7 ASN A 301  HOH A5128  HOH A5129
SITE     1 AC5  5 GLN A 829  GLU A 841  ADP A2007  HOH A5501
SITE     2 AC5  5 HOH A5502
SITE     1 AC6  3 GLU A 841  ASN A 843  ADP A2007
SITE     1 AC7  6 GLU A 761  HIS A 781  GLU A 783  GLN A 784
SITE     2 AC7  6 VAL A 787  SER A 792
SITE     1 AC8  3 THR A 143  ALA A 144  HOH A5134
SITE     1 AC9  5 GLY A 382  GLU A 383  ASN A 570  ASN A 602
SITE     2 AC9  5 GLU A 604
SITE     1 BC1  4 ASP A  84  GLY A 112  THR A 114  HOH A5026
SITE     1 BC2  4 HOH A5421  HIS B  16  ASP B 112  HOH B5068
SITE     1 BC3  5 GLN A  93  THR A 173  MET A 174  HOH A5047
SITE     2 BC3  5 HOH A5095
SITE     1 BC4  3 ASN A 289  ASN A 292  ARG A 294
SITE     1 BC5  4 ASN A 371  PHE A 900  PRO A 901  GLY A 902
SITE     1 BC6  2 LYS A 475  ASN A 485
SITE     1 BC7  4 GLU A 549  PHE B  15  ASP B 114  HOH B5069
SITE     1 BC8  5 GLU C 299  ASN C 301  ADP C2023  PO4 C2028
SITE     2 BC8  5 HOH C5151
SITE     1 BC9  5 GLN C 285  GLU C 299  ADP C2023  PO4 C2028
SITE     2 BC9  5 HOH C5205
SITE     1 CC1  6 GLU C 215  ASN C 236  ASP C 238  ALA C 239
SITE     2 CC1  6 ILE C 242  SER C 247
SITE     1 CC2  7 ALA C 126  GLU C 127  GLU C 299  MET C 300
SITE     2 CC2  7 ASN C 301  HOH C5150  HOH C5618
SITE     1 CC3  5 GLN C 829  GLU C 841  ADP C2029  HOH C5518
SITE     2 CC3  5 HOH C5519
SITE     1 CC4  3 GLU C 841  ASN C 843  ADP C2029
SITE     1 CC5  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784
SITE     2 CC5  6 VAL C 787  SER C 792
SITE     1 CC6  3 THR C 143  ALA C 144  HOH C5156
SITE     1 CC7  5 GLY C 382  GLU C 383  ASN C 570  ASN C 602
SITE     2 CC7  5 GLU C 604
SITE     1 CC8  4 ASP C  84  GLY C 112  THR C 114  HOH C5047
SITE     1 CC9  3 HOH C5439  HIS D  16  ASP D 112
SITE     1 DC1  2 THR C 173  MET C 174
SITE     1 DC2  3 ASN C 289  ASN C 292  ARG C 294
SITE     1 DC3  5 ALA C 370  ASN C 371  PHE C 900  PRO C 901
SITE     2 DC3  5 GLY C 902
SITE     1 DC4  2 LYS C 475  ASN C 485
SITE     1 DC5  4 GLU C 549  HOH C5439  ASP D 114  HOH D1763
SITE     1 DC6  4 PHE C 578  ARG C 845  ALA C 847  ARG C 848
SITE     1 DC7  6 GLU E 299  ASN E 301  ADP E2045   MN E2047
SITE     2 DC7  6 PO4 E2050  HOH E5178
SITE     1 DC8  6 GLN E 285  GLU E 299  ADP E2045   MN E2046
SITE     2 DC8  6 PO4 E2050  HOH E5232
SITE     1 DC9  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239
SITE     2 DC9  6 ILE E 242  SER E 247
SITE     1 EC1  7 ALA E 126  GLU E 127  GLU E 299  MET E 300
SITE     2 EC1  7 ASN E 301  HOH E5177  HOH E5178
SITE     1 EC2  5 GLN E 829  GLU E 841  ADP E2051  HOH E5543
SITE     2 EC2  5 HOH E5544
SITE     1 EC3  5 GLU E 841  ASN E 843  ADP E2051  HOH E5547
SITE     2 EC3  5 HOH E5816
SITE     1 EC4  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784
SITE     2 EC4  6 VAL E 787  SER E 792
SITE     1 EC5  4 THR E 143  ALA E 144  HOH E5183  HOH E5188
SITE     1 EC6  5 GLY E 382  GLU E 383  ASN E 570  ASN E 602
SITE     2 EC6  5 GLU E 604
SITE     1 EC7  5 ASP E  84  GLY E 112  THR E 114  HOH E5073
SITE     2 EC7  5 HOH E5074
SITE     1 EC8  4 HOH E5465  HIS F  16  ASP F 112  HOH F2843
SITE     1 EC9  4 GLN E  93  THR E 173  MET E 174  HOH E5141
SITE     1 FC1  3 ASN E 289  ASN E 292  ARG E 294
SITE     1 FC2  5 ALA E 370  ASN E 371  PHE E 900  PRO E 901
SITE     2 FC2  5 GLY E 902
SITE     1 FC3  3 LYS E 475  ASN E 485  HOH E5420
SITE     1 FC4  2 ASP F 114  HOH F2844
SITE     1 FC5  7 MET G 174  GLU G 299  ASN G 301  ADP G2066
SITE     2 FC5  7  MN G2068  PO4 G2071  HOH G3501
SITE     1 FC6  6 GLN G 285  GLU G 299  ADP G2066   MN G2067
SITE     2 FC6  6 PO4 G2071  HOH G3558
SITE     1 FC7  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239
SITE     2 FC7  6 ILE G 242  SER G 247
SITE     1 FC8  7 ALA G 126  GLU G 127  GLU G 299  MET G 300
SITE     2 FC8  7 ASN G 301  HOH G3500  HOH G3501
SITE     1 FC9  5 GLN G 829  GLU G 841  ADP G2072  HOH G3912
SITE     2 FC9  5 HOH G3913
SITE     1 GC1  5 GLU G 841  ASN G 843  ADP G2072  HOH G3879
SITE     2 GC1  5 HOH G3916
SITE     1 GC2  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784
SITE     2 GC2  6 VAL G 787  SER G 792
SITE     1 GC3  4 THR G 143  ALA G 144  HOH G3506  HOH G3511
SITE     1 GC4  5 GLY G 382  GLU G 383  ASN G 570  ASN G 602
SITE     2 GC4  5 GLU G 604
SITE     1 GC5  4 ASP G  84  GLY G 112  THR G 114  HOH G3396
SITE     1 GC6  2 HIS H  16  ASP H 112
SITE     1 GC7  4 GLN G  93  THR G 173  MET G 174  HOH G3464
SITE     1 GC8  3 ASN G 289  ASN G 292  ARG G 294
SITE     1 GC9  6 ALA G 370  ASN G 371  PHE G 900  PRO G 901
SITE     2 GC9  6 GLY G 902  HOH G3713
SITE     1 HC1  2 LYS G 475  ASN G 485
SITE     1 HC2  2 PHE H  15  ASP H 114
SITE     1 HC3 14 MET A 174  GLY A 175  HIS A 243  GLN A 285
SITE     2 HC3 14 GLU A 299  ASN A 301  ARG A 303  ARG A 306
SITE     3 HC3 14 ADP A2001   MN A2002   MN A2003  HOH A5185
SITE     4 HC3 14 HOH A5240  HOH A5577
SITE     1 HC4 13 MET C 174  GLY C 175  HIS C 243  GLN C 285
SITE     2 HC4 13 GLU C 299  ASN C 301  ARG C 303  ARG C 306
SITE     3 HC4 13 ADP C2023   MN C2024   MN C2025  HOH C5259
SITE     4 HC4 13 HOH C5592
SITE     1 HC5 13 MET E 174  GLY E 175  HIS E 243  GLN E 285
SITE     2 HC5 13 GLU E 299  ASN E 301  ARG E 303  ARG E 306
SITE     3 HC5 13 ADP E2045   MN E2046   MN E2047  HOH E5103
SITE     4 HC5 13 HOH E5621
SITE     1 HC6 13 MET G 174  GLY G 175  HIS G 243  GLN G 285
SITE     2 HC6 13 GLU G 299  ASN G 301  ARG G 303  ARG G 306
SITE     3 HC6 13 ADP G2066   MN G2067   MN G2068  HOH G3426
SITE     4 HC6 13 HOH G4112
SITE     1 HC7 27 ARG A 129  ILE A 167  ARG A 169  THR A 173
SITE     2 HC7 27 MET A 174  GLY A 175  GLY A 176  GLU A 208
SITE     3 HC7 27 LEU A 210  ILE A 211  GLU A 215  MET A 240
SITE     4 HC7 27 GLY A 241  ILE A 242  HIS A 243  THR A 244
SITE     5 HC7 27 GLN A 285  ILE A 298  GLU A 299  THR A 376
SITE     6 HC7 27  MN A2002   MN A2003  PO4 A2006  HOH A5129
SITE     7 HC7 27 HOH A5170  HOH A5185  HOH A5631
SITE     1 HC8 24 PRO A 690  ARG A 715  MET A 725  HIS A 754
SITE     2 HC8 24 PHE A 755  LEU A 756  GLU A 761  ALA A 785
SITE     3 HC8 24 GLY A 786  VAL A 787  HIS A 788  SER A 789
SITE     4 HC8 24 GLN A 829  GLU A 841   MN A5008    K A5009
SITE     5 HC8 24 HOH A5441  HOH A5470  HOH A5501  HOH A5502
SITE     6 HC8 24 HOH A5504  HOH A5768  HOH A5840  HOH A5849
SITE     1 HC9 10 GLU A 783  ASP A 791  GLU A 892  LEU A 907
SITE     2 HC9 10 TYR A1040  ASP A1041  THR A1042  HOH A5482
SITE     3 HC9 10 HOH A5525  HOH A5781
SITE     1 IC1  3 GLN A  22  THR A  94  HOH A5045
SITE     1 IC2 27 ARG C 129  ILE C 167  ARG C 169  THR C 173
SITE     2 IC2 27 MET C 174  GLY C 175  GLY C 176  GLU C 208
SITE     3 IC2 27 LEU C 210  ILE C 211  GLU C 215  MET C 240
SITE     4 IC2 27 GLY C 241  ILE C 242  HIS C 243  THR C 244
SITE     5 IC2 27 GLN C 285  ILE C 298  GLU C 299  THR C 376
SITE     6 IC2 27  MN C2024   MN C2025  PO4 C2028  HOH C5151
SITE     7 IC2 27 HOH C5190  HOH C5205  HOH C5610
SITE     1 IC3 22 PRO C 690  ARG C 715  MET C 725  HIS C 754
SITE     2 IC3 22 PHE C 755  LEU C 756  GLU C 761  ALA C 785
SITE     3 IC3 22 GLY C 786  VAL C 787  HIS C 788  SER C 789
SITE     4 IC3 22 GLN C 829  GLU C 841   MN C2030    K C5031
SITE     5 IC3 22 HOH C5459  HOH C5487  HOH C5518  HOH C5519
SITE     6 IC3 22 HOH C5522  HOH C5801
SITE     1 IC4 10 GLU C 783  ASP C 791  ALA C 793  GLU C 892
SITE     2 IC4 10 LEU C 907  TYR C1040  ASP C1041  THR C1042
SITE     3 IC4 10 HOH C5499  HOH C5543
SITE     1 IC5  5 GLN C  22  THR C  94  ASN C  97  ASN C 936
SITE     2 IC5  5 HOH C5069
SITE     1 IC6 26 ARG E 129  ILE E 167  ARG E 169  THR E 173
SITE     2 IC6 26 MET E 174  GLY E 175  GLY E 176  GLU E 208
SITE     3 IC6 26 LEU E 210  ILE E 211  GLU E 215  MET E 240
SITE     4 IC6 26 GLY E 241  ILE E 242  HIS E 243  THR E 244
SITE     5 IC6 26 GLN E 285  ILE E 298  GLU E 299  THR E 376
SITE     6 IC6 26  MN E2046   MN E2047  PO4 E2050  HOH E5178
SITE     7 IC6 26 HOH E5219  HOH E5232
SITE     1 IC7 22 PRO E 690  VAL E 713  ARG E 715  MET E 725
SITE     2 IC7 22 HIS E 754  PHE E 755  LEU E 756  GLU E 761
SITE     3 IC7 22 ALA E 785  GLY E 786  VAL E 787  HIS E 788
SITE     4 IC7 22 SER E 789  GLN E 829  GLU E 841   MN E2052
SITE     5 IC7 22   K E5053  HOH E5484  HOH E5512  HOH E5544
SITE     6 IC7 22 HOH E5547  HOH E5816
SITE     1 IC8 11 GLU E 783  ASP E 791  GLU E 892  LEU E 907
SITE     2 IC8 11 TYR E1040  ASP E1041  THR E1042  HOH E5524
SITE     3 IC8 11 HOH E5568  HOH E5570  HOH E5872
SITE     1 IC9  3 GLN E  93  THR E  94  HOH E5095
SITE     1 JC1 24 ARG G 129  ILE G 167  ARG G 169  THR G 173
SITE     2 JC1 24 MET G 174  GLY G 175  GLY G 176  GLU G 208
SITE     3 JC1 24 LEU G 210  ILE G 211  GLU G 215  MET G 240
SITE     4 JC1 24 GLY G 241  ILE G 242  HIS G 243  THR G 244
SITE     5 JC1 24 GLN G 285  GLU G 299  THR G 376   MN G2067
SITE     6 JC1 24  MN G2068  PO4 G2071  HOH G3543  HOH G3558
SITE     1 JC2 20 ARG G 715  MET G 725  HIS G 754  PHE G 755
SITE     2 JC2 20 LEU G 756  GLU G 761  ALA G 785  GLY G 786
SITE     3 JC2 20 VAL G 787  HIS G 788  SER G 789  GLN G 829
SITE     4 JC2 20 GLU G 841   MN G2073  HOH G3852  HOH G3879
SITE     5 JC2 20 HOH G3912  HOH G3913  HOH G3916    K G5074
SITE     1 JC3 10 GLU G 783  ASP G 791  GLU G 892  LEU G 895
SITE     2 JC3 10 LEU G 907  TYR G1040  ASP G1041  THR G1042
SITE     3 JC3 10 HOH G3893  HOH G3937
SITE     1 JC4  4 GLN G  22  THR G  94  ASN G  97  HOH G3416
CRYST1  152.400  164.400  333.200  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      0.006562  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006083  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003001        0.00000
      
PROCHECK
Go to PROCHECK summary
 References