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PDBsum entry 2nt1

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2nt1
Jmol
Contents
Protein chain
497 a.a.
Ligands
NAG ×4
PO4 ×78
Waters ×1344
HEADER    HYDROLASE                               06-NOV-06   2NT1
TITLE     STRUCTURE OF ACID-BETA-GLUCOSIDASE AT NEUTRAL PH
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND   3 CHAIN: A, B, C, D;
COMPND   4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL-
COMPND   5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;
COMPND   6 EC: 3.2.1.45;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: GBA;
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: OVARY
KEYWDS    ACID-BETA-GLUCOSIDASE, CEREZYME, GLUCOSYLCERAMIDE, GAUCHER DISEASE,
KEYWDS   2 HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.LIEBERMAN,G.A.PETSKO,D.RINGE
REVDAT   4   13-JUL-11 2NT1    1       VERSN
REVDAT   3   24-FEB-09 2NT1    1       VERSN
REVDAT   2   30-JAN-07 2NT1    1       JRNL
REVDAT   1   26-DEC-06 2NT1    0
JRNL        AUTH   R.L.LIEBERMAN,B.A.WUSTMAN,P.HUERTAS,A.C.POWE,C.W.PINE,
JRNL        AUTH 2 R.KHANNA,M.G.SCHLOSSMACHER,D.RINGE,G.A.PETSKO
JRNL        TITL   STRUCTURE OF ACID BETA-GLUCOSIDASE WITH PHARMACOLOGICAL
JRNL        TITL 2 CHAPERONE PROVIDES INSIGHT INTO GAUCHER DISEASE.
JRNL        REF    NAT.CHEM.BIOL.                V.   3   101 2007
JRNL        REFN                   ISSN 1552-4450
JRNL        PMID   17187079
JRNL        DOI    10.1038/NCHEMBIO850
REMARK   2
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.94
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8
REMARK   3   NUMBER OF REFLECTIONS             : 119536
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178
REMARK   3   R VALUE            (WORKING SET) : 0.175
REMARK   3   FREE R VALUE                     : 0.240
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6021
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6627
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.46
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540
REMARK   3   BIN FREE R VALUE SET COUNT          : 362
REMARK   3   BIN FREE R VALUE                    : 0.3170
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 15720
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 446
REMARK   3   SOLVENT ATOMS            : 1344
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 29.10
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.10
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.07000
REMARK   3    B22 (A**2) : -0.09000
REMARK   3    B33 (A**2) : 0.21000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.06000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.265
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.225
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.679
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16584 ; 0.022 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 22668 ; 1.969 ; 1.971
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1984 ; 8.180 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   720 ;37.509 ;23.444
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2516 ;17.744 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;23.386 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2412 ; 0.135 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12532 ; 0.008 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8004 ; 0.223 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 10701 ; 0.311 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1340 ; 0.236 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    64 ; 0.171 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.158 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 10226 ; 1.095 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.798 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7349 ; 2.766 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6596 ; 4.083 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 1
REMARK   3     CHAIN NAMES                    : A C
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     A      1       A     497      5
REMARK   3           1     C      1       C     497      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1988 ; 0.110 ; 0.500
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1942 ; 0.300 ; 5.000
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1988 ; 0.630 ; 2.000
REMARK   3   LOOSE THERMAL      1    A (A**2):   1942 ; 1.280 ;10.000
REMARK   3
REMARK   3  NCS GROUP NUMBER               : 2
REMARK   3     CHAIN NAMES                    : B D
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE
REMARK   3           1     B      1       B     497      5
REMARK   3           1     D      1       D     497      5
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1988 ; 0.110 ; 0.500
REMARK   3   LOOSE POSITIONAL   2    B    (A):   1942 ; 0.400 ; 5.000
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1988 ; 0.550 ; 2.000
REMARK   3   LOOSE THERMAL      2    B (A**2):   1942 ; 1.280 ;10.000
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 2NT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB040265.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-B
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 119558
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1
REMARK 200  DATA REDUNDANCY                : 3.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.10600
REMARK 200   FOR THE DATA SET  : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.6
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90
REMARK 200  R MERGE FOR SHELL          (I) : 0.45400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2NT0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 62.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8 M NA DIHYDROGEN PHOSPHATE  0.8 M K
REMARK 280  DIHYDROGEN PHOSPHATE 0.1 M HEPES BUFFER PH 7.5 CRYOPROTECTED IN 2
REMARK 280  M LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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        0.00000
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       45.89600
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 69610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -435.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   O    HOH C  1157     O    HOH C  1165              0.00
REMARK 500   O    HOH C  1157     O    HOH C  1166              0.00
REMARK 500   O    HOH C  1165     O    HOH C  1166              0.00
REMARK 500   OE1  GLN A    73     O    HOH A   800              1.83
REMARK 500   O4   NAG D   498     O    HOH D   769              1.93
REMARK 500   O    SER C   339     O3   PO4 C   517              1.98
REMARK 500   OH   TYR A   133     O4   PO4 A   515              2.05
REMARK 500   O    HOH A   520     O    HOH A   853              2.06
REMARK 500   O    SER A   339     O2   PO4 A   518              2.10
REMARK 500   O    HOH A   765     O    HOH A   863              2.10
REMARK 500   O3   PO4 C   514     O    HOH C  1147              2.11
REMARK 500   NE2  GLN D   207     OD1  ASP D   263              2.12
REMARK 500   O    HOH B   529     O    HOH B   784              2.13
REMARK 500   NE2  GLN A   207     OD1  ASP A   263              2.14
REMARK 500   O    HOH A   732     O    HOH A   851              2.14
REMARK 500   NE2  GLN B   207     OD1  ASP B   263              2.14
REMARK 500   O    HOH D   696     O    HOH D   795              2.16
REMARK 500   OH   TYR C   133     O3   PO4 C   518              2.16
REMARK 500   O    HOH A   796     O    HOH A   847              2.17
REMARK 500   O    HOH C  1010     O    HOH C  1048              2.17
REMARK 500   O    HOH D   522     O    HOH D   798              2.17
REMARK 500   O1   PO4 A   514     O    HOH A   734              2.18
REMARK 500   O    HOH C  1084     O    HOH C  1114              2.18
REMARK 500   O1   PO4 A   508     O    HOH A   821              2.19
REMARK 500   CB   ASP A   358     O    HOH A   878              2.19
REMARK 500   N    PHE B   347     O    HOH B   800              2.19
REMARK 500   O4   NAG A   498     O    HOH A   765              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLU A 111   CG    GLU A 111   CD      0.109
REMARK 500    GLN A 169   CB    GLN A 169   CG      0.164
REMARK 500    TRP A 378   CB    TRP A 378   CG     -0.118
REMARK 500    CYS B 126   CB    CYS B 126   SG     -0.101
REMARK 500    GLU C 111   CG    GLU C 111   CD      0.092
REMARK 500    GLU D 112   CG    GLU D 112   CD      0.092
REMARK 500    CYS D 126   CB    CYS D 126   SG     -0.104
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 153   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    GLY A 344   N   -  CA  -  C   ANGL. DEV. =  16.3 DEGREES
REMARK 500    LEU B 286   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES
REMARK 500    LEU B 317   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES
REMARK 500    LEU B 480   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES
REMARK 500    PRO C  29   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES
REMARK 500    ARG C  39   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES
REMARK 500    ARG C  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    ARG C  44   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    LEU C 286   CA  -  CB  -  CG  ANGL. DEV. =  17.6 DEGREES
REMARK 500    LEU C 314   C   -  N   -  CA  ANGL. DEV. =  16.0 DEGREES
REMARK 500    LEU D  34   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES
REMARK 500    PRO D 319   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES
REMARK 500    LEU D 480   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES
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    ASN A  19     -156.83   -157.85
REMARK 500    PHE A  75     -137.53   -125.85
REMARK 500    ALA A 124     -159.28     83.12
REMARK 500    LEU A 156      -64.41   -108.24
REMARK 500    GLN A 169      -72.25    -62.87
REMARK 500    ASN A 192     -159.55   -133.87
REMARK 500    ASP A 203     -176.30    -69.82
REMARK 500    GLU A 233      133.09    165.25
REMARK 500    GLU A 235       61.61     38.44
REMARK 500    LEU A 249      112.72   -167.57
REMARK 500    ASP A 263      -65.96   -124.79
REMARK 500    LEU A 281      -83.23     75.21
REMARK 500    THR A 323      -75.11   -112.10
REMARK 500    SER A 345       62.86    177.54
REMARK 500    LYS A 346      108.82    103.07
REMARK 500    HIS A 374        4.54     81.84
REMARK 500    TRP A 381     -142.42    -72.68
REMARK 500    ARG A 395      132.05    174.55
REMARK 500    THR B  63      -47.58     95.47
REMARK 500    PHE B  75     -138.70   -121.60
REMARK 500    ALA B 124     -150.85     67.71
REMARK 500    LEU B 156      -71.07   -103.34
REMARK 500    PRO B 182      142.76    -39.40
REMARK 500    ASN B 192     -168.80   -122.34
REMARK 500    GLU B 233      134.26    172.40
REMARK 500    ASP B 263      -65.57   -125.23
REMARK 500    LEU B 281      -80.75     76.37
REMARK 500    THR B 323      -74.58   -112.81
REMARK 500    SER B 345     -152.03   -103.20
REMARK 500    LYS B 346       90.23     87.49
REMARK 500    HIS B 374        0.05     82.61
REMARK 500    TRP B 381     -148.76    -79.96
REMARK 500    ASN B 382      121.11    -29.74
REMARK 500    VAL B 477      -33.07   -141.37
REMARK 500    ASN C  19     -158.24   -147.54
REMARK 500    PRO C  29      131.07    -39.23
REMARK 500    PHE C  75     -131.42   -121.05
REMARK 500    ALA C 124     -157.65     78.73
REMARK 500    PHE C 128       46.53    -76.61
REMARK 500    TYR C 133      144.94    179.91
REMARK 500    LEU C 156      -68.80    -99.84
REMARK 500    PRO C 182      140.71    -39.41
REMARK 500    ASN C 192     -152.70   -127.10
REMARK 500    GLU C 233      136.35    168.08
REMARK 500    LEU C 249      110.55   -163.56
REMARK 500    LEU C 281      -83.36     76.05
REMARK 500    TYR C 313      -67.15   -169.35
REMARK 500    LEU C 314      -28.28     77.91
REMARK 500    THR C 323      -76.50   -108.42
REMARK 500    TRP C 381     -132.58    -83.40
REMARK 500
REMARK 500 THIS ENTRY HAS      71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 SER B  345     LYS B  346                 -141.71
REMARK 500 LEU C   91     ASN C   92                 -146.99
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    ILE A 114        24.3      L          L   OUTSIDE RANGE
REMARK 500    THR B  63        21.2      L          L   OUTSIDE RANGE
REMARK 500    TYR C 313        19.1      L          L   OUTSIDE RANGE
REMARK 500    LEU C 314        13.4      L          L   OUTSIDE RANGE
REMARK 500    THR C 410        24.9      L          L   OUTSIDE RANGE
REMARK 500    ILE D  93        22.6      L          L   OUTSIDE RANGE
REMARK 500    SER D 345        24.9      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 A 866        DISTANCE =  5.18 ANGSTROMS
REMARK 525    HOH B 797        DISTANCE =  5.97 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 498
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 499
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 519
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NSX   RELATED DB: PDB
REMARK 900 RELATED ID: 2NT0   RELATED DB: PDB
DBREF  2NT1 A    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2NT1 B    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2NT1 C    1   497  UNP    P04062   GLCM_HUMAN      40    536
DBREF  2NT1 D    1   497  UNP    P04062   GLCM_HUMAN      40    536
SEQADV 2NT1 HIS A  495  UNP  P04062    ARG   534 CONFLICT
SEQADV 2NT1 HIS B  495  UNP  P04062    ARG   534 CONFLICT
SEQADV 2NT1 HIS C  495  UNP  P04062    ARG   534 CONFLICT
SEQADV 2NT1 HIS D  495  UNP  P04062    ARG   534 CONFLICT
SEQRES   1 A  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 A  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 A  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 A  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 A  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 A  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 A  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 A  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 A  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 A  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 A  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 A  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 A  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 A  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 A  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 A  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 A  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 A  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 A  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 A  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 A  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 A  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 A  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 A  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 A  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 A  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 A  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 A  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 A  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 A  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 A  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 A  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 A  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 A  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 A  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 A  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 A  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 A  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 A  497  HIS ARG GLN
SEQRES   1 B  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 B  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 B  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 B  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 B  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 B  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 B  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 B  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 B  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 B  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 B  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 B  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 B  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 B  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 B  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 B  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 B  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 B  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 B  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 B  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 B  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 B  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 B  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 B  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 B  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 B  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 B  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 B  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 B  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 B  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 B  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 B  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 B  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 B  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 B  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 B  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 B  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 B  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 B  497  HIS ARG GLN
SEQRES   1 C  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 C  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 C  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 C  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 C  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 C  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 C  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 C  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 C  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 C  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 C  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 C  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 C  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 C  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 C  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 C  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 C  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 C  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 C  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 C  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 C  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 C  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 C  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 C  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 C  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 C  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 C  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 C  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 C  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 C  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 C  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 C  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 C  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 C  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 C  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 C  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 C  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 C  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 C  497  HIS ARG GLN
SEQRES   1 D  497  ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES   2 D  497  VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES   3 D  497  ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES   4 D  497  TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES   5 D  497  MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES   6 D  497  LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES   7 D  497  LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES   8 D  497  ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES   9 D  497  LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES  10 D  497  ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES  11 D  497  ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES  12 D  497  LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES  13 D  497  LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES  14 D  497  ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES  15 D  497  THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES  16 D  497  SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES  17 D  497  TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES  18 D  497  GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES  19 D  497  GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES  20 D  497  CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES  21 D  497  ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES  22 D  497  HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES  23 D  497  LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES  24 D  497  GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES  25 D  497  TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES  26 D  497  GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES  27 D  497  SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES  28 D  497  VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES  29 D  497  HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES  30 D  497  TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES  31 D  497  PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES  32 D  497  VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES  33 D  497  PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES  34 D  497  GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES  35 D  497  ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES  36 D  497  ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES  37 D  497  PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES  38 D  497  THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES  39 D  497  HIS ARG GLN
MODRES 2NT1 ASN A   19  ASN  GLYCOSYLATION SITE
MODRES 2NT1 ASN B   19  ASN  GLYCOSYLATION SITE
MODRES 2NT1 ASN C   19  ASN  GLYCOSYLATION SITE
MODRES 2NT1 ASN D   19  ASN  GLYCOSYLATION SITE
HET    NAG  A 498      14
HET    NAG  B 498      14
HET    NAG  C 498      14
HET    NAG  D 498      14
HET    PO4  A 499       5
HET    PO4  B 499       5
HET    PO4  D 499       5
HET    PO4  C 499       5
HET    PO4  A 500       5
HET    PO4  B 500       5
HET    PO4  C 500       5
HET    PO4  D 500       5
HET    PO4  A 501       5
HET    PO4  C 501       5
HET    PO4  C 502       5
HET    PO4  D 501       5
HET    PO4  B 501       5
HET    PO4  A 502       5
HET    PO4  C 503       5
HET    PO4  D 502       5
HET    PO4  D 503       5
HET    PO4  B 502       5
HET    PO4  B 503       5
HET    PO4  A 503       5
HET    PO4  A 504       5
HET    PO4  A 505       5
HET    PO4  C 504       5
HET    PO4  D 504       5
HET    PO4  B 504       5
HET    PO4  B 505       5
HET    PO4  B 506       5
HET    PO4  D 505       5
HET    PO4  A 506       5
HET    PO4  D 506       5
HET    PO4  B 507       5
HET    PO4  B 508       5
HET    PO4  C 505       5
HET    PO4  B 509       5
HET    PO4  D 507       5
HET    PO4  D 508       5
HET    PO4  B 510       5
HET    PO4  D 509       5
HET    PO4  C 506       5
HET    PO4  C 507       5
HET    PO4  B 511       5
HET    PO4  A 507       5
HET    PO4  B 512       5
HET    PO4  C 508       5
HET    PO4  A 508       5
HET    PO4  C 509       5
HET    PO4  C 510       5
HET    PO4  C 511       5
HET    PO4  A 509       5
HET    PO4  A 510       5
HET    PO4  C 512       5
HET    PO4  C 513       5
HET    PO4  C 514       5
HET    PO4  A 511       5
HET    PO4  A 512       5
HET    PO4  D 510       5
HET    PO4  A 513       5
HET    PO4  A 514       5
HET    PO4  B 513       5
HET    PO4  C 515       5
HET    PO4  C 516       5
HET    PO4  D 511       5
HET    PO4  A 515       5
HET    PO4  C 517       5
HET    PO4  D 512       5
HET    PO4  A 516       5
HET    PO4  C 518       5
HET    PO4  D 513       5
HET    PO4  A 517       5
HET    PO4  B 514       5
HET    PO4  A 518       5
HET    PO4  B 515       5
HET    PO4  D 514       5
HET    PO4  C 519       5
HET    PO4  C 520       5
HET    PO4  C 521       5
HET    PO4  B 516       5
HET    PO4  A 519       5
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     PO4 PHOSPHATE ION
FORMUL   5  NAG    4(C8 H15 N O6)
FORMUL   9  PO4    78(O4 P 3-)
FORMUL  87  HOH   *1344(H2 O)
HELIX    1   1 THR A   86  ALA A   95  1                                  10
HELIX    2   2 SER A   97  SER A  110  1                                  14
HELIX    3   3 PRO A  150  LEU A  156  1                                   7
HELIX    4   4 LEU A  156  ALA A  168  1                                  13
HELIX    5   5 PRO A  182  LYS A  186  5                                   5
HELIX    6   6 ASP A  203  HIS A  223  1                                  21
HELIX    7   7 SER A  237  LEU A  241  5                                   5
HELIX    8   8 THR A  252  ASP A  263  1                                  12
HELIX    9   9 ASP A  263  ASN A  270  1                                   8
HELIX   10  10 LEU A  286  LEU A  288  5                                   3
HELIX   11  11 PRO A  289  THR A  297  1                                   9
HELIX   12  12 ASP A  298  LYS A  303  1                                   6
HELIX   13  13 LEU A  314  ALA A  318  5                                   5
HELIX   14  14 PRO A  319  PHE A  331  1                                  13
HELIX   15  15 SER A  356  TYR A  373  1                                  18
HELIX   16  16 GLN A  414  LYS A  425  1                                  12
HELIX   17  17 THR B   86  ALA B   95  1                                  10
HELIX   18  18 SER B   97  SER B  110  1                                  14
HELIX   19  19 PRO B  150  LYS B  155  1                                   6
HELIX   20  20 LEU B  156  ALA B  168  1                                  13
HELIX   21  21 PRO B  182  LYS B  186  5                                   5
HELIX   22  22 ASP B  203  HIS B  223  1                                  21
HELIX   23  23 GLU B  235  LEU B  241  5                                   7
HELIX   24  24 THR B  252  ASP B  263  1                                  12
HELIX   25  25 ASP B  263  ASN B  270  1                                   8
HELIX   26  26 LEU B  286  LEU B  288  5                                   3
HELIX   27  27 PRO B  289  THR B  297  1                                   9
HELIX   28  28 ASP B  298  LYS B  303  1                                   6
HELIX   29  29 THR B  323  PHE B  331  1                                   9
HELIX   30  30 SER B  356  TYR B  373  1                                  18
HELIX   31  31 ILE B  406  ASP B  409  5                                   4
HELIX   32  32 GLN B  414  LYS B  425  1                                  12
HELIX   33  33 THR C   86  LEU C   94  1                                   9
HELIX   34  34 SER C   97  SER C  110  1                                  14
HELIX   35  35 PRO C  150  LEU C  156  1                                   7
HELIX   36  36 LEU C  156  ALA C  168  1                                  13
HELIX   37  37 PRO C  182  LYS C  186  5                                   5
HELIX   38  38 ASP C  203  HIS C  223  1                                  21
HELIX   39  39 GLU C  235  LEU C  241  5                                   7
HELIX   40  40 THR C  252  ASP C  263  1                                  12
HELIX   41  41 ASP C  263  ASN C  270  1                                   8
HELIX   42  42 LEU C  286  LEU C  288  5                                   3
HELIX   43  43 PRO C  289  THR C  297  1                                   9
HELIX   44  44 ASP C  298  LYS C  303  1                                   6
HELIX   45  45 LEU C  314  ALA C  318  5                                   5
HELIX   46  46 THR C  323  PHE C  331  1                                   9
HELIX   47  47 SER C  356  TYR C  373  1                                  18
HELIX   48  48 GLN C  414  LYS C  425  1                                  12
HELIX   49  49 THR D   86  ALA D   95  1                                  10
HELIX   50  50 SER D   97  SER D  110  1                                  14
HELIX   51  51 PRO D  150  LYS D  155  1                                   6
HELIX   52  52 LEU D  156  ALA D  168  1                                  13
HELIX   53  53 PRO D  182  LYS D  186  5                                   5
HELIX   54  54 ASP D  203  HIS D  223  1                                  21
HELIX   55  55 SER D  237  LEU D  241  5                                   5
HELIX   56  56 THR D  252  ASP D  263  1                                  12
HELIX   57  57 ASP D  263  ASN D  270  1                                   8
HELIX   58  58 LEU D  286  LEU D  288  5                                   3
HELIX   59  59 PRO D  289  THR D  297  1                                   9
HELIX   60  60 ASP D  298  LYS D  303  1                                   6
HELIX   61  61 THR D  323  PHE D  331  1                                   9
HELIX   62  62 SER D  356  TYR D  373  1                                  18
HELIX   63  63 ILE D  406  ASP D  409  5                                   4
HELIX   64  64 GLN D  414  LYS D  425  1                                  12
SHEET    1   A 5 PRO A   6  LYS A   7  0
SHEET    2   A 5 VAL A  15  CYS A  18 -1  O  VAL A  15   N  LYS A   7
SHEET    3   A 5 THR A 410  LYS A 413 -1  O  PHE A 411   N  CYS A  18
SHEET    4   A 5 ILE A 402  ASP A 405 -1  N  ILE A 403   O  TYR A 412
SHEET    5   A 5 ALA A 384  LEU A 385  1  N  LEU A 385   O  VAL A 404
SHEET    1   B 9 GLU A  50  PRO A  55  0
SHEET    2   B 9 THR A  36  THR A  43 -1  N  ARG A  39   O  SER A  52
SHEET    3   B 9 SER A 488  TRP A 494 -1  O  THR A 491   N  TYR A  40
SHEET    4   B 9 ALA A 456  ASN A 462 -1  N  VAL A 458   O  TYR A 492
SHEET    5   B 9 ASP A 445  MET A 450 -1  N  ASP A 445   O  LEU A 461
SHEET    6   B 9 GLN A 432  ALA A 438 -1  N  GLN A 432   O  MET A 450
SHEET    7   B 9 LEU A  65  LYS A  77 -1  N  THR A  68   O  VAL A 437
SHEET    8   B 9 VAL A 468  ASP A 474  1  O  LYS A 473   N  LEU A  69
SHEET    9   B 9 GLY A 478  SER A 484 -1  O  SER A 484   N  VAL A 468
SHEET    1   C 9 GLY A  80  ALA A  84  0
SHEET    2   C 9 ILE A 118  MET A 123  1  O  ARG A 120   N  GLY A  83
SHEET    3   C 9 SER A 173  PRO A 178  1  O  LEU A 175   N  VAL A 121
SHEET    4   C 9 ALA A 229  THR A 231  1  O  THR A 231   N  ALA A 176
SHEET    5   C 9 ARG A 277  GLN A 284  1  O  ARG A 277   N  VAL A 230
SHEET    6   C 9 GLY A 307  HIS A 311  1  O  ALA A 309   N  MET A 280
SHEET    7   C 9 MET A 335  ALA A 341  1  O  PHE A 337   N  VAL A 310
SHEET    8   C 9 VAL A 375  ASN A 382  1  O  GLY A 377   N  ALA A 338
SHEET    9   C 9 GLY A  80  ALA A  84  1  N  GLY A  82   O  ASP A 380
SHEET    1   D 4 PRO B   6  LYS B   7  0
SHEET    2   D 4 VAL B  15  CYS B  18 -1  O  VAL B  15   N  LYS B   7
SHEET    3   D 4 THR B 410  LYS B 413 -1  O  PHE B 411   N  CYS B  18
SHEET    4   D 4 ILE B 402  ASP B 405 -1  N  ASP B 405   O  THR B 410
SHEET    1   E 9 GLU B  50  PRO B  55  0
SHEET    2   E 9 THR B  36  THR B  43 -1  N  ARG B  39   O  SER B  52
SHEET    3   E 9 SER B 488  TRP B 494 -1  O  LEU B 493   N  SER B  38
SHEET    4   E 9 ALA B 456  ASN B 462 -1  N  VAL B 458   O  TYR B 492
SHEET    5   E 9 LEU B 444  MET B 450 -1  N  ASP B 445   O  LEU B 461
SHEET    6   E 9 GLN B 432  ALA B 438 -1  N  GLN B 432   O  MET B 450
SHEET    7   E 9 LEU B  65  LYS B  77 -1  N  THR B  68   O  VAL B 437
SHEET    8   E 9 VAL B 468  ASP B 474  1  O  LYS B 473   N  LEU B  69
SHEET    9   E 9 GLY B 478  SER B 484 -1  O  GLY B 478   N  ASP B 474
SHEET    1   F 9 GLY B  80  ALA B  84  0
SHEET    2   F 9 ILE B 118  MET B 123  1  O  ARG B 120   N  GLY B  83
SHEET    3   F 9 SER B 173  PRO B 178  1  O  LEU B 175   N  VAL B 121
SHEET    4   F 9 ALA B 229  THR B 231  1  O  THR B 231   N  ALA B 176
SHEET    5   F 9 ARG B 277  GLN B 284  1  O  LEU B 279   N  VAL B 230
SHEET    6   F 9 GLY B 307  TYR B 313  1  O  ALA B 309   N  MET B 280
SHEET    7   F 9 MET B 335  CYS B 342  1  O  PHE B 337   N  VAL B 310
SHEET    8   F 9 VAL B 375  ASN B 382  1  O  VAL B 376   N  LEU B 336
SHEET    9   F 9 GLY B  80  ALA B  84  1  N  GLY B  82   O  ASP B 380
SHEET    1   G 4 PRO C   6  LYS C   7  0
SHEET    2   G 4 VAL C  15  CYS C  18 -1  O  VAL C  15   N  LYS C   7
SHEET    3   G 4 THR C 410  LYS C 413 -1  O  PHE C 411   N  CYS C  18
SHEET    4   G 4 ILE C 402  ASP C 405 -1  N  ASP C 405   O  THR C 410
SHEET    1   H 9 GLU C  50  PRO C  55  0
SHEET    2   H 9 THR C  36  THR C  43 -1  N  ARG C  39   O  SER C  52
SHEET    3   H 9 SER C 488  TRP C 494 -1  O  THR C 491   N  TYR C  40
SHEET    4   H 9 ALA C 456  ASN C 462 -1  N  VAL C 458   O  TYR C 492
SHEET    5   H 9 ASP C 445  MET C 450 -1  N  LEU C 449   O  VAL C 457
SHEET    6   H 9 GLN C 432  ALA C 438 -1  N  GLN C 432   O  MET C 450
SHEET    7   H 9 LEU C  65  LYS C  77 -1  N  GLN C  76   O  ARG C 433
SHEET    8   H 9 VAL C 468  ASP C 474  1  O  LYS C 473   N  LEU C  69
SHEET    9   H 9 GLY C 478  SER C 484 -1  O  GLY C 478   N  ASP C 474
SHEET    1   I 9 GLY C  80  ALA C  84  0
SHEET    2   I 9 ILE C 118  MET C 123  1  O  ARG C 120   N  GLY C  83
SHEET    3   I 9 SER C 173  PRO C 178  1  O  LEU C 175   N  VAL C 121
SHEET    4   I 9 ALA C 229  THR C 231  1  O  THR C 231   N  ALA C 176
SHEET    5   I 9 ARG C 277  GLN C 284  1  O  LEU C 279   N  VAL C 230
SHEET    6   I 9 GLY C 307  HIS C 311  1  O  ALA C 309   N  MET C 280
SHEET    7   I 9 MET C 335  GLU C 340  1  O  MET C 335   N  ILE C 308
SHEET    8   I 9 VAL C 375  ASN C 382  1  O  GLY C 377   N  ALA C 338
SHEET    9   I 9 GLY C  80  ALA C  84  1  N  GLY C  82   O  ASP C 380
SHEET    1   J 4 PRO D   6  LYS D   7  0
SHEET    2   J 4 VAL D  15  CYS D  18 -1  O  VAL D  15   N  LYS D   7
SHEET    3   J 4 THR D 410  LYS D 413 -1  O  PHE D 411   N  CYS D  18
SHEET    4   J 4 ILE D 402  ASP D 405 -1  N  ILE D 403   O  TYR D 412
SHEET    1   K 9 GLU D  50  PRO D  55  0
SHEET    2   K 9 THR D  36  THR D  43 -1  N  ARG D  39   O  SER D  52
SHEET    3   K 9 SER D 488  TRP D 494 -1  O  LEU D 493   N  SER D  38
SHEET    4   K 9 ALA D 456  ASN D 462 -1  N  ASN D 462   O  SER D 488
SHEET    5   K 9 LEU D 444  MET D 450 -1  N  ASP D 445   O  LEU D 461
SHEET    6   K 9 GLN D 432  ALA D 438 -1  N  GLN D 432   O  MET D 450
SHEET    7   K 9 LEU D  65  LYS D  77 -1  N  PHE D  75   O  ARG D 433
SHEET    8   K 9 VAL D 468  ASP D 474  1  O  LYS D 473   N  LEU D  67
SHEET    9   K 9 GLY D 478  SER D 484 -1  O  GLY D 478   N  ASP D 474
SHEET    1   L 9 GLY D  80  ALA D  84  0
SHEET    2   L 9 ILE D 118  MET D 123  1  O  ARG D 120   N  GLY D  83
SHEET    3   L 9 SER D 173  PRO D 178  1  O  LEU D 175   N  VAL D 121
SHEET    4   L 9 ALA D 229  THR D 231  1  O  THR D 231   N  ALA D 176
SHEET    5   L 9 ARG D 277  GLN D 284  1  O  LEU D 279   N  VAL D 230
SHEET    6   L 9 GLY D 307  TYR D 313  1  O  ALA D 309   N  MET D 280
SHEET    7   L 9 MET D 335  CYS D 342  1  O  MET D 335   N  ILE D 308
SHEET    8   L 9 VAL D 375  ASN D 382  1  O  VAL D 376   N  LEU D 336
SHEET    9   L 9 GLY D  80  ALA D  84  1  N  GLY D  82   O  ASP D 380
SSBOND   1 CYS A    4    CYS A   16                          1555   1555  2.09
SSBOND   2 CYS A   18    CYS A   23                          1555   1555  2.15
SSBOND   3 CYS B    4    CYS B   16                          1555   1555  2.15
SSBOND   4 CYS B   18    CYS B   23                          1555   1555  2.20
SSBOND   5 CYS C    4    CYS C   16                          1555   1555  2.11
SSBOND   6 CYS C   18    CYS C   23                          1555   1555  2.14
SSBOND   7 CYS D    4    CYS D   16                          1555   1555  2.15
SSBOND   8 CYS D   18    CYS D   23                          1555   1555  2.21
LINK         ND2 ASN A  19                 C1  NAG A 498     1555   1555  1.48
LINK         ND2 ASN B  19                 C1  NAG B 498     1555   1555  1.46
LINK         ND2 ASN C  19                 C1  NAG C 498     1555   1555  1.46
LINK         ND2 ASN D  19                 C1  NAG D 498     1555   1555  1.46
CISPEP   1 LEU A  288    PRO A  289          0         1.88
CISPEP   2 GLY A  344    SER A  345          0        -9.35
CISPEP   3 GLY A  390    PRO A  391          0        -0.87
CISPEP   4 GLY B   62    THR B   63          0        18.52
CISPEP   5 LEU B  288    PRO B  289          0        -0.99
CISPEP   6 GLY B  390    PRO B  391          0         0.41
CISPEP   7 LEU C  288    PRO C  289          0         6.00
CISPEP   8 TYR C  313    LEU C  314          0        12.12
CISPEP   9 VAL C  343    GLY C  344          0        26.37
CISPEP  10 GLY C  390    PRO C  391          0        -0.65
CISPEP  11 LEU D  288    PRO D  289          0         0.40
CISPEP  12 GLY D  390    PRO D  391          0        -1.81
SITE     1 AC1  8 ASN A  19  HOH A 564  HOH A 617  HOH A 704
SITE     2 AC1  8 HOH A 728  HOH A 765  HOH A 819  HOH A 875
SITE     1 AC2  5 ILE B   5  ASN B  19  HOH B 743  HOH B 760
SITE     2 AC2  5 HOH B 763
SITE     1 AC3  8 ASN C  19  TYR C  22  HOH C 972  HOH C1018
SITE     2 AC3  8 HOH C1058  HOH C1071  HOH C1083  HOH C1116
SITE     1 AC4  6 ILE D   5  ASN D  19  HOH D 670  HOH D 699
SITE     2 AC4  6 HOH D 757  HOH D 769
SITE     1 AC5  6 TYR A  11  SER A  12  ARG A 353  SER A 356
SITE     2 AC5  6 TRP A 357  ASP A 358
SITE     1 AC6  6 TYR B  11  SER B  12  ARG B 353  SER B 356
SITE     2 AC6  6 TRP B 357  ASP B 358
SITE     1 AC7  6 TYR D  11  SER D  12  ARG D 353  SER D 356
SITE     2 AC7  6 TRP D 357  ASP D 358
SITE     1 AC8  6 TYR C  11  SER C  12  ARG C 353  SER C 356
SITE     2 AC8  6 TRP C 357  ASP C 358
SITE     1 AC9  6 THR A  63  GLN A 440  HOH A 742  HOH A 751
SITE     2 AC9  6 LYS C 473  HOH C 853
SITE     1 BC1  8 GLY B 193  LYS B 194  SER B 242  GLY B 243
SITE     2 BC1  8 HOH B 525  HOH B 582  HOH B 774  HOH B 806
SITE     1 BC2  6 LYS A 473  HOH A 550  THR C  63  GLN C 440
SITE     2 BC2  6 HOH C 967  HOH C1012
SITE     1 BC3  9 GLY D 193  LYS D 194  SER D 242  GLY D 243
SITE     2 BC3  9 HOH D 588  HOH D 662  HOH D 692  HOH D 717
SITE     3 BC3  9 HOH D 723
SITE     1 BC4  5 LYS A  79  TRP A 228  ARG A 277  HIS A 306
SITE     2 BC4  5 HOH A 573
SITE     1 BC5  4 ARG C  44  SER C  45  HOH C 837  HOH C1140
SITE     1 BC6  5 LYS C  79  TRP C 228  ARG C 277  HIS C 306
SITE     2 BC6  5 HOH C1075
SITE     1 BC7  4 LYS D  79  TRP D 228  ARG D 277  HIS D 306
SITE     1 BC8  3 LYS B  79  TRP B 228  ARG B 277
SITE     1 BC9  3 ARG A  44  SER A  45  HOH A 608
SITE     1 CC1  6 GLN C 226  THR C 272  HIS C 273  HOH C 977
SITE     2 CC1  6 HOH C1001  HOH C1040
SITE     1 CC2  6 GLN D 226  THR D 272  HIS D 273  VAL D 276
SITE     2 CC2  6 HOH D 517  HOH D 752
SITE     1 CC3  3 ARG D  44  SER D  45  HOH D 551
SITE     1 CC4  3 ARG B  44  SER B  45  HOH B 553
SITE     1 CC5  6 GLN B 226  THR B 272  HIS B 273  VAL B 276
SITE     2 CC5  6 HOH B 519  HOH B 669
SITE     1 CC6  3 ARG A  44  TYR A 487  HOH A 670
SITE     1 CC7  6 GLN A 226  THR A 272  HIS A 273  VAL A 276
SITE     2 CC7  6 HOH A 683  HOH A 804
SITE     1 CC8  6 PHE A  75  HIS A 328  HIS A 374  HOH A 620
SITE     2 CC8  6 HOH A 663  HOH A 783
SITE     1 CC9  5 TYR C  11  TRP C 348  GLU C 349  GLN C 350
SITE     2 CC9  5 ARG C 353
SITE     1 DC1  7 ILE D 158  PRO D 159  HIS D 162  HOH D 564
SITE     2 DC1  7 HOH D 594  HOH D 703  HOH D 735
SITE     1 DC2  5 THR B 187  LYS B 194  GLY B 195  SER B 196
SITE     2 DC2  5 HOH B 552
SITE     1 DC3  5 LYS B 198  GLY B 199  HOH B 602  HOH B 723
SITE     2 DC3  5 HOH B 765
SITE     1 DC4  3 HIS B 290  LYS B 293  HOH B 731
SITE     1 DC5  2 HIS D 290  LYS D 293
SITE     1 DC6  6 LEU A 165  PRO A 171  VAL A 172  HOH A 693
SITE     2 DC6  6 HOH A 767  HOH A 772
SITE     1 DC7  4 THR D 187  LYS D 198  GLY D 199  HOH D 721
SITE     1 DC8  4 PHE B 331  PRO B 332  ASN B 333  THR B 334
SITE     1 DC9  3 ARG B 277  VAL B 305  HIS B 306
SITE     1 EC1  2 ARG C 170  PRO C 428
SITE     1 EC2  3 ARG B 262  HOH B 601  HOH B 729
SITE     1 EC3  5 TYR D  11  TRP D 348  GLU D 349  GLN D 350
SITE     2 EC3  5 ARG D 353
SITE     1 EC4  3 GLN D 207  ARG D 211  HOH D 737
SITE     1 EC5  3 PRO B  99  ASN B 102  HOH B 675
SITE     1 EC6  3 ARG D  44  SER D 465  TYR D 487
SITE     1 EC7  2 ALA C  58  HOH C1024
SITE     1 EC8  3 LYS C 466  ASP C 467  HOH C1066
SITE     1 EC9  2 PRO B 171  VAL B 172
SITE     1 FC1  4 HIS A 290  LYS A 293  HOH A 770  HOH A 885
SITE     1 FC2  3 GLN B 207  ARG B 211  HOH B 728
SITE     1 FC3  5 ILE C 158  PRO C 159  HIS C 162  HOH C1072
SITE     2 FC3  5 HOH C1089
SITE     1 FC4  4 ALA A 438  ASN A 442  HOH A 808  HOH A 821
SITE     1 FC5  4 ALA C 438  ASN C 442  HOH C 794  HOH C1132
SITE     1 FC6  2 GLU B 254  ARG B 257
SITE     1 FC7  4 THR C 252  HIS C 255  HOH C 941  HOH C1159
SITE     1 FC8  1 ARG D 257
SITE     1 FC9  2 GLN A  57  ALA A  58
SITE     1 GC1  3 GLU C 254  ARG C 257  HOH C1079
SITE     1 GC2  6 ARG C 277  VAL C 305  HIS C 306  HOH C1005
SITE     2 GC2  6 HOH C1022  HOH C1038
SITE     1 GC3  8 THR B 407  GLY C 193  LYS C 194  SER C 242
SITE     2 GC3  8 GLY C 243  HOH C 942  HOH C1067  HOH C1147
SITE     1 GC4  4 ARG A 277  HIS A 306  HOH A 575  HOH A 623
SITE     1 GC5  5 GLU A 254  ARG A 257  HOH A 733  HOH A 758
SITE     2 GC5  5 LYS B 441
SITE     1 GC6  4 PRO D 171  VAL D 172  HOH D 641  HOH D 704
SITE     1 GC7  3 ARG A 329  LYS D 321  ARG D 329
SITE     1 GC8  8 GLY A 193  LYS A 194  SER A 242  GLY A 243
SITE     2 GC8  8 HOH A 687  HOH A 727  HOH A 734  THR D 407
SITE     1 GC9  4 LYS B 321  ARG B 329  ARG C 329  LEU C 330
SITE     1 HC1  3 ARG C  44  TYR C 487  HOH C 904
SITE     1 HC2  6 PHE C  75  HIS C 328  HIS C 374  HOH C 865
SITE     2 HC2  6 HOH C 960  HOH C 980
SITE     1 HC3  3 ARG D 277  HIS D 306  HOH D 664
SITE     1 HC4 10 ASP A  87  PRO A 122  ALA A 124  TYR A 133
SITE     2 HC4 10 TYR A 135  PRO A 150  GLU A 152  ASP A 153
SITE     3 HC4 10 LYS A 157  HOH A 537
SITE     1 HC5  7 ALA C  84  ARG C 120  SER C 339  GLU C 340
SITE     2 HC5  7 THR C 379  ASP C 380  TRP C 381
SITE     1 HC6  5 THR D 187  LYS D 194  GLY D 195  SER D 196
SITE     2 HC6  5 HOH D 671
SITE     1 HC7  3 THR A 187  LYS A 198  GLY A 199
SITE     1 HC8 10 ASP C  87  PRO C 122  ALA C 124  TYR C 133
SITE     2 HC8 10 TYR C 135  PRO C 150  GLU C 152  ASP C 153
SITE     3 HC8 10 LYS C 157  HOH C 839
SITE     1 HC9  5 ALA D 438  ASN D 442  LEU D 444  HOH D 657
SITE     2 HC9  5 HOH D 659
SITE     1 IC1  5 TYR A  11  TRP A 348  GLU A 349  GLN A 350
SITE     2 IC1  5 ARG A 353
SITE     1 IC2  3 ARG B  44  SER B 465  TYR B 487
SITE     1 IC3  8 ALA A  84  ARG A 120  SER A 339  GLU A 340
SITE     2 IC3  8 ALA A 341  THR A 379  ASP A 380  TRP A 381
SITE     1 IC4  7 ALA B 438  ASN B 442  LEU B 444  HOH B 618
SITE     2 IC4  7 HOH B 654  HOH B 730  HOH B 809
SITE     1 IC5  9 PRO D   3  CYS D   4  ILE D   5  CYS D  16
SITE     2 IC5  9 VAL D  17  CYS D  18  TYR D  22  CYS D  23
SITE     3 IC5  9 ASP D  24
SITE     1 IC6  5 LEU C 165  PRO C 171  VAL C 172  HOH C 894
SITE     2 IC6  5 HOH C 996
SITE     1 IC7  7 GLU B 151  ASP C  87  SER C 129  ILE C 130
SITE     2 IC7  7 ARG C 131  TYR C 133  GLU C 152
SITE     1 IC8  3 HIS C 290  LYS C 293  HOH C1163
SITE     1 IC9  7 ILE B 158  PRO B 159  HIS B 162  HOH B 524
SITE     2 IC9  7 HOH B 566  HOH B 597  HOH B 739
SITE     1 JC1  2 ARG A 170  PRO A 428
CRYST1  110.185   91.792  153.036  90.00 110.91  90.00 P 1 21 1      8
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      0.009076  0.000000  0.003467        0.00000
SCALE2      0.000000  0.010894  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006995        0.00000
      
PROCHECK
Go to PROCHECK summary
 References