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PDBsum entry 3b1b

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Top Page protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3b1b
Jmol
Contents
Protein chains
310 a.a.
Ligands
SO4 ×3
NAG ×5
Metals
_ZN ×2
Waters ×888
HEADER    LYASE                                   29-JUN-11   3B1B
TITLE     THE UNIQUE STRUCTURE OF WILD TYPE CARBONIC ANHYDRASE ALPHA-CA1 FROM
TITLE    2 CHLAMYDOMONAS REINHARDTII
CAVEAT     3B1B    NAG A 382 AND NAG B 382 HAVE WRONG GEOMETRY.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CARBONIC ANHYDRASE 1;
COMPND   3 CHAIN: A, B;
COMPND   4 SYNONYM: CARBONATE DEHYDRATASE 1, CA1;
COMPND   5 EC: 4.2.1.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE   3 ORGANISM_TAXID: 3055
KEYWDS    N-GLYCOSYLATION, ZINC-FINGER, CARBONIC ANHYDRASE, LYASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.SHIMIZU,A.TAKENAKA
REVDAT   2   25-APR-12 3B1B    1       JRNL
REVDAT   1   16-NOV-11 3B1B    0
JRNL        AUTH   K.SUZUKI,S.Y.YANG,S.SHIMIZU,E.C.MORISHITA,J.JIANG,F.ZHANG,
JRNL        AUTH 2 M.M.HOQUE,Y.SATO,M.TSUNODA,T.SEKIGUCHI,A.TAKENAKA
JRNL        TITL   THE UNIQUE STRUCTURE OF CARBONIC ANHYDRASE ALPHA CA1 FROM
JRNL        TITL 2 CHLAMYDOMONAS REINHARDTII
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  67   894 2011
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   21931221
JRNL        DOI    10.1107/S0907444911032884
REMARK   2
REMARK   2 RESOLUTION.    1.88 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
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) : 1.88
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.30
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 94307
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) : 0.189
REMARK   3   R VALUE            (WORKING SET) : 0.187
REMARK   3   FREE R VALUE                     : 0.218
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 4965
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) : 1.88
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.93
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6923
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430
REMARK   3   BIN FREE R VALUE SET COUNT          : 394
REMARK   3   BIN FREE R VALUE                    : 0.2640
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4859
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 87
REMARK   3   SOLVENT ATOMS            : 888
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.29
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 1.12000
REMARK   3    B22 (A**2) : 1.12000
REMARK   3    B33 (A**2) : -1.68000
REMARK   3    B12 (A**2) : 0.56000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.103
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.104
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.072
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.374
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5128 ; 0.015 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6990 ; 1.546 ; 1.948
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   630 ; 6.535 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   243 ;36.364 ;24.444
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   794 ;13.812 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;22.302 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   754 ; 0.114 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3948 ; 0.007 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2295 ; 0.204 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3433 ; 0.307 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   731 ; 0.161 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.164 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    31 ; 0.161 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.174 ; 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):  3177 ; 0.988 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5011 ; 1.660 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2222 ; 2.396 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1973 ; 3.667 ; 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 : NULL
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   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS:
REMARK   3  TREATMENT OF N-ACETYLGLUCANS
REMARK   3  THE THREE SUGAR MOIETIES BOUND TO THE ASPARAGINE RESIDUES OF A
REMARK   3  SUBUNIT ARE ASSUMED TO BE N-ACETYLGLUCANS THOUGH THE ELECTRON
REMARK   3  DENSITY SUGGESTS LARGER GLUCANS. IN THE REFINEMENT, HOWEVER, THESE
REMARK   3  MOIETIES WERE REFINED WITHOUT GEOMETRICAL RESTRAINS.
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK   4
REMARK   4 3B1B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-11.
REMARK 100 THE RCSB ID CODE IS RCSB029953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 27-JUN-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY
REMARK 200  BEAMLINE                       : AR-NW12A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00, 1.28254, 1.28297
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 99548
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.880
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 10.600
REMARK 200  R MERGE                    (I) : 0.08200
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 60.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.00
REMARK 200  R MERGE FOR SHELL          (I) : 0.31400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 8.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 67.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0-2.0M AMMONIUM SULFATE, 100MM TRIS-
REMARK 280  HCL (PH8.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+1/6
REMARK 290       6555   X-Y,X,Z+5/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       80.06667
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       40.03333
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       60.05000
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       20.01667
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      100.08333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 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 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     MET A     1
REMARK 465     ALA A     2
REMARK 465     ARG A     3
REMARK 465     THR A     4
REMARK 465     GLY A     5
REMARK 465     ALA A     6
REMARK 465     LEU A     7
REMARK 465     LEU A     8
REMARK 465     LEU A     9
REMARK 465     VAL A    10
REMARK 465     ALA A    11
REMARK 465     LEU A    12
REMARK 465     ALA A    13
REMARK 465     LEU A    14
REMARK 465     ALA A    15
REMARK 465     GLY A    16
REMARK 465     CYS A    17
REMARK 465     ALA A    18
REMARK 465     GLN A    19
REMARK 465     ALA A    20
REMARK 465     SER A   298
REMARK 465     THR A   299
REMARK 465     GLU A   300
REMARK 465     THR A   301
REMARK 465     ALA A   302
REMARK 465     ALA A   303
REMARK 465     ASP A   304
REMARK 465     ALA A   305
REMARK 465     GLY A   306
REMARK 465     HIS A   307
REMARK 465     HIS A   308
REMARK 465     HIS A   309
REMARK 465     HIS A   310
REMARK 465     HIS A   311
REMARK 465     ARG A   312
REMARK 465     ARG A   313
REMARK 465     LEU A   314
REMARK 465     LEU A   315
REMARK 465     HIS A   316
REMARK 465     ASN A   317
REMARK 465     HIS A   318
REMARK 465     ALA A   319
REMARK 465     HIS A   320
REMARK 465     LEU A   321
REMARK 465     GLU A   322
REMARK 465     GLU A   323
REMARK 465     VAL A   324
REMARK 465     PRO A   325
REMARK 465     ALA A   326
REMARK 465     ALA A   327
REMARK 465     THR A   328
REMARK 465     SER A   329
REMARK 465     GLU A   330
REMARK 465     PRO A   331
REMARK 465     LYS A   332
REMARK 465     HIS A   333
REMARK 465     TYR A   334
REMARK 465     PHE A   335
REMARK 465     ARG A   336
REMARK 465     ARG A   337
REMARK 465     VAL A   338
REMARK 465     MET A   339
REMARK 465     LEU A   340
REMARK 465     ALA A   341
REMARK 465     GLU A   342
REMARK 465     SER A   343
REMARK 465     ALA A   344
REMARK 465     MET B     1
REMARK 465     ALA B     2
REMARK 465     ARG B     3
REMARK 465     THR B     4
REMARK 465     GLY B     5
REMARK 465     ALA B     6
REMARK 465     LEU B     7
REMARK 465     LEU B     8
REMARK 465     LEU B     9
REMARK 465     VAL B    10
REMARK 465     ALA B    11
REMARK 465     LEU B    12
REMARK 465     ALA B    13
REMARK 465     LEU B    14
REMARK 465     ALA B    15
REMARK 465     GLY B    16
REMARK 465     CYS B    17
REMARK 465     ALA B    18
REMARK 465     GLN B    19
REMARK 465     ALA B    20
REMARK 465     GLU B   300
REMARK 465     THR B   301
REMARK 465     ALA B   302
REMARK 465     ALA B   303
REMARK 465     ASP B   304
REMARK 465     ALA B   305
REMARK 465     GLY B   306
REMARK 465     HIS B   307
REMARK 465     HIS B   308
REMARK 465     HIS B   309
REMARK 465     HIS B   310
REMARK 465     HIS B   311
REMARK 465     ARG B   312
REMARK 465     ARG B   313
REMARK 465     LEU B   314
REMARK 465     LEU B   315
REMARK 465     HIS B   316
REMARK 465     ASN B   317
REMARK 465     HIS B   318
REMARK 465     ALA B   319
REMARK 465     HIS B   320
REMARK 465     LEU B   321
REMARK 465     GLU B   322
REMARK 465     GLU B   323
REMARK 465     VAL B   324
REMARK 465     PRO B   325
REMARK 465     ALA B   326
REMARK 465     ALA B   327
REMARK 465     THR B   328
REMARK 465     SER B   329
REMARK 465     GLU B   330
REMARK 465     PRO B   331
REMARK 465     LYS B   332
REMARK 465     HIS B   333
REMARK 465     TYR B   334
REMARK 465     PHE B   335
REMARK 465     ARG B   336
REMARK 465     ARG B   337
REMARK 465     VAL B   338
REMARK 465     MET B   339
REMARK 465     LEU B   340
REMARK 465     ALA B   341
REMARK 465     GLU B   342
REMARK 465     SER B   343
REMARK 465     ALA B   344
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    VAL A  77      -85.46   -132.70
REMARK 500    LYS A 190      -58.86     72.85
REMARK 500    ARG A 250       35.84    -90.71
REMARK 500    VAL B  77      -81.74   -136.75
REMARK 500    GLN B 161      161.97    176.71
REMARK 500    THR B 167     -172.50    -68.59
REMARK 500    LYS B 190      -64.74     71.68
REMARK 500    ARG B 250       39.43    -94.78
REMARK 500    ASN B 359       61.08   -151.00
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 LYS A  195     GLY A  196                  -31.91
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    ARG A 250        24.8      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 568        DISTANCE =  5.22 ANGSTROMS
REMARK 525    HOH A 572        DISTANCE =  5.44 ANGSTROMS
REMARK 525    HOH A 574        DISTANCE =  5.30 ANGSTROMS
REMARK 525    HOH A 703        DISTANCE =  6.06 ANGSTROMS
REMARK 525    HOH A 730        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A 762        DISTANCE =  5.80 ANGSTROMS
REMARK 525    HOH B 563        DISTANCE =  5.92 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                              ZN B 378  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 182   ND1
REMARK 620 2 HIS B 163   NE2 115.0
REMARK 620 3 HIS B 165   NE2  93.6 106.2
REMARK 620 4 HOH B 794   O   133.1 102.3 102.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 378  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 182   ND1
REMARK 620 2 HIS A 163   NE2 114.3
REMARK 620 3 HIS A 165   NE2  98.2 101.1
REMARK 620 4 HOH A 714   O    83.2  87.6 169.6
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 382
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 378
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 382
DBREF  3B1B A    1   377  UNP    P20507   CAH1_CHLRE       1    377
DBREF  3B1B B    1   377  UNP    P20507   CAH1_CHLRE       1    377
SEQRES   1 A  377  MET ALA ARG THR GLY ALA LEU LEU LEU VAL ALA LEU ALA
SEQRES   2 A  377  LEU ALA GLY CYS ALA GLN ALA CYS ILE TYR LYS PHE GLY
SEQRES   3 A  377  THR SER PRO ASP SER LYS ALA THR VAL SER GLY ASP HIS
SEQRES   4 A  377  TRP ASP HIS GLY LEU ASN GLY GLU ASN TRP GLU GLY LYS
SEQRES   5 A  377  ASP GLY ALA GLY ASN ALA TRP VAL CYS LYS THR GLY ARG
SEQRES   6 A  377  LYS GLN SER PRO ILE ASN VAL PRO GLN TYR GLN VAL LEU
SEQRES   7 A  377  ASP GLY LYS GLY SER LYS ILE ALA ASN GLY LEU GLN THR
SEQRES   8 A  377  GLN TRP SER TYR PRO ASP LEU MET SER ASN GLY THR SER
SEQRES   9 A  377  VAL GLN VAL ILE ASN ASN GLY HIS THR ILE GLN VAL GLN
SEQRES  10 A  377  TRP THR TYR ASN TYR ALA GLY HIS ALA THR ILE ALA ILE
SEQRES  11 A  377  PRO ALA MET HIS ASN GLN THR ASN ARG ILE VAL ASP VAL
SEQRES  12 A  377  LEU GLU MET ARG PRO ASN ASP ALA ALA ASP ARG VAL THR
SEQRES  13 A  377  ALA VAL PRO THR GLN PHE HIS PHE HIS SER THR SER GLU
SEQRES  14 A  377  HIS LEU LEU ALA GLY LYS ILE TYR PRO LEU GLU LEU HIS
SEQRES  15 A  377  ILE VAL HIS GLN VAL THR GLU LYS LEU GLU ALA CYS LYS
SEQRES  16 A  377  GLY GLY CYS PHE SER VAL THR GLY ILE LEU PHE GLN LEU
SEQRES  17 A  377  ASP ASN GLY PRO ASP ASN GLU LEU LEU GLU PRO ILE PHE
SEQRES  18 A  377  ALA ASN MET PRO SER ARG GLU GLY THR PHE SER ASN LEU
SEQRES  19 A  377  PRO ALA GLY THR THR ILE LYS LEU GLY GLU LEU LEU PRO
SEQRES  20 A  377  SER ASP ARG ASP TYR VAL THR TYR GLU GLY SER LEU THR
SEQRES  21 A  377  THR PRO PRO CYS SER GLU GLY LEU LEU TRP HIS VAL MET
SEQRES  22 A  377  THR GLN PRO GLN ARG ILE SER PHE GLY GLN TRP ASN ARG
SEQRES  23 A  377  TYR ARG LEU ALA VAL GLY LEU LYS GLU CYS ASN SER THR
SEQRES  24 A  377  GLU THR ALA ALA ASP ALA GLY HIS HIS HIS HIS HIS ARG
SEQRES  25 A  377  ARG LEU LEU HIS ASN HIS ALA HIS LEU GLU GLU VAL PRO
SEQRES  26 A  377  ALA ALA THR SER GLU PRO LYS HIS TYR PHE ARG ARG VAL
SEQRES  27 A  377  MET LEU ALA GLU SER ALA ASN PRO ASP ALA TYR THR CYS
SEQRES  28 A  377  LYS ALA VAL ALA PHE GLY GLN ASN PHE ARG ASN PRO GLN
SEQRES  29 A  377  TYR ALA ASN GLY ARG THR ILE LYS LEU ALA ARG TYR HIS
SEQRES   1 B  377  MET ALA ARG THR GLY ALA LEU LEU LEU VAL ALA LEU ALA
SEQRES   2 B  377  LEU ALA GLY CYS ALA GLN ALA CYS ILE TYR LYS PHE GLY
SEQRES   3 B  377  THR SER PRO ASP SER LYS ALA THR VAL SER GLY ASP HIS
SEQRES   4 B  377  TRP ASP HIS GLY LEU ASN GLY GLU ASN TRP GLU GLY LYS
SEQRES   5 B  377  ASP GLY ALA GLY ASN ALA TRP VAL CYS LYS THR GLY ARG
SEQRES   6 B  377  LYS GLN SER PRO ILE ASN VAL PRO GLN TYR GLN VAL LEU
SEQRES   7 B  377  ASP GLY LYS GLY SER LYS ILE ALA ASN GLY LEU GLN THR
SEQRES   8 B  377  GLN TRP SER TYR PRO ASP LEU MET SER ASN GLY THR SER
SEQRES   9 B  377  VAL GLN VAL ILE ASN ASN GLY HIS THR ILE GLN VAL GLN
SEQRES  10 B  377  TRP THR TYR ASN TYR ALA GLY HIS ALA THR ILE ALA ILE
SEQRES  11 B  377  PRO ALA MET HIS ASN GLN THR ASN ARG ILE VAL ASP VAL
SEQRES  12 B  377  LEU GLU MET ARG PRO ASN ASP ALA ALA ASP ARG VAL THR
SEQRES  13 B  377  ALA VAL PRO THR GLN PHE HIS PHE HIS SER THR SER GLU
SEQRES  14 B  377  HIS LEU LEU ALA GLY LYS ILE TYR PRO LEU GLU LEU HIS
SEQRES  15 B  377  ILE VAL HIS GLN VAL THR GLU LYS LEU GLU ALA CYS LYS
SEQRES  16 B  377  GLY GLY CYS PHE SER VAL THR GLY ILE LEU PHE GLN LEU
SEQRES  17 B  377  ASP ASN GLY PRO ASP ASN GLU LEU LEU GLU PRO ILE PHE
SEQRES  18 B  377  ALA ASN MET PRO SER ARG GLU GLY THR PHE SER ASN LEU
SEQRES  19 B  377  PRO ALA GLY THR THR ILE LYS LEU GLY GLU LEU LEU PRO
SEQRES  20 B  377  SER ASP ARG ASP TYR VAL THR TYR GLU GLY SER LEU THR
SEQRES  21 B  377  THR PRO PRO CYS SER GLU GLY LEU LEU TRP HIS VAL MET
SEQRES  22 B  377  THR GLN PRO GLN ARG ILE SER PHE GLY GLN TRP ASN ARG
SEQRES  23 B  377  TYR ARG LEU ALA VAL GLY LEU LYS GLU CYS ASN SER THR
SEQRES  24 B  377  GLU THR ALA ALA ASP ALA GLY HIS HIS HIS HIS HIS ARG
SEQRES  25 B  377  ARG LEU LEU HIS ASN HIS ALA HIS LEU GLU GLU VAL PRO
SEQRES  26 B  377  ALA ALA THR SER GLU PRO LYS HIS TYR PHE ARG ARG VAL
SEQRES  27 B  377  MET LEU ALA GLU SER ALA ASN PRO ASP ALA TYR THR CYS
SEQRES  28 B  377  LYS ALA VAL ALA PHE GLY GLN ASN PHE ARG ASN PRO GLN
SEQRES  29 B  377  TYR ALA ASN GLY ARG THR ILE LYS LEU ALA ARG TYR HIS
MODRES 3B1B ASN B  101  ASN  GLYCOSYLATION SITE
MODRES 3B1B ASN A  135  ASN  GLYCOSYLATION SITE
MODRES 3B1B ASN A  101  ASN  GLYCOSYLATION SITE
MODRES 3B1B ASN B  135  ASN  GLYCOSYLATION SITE
MODRES 3B1B ASN B  297  ASN  GLYCOSYLATION SITE
HET     ZN  A 378       1
HET    SO4  A 379       5
HET    SO4  A 380       5
HET    NAG  A 381      14
HET    NAG  A 382      14
HET     ZN  B 378       1
HET    SO4  B 379       5
HET    NAG  B 380      14
HET    NAG  B 381      14
HET    NAG  B 382      14
HETNAM      ZN ZINC ION
HETNAM     SO4 SULFATE ION
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
FORMUL   3   ZN    2(ZN 2+)
FORMUL   4  SO4    3(O4 S 2-)
FORMUL   6  NAG    5(C8 H15 N O6)
FORMUL  13  HOH   *888(H2 O)
HELIX    1   1 ALA A   86  GLN A   90  5                                   5
HELIX    2   2 VAL A  141  MET A  146  5                                   6
HELIX    3   3 LEU A  191  LYS A  195  5                                   5
HELIX    4   4 LEU A  217  ALA A  222  1                                   6
HELIX    5   5 LYS A  241  LEU A  246  1                                   6
HELIX    6   6 PHE A  281  VAL A  291  1                                  11
HELIX    7   7 ASN A  345  TYR A  349  5                                   5
HELIX    8   8 ALA B   86  GLN B   90  5                                   5
HELIX    9   9 ARG B  139  MET B  146  5                                   8
HELIX   10  10 LEU B  191  LYS B  195  5                                   5
HELIX   11  11 ASN B  214  LEU B  216  5                                   3
HELIX   12  12 LEU B  217  ALA B  222  1                                   6
HELIX   13  13 LYS B  241  LEU B  246  1                                   6
HELIX   14  14 PHE B  281  VAL B  291  1                                  11
HELIX   15  15 ASN B  345  ASP B  347  5                                   3
SHEET    1   A 2 ASN A  71  VAL A  72  0
SHEET    2   A 2 LEU A 171  LEU A 172  1  O  LEU A 171   N  VAL A  72
SHEET    1   B 6 GLN A  92  SER A  94  0
SHEET    2   B 6 HIS A 125  PRO A 131 -1  O  HIS A 125   N  SER A  94
SHEET    3   B 6 ALA A 152  HIS A 165 -1  O  ALA A 157   N  ALA A 126
SHEET    4   B 6 LEU A 179  VAL A 187 -1  O  VAL A 184   N  THR A 160
SHEET    5   B 6 CYS A 198  ASP A 209 -1  O  THR A 202   N  ILE A 183
SHEET    6   B 6 GLN A 277  SER A 280  1  O  GLN A 277   N  LEU A 205
SHEET    1   C 9 THR A 230  ASN A 233  0
SHEET    2   C 9 VAL A 105  ASN A 109 -1  N  ASN A 109   O  THR A 230
SHEET    3   C 9 ILE A 114  TRP A 118 -1  O  GLN A 115   N  ILE A 108
SHEET    4   C 9 ALA A 152  HIS A 165 -1  O  PHE A 162   N  VAL A 116
SHEET    5   C 9 LEU A 179  VAL A 187 -1  O  VAL A 184   N  THR A 160
SHEET    6   C 9 CYS A 198  ASP A 209 -1  O  THR A 202   N  ILE A 183
SHEET    7   C 9 GLU A 266  MET A 273  1  O  HIS A 271   N  GLY A 203
SHEET    8   C 9 TYR A 252  SER A 258 -1  N  TYR A 255   O  TRP A 270
SHEET    9   C 9 ILE A 371  ALA A 374 -1  O  ALA A 374   N  TYR A 252
SHEET    1   D 2 LEU A  98  MET A  99  0
SHEET    2   D 2 THR A 239  ILE A 240 -1  O  ILE A 240   N  LEU A  98
SHEET    1   E 2 LEU A 293  ASN A 297  0
SHEET    2   E 2 THR A 350  ALA A 355 -1  O  VAL A 354   N  LEU A 293
SHEET    1   F 2 ASN B  71  VAL B  72  0
SHEET    2   F 2 LEU B 171  LEU B 172  1  O  LEU B 171   N  VAL B  72
SHEET    1   G 6 GLN B  92  SER B  94  0
SHEET    2   G 6 HIS B 125  PRO B 131 -1  O  HIS B 125   N  SER B  94
SHEET    3   G 6 ALA B 152  HIS B 165 -1  O  ALA B 157   N  ALA B 126
SHEET    4   G 6 LEU B 179  VAL B 187 -1  O  VAL B 184   N  THR B 160
SHEET    5   G 6 CYS B 198  ASP B 209 -1  O  ILE B 204   N  LEU B 181
SHEET    6   G 6 GLN B 277  SER B 280  1  O  GLN B 277   N  LEU B 205
SHEET    1   H 9 THR B 230  ASN B 233  0
SHEET    2   H 9 VAL B 105  ASN B 109 -1  N  ASN B 109   O  THR B 230
SHEET    3   H 9 ILE B 114  TRP B 118 -1  O  GLN B 115   N  ILE B 108
SHEET    4   H 9 ALA B 152  HIS B 165 -1  O  PHE B 162   N  VAL B 116
SHEET    5   H 9 LEU B 179  VAL B 187 -1  O  VAL B 184   N  THR B 160
SHEET    6   H 9 CYS B 198  ASP B 209 -1  O  ILE B 204   N  LEU B 181
SHEET    7   H 9 GLU B 266  MET B 273  1  O  HIS B 271   N  GLY B 203
SHEET    8   H 9 TYR B 252  SER B 258 -1  N  VAL B 253   O  VAL B 272
SHEET    9   H 9 ILE B 371  ALA B 374 -1  O  ALA B 374   N  TYR B 252
SHEET    1   I 2 LEU B  98  MET B  99  0
SHEET    2   I 2 THR B 239  ILE B 240 -1  O  ILE B 240   N  LEU B  98
SHEET    1   J 2 LEU B 293  SER B 298  0
SHEET    2   J 2 TYR B 349  ALA B 355 -1  O  THR B 350   N  ASN B 297
SSBOND   1 CYS A   21    CYS B   21                          1555   1555  2.05
SSBOND   2 CYS A   61    CYS A  264                          1555   1555  2.12
SSBOND   3 CYS A  194    CYS A  198                          1555   1555  2.06
SSBOND   4 CYS A  296    CYS A  351                          1555   1555  2.05
SSBOND   5 CYS B   61    CYS B  264                          1555   1555  2.14
SSBOND   6 CYS B  194    CYS B  198                          1555   1555  2.52
SSBOND   7 CYS B  296    CYS B  351                          1555   1555  2.04
LINK         ND2 ASN B 101                 C1  NAG B 380     1555   1555  1.44
LINK         ND2 ASN A 135                 C1  NAG A 382     1555   1555  1.45
LINK         ND2 ASN A 101                 C1  NAG A 381     1555   1555  1.45
LINK         ND2 ASN B 135                 C1  NAG B 381     1555   1555  1.45
LINK         ND2 ASN B 297                 C1  NAG B 382     1555   1555  1.47
LINK         ND1 HIS B 182                ZN    ZN B 378     1555   1555  2.02
LINK         ND1 HIS A 182                ZN    ZN A 378     1555   1555  2.03
LINK         NE2 HIS B 163                ZN    ZN B 378     1555   1555  2.07
LINK         NE2 HIS A 163                ZN    ZN A 378     1555   1555  2.07
LINK         NE2 HIS B 165                ZN    ZN B 378     1555   1555  2.07
LINK         NE2 HIS A 165                ZN    ZN A 378     1555   1555  2.14
LINK        ZN    ZN B 378                 O   HOH B 794     1555   1555  1.79
LINK        ZN    ZN A 378                 O   HOH A 714     1555   1555  2.63
CISPEP   1 SER A   68    PRO A   69          0        -2.85
CISPEP   2 SER A  166    THR A  167          0       -12.73
CISPEP   3 PRO A  262    PRO A  263          0         4.24
CISPEP   4 CYS B   21    ILE B   22          0        12.43
CISPEP   5 SER B   68    PRO B   69          0         0.42
CISPEP   6 SER B  166    THR B  167          0       -15.45
CISPEP   7 PRO B  262    PRO B  263          0         9.46
SITE     1 AC1  4 HIS A 163  HIS A 165  HIS A 182  HOH A 714
SITE     1 AC2  9 TYR A 365  ALA A 366  ASN A 367  HOH A 404
SITE     2 AC2  9 HOH A 512  HOH A 647  HOH A 779  HOH A 855
SITE     3 AC2  9 ASN B 210
SITE     1 AC3  4 LYS A  32  THR A 230  PHE A 231  HOH A 573
SITE     1 AC4  7 ASN A 101  SER A 104  THR A 119  TYR A 120
SITE     2 AC4  7 HOH A 709  HOH A 876  HOH A 878
SITE     1 AC5  3 ASN A 135  THR A 137  HOH A 667
SITE     1 AC6  4 HIS B 163  HIS B 165  HIS B 182  HOH B 794
SITE     1 AC7  8 ASN A 210  TYR B 365  ALA B 366  ASN B 367
SITE     2 AC7  8 HOH B 436  HOH B 561  HOH B 777  HOH B 781
SITE     1 AC8  7 ASN B 101  THR B 103  SER B 104  THR B 119
SITE     2 AC8  7 TYR B 120  HOH B 444  HOH B 740
SITE     1 AC9  6 HOH A 426  HOH A 439  ASN B 135  HOH B 528
SITE     2 AC9  6 HOH B 596  HOH B 910
SITE     1 BC1  4 GLU B 295  ASN B 297  THR B 350  LYS B 352
CRYST1  134.300  134.300  120.100  90.00  90.00 120.00 P 65         12
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      0.007448  0.004300  0.000000        0.00000
SCALE2      0.000000  0.008600  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008323        0.00000
      
PROCHECK
Go to PROCHECK summary
 References