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PDBsum entry 3cye

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
3cye
Jmol
Contents
Protein chains
385 a.a.
Ligands
NAG
GOL ×10
ACT ×5
PO4
NAG-NAG-MAN-MAN
Metals
_CA ×5
Waters ×756
HEADER    HYDROLASE                               25-APR-08   3CYE
TITLE     CYRSTAL STRUCTURE OF THE NATIVE 1918 H1N1 NEURAMINIDASE FROM A CRYSTAL
TITLE    2 WITH LATTICE-TRANSLOCATION DEFECTS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: NEURAMINIDASE;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: ECTODOMAIN OF NEURAMINIDASE;
COMPND   5 EC: 3.2.1.18;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS;
SOURCE   3 STRAIN: A/BREVIG MISSION/1/1918;
SOURCE   4 GENE: NA;
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: HIGH-FIVE BTI-TN-5B1-4;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PACGP67
KEYWDS    6-BLADED BETA-PROPELLER, GLYCOPROTEIN, GLYCOSIDASE, HYDROLASE,
KEYWDS   2 MEMBRANE, METAL-BINDING, SIGNAL-ANCHOR, TRANSMEMBRANE, VIRION,
KEYWDS   3 LATTICE-TRANSLOCATION
EXPDTA    X-RAY DIFFRACTION
NUMMDL    2
AUTHOR    X.ZHU,X.XU,I.A.WILSON
REVDAT   3   13-JUL-11 3CYE    1       VERSN
REVDAT   2   24-FEB-09 3CYE    1       VERSN
REVDAT   1   05-AUG-08 3CYE    0
JRNL        AUTH   X.ZHU,X.XU,I.A.WILSON
JRNL        TITL   STRUCTURE DETERMINATION OF THE 1918 H1N1 NEURAMINIDASE FROM
JRNL        TITL 2 A CRYSTAL WITH LATTICE-TRANSLOCATION DEFECTS
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  64   843 2008
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   18645233
JRNL        DOI    10.1107/S0907444908016648
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   X.XU,X.ZHU,J.STEVENS,P.M.RUDD,R.A.DWEK,I.A.WILSON
REMARK   1  TITL   STRUCTURAL CHARACTERIZATION OF THE 1918 INFLUENZA H1N1
REMARK   1  TITL 2 NEURAMINIDASE
REMARK   1  REF    TO BE PUBLISHED
REMARK   1  REFN
REMARK   2
REMARK   2 RESOLUTION.    1.65 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) : 1.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.86
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1
REMARK   3   NUMBER OF REFLECTIONS             : 113058
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.231
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 5652
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) : 1.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6184
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.57
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890
REMARK   3   BIN FREE R VALUE SET COUNT          : 332
REMARK   3   BIN FREE R VALUE                    : 0.3710
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5926
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 154
REMARK   3   SOLVENT ATOMS            : 754
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.73
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -1.25000
REMARK   3    B22 (A**2) : 2.27000
REMARK   3    B33 (A**2) : -1.02000
REMARK   3    B12 (A**2) : 0.00000
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): 0.167
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.140
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12516 ; 0.012 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16988 ; 1.323 ; 1.947
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1536 ; 6.806 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   544 ;33.450 ;23.971
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1880 ;12.452 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    68 ;11.825 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1782 ; 0.090 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9556 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3513 ; 0.222 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6813 ; 0.301 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   700 ; 0.138 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    20 ; 0.089 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    91 ; 0.184 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    36 ; 0.160 ; 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):  7844 ; 0.768 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12330 ; 1.183 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5472 ; 1.829 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4658 ; 2.602 ; 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   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3CYE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-APR-08.
REMARK 100 THE RCSB ID CODE IS RCSB047365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-06
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL9-2
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00797
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113144
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3
REMARK 200  DATA REDUNDANCY                : 4.200
REMARK 200  R MERGE                    (I) : 0.09300
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.4
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.52800
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2HTY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16 M CALCIUM ACETATE; 0.08 M
REMARK 280  CACODYLATE; 14.4% PEG8000; 20% GLYCEROL, PH 6.50, VAPOR
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.93000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.93000
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        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       58.86400
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.23600
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       58.86400
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.23600
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       58.93000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       58.86400
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.23600
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       58.93000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       58.86400
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       69.23600
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 22810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -184.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -58.93000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375      HOH B3266  LIES ON A SPECIAL POSITION.
REMARK 375      HOH B3278  LIES ON A SPECIAL POSITION.
REMARK 375 CA    CA A   5  LIES ON A SPECIAL POSITION.
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   1 ASP A   469
REMARK 465   1 LYS A   470
REMARK 465   1 ASP B   469
REMARK 465   1 LYS B   470
REMARK 465   2 ASP A   469
REMARK 465   2 LYS A   470
REMARK 465   2 ASP B   469
REMARK 465   2 LYS B   470
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  1 SER A 125     -160.89   -102.01
REMARK 500  1 ILE A 222       67.64     60.37
REMARK 500  1 THR A 225     -157.85   -136.18
REMARK 500  1 ALA A 250     -169.35   -127.50
REMARK 500  1 ASP A 283      114.63   -160.37
REMARK 500  1 HIS A 296       37.50   -160.94
REMARK 500  1 ASN A 347     -174.22     68.89
REMARK 500  1 ASP A 357     -128.23     63.89
REMARK 500  1 SER A 404     -136.54   -120.15
REMARK 500  1 ASN A 450       64.33   -100.09
REMARK 500  1 PHE A 466     -137.80    -85.57
REMARK 500  1 ASN B 221       74.36   -151.30
REMARK 500  1 ILE B 222       68.04     61.96
REMARK 500  1 THR B 225     -157.65   -136.41
REMARK 500  1 ASN B 272       -6.00     73.53
REMARK 500  1 ASP B 283      115.90   -160.59
REMARK 500  1 CYS B 291     -166.55   -129.82
REMARK 500  1 HIS B 296       35.77   -160.14
REMARK 500  1 ASN B 347     -175.17     71.20
REMARK 500  1 ASP B 357     -128.66     61.90
REMARK 500  1 SER B 404     -134.35   -118.75
REMARK 500  2 SER A 125     -150.69   -101.82
REMARK 500  2 LYS A 150      150.04    -41.35
REMARK 500  2 ALA A 177      132.56   -170.01
REMARK 500  2 ASN A 221       76.60   -152.16
REMARK 500  2 ILE A 222       72.13     51.40
REMARK 500  2 THR A 225     -152.53   -137.09
REMARK 500  2 ALA A 270       50.75   -141.01
REMARK 500  2 ASN A 272        4.67     81.03
REMARK 500  2 THR A 284       50.43     37.74
REMARK 500  2 CYS A 291     -160.33   -128.63
REMARK 500  2 TRP A 295      -63.27    -95.35
REMARK 500  2 HIS A 296       42.09   -156.07
REMARK 500  2 ASN A 347     -175.56     67.38
REMARK 500  2 ASP A 357     -121.78     61.35
REMARK 500  2 SER A 404     -132.95   -116.31
REMARK 500  2 ASN A 450       60.02   -104.62
REMARK 500  2 TRP A 456     -166.12   -172.75
REMARK 500  2 TRP A 458       71.64   -119.29
REMARK 500  2 PHE A 466     -150.30    -94.62
REMARK 500  2 LYS B 111      -42.31   -135.35
REMARK 500  2 SER B 125     -156.42    -95.94
REMARK 500  2 ASN B 146      125.69    -38.46
REMARK 500  2 ILE B 222       72.11     59.16
REMARK 500  2 THR B 225     -150.19   -134.41
REMARK 500  2 CYS B 230     -178.24    -65.54
REMARK 500  2 ASN B 272       -3.20     83.96
REMARK 500  2 CYS B 291     -165.66   -124.99
REMARK 500  2 TRP B 295      -62.83    -95.96
REMARK 500  2 HIS B 296       36.83   -152.90
REMARK 500
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
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                           1  CA A   1  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 293   O
REMARK 620 2 GLY A 297   O    87.2
REMARK 620 3 ASP A 324   OD2  94.6  89.6
REMARK 620 4 GLY A 345   O    99.2  83.8 164.3
REMARK 620 5 ASN A 347   O    90.3 169.2 101.1  86.3
REMARK 620 6 HOH A3044   O   178.9  92.2  86.2  79.9  90.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA A   2  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 379   OD1
REMARK 620 2 ASP A 379   OD2  51.6
REMARK 620 3 ASN A 381   OD1  77.2 108.9
REMARK 620 4 ASP A 387   OD1 171.8 130.8 107.1
REMARK 620 5 SER A 389   O    84.8  76.4 150.1  88.4
REMARK 620 6 HOH A3043   O   111.8  74.6  86.0  75.8 123.1
REMARK 620 7 HOH A3108   O    86.2 133.3  73.9  88.3  81.4 149.5
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA B   4  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 293   O
REMARK 620 2 GLY B 297   O    85.9
REMARK 620 3 ASP B 324   OD2  95.0  90.6
REMARK 620 4 GLY B 345   O    97.8  82.8 165.2
REMARK 620 5 ASN B 347   O    91.1 168.8 100.4  86.9
REMARK 620 6 HOH B3057   O   177.9  92.1  85.2  81.7  90.9
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA B   3  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 379   OD1
REMARK 620 2 ASP B 379   OD2  52.3
REMARK 620 3 ASN B 381   OD1  79.0 108.3
REMARK 620 4 ASP B 387   OD1 168.8 130.0 108.0
REMARK 620 5 SER B 389   O    82.2  76.0 151.2  87.9
REMARK 620 6 HOH B3092   O    86.8 134.1  78.4  86.2  79.0
REMARK 620 7 HOH B3023   O   112.0  73.9  82.6  78.1 124.9 150.2
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                           1  CA A   5  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A3186   O
REMARK 620 2 HOH B3262   O    86.3
REMARK 620 N                    1
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1009
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BEQ   RELATED DB: PDB
REMARK 900 THE SAME CRYSTAL BUT THE STRUCTURE WAS DETERMINED WITH
REMARK 900 DIFFERENT METHOD.
DBREF  3CYE A   83   470  UNP    Q9IGQ6   NRAM_I18A0      83    469
DBREF  3CYE B   83   470  UNP    Q9IGQ6   NRAM_I18A0      83    469
SEQRES   1 A  387  VAL ILE LEU THR GLY ASN SER SER LEU CYS PRO ILE SER
SEQRES   2 A  387  GLY TRP ALA ILE TYR SER LYS ASP ASN GLY ILE ARG ILE
SEQRES   3 A  387  GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO PHE
SEQRES   4 A  387  ILE SER CYS SER HIS LEU GLU CYS ARG THR PHE PHE LEU
SEQRES   5 A  387  THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY
SEQRES   6 A  387  THR VAL LYS ASP ARG SER PRO TYR ARG THR LEU MET SER
SEQRES   7 A  387  CYS PRO VAL GLY GLU ALA PRO SER PRO TYR ASN SER ARG
SEQRES   8 A  387  PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS ASP
SEQRES   9 A  387  GLY MET GLY TRP LEU THR ILE GLY ILE SER GLY PRO ASP
SEQRES  10 A  387  ASN GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE
SEQRES  11 A  387  THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU ARG
SEQRES  12 A  387  THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER CYS
SEQRES  13 A  387  PHE THR ILE MET THR ASP GLY PRO SER ASN GLY GLN ALA
SEQRES  14 A  387  SER TYR LYS ILE LEU LYS ILE GLU LYS GLY LYS VAL THR
SEQRES  15 A  387  LYS SER ILE GLU LEU ASN ALA PRO ASN TYR HIS TYR GLU
SEQRES  16 A  387  GLU CYS SER CYS TYR PRO ASP THR GLY LYS VAL MET CYS
SEQRES  17 A  387  VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO TRP
SEQRES  18 A  387  VAL SER PHE ASP GLN ASN LEU ASP TYR GLN ILE GLY TYR
SEQRES  19 A  387  ILE CYS SER GLY VAL PHE GLY ASP ASN PRO ARG PRO ASN
SEQRES  20 A  387  ASP GLY THR GLY SER CYS GLY PRO VAL SER SER ASN GLY
SEQRES  21 A  387  ALA ASN GLY ILE LYS GLY PHE SER PHE ARG TYR ASP ASN
SEQRES  22 A  387  GLY VAL TRP ILE GLY ARG THR LYS SER THR SER SER ARG
SEQRES  23 A  387  SER GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP THR
SEQRES  24 A  387  GLU THR ASP SER SER PHE SER VAL ARG GLN ASP ILE VAL
SEQRES  25 A  387  ALA ILE THR ASP TRP SER GLY TYR SER GLY SER PHE VAL
SEQRES  26 A  387  GLN HIS PRO GLU LEU THR GLY LEU ASP CYS MET ARG PRO
SEQRES  27 A  387  CYS PHE TRP VAL GLU LEU ILE ARG GLY GLN PRO LYS GLU
SEQRES  28 A  387  ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE CYS
SEQRES  29 A  387  GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO ASP
SEQRES  30 A  387  GLY ALA GLU LEU PRO PHE SER ILE ASP LYS
SEQRES   1 B  387  VAL ILE LEU THR GLY ASN SER SER LEU CYS PRO ILE SER
SEQRES   2 B  387  GLY TRP ALA ILE TYR SER LYS ASP ASN GLY ILE ARG ILE
SEQRES   3 B  387  GLY SER LYS GLY ASP VAL PHE VAL ILE ARG GLU PRO PHE
SEQRES   4 B  387  ILE SER CYS SER HIS LEU GLU CYS ARG THR PHE PHE LEU
SEQRES   5 B  387  THR GLN GLY ALA LEU LEU ASN ASP LYS HIS SER ASN GLY
SEQRES   6 B  387  THR VAL LYS ASP ARG SER PRO TYR ARG THR LEU MET SER
SEQRES   7 B  387  CYS PRO VAL GLY GLU ALA PRO SER PRO TYR ASN SER ARG
SEQRES   8 B  387  PHE GLU SER VAL ALA TRP SER ALA SER ALA CYS HIS ASP
SEQRES   9 B  387  GLY MET GLY TRP LEU THR ILE GLY ILE SER GLY PRO ASP
SEQRES  10 B  387  ASN GLY ALA VAL ALA VAL LEU LYS TYR ASN GLY ILE ILE
SEQRES  11 B  387  THR ASP THR ILE LYS SER TRP ARG ASN ASN ILE LEU ARG
SEQRES  12 B  387  THR GLN GLU SER GLU CYS ALA CYS VAL ASN GLY SER CYS
SEQRES  13 B  387  PHE THR ILE MET THR ASP GLY PRO SER ASN GLY GLN ALA
SEQRES  14 B  387  SER TYR LYS ILE LEU LYS ILE GLU LYS GLY LYS VAL THR
SEQRES  15 B  387  LYS SER ILE GLU LEU ASN ALA PRO ASN TYR HIS TYR GLU
SEQRES  16 B  387  GLU CYS SER CYS TYR PRO ASP THR GLY LYS VAL MET CYS
SEQRES  17 B  387  VAL CYS ARG ASP ASN TRP HIS GLY SER ASN ARG PRO TRP
SEQRES  18 B  387  VAL SER PHE ASP GLN ASN LEU ASP TYR GLN ILE GLY TYR
SEQRES  19 B  387  ILE CYS SER GLY VAL PHE GLY ASP ASN PRO ARG PRO ASN
SEQRES  20 B  387  ASP GLY THR GLY SER CYS GLY PRO VAL SER SER ASN GLY
SEQRES  21 B  387  ALA ASN GLY ILE LYS GLY PHE SER PHE ARG TYR ASP ASN
SEQRES  22 B  387  GLY VAL TRP ILE GLY ARG THR LYS SER THR SER SER ARG
SEQRES  23 B  387  SER GLY PHE GLU MET ILE TRP ASP PRO ASN GLY TRP THR
SEQRES  24 B  387  GLU THR ASP SER SER PHE SER VAL ARG GLN ASP ILE VAL
SEQRES  25 B  387  ALA ILE THR ASP TRP SER GLY TYR SER GLY SER PHE VAL
SEQRES  26 B  387  GLN HIS PRO GLU LEU THR GLY LEU ASP CYS MET ARG PRO
SEQRES  27 B  387  CYS PHE TRP VAL GLU LEU ILE ARG GLY GLN PRO LYS GLU
SEQRES  28 B  387  ASN THR ILE TRP THR SER GLY SER SER ILE SER PHE CYS
SEQRES  29 B  387  GLY VAL ASN SER ASP THR VAL GLY TRP SER TRP PRO ASP
SEQRES  30 B  387  GLY ALA GLU LEU PRO PHE SER ILE ASP LYS
MODRES 3CYE ASN A  146  ASN  GLYCOSYLATION SITE
MODRES 3CYE ASN B  146  ASN  GLYCOSYLATION SITE
HET    NAG  A1001      14
HET    NAG  B2001      14
HET    NAG  B2002      14
HET    MAN  B2003      11
HET    MAN  B2004      11
HET     CA  A   1       1
HET     CA  A   2       1
HET     CA  A   5       1
HET    ACT  A3000       4
HET    ACT  A3002       4
HET    ACT  A3003       4
HET    PO4  A1000       5
HET     CA  B   3       1
HET     CA  B   4       1
HET    ACT  B3001       4
HET    ACT  B3004       4
HET    GOL  A3004       6
HET    GOL  A3005       6
HET    GOL  A1003       6
HET    GOL  A1005       6
HET    GOL  A1009       6
HET    GOL  B1002       6
HET    GOL  B1004       6
HET    GOL  B1006       6
HET    GOL  B1007       6
HET    GOL  B1008       6
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE
HETNAM     MAN ALPHA-D-MANNOSE
HETNAM      CA CALCIUM ION
HETNAM     ACT ACETATE ION
HETNAM     PO4 PHOSPHATE ION
HETNAM     GOL GLYCEROL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  NAG    3(C8 H15 N O6)
FORMUL   4  MAN    2(C6 H12 O6)
FORMUL   5   CA    5(CA 2+)
FORMUL   8  ACT    5(C2 H3 O2 1-)
FORMUL  11  PO4    O4 P 3-
FORMUL  16  GOL    10(C3 H8 O3)
FORMUL  26  HOH   *754(H2 O)
HELIX    1   1 ASN A  104  SER A  110  1                                   7
HELIX    2   2 ASP A  142  ASN A  146  5                                   5
HELIX    3   3 HIS A  412A GLY A  414  1                                   6
HELIX    4   4 ASN B  104  SER B  110  1                                   7
HELIX    5   5 ASP B  142  ASN B  146  5                                   5
HELIX    6   6 HIS B  412A GLY B  414  1                                   6
SHEET    1   A 4 GLY A  96  LYS A 102  0
SHEET    2   A 4 THR A 439  VAL A 449 -1  O  CYS A 447   N  ALA A  98
SHEET    3   A 4 ARG A 419  GLY A 429 -1  N  ARG A 428   O  SER A 440
SHEET    4   A 4 SER A 407  GLN A 412 -1  N  PHE A 410   O  CYS A 421
SHEET    1   B 4 PHE A 115  CYS A 124  0
SHEET    2   B 4 CYS A 129  LEU A 139 -1  O  PHE A 132   N  PHE A 121
SHEET    3   B 4 THR A 157  PRO A 162 -1  O  CYS A 161   N  THR A 131
SHEET    4   B 4 ARG A 172  VAL A 176 -1  O  ARG A 172   N  SER A 160
SHEET    1   C 4 SER A 179  HIS A 184  0
SHEET    2   C 4 TRP A 189  SER A 195 -1  O  LEU A 190   N  CYS A 183
SHEET    3   C 4 VAL A 202  TYR A 207 -1  O  VAL A 202   N  SER A 195
SHEET    4   C 4 ILE A 210  LYS A 216 -1  O  ILE A 215   N  ALA A 203
SHEET    1   D 4 ALA A 231  VAL A 233  0
SHEET    2   D 4 SER A 236  ASP A 243 -1  O  SER A 236   N  VAL A 233
SHEET    3   D 4 SER A 251  GLU A 258 -1  O  ILE A 257   N  CYS A 237
SHEET    4   D 4 LYS A 261  GLU A 267 -1  O  LYS A 261   N  GLU A 258
SHEET    1   E 4 GLU A 276  ASP A 283  0
SHEET    2   E 4 LYS A 286  ARG A 292 -1  O  MET A 288   N  TYR A 281
SHEET    3   E 4 PRO A 301  PHE A 305 -1  O  PRO A 301   N  CYS A 291
SHEET    4   E 4 TYR A 312  TYR A 316 -1  O  GLY A 315   N  TRP A 302
SHEET    1   F 4 SER A 353  TYR A 356  0
SHEET    2   F 4 GLY A 359  ARG A 364 -1  O  GLY A 359   N  TYR A 356
SHEET    3   F 4 SER A 372  ASP A 379 -1  O  ILE A 377   N  ILE A 362
SHEET    4   F 4 VAL A 392  TRP A 403 -1  O  GLN A 395   N  MET A 376
SHEET    1   G 4 GLY B  96  LYS B 102  0
SHEET    2   G 4 THR B 439  VAL B 449 -1  O  SER B 445   N  TYR B 100
SHEET    3   G 4 ARG B 419  GLY B 429 -1  N  PRO B 420   O  GLY B 448
SHEET    4   G 4 SER B 407  GLN B 412 -1  N  PHE B 410   O  CYS B 421
SHEET    1   H 4 PHE B 115  CYS B 124  0
SHEET    2   H 4 CYS B 129  LEU B 139 -1  O  PHE B 132   N  PHE B 121
SHEET    3   H 4 THR B 157  PRO B 162 -1  O  CYS B 161   N  THR B 131
SHEET    4   H 4 ARG B 172  VAL B 176 -1  O  SER B 175   N  LEU B 158
SHEET    1   I 4 SER B 179  HIS B 184  0
SHEET    2   I 4 TRP B 189  SER B 195 -1  O  LEU B 190   N  CYS B 183
SHEET    3   I 4 VAL B 202  TYR B 207 -1  O  VAL B 202   N  SER B 195
SHEET    4   I 4 ILE B 210  LYS B 216 -1  O  ILE B 215   N  ALA B 203
SHEET    1   J 4 ALA B 231  VAL B 233  0
SHEET    2   J 4 SER B 236  ASP B 243 -1  O  PHE B 238   N  ALA B 231
SHEET    3   J 4 SER B 251  GLU B 258 -1  O  ILE B 257   N  CYS B 237
SHEET    4   J 4 LYS B 261  GLU B 267 -1  O  LYS B 261   N  GLU B 258
SHEET    1   K 4 GLU B 276  ASP B 283  0
SHEET    2   K 4 LYS B 286  ARG B 292 -1  O  MET B 288   N  TYR B 281
SHEET    3   K 4 PRO B 301  PHE B 305 -1  O  PRO B 301   N  CYS B 291
SHEET    4   K 4 TYR B 312  TYR B 316 -1  O  GLY B 315   N  TRP B 302
SHEET    1   L 4 SER B 353  TYR B 356  0
SHEET    2   L 4 GLY B 359  ARG B 364 -1  O  GLY B 359   N  TYR B 356
SHEET    3   L 4 SER B 372  ASP B 379 -1  O  ILE B 377   N  ILE B 362
SHEET    4   L 4 VAL B 392  TRP B 403 -1  O  GLN B 395   N  MET B 376
SSBOND   1 CYS A   92    CYS A  417                          1555   1555  2.08
SSBOND   2 CYS A  124    CYS A  129                          1555   1555  2.08
SSBOND   3 CYS A  183    CYS A  230                          1555   1555  2.04
SSBOND   4 CYS A  232    CYS A  237                          1555   1555  2.09
SSBOND   5 CYS A  278    CYS A  291                          1555   1555  2.16
SSBOND   6 CYS A  280    CYS A  289                          1555   1555  2.04
SSBOND   7 CYS A  318    CYS A  336                          1555   1555  2.04
SSBOND   8 CYS A  421    CYS A  447                          1555   1555  2.16
SSBOND   9 CYS B   92    CYS B  417                          1555   1555  2.07
SSBOND  10 CYS B  124    CYS B  129                          1555   1555  2.09
SSBOND  11 CYS B  183    CYS B  230                          1555   1555  2.03
SSBOND  12 CYS B  232    CYS B  237                          1555   1555  2.10
SSBOND  13 CYS B  278    CYS B  291                          1555   1555  2.17
SSBOND  14 CYS B  280    CYS B  289                          1555   1555  2.08
SSBOND  15 CYS B  318    CYS B  336                          1555   1555  2.04
SSBOND  16 CYS B  421    CYS B  447                          1555   1555  2.19
LINK         ND2AASN A 146                 C1 ANAG A1001     1555   1555  1.45
LINK         O  AASP A 293                CA  A CA A   1     1555   1555  2.37
LINK         O  AGLY A 297                CA  A CA A   1     1555   1555  2.39
LINK         OD2AASP A 324                CA  A CA A   1     1555   1555  2.29
LINK         O  AGLY A 345                CA  A CA A   1     1555   1555  2.36
LINK         O  AASN A 347                CA  A CA A   1     1555   1555  2.38
LINK         OD1AASP A 379                CA  A CA A   2     1555   1555  2.36
LINK         OD2AASP A 379                CA  A CA A   2     1555   1555  2.65
LINK         OD1AASN A 381                CA  A CA A   2     1555   1555  2.25
LINK         OD1AASP A 387                CA  A CA A   2     1555   1555  2.38
LINK         O  ASER A 389                CA  A CA A   2     1555   1555  2.43
LINK         ND2AASN B 146                 C1 ANAG B2001     1555   1555  1.45
LINK         O  AASP B 293                CA  A CA B   4     1555   1555  2.38
LINK         O  AGLY B 297                CA  A CA B   4     1555   1555  2.36
LINK         OD2AASP B 324                CA  A CA B   4     1555   1555  2.26
LINK         O  AGLY B 345                CA  A CA B   4     1555   1555  2.35
LINK         O  AASN B 347                CA  A CA B   4     1555   1555  2.36
LINK         OD1AASP B 379                CA  A CA B   3     1555   1555  2.38
LINK         OD2AASP B 379                CA  A CA B   3     1555   1555  2.62
LINK         OD1AASN B 381                CA  A CA B   3     1555   1555  2.19
LINK         OD1AASP B 387                CA  A CA B   3     1555   1555  2.43
LINK         O  ASER B 389                CA  A CA B   3     1555   1555  2.40
LINK         O4 ANAG B2001                 C1 ANAG B2002     1555   1555  1.44
LINK         O4 ANAG B2002                 C1 AMAN B2003     1555   1555  1.46
LINK         O3 AMAN B2003                 C1 AMAN B2004     1555   1555  1.45
LINK        CA  A CA A   1                 O  AHOH A3044     1555   1555  2.39
LINK        CA  A CA A   2                 O  AHOH A3043     1555   1555  2.42
LINK        CA  A CA A   2                 O  AHOH A3108     1555   1555  2.52
LINK        CA  A CA A   5                 O  AHOH A3186     1555   1555  2.61
LINK        CA  A CA A   5                 O  AHOH B3262     1555   1555  2.62
LINK        CA  A CA B   3                 O  AHOH B3092     1555   1555  2.34
LINK        CA  A CA B   3                 O  AHOH B3023     1555   1555  2.45
LINK        CA  A CA B   4                 O  AHOH B3057     1555   1555  2.37
CISPEP   1 ASN A  325    PRO A  326          1         5.07
CISPEP   2 GLN A  430    PRO A  431          1         0.72
CISPEP   3 LEU A  464    PRO A  465          1        -1.22
CISPEP   4 ASN B  325    PRO B  326          1         5.81
CISPEP   5 GLN B  430    PRO B  431          1        -1.67
CISPEP   6 LEU B  464    PRO B  465          1        -1.88
CISPEP   7 ASN A  325    PRO A  326          2         6.02
CISPEP   8 GLN A  430    PRO A  431          2        -0.64
CISPEP   9 LEU A  464    PRO A  465          2        -2.16
CISPEP  10 ASN B  325    PRO B  326          2         5.93
CISPEP  11 GLN B  430    PRO B  431          2        -3.75
CISPEP  12 LEU B  464    PRO B  465          2        -1.88
SITE     1 AC1  3 ASN A 146  THR A 148  ILE A 437
SITE     1 AC2  2 ASN B 146  THR B 148
SITE     1 AC5  4 LYS A 366  GLU A 375  ARG A 394  ILE A 400
SITE     1 AC6  5 ASP A 293  GLY A 297  ASP A 324  GLY A 345
SITE     2 AC6  5 ASN A 347
SITE     1 AC7  4 ASP A 379  ASN A 381  ASP A 387  SER A 389
SITE     1 AC8  4 ASP B 379  ASN B 381  ASP B 387  SER B 389
SITE     1 AC9  5 ASP B 293  GLY B 297  ASP B 324  GLY B 345
SITE     2 AC9  5 ASN B 347
SITE     1 BC2  7 GLN A 249  ALA A 250  LEU A 268  ASN A 269
SITE     2 BC2  7 ALA A 270  PRO A 271  ASP B 311
SITE     1 BC3  3 ARG B 152  TRP B 178  SER B 179
SITE     1 BC4  3 THR A 225  GLU A 227  GLU A 277
SITE     1 BC5  2 ARG A 152  TRP A 178
SITE     1 BC6  3 THR B 225  GLU B 227  GLU B 277
SITE     1 BC7  5 ARG A 224  GLU A 276  GLU A 277  ARG A 292
SITE     2 BC7  5 ASN A 294
SITE     1 BC8  3 ASN A 170  SER A 171  GLU B 165
SITE     1 BC9  4 PRO A  93  ILE A  94  TYR A 356  TRP A 361
SITE     1 CC1  5 PRO B  93  ILE B  94  TYR B 356  TRP B 361
SITE     2 CC1  5 TRP B 378
SITE     1 CC2  5 SER A  90  LEU A  91  ASP A 283  ARG A 355
SITE     2 CC2  5 ASP A 357
SITE     1 CC3  4 SER B 246  GLU B 276  GLU B 277  ARG B 292
SITE     1 CC4  5 GLU A 165  ASN A 170  TYR B 169A ASN B 170
SITE     2 CC4  5 SER B 171
SITE     1 CC5  3 ASP B 283  MET B 288  ARG B 355
SITE     1 CC6  6 SER B  90  LEU B  91  ASP B 283  ARG B 355
SITE     2 CC6  6 TYR B 356  ASP B 357
SITE     1 CC7  5 ARG B 118  GLU B 119  ASP B 151  ARG B 156
SITE     2 CC7  5 TRP B 178
SITE     1 CC8  4 GLY A 331  THR A 332  ASP A 387  SER A 388
CRYST1  117.728  138.472  117.860  90.00  90.00  90.00 C 2 2 21     16
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.008494  0.000000  0.000000        0.00000
SCALE2      0.000000  0.007222  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008485        0.00000
      
PROCHECK
Go to PROCHECK summary
 References