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PDBsum entry 2vvz

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Top Page protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
2vvz
Jmol
Contents
Protein chains
470 a.a.
Ligands
DAN ×2
Metals
_CL
Waters ×124
HEADER    HYDROLASE                               13-JUN-08   2VVZ
TITLE     STRUCTURE OF THE CATALYTIC DOMAIN OF STREPTOCOCCUS
TITLE    2 PNEUMONIAE SIALIDASE NANA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: SIALIDASE A;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 319-822;
COMPND   5 SYNONYM: NANA SIALIDASE, NEURAMINIDASE A;
COMPND   6 EC: 3.2.1.18;
COMPND   7 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE   3 ORGANISM_TAXID: 1313;
SOURCE   4 STRAIN: R36A;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS    SECRETED, CELL WALL, SIALIDASE, HYDROLASE,
KEYWDS   2 PEPTIDOGLYCAN-ANCHOR, GLYCOSIDASE, NEURAMINIDASE,
KEYWDS   3 VIRULENCE FACTOR
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.XU,X.LI,P.W.ANDREW,G.L.TAYLOR
REVDAT   3   24-FEB-09 2VVZ    1       VERSN
REVDAT   2   16-SEP-08 2VVZ    1       JRNL
REVDAT   1   24-JUN-08 2VVZ    0
JRNL        AUTH   G.XU,X.LI,P.W.ANDREW,G.L.TAYLOR
JRNL        TITL   STRUCTURE OF THE CATALYTIC DOMAIN OF STREPTOCOCCUS
JRNL        TITL 2 PNEUMONIAE SIALIDASE NANA.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  64   772 2008
JRNL        REFN                   ISSN 1744-3091
JRNL        PMID   18765901
JRNL        DOI    10.1107/S1744309108024044
REMARK   2
REMARK   2 RESOLUTION.    2.5  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) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4
REMARK   3   NUMBER OF REFLECTIONS             : 34868
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) : 0.246
REMARK   3   R VALUE            (WORKING SET) : 0.243
REMARK   3   FREE R VALUE                     : 0.298
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 1830
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) : 2.50
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2076
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3270
REMARK   3   BIN FREE R VALUE SET COUNT          : 87
REMARK   3   BIN FREE R VALUE                    : 0.4590
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 7442
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 41
REMARK   3   SOLVENT ATOMS            : 124
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.32
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.29000
REMARK   3    B22 (A**2) : 0.72000
REMARK   3    B33 (A**2) : -0.43000
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): 0.818
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.358
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.257
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.482
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.903
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.852
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7644 ; 0.007 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10326 ; 1.145 ; 1.952
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   938 ; 7.367 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   366 ;34.184 ;24.426
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1344 ;14.443 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;14.829 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1092 ; 0.081 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5842 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3453 ; 0.206 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5031 ; 0.303 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   385 ; 0.145 ; 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):    34 ; 0.187 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.123 ; 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):  4788 ; 0.358 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7482 ; 0.633 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3292 ; 0.642 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2844 ; 1.063 ; 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS.
REMARK   4
REMARK   4 2VVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-08.
REMARK 100 THE PDBE ID CODE IS EBI-36556.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.4
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MRICOMAX-007 HF
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD (SATURN 944)
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200  DATA SCALING SOFTWARE          : HKL2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36773
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0
REMARK 200  DATA REDUNDANCY                : 2.9
REMARK 200  R MERGE                    (I) : 0.06
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 27.00
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54
REMARK 200  COMPLETENESS FOR SHELL     (%) : 71.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.5
REMARK 200  R MERGE FOR SHELL          (I) : 0.25
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 4.60
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 2BF6
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.1M MES PH 6.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.60300
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.29800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.81300
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.29800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.60300
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.81300
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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     GLU A   319
REMARK 465     GLY A   320
REMARK 465     ALA A   321
REMARK 465     ASP A   792
REMARK 465     LEU A   793
REMARK 465     ILE A   794
REMARK 465     SER A   795
REMARK 465     PRO A   796
REMARK 465     THR A   797
REMARK 465     GLU A   798
REMARK 465     ALA A   799
REMARK 465     LYS A   800
REMARK 465     VAL A   801
REMARK 465     LYS A   802
REMARK 465     ARG A   803
REMARK 465     THR A   804
REMARK 465     ARG A   805
REMARK 465     GLU A   806
REMARK 465     MET A   807
REMARK 465     GLY A   808
REMARK 465     LYS A   809
REMARK 465     GLY A   810
REMARK 465     VAL A   811
REMARK 465     ILE A   812
REMARK 465     GLY A   813
REMARK 465     LEU A   814
REMARK 465     GLU A   815
REMARK 465     PHE A   816
REMARK 465     ASP A   817
REMARK 465     SER A   818
REMARK 465     GLU A   819
REMARK 465     VAL A   820
REMARK 465     LEU A   821
REMARK 465     VAL A   822
REMARK 465     GLU B   319
REMARK 465     GLY B   320
REMARK 465     ALA B   321
REMARK 465     ASP B   792
REMARK 465     LEU B   793
REMARK 465     ILE B   794
REMARK 465     SER B   795
REMARK 465     PRO B   796
REMARK 465     THR B   797
REMARK 465     GLU B   798
REMARK 465     ALA B   799
REMARK 465     LYS B   800
REMARK 465     VAL B   801
REMARK 465     LYS B   802
REMARK 465     ARG B   803
REMARK 465     THR B   804
REMARK 465     ARG B   805
REMARK 465     GLU B   806
REMARK 465     MET B   807
REMARK 465     GLY B   808
REMARK 465     LYS B   809
REMARK 465     GLY B   810
REMARK 465     VAL B   811
REMARK 465     ILE B   812
REMARK 465     GLY B   813
REMARK 465     LEU B   814
REMARK 465     GLU B   815
REMARK 465     PHE B   816
REMARK 465     ASP B   817
REMARK 465     SER B   818
REMARK 465     GLU B   819
REMARK 465     VAL B   820
REMARK 465     LEU B   821
REMARK 465     VAL B   822
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   OG   SER A   332  -  O    HOH A  2002              2.15
REMARK 500   O    THR A   703  -  O    GLU A   709              1.96
REMARK 500   N    ALA A   776  -  O    HOH A  2002              2.19
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 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    ARG A 347      -88.10   -141.38
REMARK 500    HIS A 369     -136.34   -165.05
REMARK 500    ASP A 372       40.46    -78.18
REMARK 500    ASP A 385       32.17    -91.86
REMARK 500    ASP A 417      112.13     66.48
REMARK 500    ILE A 442      -39.52     98.94
REMARK 500    ALA A 472      -99.28    -40.31
REMARK 500    TYR A 473      119.11     66.47
REMARK 500    GLU A 477     -103.19     44.84
REMARK 500    VAL A 481      -82.40    -62.59
REMARK 500    TYR A 482      131.16     97.39
REMARK 500    ALA A 488       76.76    -67.80
REMARK 500    ASP A 490     -152.92    -60.93
REMARK 500    TYR A 491      -56.91     66.11
REMARK 500    LYS A 499      -83.65    169.72
REMARK 500    PRO A 500     -147.49    -75.73
REMARK 500    ALA A 501       34.64    -78.80
REMARK 500    LEU A 514     -120.53    -69.13
REMARK 500    LYS A 564      -82.60    -89.30
REMARK 500    HIS A 597     -112.06     47.51
REMARK 500    THR A 646     -118.95   -118.56
REMARK 500    TYR A 695       61.68     69.51
REMARK 500    GLU A 709      -55.89   -141.67
REMARK 500    TYR A 710      144.34     69.09
REMARK 500    LYS A 720      177.33     78.46
REMARK 500    GLU A 732      -91.75    -79.26
REMARK 500    GLU A 733      -61.89   -140.97
REMARK 500    ALA A 751     -118.66   -124.40
REMARK 500    ALA A 776      103.24    112.21
REMARK 500    ASN B 339     -166.64    -72.09
REMARK 500    ILE B 348       83.08     62.52
REMARK 500    ASP B 372       43.65    -77.60
REMARK 500    ASP B 385       40.23   -102.78
REMARK 500    ASP B 417      123.20     67.42
REMARK 500    PRO B 437     -176.23    -65.90
REMARK 500    ILE B 442      -43.30     99.82
REMARK 500    LYS B 459       95.56     56.96
REMARK 500    ALA B 472      -92.48    -51.75
REMARK 500    TYR B 473      121.85     73.55
REMARK 500    ARG B 476     -150.84   -103.36
REMARK 500    ASP B 490      -51.48     57.52
REMARK 500    LYS B 499      -77.76   -110.58
REMARK 500    PRO B 500     -109.71    -38.64
REMARK 500    ASP B 543       41.70    -96.24
REMARK 500    LYS B 564      -73.26    -88.65
REMARK 500    HIS B 597     -123.34     45.87
REMARK 500    THR B 646     -116.85   -109.49
REMARK 500    TYR B 695       71.11     62.32
REMARK 500    GLU B 709      -30.11   -136.77
REMARK 500    TYR B 710      125.04     70.33
REMARK 500    ASN B 715     -167.06   -163.33
REMARK 500    LYS B 720      178.24     85.26
REMARK 500    LEU B 740      -66.39   -103.59
REMARK 500    ALA B 751     -100.20   -132.64
REMARK 500    ALA B 776      112.08     79.03
REMARK 500    LEU B 779       95.08     48.74
REMARK 500    PHE B 784      149.93    163.07
REMARK 500    TRP B 786      -38.43    154.12
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 LEU A  368     HIS A  369                   74.19
REMARK 500 VAL A  498     LYS A  499                  -45.87
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 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    LYS A 499        21.8      L          L   OUTSIDE RANGE
REMARK 500    LYS B 459        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 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN A1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DAN B1792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1793
DBREF  2VVZ A  319   822  UNP    P62575   NANA_STRPN     319    822
DBREF  2VVZ B  319   822  UNP    P62575   NANA_STRPN     319    822
SEQRES   1 A  504  GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU
SEQRES   2 A  504  SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS
SEQRES   3 A  504  SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY
SEQRES   4 A  504  THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER
SEQRES   5 A  504  SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER
SEQRES   6 A  504  GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE
SEQRES   7 A  504  THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER
SEQRES   8 A  504  ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN
SEQRES   9 A  504  ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET
SEQRES  10 A  504  PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN
SEQRES  11 A  504  LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR
SEQRES  12 A  504  GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR
SEQRES  13 A  504  ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS
SEQRES  14 A  504  ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO
SEQRES  15 A  504  ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN
SEQRES  16 A  504  LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS THR SER
SEQRES  17 A  504  PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER
SEQRES  18 A  504  TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN
SEQRES  19 A  504  ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE
SEQRES  20 A  504  LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN
SEQRES  21 A  504  GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR
SEQRES  22 A  504  THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN SER SER
SEQRES  23 A  504  ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS
SEQRES  24 A  504  ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY
SEQRES  25 A  504  GLN LYS ILE HIS SER SER THR MET ASN ASN ARG ARG ALA
SEQRES  26 A  504  GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY
SEQRES  27 A  504  ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU
SEQRES  28 A  504  GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU
SEQRES  29 A  504  LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR
SEQRES  30 A  504  VAL GLN MET SER ALA ILE HIS THR MET HIS GLU GLY LYS
SEQRES  31 A  504  GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG
SEQRES  32 A  504  GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN
SEQRES  33 A  504  GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS
SEQRES  34 A  504  GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN
SEQRES  35 A  504  GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY
SEQRES  36 A  504  GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP
SEQRES  37 A  504  ASP PHE LEU SER LYS ASP LEU ILE SER PRO THR GLU ALA
SEQRES  38 A  504  LYS VAL LYS ARG THR ARG GLU MET GLY LYS GLY VAL ILE
SEQRES  39 A  504  GLY LEU GLU PHE ASP SER GLU VAL LEU VAL
SEQRES   1 B  504  GLU GLY ALA ALA LEU THR GLU LYS THR ASP ILE PHE GLU
SEQRES   2 B  504  SER GLY ARG ASN GLY LYS PRO ASN LYS ASP GLY ILE LYS
SEQRES   3 B  504  SER TYR ARG ILE PRO ALA LEU LEU LYS THR ASP LYS GLY
SEQRES   4 B  504  THR LEU ILE ALA GLY ALA ASP GLU ARG ARG LEU HIS SER
SEQRES   5 B  504  SER ASP TRP GLY ASP ILE GLY MET VAL ILE ARG ARG SER
SEQRES   6 B  504  GLU ASP ASN GLY LYS THR TRP GLY ASP ARG VAL THR ILE
SEQRES   7 B  504  THR ASN LEU ARG ASP ASN PRO LYS ALA SER ASP PRO SER
SEQRES   8 B  504  ILE GLY SER PRO VAL ASN ILE ASP MET VAL LEU VAL GLN
SEQRES   9 B  504  ASP PRO GLU THR LYS ARG ILE PHE SER ILE TYR ASP MET
SEQRES  10 B  504  PHE PRO GLU GLY LYS GLY ILE PHE GLY MET SER SER GLN
SEQRES  11 B  504  LYS GLU GLU ALA TYR LYS LYS ILE ASP GLY LYS THR TYR
SEQRES  12 B  504  GLN ILE LEU TYR ARG GLU GLY GLU LYS GLY ALA TYR THR
SEQRES  13 B  504  ILE ARG GLU ASN GLY THR VAL TYR THR PRO ASP GLY LYS
SEQRES  14 B  504  ALA THR ASP TYR ARG VAL VAL VAL ASP PRO VAL LYS PRO
SEQRES  15 B  504  ALA TYR SER ASP LYS GLY ASP LEU TYR LYS GLY ASN GLN
SEQRES  16 B  504  LEU LEU GLY ASN ILE TYR PHE THR THR ASN LYS THR SER
SEQRES  17 B  504  PRO PHE ARG ILE ALA LYS ASP SER TYR LEU TRP MET SER
SEQRES  18 B  504  TYR SER ASP ASP ASP GLY LYS THR TRP SER ALA PRO GLN
SEQRES  19 B  504  ASP ILE THR PRO MET VAL LYS ALA ASP TRP MET LYS PHE
SEQRES  20 B  504  LEU GLY VAL GLY PRO GLY THR GLY ILE VAL LEU ARG ASN
SEQRES  21 B  504  GLY PRO HIS LYS GLY ARG ILE LEU ILE PRO VAL TYR THR
SEQRES  22 B  504  THR ASN ASN VAL SER HIS LEU ASN GLY SER GLN SER SER
SEQRES  23 B  504  ARG ILE ILE TYR SER ASP ASP HIS GLY LYS THR TRP HIS
SEQRES  24 B  504  ALA GLY GLU ALA VAL ASN ASP ASN ARG GLN VAL ASP GLY
SEQRES  25 B  504  GLN LYS ILE HIS SER SER THR MET ASN ASN ARG ARG ALA
SEQRES  26 B  504  GLN ASN THR GLU SER THR VAL VAL GLN LEU ASN ASN GLY
SEQRES  27 B  504  ASP VAL LYS LEU PHE MET ARG GLY LEU THR GLY ASP LEU
SEQRES  28 B  504  GLN VAL ALA THR SER LYS ASP GLY GLY VAL THR TRP GLU
SEQRES  29 B  504  LYS ASP ILE LYS ARG TYR PRO GLN VAL LYS ASP VAL TYR
SEQRES  30 B  504  VAL GLN MET SER ALA ILE HIS THR MET HIS GLU GLY LYS
SEQRES  31 B  504  GLU TYR ILE ILE LEU SER ASN ALA GLY GLY PRO LYS ARG
SEQRES  32 B  504  GLU ASN GLY MET VAL HIS LEU ALA ARG VAL GLU GLU ASN
SEQRES  33 B  504  GLY GLU LEU THR TRP LEU LYS HIS ASN PRO ILE GLN LYS
SEQRES  34 B  504  GLY GLU PHE ALA TYR ASN SER LEU GLN GLU LEU GLY ASN
SEQRES  35 B  504  GLY GLU TYR GLY ILE LEU TYR GLU HIS THR GLU LYS GLY
SEQRES  36 B  504  GLN ASN ALA TYR THR LEU SER PHE ARG LYS PHE ASN TRP
SEQRES  37 B  504  ASP PHE LEU SER LYS ASP LEU ILE SER PRO THR GLU ALA
SEQRES  38 B  504  LYS VAL LYS ARG THR ARG GLU MET GLY LYS GLY VAL ILE
SEQRES  39 B  504  GLY LEU GLU PHE ASP SER GLU VAL LEU VAL
HET    DAN  A1792      20
HET    DAN  B1792      20
HET     CL  A1793       1
HETNAM      CL CHLORIDE ION
HETNAM     DAN 2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC ACID
FORMUL   3   CL    CL 1-
FORMUL   4  DAN    2(C11 H17 N O8)
FORMUL   5  HOH   *124(H2 O1)
HELIX    1   1 ILE A  554  LYS A  559  1                                   6
HELIX    2   2 TRP A  786  LYS A  791  1                                   6
HELIX    3   3 ASP B  407  GLY B  411  5                                   5
HELIX    4   4 ILE B  554  LYS B  559  1                                   6
HELIX    5   5 ASN B  578  LYS B  582  5                                   5
HELIX    6   6 SER B  596  SER B  601  1                                   6
HELIX    7   7 TRP B  786  LYS B  791  1                                   6
SHEET    1  AA 4 THR A 327  PHE A 330  0
SHEET    2  AA 4 THR A 778  ASN A 785 -1  O  LEU A 779   N  ILE A 329
SHEET    3  AA 4 GLU A 762  HIS A 769 -1  O  TYR A 763   N  PHE A 784
SHEET    4  AA 4 ASN A 753  GLY A 759 -1  O  SER A 754   N  LEU A 766
SHEET    1  AB 3 SER A 345  TYR A 346  0
SHEET    2  AB 3 LEU A 359  ARG A 366 -1  O  ARG A 366   N  SER A 345
SHEET    3  AB 3 ALA A 350  LYS A 353 -1  O  ALA A 350   N  GLY A 362
SHEET    1  AC 4 SER A 345  TYR A 346  0
SHEET    2  AC 4 LEU A 359  ARG A 366 -1  O  ARG A 366   N  SER A 345
SHEET    3  AC 4 ILE A 376  SER A 383 -1  O  GLY A 377   N  GLU A 365
SHEET    4  AC 4 VAL A 394  THR A 397 -1  O  VAL A 394   N  ILE A 380
SHEET    1  AD 5 GLN A 552  ASP A 553  0
SHEET    2  AD 5 TYR A 535  SER A 541 -1  O  MET A 538   N  GLN A 552
SHEET    3  AD 5 ILE A 429  PHE A 436 -1  O  ILE A 429   N  SER A 541
SHEET    4  AD 5 VAL A 414  GLN A 422 -1  O  VAL A 414   N  PHE A 436
SHEET    5  AD 5 GLY A 571  THR A 572  1  O  GLY A 571   N  LEU A 420
SHEET    1  AE 2 TYR A 453  ILE A 456  0
SHEET    2  AE 2 LYS A 459  GLN A 462 -1  O  LYS A 459   N  ILE A 456
SHEET    1  AF 2 TYR A 465  ARG A 466  0
SHEET    2  AF 2 PHE A 528  ARG A 529 -1  O  ARG A 529   N  TYR A 465
SHEET    1  AG 3 VAL A 493  VAL A 494  0
SHEET    2  AG 3 ASP A 507  TYR A 509 -1  O  TYR A 509   N  VAL A 493
SHEET    3  AG 3 LEU A 515  ASN A 517 -1  O  GLY A 516   N  LEU A 508
SHEET    1  AH 3 LEU A 566  VAL A 568  0
SHEET    2  AH 3 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3  AH 3 ILE A 574  VAL A 575 -1  O  ILE A 574   N  LEU A 586
SHEET    1  AI 4 LEU A 566  VAL A 568  0
SHEET    2  AI 4 ILE A 585  THR A 591 -1  O  TYR A 590   N  GLY A 567
SHEET    3  AI 4 SER A 603  SER A 609 -1  O  SER A 603   N  THR A 591
SHEET    4  AI 4 HIS A 617  ALA A 618 -1  O  HIS A 617   N  TYR A 608
SHEET    1  AJ 2 ARG A 626  VAL A 628  0
SHEET    2  AJ 2 GLN A 631  ILE A 633 -1  O  GLN A 631   N  VAL A 628
SHEET    1  AK 4 SER A 648  GLN A 652  0
SHEET    2  AK 4 VAL A 658  MET A 662 -1  O  LYS A 659   N  VAL A 651
SHEET    3  AK 4 ASP A 668  SER A 674 -1  O  GLN A 670   N  MET A 662
SHEET    4  AK 4 LYS A 686  LYS A 692 -1  O  LYS A 686   N  VAL A 671
SHEET    1  AL 4 SER A 699  HIS A 702  0
SHEET    2  AL 4 ILE A 711  ALA A 716 -1  O  ILE A 712   N  ILE A 701
SHEET    3  AL 4 GLU A 722  VAL A 731 -1  O  MET A 725   N  ASN A 715
SHEET    4  AL 4 LEU A 737  GLU A 749 -1  O  THR A 738   N  ARG A 730
SHEET    1  BA 7 THR B 327  ASP B 328  0
SHEET    2  BA 7 SER B 780  PHE B 784 -1  O  PHE B 781   N  THR B 327
SHEET    3  BA 7 GLU B 762  HIS B 769 -1  O  TYR B 763   N  PHE B 784
SHEET    4  BA 7 LEU B 737  GLY B 759 -1  N  ALA B 751   O  GLU B 768
SHEET    5  BA 7 GLU B 722  VAL B 731 -1  N  ASN B 723   O  GLY B 748
SHEET    6  BA 7 ILE B 711  ASN B 715 -1  O  ILE B 711   N  ALA B 729
SHEET    7  BA 7 SER B 699  HIS B 702 -1  O  SER B 699   N  SER B 714
SHEET    1  BB 4 SER B 345  LYS B 353  0
SHEET    2  BB 4 LEU B 359  ARG B 366 -1  O  ILE B 360   N  LEU B 352
SHEET    3  BB 4 ILE B 376  SER B 383 -1  O  GLY B 377   N  GLU B 365
SHEET    4  BB 4 VAL B 394  THR B 397 -1  O  VAL B 394   N  ILE B 380
SHEET    1  BC 5 GLN B 552  ASP B 553  0
SHEET    2  BC 5 TYR B 535  SER B 541 -1  O  MET B 538   N  GLN B 552
SHEET    3  BC 5 ILE B 429  PHE B 436 -1  O  ILE B 429   N  SER B 541
SHEET    4  BC 5 VAL B 414  GLN B 422 -1  O  VAL B 414   N  PHE B 436
SHEET    5  BC 5 GLY B 571  THR B 572  1  O  GLY B 571   N  LEU B 420
SHEET    1  BD 7 TYR B 453  LYS B 455  0
SHEET    2  BD 7 THR B 460  ARG B 466 -1  O  TYR B 461   N  LYS B 454
SHEET    3  BD 7 THR B 474  ILE B 475 -1  O  ILE B 475   N  GLN B 462
SHEET    4  BD 7 THR B 480  TYR B 482 -1  O  TYR B 482   N  THR B 474
SHEET    5  BD 7 ALA B 488  VAL B 494 -1  N  THR B 489   O  VAL B 481
SHEET    6  BD 7 ASP B 507  LYS B 510 -1  O  TYR B 509   N  VAL B 493
SHEET    7  BD 7 GLN B 513  ASN B 517 -1  O  GLN B 513   N  LYS B 510
SHEET    1  BE 3 TYR B 453  LYS B 455  0
SHEET    2  BE 3 THR B 460  ARG B 466 -1  O  TYR B 461   N  LYS B 454
SHEET    3  BE 3 PHE B 528  ILE B 530 -1  O  ARG B 529   N  TYR B 465
SHEET    1  BF 7 LEU B 566  VAL B 568  0
SHEET    2  BF 7 ILE B 585  THR B 591 -1  O  TYR B 590   N  GLY B 567
SHEET    3  BF 7 ILE B 574  VAL B 575 -1  O  ILE B 574   N  LEU B 586
SHEET    4  BF 7 ILE B 585  THR B 591 -1  O  LEU B 586   N  ILE B 574
SHEET    5  BF 7 HIS B 617  ALA B 618
SHEET    6  BF 7 SER B 603  SER B 609 -1  O  TYR B 608   N  HIS B 617
SHEET    7  BF 7 ILE B 585  THR B 591 -1  O  ILE B 585   N  SER B 609
SHEET    1  BG 2 ARG B 626  VAL B 628  0
SHEET    2  BG 2 GLN B 631  ILE B 633 -1  O  GLN B 631   N  VAL B 628
SHEET    1  BH 4 SER B 648  GLN B 652  0
SHEET    2  BH 4 VAL B 658  MET B 662 -1  O  LYS B 659   N  VAL B 651
SHEET    3  BH 4 ASP B 668  SER B 674 -1  O  GLN B 670   N  MET B 662
SHEET    4  BH 4 LYS B 686  LYS B 692 -1  O  LYS B 686   N  VAL B 671
CISPEP   1 LYS A  708    GLU A  709          0       -18.28
CISPEP   2 GLY A  718    PRO A  719          0        -6.62
CISPEP   3 ASN A  734    GLY A  735          0       -10.72
CISPEP   4 ALA A  776    TYR A  777          0        -8.46
CISPEP   5 GLY B  458    LYS B  459          0        -9.99
CISPEP   6 LYS B  708    GLU B  709          0         1.77
CISPEP   7 GLY B  718    PRO B  719          0        -2.66
CISPEP   8 ASN B  734    GLY B  735          0         0.23
CISPEP   9 ALA B  776    TYR B  777          0         0.42
CISPEP  10 ASN B  785    TRP B  786          0        -7.97
SITE     1 AC1 16 ARG A 347  ILE A 348  ARG A 366  ASP A 372
SITE     2 AC1 16 ILE A 416  ASP A 417  ASP A 434  ILE A 442
SITE     3 AC1 16 TYR A 590  LEU A 598  GLN A 602  ARG A 663
SITE     4 AC1 16 TYR A 695  ARG A 721  TYR A 752  HOH A2094
SITE     1 AC2 14 ARG B 347  ILE B 348  ARG B 366  ASP B 372
SITE     2 AC2 14 ILE B 416  ASP B 417  ASP B 434  ILE B 442
SITE     3 AC2 14 TYR B 590  GLN B 602  ARG B 663  TYR B 695
SITE     4 AC2 14 ARG B 721  TYR B 752
SITE     1 AC3  6 GLY A 516  ASN A 517  PHE A 520  LYS A 524
SITE     2 AC3  6 THR A 525  SER A 526
CRYST1   49.206   95.626  226.596  90.00  90.00  90.00 P 21 21 21    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      0.020323  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010457  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004413        0.00000
      
PROCHECK
Go to PROCHECK summary
 References