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PDBsum entry 3voc

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Hydrolase PDB id
3voc
Jmol
Contents
Protein chain
416 a.a.
Ligands
EDO ×3
GOL ×3
TRS ×2
PEG
Metals
_CA
_CL
Waters ×282
HEADER    HYDROLASE                               21-JAN-12   3VOC
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF BETA-AMYLASE FROM
TITLE    2 PAENIBACILLUS POLYMYXA
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BETA/ALPHA-AMYLASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: BETA-AMYLASE, UNP RESIDUES 36-454;
COMPND   5 EC: 3.2.1.2;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: PAENIBACILLUS POLYMYXA;
SOURCE   3 ORGANISM_TAXID: 1406;
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-21D
KEYWDS    TIM BARREL, AMYLASE, CARBOHYDRATE METABOLISM, GLYCOSIDE HYDROLASE,
KEYWDS   2 POLYSACCHARIDE DEGRADATION, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.NISHIMURA,T.FUJIOKA,T.NAKANIWA,T.TADA
REVDAT   1   20-FEB-13 3VOC    0
JRNL        AUTH   S.NISHIMURA,T.FUJIOKA,R.TAKAHASHI,T.NAKANIWA,H.FUKADA,
JRNL        AUTH 2 T.INUI,T.TADA,T.KAWAGUCHI,J.SUMITANI
JRNL        TITL   STRUCTURAL ANALYSIS BY X-RAY CRYSTALLOGRAPHY AND SMALL-ANGLE
JRNL        TITL 2 SCATTERING OF THE MULTI-DOMAIN BETA-AMYLASE FROM
JRNL        TITL 3 PAENIBACILLUS POLYMYXA
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.5.0109
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) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 27870
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) : 0.155
REMARK   3   R VALUE            (WORKING SET) : 0.153
REMARK   3   FREE R VALUE                     : 0.190
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 1487
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) : 1.95
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2049
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1650
REMARK   3   BIN FREE R VALUE SET COUNT          : 98
REMARK   3   BIN FREE R VALUE                    : 0.2330
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 3216
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 55
REMARK   3   SOLVENT ATOMS            : 282
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.73
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
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): 0.158
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.136
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.870
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3415 ; 0.011 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4630 ; 1.163 ; 1.950
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   433 ; 5.577 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;36.590 ;25.000
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   535 ;12.594 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;19.606 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   472 ; 0.083 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2623 ; 0.005 ; 0.021
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
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):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
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):  2098 ; 0.548 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3353 ; 1.053 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1317 ; 1.824 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1270 ; 2.897 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK   3  POSITIONS
REMARK   4
REMARK   4 3VOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB095296.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-11
REMARK 200  TEMPERATURE           (KELVIN) : 95
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                       : BL-17A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29847
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.940
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     (%) : 19.0
REMARK 200  DATA REDUNDANCY                : 7.100
REMARK 200  R MERGE                    (I) : 0.09600
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 29.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 5.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER_MR 2.1.4
REMARK 200 STARTING MODEL: 5BCA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 42.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M TRIS, 25%
REMARK 280  PEG 6000, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
REMARK 290       4555   X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.51400
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.95200
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.25950
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.95200
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.51400
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.25950
REMARK 290   SMTRY3   4  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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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     ASP A   417
REMARK 465     ASN A   418
REMARK 465     ASN A   419
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    THR A  80       47.90    -84.48
REMARK 500    LYS A 153      148.12   -170.04
REMARK 500    PRO A 178       40.87    -99.97
REMARK 500    ASP A 227       91.85   -173.52
REMARK 500    MET A 292       59.16   -141.71
REMARK 500    SER A 329      -66.79   -123.55
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                              CA A 501  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 135   OE1
REMARK 620 2 ASP A  52   OD1  99.8
REMARK 620 3 GLN A 132   OE1  85.0  89.2
REMARK 620 4 HOH A1046   O    93.8 165.0  85.6
REMARK 620 5 GLU A  48   OE2 166.0  88.4 106.6  79.7
REMARK 620 6 ASN A  53   OD1  81.4  84.9 164.0 103.6  88.1
REMARK 620 N                    1     2     3     4     5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 511
DBREF  3VOC A    1   419  UNP    P21543   AMYB_PAEPO      36    454
SEQRES   1 A  419  ALA VAL ALA ASP ASP PHE GLN ALA SER VAL MET GLY PRO
SEQRES   2 A  419  LEU ALA LYS ILE ASN ASP TRP GLY SER PHE LYS LYS GLN
SEQRES   3 A  419  LEU GLN THR LEU LYS ASN ASN GLY VAL TYR ALA ILE THR
SEQRES   4 A  419  THR ASP VAL TRP TRP GLY TYR VAL GLU SER ALA GLY ASP
SEQRES   5 A  419  ASN GLN PHE ASP TRP SER TYR TYR LYS THR TYR ALA ASN
SEQRES   6 A  419  ALA VAL LYS GLU ALA GLY LEU LYS TRP VAL PRO ILE ILE
SEQRES   7 A  419  SER THR HIS LYS CYS GLY GLY ASN VAL GLY ASP ASP CYS
SEQRES   8 A  419  ASN ILE PRO LEU PRO SER TRP LEU SER SER LYS GLY SER
SEQRES   9 A  419  ALA ASP GLU MET GLN PHE LYS ASP GLU SER GLY TYR ALA
SEQRES  10 A  419  ASN SER GLU ALA LEU SER PRO LEU TRP SER GLY THR GLY
SEQRES  11 A  419  LYS GLN TYR ASP GLU LEU TYR ALA SER PHE ALA GLU ASN
SEQRES  12 A  419  PHE ALA GLY TYR LYS SER ILE ILE PRO LYS ILE TYR LEU
SEQRES  13 A  419  SER GLY GLY PRO SER GLY GLU LEU ARG TYR PRO SER TYR
SEQRES  14 A  419  TYR PRO ALA ALA GLY TRP SER TYR PRO GLY ARG GLY LYS
SEQRES  15 A  419  PHE GLN ALA TYR THR GLU THR ALA LYS ASN ALA PHE ARG
SEQRES  16 A  419  THR ALA MET ASN ASP LYS TYR GLY SER LEU ASP LYS ILE
SEQRES  17 A  419  ASN ALA ALA TRP GLY THR LYS LEU THR SER LEU SER GLN
SEQRES  18 A  419  ILE ASN PRO PRO THR ASP GLY ASP GLY PHE TYR THR ASN
SEQRES  19 A  419  GLY GLY TYR ASN SER ALA TYR GLY LYS ASP PHE LEU SER
SEQRES  20 A  419  TRP TYR GLN SER VAL LEU GLU LYS HIS LEU GLY VAL ILE
SEQRES  21 A  419  GLY ALA ALA ALA HIS LYS ASN PHE ASP SER VAL PHE GLY
SEQRES  22 A  419  VAL ARG ILE GLY ALA LYS ILE SER GLY LEU HIS TRP GLN
SEQRES  23 A  419  MET ASN ASN PRO ALA MET PRO HIS GLY THR GLU GLN ALA
SEQRES  24 A  419  GLY GLY TYR TYR ASP TYR ASN ARG LEU ILE GLN LYS PHE
SEQRES  25 A  419  LYS ASP ALA ASP LEU ASP LEU THR PHE THR CYS LEU GLU
SEQRES  26 A  419  MET SER ASP SER GLY THR ALA PRO ASN TYR SER LEU PRO
SEQRES  27 A  419  SER THR LEU VAL ASP THR VAL SER SER ILE ALA ASN ALA
SEQRES  28 A  419  LYS GLY VAL ARG LEU ASN GLY GLU ASN ALA LEU PRO THR
SEQRES  29 A  419  GLY GLY SER GLY PHE GLN LYS ILE GLU GLU LYS ILE THR
SEQRES  30 A  419  LYS PHE GLY TYR HIS GLY PHE THR LEU LEU ARG ILE ASN
SEQRES  31 A  419  ASN LEU VAL ASN ASN ASP GLY SER PRO THR GLY GLU LEU
SEQRES  32 A  419  SER GLY PHE LYS GLN TYR ILE ILE SER LYS ALA LYS PRO
SEQRES  33 A  419  ASP ASN ASN
HET     CA  A 501       1
HET     CL  A 502       1
HET    EDO  A 503       4
HET    EDO  A 504       4
HET    EDO  A 505       4
HET    GOL  A 506       6
HET    GOL  A 507       6
HET    GOL  A 508       6
HET    TRS  A 509       8
HET    TRS  A 510       8
HET    PEG  A 511       7
HETNAM      CA CALCIUM ION
HETNAM      CL CHLORIDE ION
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     GOL GLYCEROL
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM     PEG DI(HYDROXYETHYL)ETHER
HETSYN     EDO ETHYLENE GLYCOL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN     TRS TRIS BUFFER
FORMUL   2   CA    CA 2+
FORMUL   3   CL    CL 1-
FORMUL   4  EDO    3(C2 H6 O2)
FORMUL   7  GOL    3(C3 H8 O3)
FORMUL  10  TRS    2(C4 H12 N O3 1+)
FORMUL  12  PEG    C4 H10 O3
FORMUL  13  HOH   *282(H2 O)
HELIX    1   1 ASP A   19  ASN A   33  1                                  15
HELIX    2   2 TRP A   44  GLU A   48  1                                   5
HELIX    3   3 TRP A   57  ALA A   70  1                                  14
HELIX    4   4 PRO A   96  LYS A  102  5                                   7
HELIX    5   5 SER A  104  GLN A  109  1                                   6
HELIX    6   6 SER A  127  ALA A  145  1                                  19
HELIX    7   7 GLY A  146  ILE A  151  5                                   6
HELIX    8   8 GLY A  159  GLU A  163  5                                   5
HELIX    9   9 TYR A  170  GLY A  174  5                                   5
HELIX   10  10 THR A  187  GLY A  203  1                                  17
HELIX   11  11 SER A  204  GLY A  213  1                                  10
HELIX   12  12 SER A  218  ILE A  222  5                                   5
HELIX   13  13 SER A  239  ASP A  269  1                                  31
HELIX   14  14 HIS A  294  GLY A  301  1                                   8
HELIX   15  15 ASP A  304  ASP A  316  1                                  13
HELIX   16  16 LEU A  337  GLY A  353  1                                  17
HELIX   17  17 GLY A  366  PHE A  379  1                                  14
HELIX   18  18 ARG A  388  LEU A  392  5                                   5
HELIX   19  19 GLU A  402  ILE A  410  1                                   9
HELIX   20  20 ILE A  411  ALA A  414  5                                   4
SHEET    1   A 9 GLN A   7  MET A  11  0
SHEET    2   A 9 ALA A  37  TRP A  43  1  O  THR A  39   N  VAL A  10
SHEET    3   A 9 LYS A  73  SER A  79  1  O  VAL A  75   N  ILE A  38
SHEET    4   A 9 LYS A 153  LEU A 156  1  O  TYR A 155   N  PRO A  76
SHEET    5   A 9 ARG A 275  LYS A 279  1  O  GLY A 277   N  LEU A 156
SHEET    6   A 9 ASP A 318  PHE A 321  1  O  ASP A 318   N  ILE A 276
SHEET    7   A 9 LEU A 356  GLU A 359  1  O  ASN A 357   N  LEU A 319
SHEET    8   A 9 GLY A 383  LEU A 386  1  O  THR A 385   N  GLY A 358
SHEET    9   A 9 GLN A   7  MET A  11  1  N  SER A   9   O  PHE A 384
SHEET    1   B 2 CYS A  83  GLY A  84  0
SHEET    2   B 2 ASN A  92  ILE A  93 -1  O  ILE A  93   N  CYS A  83
SHEET    1   C 2 PHE A 110  LYS A 111  0
SHEET    2   C 2 ALA A 117  ASN A 118 -1  O  ASN A 118   N  PHE A 110
SSBOND   1 CYS A   83    CYS A   91                          1555   1555  2.03
LINK         OE1 GLU A 135                CA    CA A 501     1555   1555  2.25
LINK         OD1 ASP A  52                CA    CA A 501     1555   1555  2.28
LINK         OE1 GLN A 132                CA    CA A 501     1555   1555  2.33
LINK        CA    CA A 501                 O   HOH A1046     1555   1555  2.34
LINK         OE2 GLU A  48                CA    CA A 501     1555   1555  2.35
LINK         OD1 ASN A  53                CA    CA A 501     1555   1555  2.38
CISPEP   1 TYR A  177    PRO A  178          0         2.02
CISPEP   2 ALA A  332    PRO A  333          0         1.13
CISPEP   3 LEU A  387    ARG A  388          0        -9.47
SITE     1 AC1  6 GLU A  48  ASP A  52  ASN A  53  GLN A 132
SITE     2 AC1  6 GLU A 135  HOH A1046
SITE     1 AC2  4 CYS A  91  ASN A  92  HOH A1034  HOH A1189
SITE     1 AC3  1 LYS A  16
SITE     1 AC4  3 GLN A 298  TYR A 302  TYR A 305
SITE     1 AC5  2 ASP A 314  HOH A1012
SITE     1 AC6  6 LEU A 205  ASP A 206  THR A 217  ASP A 343
SITE     2 AC6  6 SER A 347  HOH A1254
SITE     1 AC7  2 THR A 233  GLY A 235
SITE     1 AC8  6 VAL A  87  ASP A 328  SER A 339  ASP A 343
SITE     2 AC8  6 LYS A 375  HOH A1275
SITE     1 AC9  6 ASN A  18  ASP A  19  SER A  22  GLN A  26
SITE     2 AC9  6 ASN A 395  HOH A1258
SITE     1 BC1  3 GLY A  88  PRO A 293  HIS A 294
CRYST1   61.028   68.519   93.904  90.00  90.00  90.00 P 21 21 21    4
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      0.016386  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014594  0.000000        0.00000
SCALE3      0.000000  0.000000  0.010649        0.00000
      
PROCHECK
Go to PROCHECK summary
 References