spacer
spacer

PDBsum entry 1avc

Go to PDB code: 
Top Page protein metals links
Calcium/phospholipid-binding protein PDB id
1avc
Jmol
Contents
Protein chain
642 a.a.
Metals
_CA ×6
Waters ×117
HEADER    CALCIUM/PHOSPHOLIPID-BINDING PROTEIN    16-SEP-97   1AVC
TITLE     BOVINE ANNEXIN VI (CALCIUM-BOUND)
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANNEXIN VI;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: P68, PROTEIN III, 67-KDA-CALCIMEDIN, LIPOCORTIN
COMPND   5 VI, 67-KDA-CALELECTRIN, CHROMOBINDIN 20, CALPHOBINDIN II
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 ORGAN: LIVER;
SOURCE   6 CELLULAR_LOCATION: MEMBRANE-PERIPHERAL
KEYWDS    ANNEXIN, CALCIUM-BINDING, MEMBRANE-BINDING,
KEYWDS   2 CALCIUM/PHOSPHOLIPID-BINDING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.J.AVILA-SAKAR,C.E.CREUTZ,R.H.KRETSINGER
REVDAT   2   24-FEB-09 1AVC    1       VERSN
REVDAT   1   28-JAN-98 1AVC    0
JRNL        AUTH   A.J.AVILA-SAKAR,C.E.CREUTZ,R.H.KRETSINGER
JRNL        TITL   CRYSTAL STRUCTURE OF BOVINE ANNEXIN VI IN A
JRNL        TITL 2 CALCIUM-BOUND STATE.
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1387   103 1998
JRNL        REFN                   ISSN 0006-3002
JRNL        PMID   9748523
JRNL        DOI    10.1016/S0167-4838(98)00111-3
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   H.KAWASAKI,A.AVILA-SAKAR,C.E.CREUTZ,R.H.KRETSINGER
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF ANNEXIN VI INDICATES
REMARK   1  TITL 2 RELATIVE ROTATION OF THE TWO LOBES UPON MEMBRANE
REMARK   1  TITL 3 BINDING
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1313   277 1996
REMARK   1  REFN                   ISSN 0006-3002
REMARK   2
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.7
REMARK   3   NUMBER OF REFLECTIONS             : 18978
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 SET) : 0.205
REMARK   3   FREE R VALUE                     : 0.268
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.000
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 10
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.00
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.50
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1783
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840
REMARK   3   BIN FREE R VALUE                    : 0.3270
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.90
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.028
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5231
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 117
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 45.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.30
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.40
REMARK   3   ESD FROM SIGMAA              (A) : 0.23
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 10.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.54
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.27
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.003
REMARK   3   BOND ANGLES            (DEGREES) : 0.70
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.40
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.990 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.910 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.090 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.480 ; 2.500
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : PARAMETER.ELEMENTS
REMARK   3  PARAMETER FILE  3  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOP19.SOL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT B=62.4 A**2, K=0.48
REMARK   4
REMARK   4 1AVC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-96
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               : NSLS
REMARK 200  BEAMLINE                       : X4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0093
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30424
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : 0.06600
REMARK 200  R SYM                      (I) : 0.06600
REMARK 200   FOR THE DATA SET  : 20.7000
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) : 2.60
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60
REMARK 200  R MERGE FOR SHELL          (I) : 0.30700
REMARK 200  R SYM FOR SHELL            (I) : 0.30700
REMARK 200   FOR SHELL         : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.851
REMARK 200 STARTING MODEL: BOVINE ANNEXIN VI: PDB ENTRY 1ANN
REMARK 200
REMARK 200 REMARK: PROBE ~1/2 THE MASS OF ANNEXIN VI
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 39.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION (HANGING DROP),
REMARK 280  SODIUM ACETATE 1.2 M AS PRECIPITANT, POTASSIUM CACODYLATE 0.1
REMARK 280  M, PH 6.5, CALCIUM CHLORIDE 6.2 MM ROOM TEMPERATURE, VAPOR
REMARK 280  DIFFUSION - HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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   -Y,X,Z+3/4
REMARK 290       4555   Y,-X,Z+1/4
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      100.03900
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      150.05850
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       50.01950
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 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     MET A     1
REMARK 465     ALA A     2
REMARK 465     LYS A     3
REMARK 465     ILE A     4
REMARK 465     ALA A     5
REMARK 465     GLN A     6
REMARK 465     GLY A     7
REMARK 465     ALA A     8
REMARK 465     LYS A     9
REMARK 465     ASP A   324
REMARK 465     ASP A   325
REMARK 465     ASP A   326
REMARK 465     ALA A   327
REMARK 465     ALA A   328
REMARK 465     GLY A   329
REMARK 465     GLU A   531
REMARK 465     ILE A   532
REMARK 465     ALA A   533
REMARK 465     ASP A   534
REMARK 465     THR A   535
REMARK 465     THR A   536
REMARK 465     SER A   537
REMARK 465     GLY A   538
REMARK 465     ASP A   539
REMARK 465     LYS A   540
REMARK 465     SER A   541
REMARK 465     SER A   542
REMARK 465     LEU A   543
REMARK 465     GLU A   544
REMARK 465     GLU A   672
REMARK 465     ASP A   673
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    ASP A  19       84.19     54.35
REMARK 500    LEU A  46      -72.56    -73.61
REMARK 500    TYR A  66      -14.45   -140.82
REMARK 500    ILE A 108      -83.02    -76.51
REMARK 500    ASP A 169      139.14    -26.76
REMARK 500    ASP A 170     -163.30   -168.45
REMARK 500    SER A 251      111.90   -164.40
REMARK 500    LEU A 267      141.58    -39.13
REMARK 500    ARG A 270       58.93    -93.16
REMARK 500    LEU A 284      -71.91   -124.22
REMARK 500    ASP A 285       28.52   -141.19
REMARK 500    PRO A 333      -42.36    -24.24
REMARK 500    ASP A 382       93.56    -67.39
REMARK 500    ILE A 389      -64.00    -93.29
REMARK 500    GLU A 479      -79.38    -64.60
REMARK 500    HIS A 482       84.75    -50.93
REMARK 500    LYS A 483      144.60    176.88
REMARK 500    ASN A 599       88.63   -156.08
REMARK 500    GLU A 618       79.96   -102.55
REMARK 500    ILE A 632      -64.83   -106.82
REMARK 500    ASP A 633       34.24   -149.97
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 678  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 616   O
REMARK 620 2 ASP A 656   OD1 149.1
REMARK 620 3 THR A 617   OG1  67.5  86.0
REMARK 620 4 ASP A 656   OD2 106.4  42.7  51.6
REMARK 620 5 MET A 612   O   106.7  64.7 106.6  63.7
REMARK 620 6 GLY A 614   O    88.0 118.5 155.2 146.0  82.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 674  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 378   O
REMARK 620 2 LEU A 379   O    78.8
REMARK 620 3 GLY A 380   O   101.1  86.2
REMARK 620 4 GLU A 420   OE1 140.2 127.9 108.8
REMARK 620 5 GLU A 420   OE2 102.8 103.2 155.6  47.8
REMARK 620 6 MET A 376   O    86.4 164.5 101.5  62.6  75.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 675  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A  78   O
REMARK 620 2 THR A  79   OG1  74.8
REMARK 620 3 GLU A  83   OE1  63.8  85.4
REMARK 620 4 LYS A  75   O    66.1 139.1  67.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 676  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 266   O
REMARK 620 2 GLY A 268   O    69.8
REMARK 620 3 MET A 264   O    84.6 112.7
REMARK 620 4 ASP A 308   OD1 145.9 139.3  94.3
REMARK 620 5 ASP A 308   OD2 158.2 107.1  76.7  48.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 677  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 233   OE1
REMARK 620 2 LYS A 191   O    67.9
REMARK 620 3 GLY A 188   O   130.2  62.4
REMARK 620 4 GLY A 193   O    78.0  68.8  87.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 679  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 452   O
REMARK 620 2 MET A 448   O   140.2
REMARK 620 3 ASP A 492   OD1 103.5  73.0
REMARK 620 4 ASP A 492   OD2  77.0  73.4  45.1
REMARK 620 5 GLY A 450   O   102.3 115.7 112.8 154.9
REMARK 620 N                    1     2     3     4
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 674
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 675
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 676
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 677
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 678
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 679
DBREF  1AVC A   56   673  UNP    P79134   ANXA6_BOVIN      1    618
SEQADV 1AVC ASP A  141  UNP  P79134    GLU    86 CONFLICT
SEQADV 1AVC VAL A  181  UNP  P79134    LEU   126 CONFLICT
SEQRES   1 A  673  MET ALA LYS ILE ALA GLN GLY ALA LYS TYR ARG GLY SER
SEQRES   2 A  673  ILE ARG ASP PHE PRO ASP PHE ASN PRO SER GLN ASP ALA
SEQRES   3 A  673  GLU THR LEU TYR ASN ALA MET LYS GLY PHE GLY SER ASP
SEQRES   4 A  673  LYS GLU ALA ILE ILE ASN LEU ILE THR SER ARG SER ASN
SEQRES   5 A  673  LYS GLN ARG GLN GLU ILE CYS GLN ASN TYR LYS SER LEU
SEQRES   6 A  673  TYR GLY LYS ASP LEU ILE ALA ASP LEU LYS TYR GLU LEU
SEQRES   7 A  673  THR GLY LYS PHE GLU ARG LEU ILE VAL GLY LEU MET ARG
SEQRES   8 A  673  PRO PRO ALA TYR ALA ASP ALA LYS GLU ILE LYS ASP ALA
SEQRES   9 A  673  ILE SER GLY ILE GLY THR ASP GLU LYS CYS LEU ILE GLU
SEQRES  10 A  673  ILE LEU ALA SER ARG THR ASN GLU GLN ILE HIS GLN LEU
SEQRES  11 A  673  VAL ALA ALA TYR LYS ASP ALA TYR GLU ARG ASP LEU GLU
SEQRES  12 A  673  ALA ASP ILE THR GLY ASP THR SER GLY HIS PHE ARG LYS
SEQRES  13 A  673  MET LEU VAL VAL LEU LEU GLN GLY THR ARG GLU GLU ASP
SEQRES  14 A  673  ASP VAL VAL SER GLU ASP LEU VAL GLN GLN ASP VAL GLN
SEQRES  15 A  673  ASP LEU TYR GLU ALA GLY GLU LEU LYS TRP GLY THR ASP
SEQRES  16 A  673  GLU ALA GLN PHE ILE TYR ILE LEU GLY ASN ARG SER LYS
SEQRES  17 A  673  GLN HIS LEU ARG LEU VAL PHE ASP GLU TYR LEU LYS THR
SEQRES  18 A  673  THR GLY LYS PRO ILE GLU ALA SER ILE ARG GLY GLU LEU
SEQRES  19 A  673  SER GLY ASP PHE GLU LYS LEU MET LEU ALA VAL VAL LYS
SEQRES  20 A  673  CYS ILE ARG SER THR ALA GLU TYR PHE ALA GLU ARG LEU
SEQRES  21 A  673  PHE LYS ALA MET LYS GLY LEU GLY THR ARG ASP ASN THR
SEQRES  22 A  673  LEU ILE ARG ILE MET VAL SER ARG SER GLU LEU ASP MET
SEQRES  23 A  673  LEU ASP ILE ARG GLU ILE PHE ARG THR LYS TYR GLU LYS
SEQRES  24 A  673  SER LEU TYR SER MET ILE LYS ASN ASP THR SER GLY GLU
SEQRES  25 A  673  TYR LYS LYS THR LEU LEU LYS LEU CYS GLY GLY ASP ASP
SEQRES  26 A  673  ASP ALA ALA GLY GLN PHE PHE PRO GLU ALA ALA GLN VAL
SEQRES  27 A  673  ALA TYR GLN MET TRP GLU LEU SER ALA VAL ALA ARG VAL
SEQRES  28 A  673  GLU LEU LYS GLY THR VAL ARG PRO ALA GLY ASP PHE ASN
SEQRES  29 A  673  PRO ASP ALA ASP ALA LYS ALA LEU ARG LYS ALA MET LYS
SEQRES  30 A  673  GLY LEU GLY THR ASP GLU ASP THR ILE ILE ASP ILE ILE
SEQRES  31 A  673  THR HIS ARG SER ASN ALA GLN ARG GLN GLN ILE ARG GLN
SEQRES  32 A  673  THR PHE LYS SER HIS PHE GLY ARG ASP LEU MET ALA ASP
SEQRES  33 A  673  LEU LYS SER GLU LEU SER GLY ASP LEU ALA ARG LEU ILE
SEQRES  34 A  673  LEU GLY LEU MET MET PRO PRO ALA HIS TYR ASP ALA LYS
SEQRES  35 A  673  GLN LEU LYS LYS ALA MET GLU GLY ALA GLY THR ASP GLU
SEQRES  36 A  673  LYS ALA LEU ILE GLU ILE LEU ALA THR ARG THR ASN ALA
SEQRES  37 A  673  GLU ILE GLN ALA ILE ASN LYS ALA TYR LYS GLU ASP TYR
SEQRES  38 A  673  HIS LYS THR LEU GLU ASP ALA LEU SER SER ASP THR SER
SEQRES  39 A  673  GLY HIS PHE LYS ARG ILE LEU ILE SER LEU ALA THR GLY
SEQRES  40 A  673  ASN ARG GLU GLU GLY GLY GLU ASP ARG GLU ARG ALA ARG
SEQRES  41 A  673  GLU ASP ALA GLN VAL ALA ALA GLU ILE LEU GLU ILE ALA
SEQRES  42 A  673  ASP THR THR SER GLY ASP LYS SER SER LEU GLU THR ARG
SEQRES  43 A  673  PHE MET MET ILE LEU CYS THR ARG SER TYR PRO ASP LEU
SEQRES  44 A  673  ARG ARG VAL PHE GLN GLU PHE VAL LYS MET THR ASN TYR
SEQRES  45 A  673  ASP VAL GLU HIS THR ILE LYS LYS GLU MET SER GLY ASP
SEQRES  46 A  673  VAL ARG ASP VAL PHE VAL ALA ILE VAL GLN SER VAL LYS
SEQRES  47 A  673  ASN LYS PRO LEU PHE PHE ALA ASP LYS LEU TYR LYS SER
SEQRES  48 A  673  MET LYS GLY ALA GLY THR GLU GLU LYS THR LEU THR ARG
SEQRES  49 A  673  ILE MET VAL SER ARG SER GLU ILE ASP LEU LEU ASN ILE
SEQRES  50 A  673  ARG ARG GLU PHE ILE GLU LYS TYR ASP LYS SER LEU HIS
SEQRES  51 A  673  GLN ALA ILE GLU GLY ASP THR SER GLY HIS PHE LEU LYS
SEQRES  52 A  673  ALA LEU LEU ALA ILE CYS GLY GLY GLU ASP
HET     CA  A 674       1
HET     CA  A 675       1
HET     CA  A 676       1
HET     CA  A 677       1
HET     CA  A 678       1
HET     CA  A 679       1
HETNAM      CA CALCIUM ION
FORMUL   2   CA    6(CA 2+)
FORMUL   8  HOH   *117(H2 O)
HELIX    1   1 PRO A   22  ALA A   32  1                                  11
HELIX    2   2 LYS A   40  SER A   49  1                                  10
HELIX    3   3 ASN A   52  LEU A   65  1                                  14
HELIX    4   4 LEU A   70  GLU A   77  1                                   8
HELIX    5   5 LYS A   81  MET A   90  1                                  10
HELIX    6   6 PRO A   93  ILE A  105  1                                  13
HELIX    7   7 GLU A  112  SER A  121  1                                  10
HELIX    8   8 ASN A  124  TYR A  138  1                                  15
HELIX    9   9 LEU A  142  THR A  147  1                                   6
HELIX   10  10 GLY A  152  GLN A  163  5                                  12
HELIX   11  11 GLU A  174  ALA A  187  1                                  14
HELIX   12  12 GLU A  196  ASN A  205  1                                  10
HELIX   13  13 LYS A  208  THR A  222  1                                  15
HELIX   14  14 ILE A  226  ILE A  230  1                                   5
HELIX   15  15 GLY A  236  ARG A  250  1                                  15
HELIX   16  16 THR A  252  MET A  264  1                                  13
HELIX   17  17 ASP A  271  SER A  280  1                                  10
HELIX   18  18 MET A  286  LYS A  296  1                                  11
HELIX   19  19 LEU A  301  ASP A  308  1                                   8
HELIX   20  20 GLY A  311  CYS A  321  1                                  11
HELIX   21  21 PRO A  333  VAL A  348  1                                  16
HELIX   22  22 PRO A  365  MET A  376  1                                  12
HELIX   23  23 GLU A  383  HIS A  392  1                                  10
HELIX   24  24 ASN A  395  PHE A  409  1                                  15
HELIX   25  25 LEU A  413  GLU A  420  1                                   8
HELIX   26  26 GLY A  423  MET A  433  1                                  11
HELIX   27  27 PRO A  436  ALA A  447  1                                  12
HELIX   28  28 GLU A  455  LEU A  462  1                                   8
HELIX   29  29 ASN A  467  ASP A  480  1                                  14
HELIX   30  30 LEU A  485  ASP A  492  1                                   8
HELIX   31  31 GLY A  495  THR A  506  1                                  12
HELIX   32  32 ARG A  516  ILE A  529  1                                  14
HELIX   33  33 ARG A  546  THR A  553  1                                   8
HELIX   34  34 TYR A  556  THR A  570  1                                  15
HELIX   35  35 VAL A  574  GLU A  581  1                                   8
HELIX   36  36 GLY A  584  ASN A  599  1                                  16
HELIX   37  37 LYS A  600  MET A  612  1                                  13
HELIX   38  38 GLU A  619  SER A  628  1                                  10
HELIX   39  39 LEU A  634  TYR A  645  1                                  12
HELIX   40  40 LEU A  649  ASP A  656  1                                   8
HELIX   41  41 GLY A  659  CYS A  669  1                                  11
LINK        CA    CA A 678                 O   GLY A 616     1555   1555  2.29
LINK        CA    CA A 674                 O   GLY A 378     1555   1555  2.73
LINK        CA    CA A 674                 O   LEU A 379     1555   1555  2.52
LINK        CA    CA A 674                 O   GLY A 380     1555   1555  2.46
LINK        CA    CA A 674                 OE1 GLU A 420     1555   1555  2.49
LINK        CA    CA A 674                 OE2 GLU A 420     1555   1555  2.85
LINK        CA    CA A 674                 O   MET A 376     1555   1555  3.05
LINK        CA    CA A 675                 O   LEU A  78     1555   1555  2.69
LINK        CA    CA A 675                 OG1 THR A  79     1555   1555  2.92
LINK        CA    CA A 675                 OE1 GLU A  83     1555   1555  3.21
LINK        CA    CA A 675                 O   LYS A  75     1555   1555  2.79
LINK        CA    CA A 676                 O   GLY A 266     1555   1555  2.47
LINK        CA    CA A 676                 O   GLY A 268     1555   1555  2.70
LINK        CA    CA A 676                 O   MET A 264     1555   1555  2.66
LINK        CA    CA A 676                 OD1 ASP A 308     1555   1555  2.73
LINK        CA    CA A 676                 OD2 ASP A 308     1555   1555  2.60
LINK        CA    CA A 677                 OE1 GLU A 233     1555   1555  2.63
LINK        CA    CA A 677                 O   LYS A 191     1555   1555  3.32
LINK        CA    CA A 677                 O   GLY A 188     1555   1555  2.68
LINK        CA    CA A 677                 O   GLY A 193     1555   1555  2.68
LINK        CA    CA A 678                 OD1 ASP A 656     1555   1555  3.23
LINK        CA    CA A 678                 OG1 THR A 617     1555   1555  3.02
LINK        CA    CA A 678                 OD2 ASP A 656     1555   1555  2.53
LINK        CA    CA A 678                 O   MET A 612     1555   1555  3.25
LINK        CA    CA A 678                 O   GLY A 614     1555   1555  2.76
LINK        CA    CA A 679                 O   GLY A 452     1555   1555  2.53
LINK        CA    CA A 679                 O   MET A 448     1555   1555  2.58
LINK        CA    CA A 679                 OD1 ASP A 492     1555   1555  2.65
LINK        CA    CA A 679                 OD2 ASP A 492     1555   1555  3.01
LINK        CA    CA A 679                 O   GLY A 450     1555   1555  2.54
SITE     1 AC1  6 MET A 376  GLY A 378  LEU A 379  GLY A 380
SITE     2 AC1  6 THR A 381  GLU A 420
SITE     1 AC2  4 LYS A  75  LEU A  78  THR A  79  GLU A  83
SITE     1 AC3  6 MET A 264  GLY A 266  LEU A 267  GLY A 268
SITE     2 AC3  6 THR A 269  ASP A 308
SITE     1 AC4  7 GLY A 188  GLU A 189  LYS A 191  GLY A 193
SITE     2 AC4  7 THR A 194  SER A 229  GLU A 233
SITE     1 AC5  6 MET A 612  GLY A 614  ALA A 615  GLY A 616
SITE     2 AC5  6 THR A 617  ASP A 656
SITE     1 AC6  5 MET A 448  GLU A 449  GLY A 450  GLY A 452
SITE     2 AC6  5 ASP A 492
CRYST1   67.404   67.404  200.078  90.00  90.00  90.00 P 43          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      0.014836  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014836  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004998        0.00000
      
PROCHECK
Go to PROCHECK summary
 References