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PDBsum entry 1m9i

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Lipid binding protein PDB id
1m9i
Jmol
Contents
Protein chain
664 a.a. *
Metals
_CA ×5
Waters ×148
* Residue conservation analysis
HEADER    LIPID BINDING PROTEIN                   29-JUL-02   1M9I
TITLE     CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T356D
TITLE    2 OF ANNEXIN VI
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANNEXIN VI;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: LIPOCORTIN VI, P68, P70, PROTEIN III,
COMPND   5 CHROMOBINDIN 20, 67 KDA CALELECTRIN, CALPHOBINDIN-II, CPB-
COMPND   6 II;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: ANX6;
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: DB334;
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: GAL10;
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: YEPDB60
KEYWDS    ANNEXIN, CALCIUM-BINDING, MEMBRANE-BINDING, PHOSPHORYLATION,
KEYWDS   2 MUTANT T356D, LIPID BINDING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.FREYE-MINKS,R.H.KRETSINGER,C.E.CREUTZ
REVDAT   3   24-FEB-09 1M9I    1       VERSN
REVDAT   2   15-APR-03 1M9I    1       JRNL   REMARK
REVDAT   1   07-AUG-02 1M9I    0
JRNL        AUTH   C.FREYE-MINKS,R.H.KRETSINGER,C.E.CREUTZ
JRNL        TITL   STRUCTURAL AND DYNAMIC CHANGES IN HUMAN ANNEXIN VI
JRNL        TITL 2 INDUCED BY A PHOSPHORYLATION-MIMICKING MUTATION,
JRNL        TITL 3 T356D
JRNL        REF    BIOCHEMISTRY                  V.  42   620 2003
JRNL        REFN                   ISSN 0006-2960
JRNL        PMID   12534274
JRNL        DOI    10.1021/BI026742H
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   J.BENZ,A.BERGNER,A.HOFMANN,P.DEMANGE,P.GOTTIG,
REMARK   1  AUTH 2 S.LIEMANN,R.HUBER,D.VOGES
REMARK   1  TITL   THE STRUCTURE OF RECOMBINANT HUMAN ANNEXIN VI IN
REMARK   1  TITL 2 CRYSTALS AND MEMBRANE-BOUND
REMARK   1  REF    J.MOL.BIOL.                   V. 260   638 1996
REMARK   1  REFN                   ISSN 0022-2836
REMARK   1  DOI    10.1006/JMBI.1996.0426
REMARK   1 REFERENCE 2
REMARK   1  AUTH   A.J.AVILA-SAKAR,C.E.CREUTZ,R.H.KRETSINGER
REMARK   1  TITL   CRYSTAL STRUCTURE OF BOVINE ANNEXIN VI IN A
REMARK   1  TITL 2 CALCIUM-BOUND STATE
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1387   103 1998
REMARK   1  REFN                   ISSN 0006-3002
REMARK   1  DOI    10.1016/S0167-4838(98)00111-3
REMARK   2
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.21
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.1
REMARK   3   NUMBER OF REFLECTIONS             : 26029
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) : 0.225
REMARK   3   FREE R VALUE                     : 0.279
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900
REMARK   3   FREE R VALUE TEST SET COUNT      : 1270
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           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.65
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4246
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2810
REMARK   3   BIN FREE R VALUE                    : 0.3840
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 223
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 5264
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 148
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 34.70
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.80
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) : 0.32
REMARK   3   ESD FROM SIGMAA              (A) : 0.26
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.007
REMARK   3   BOND ANGLES            (DEGREES) : 1.20
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 19.10
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.76
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) : 8.280 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 13.010; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.260; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 14.990; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
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  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ION.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : NULL
REMARK   3  TOPOLOGY FILE  3   : NULL
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1M9I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-02.
REMARK 100 THE RCSB ID CODE IS RCSB016764.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-01
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.4
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) : 0.971
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32036
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.08900
REMARK 200  R SYM                      (I) : 0.08900
REMARK 200   FOR THE DATA SET  : 22.8000
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) : 2.59
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.26600
REMARK 200  R SYM FOR SHELL            (I) : 0.26600
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: CNS
REMARK 200 STARTING MODEL: HUMAN ANNEXIN VI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 60.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M AMMONIUM SULFATE, 0.1M
REMARK 280  IMIDAZOLE, PH 7.4, VAPOR DIFFUSION, TEMPERATURE 298.0K
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      102.30000
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      153.45000
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       51.15000
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     ALA A     2
REMARK 465     LYS A     3
REMARK 465     PRO 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 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  CA    CA  A   705     O    HOH A   706              0.45
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
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    ILE A  14       98.75    -63.29
REMARK 500    HIS A  15      137.18    -30.11
REMARK 500    ASP A  16       77.75    -67.10
REMARK 500    PHE A  17      145.64     67.59
REMARK 500    PHE A  20     -166.30   -102.30
REMARK 500    GLU A  83      -70.14    -54.16
REMARK 500    ASP A 170     -105.42    173.36
REMARK 500    VAL A 171      103.82    -45.93
REMARK 500    GLU A 189      -51.86    -27.54
REMARK 500    LEU A 190        3.12    -68.81
REMARK 500    LEU A 234     -147.97   -113.56
REMARK 500    SER A 251       97.31    179.90
REMARK 500    LYS A 265      -78.54    -14.35
REMARK 500    ARG A 270       58.86   -104.27
REMARK 500    LEU A 284      -70.21   -125.56
REMARK 500    ASP A 285       27.07   -142.73
REMARK 500    GLU A 298       47.68     33.36
REMARK 500    LYS A 299      108.58   -176.14
REMARK 500    SER A 300      147.53    -25.50
REMARK 500    ASP A 324       10.34    178.64
REMARK 500    ASP A 325       84.40    -61.34
REMARK 500    ALA A 327     -146.50     55.20
REMARK 500    ALA A 328      -76.93    -74.47
REMARK 500    LYS A 377      109.16    -50.56
REMARK 500    LYS A 483      161.34    176.74
REMARK 500    GLU A 514     -118.93    -39.93
REMARK 500    ASN A 515       96.77    112.42
REMARK 500    LEU A 530      -71.21   -104.22
REMARK 500    ILE A 532       57.92   -140.60
REMARK 500    ALA A 533     -137.89    -82.99
REMARK 500    ASP A 534     -148.51     52.69
REMARK 500    PRO A 536       30.19    -77.59
REMARK 500    ASP A 539       92.41    -55.88
REMARK 500    LYS A 540       28.92    -74.99
REMARK 500    THR A 541     -109.28     62.28
REMARK 500    GLU A 544     -175.59     49.99
REMARK 500    MET A 569     -153.22    -73.40
REMARK 500    THR A 570       92.92    -19.62
REMARK 500    ASN A 571       24.25    -37.52
REMARK 500    LYS A 580      -72.74    -74.64
REMARK 500    ASN A 599       84.54   -156.21
REMARK 500    ALA A 615      -83.24    -72.95
REMARK 500    ILE A 632      -72.54   -122.56
REMARK 500    ASP A 646       19.12     47.13
REMARK 500    GLU A 672      -88.45     24.28
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 701  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 376   O
REMARK 620 2 GLY A 378   O    74.7
REMARK 620 3 LEU A 379   O   131.0  64.2
REMARK 620 4 GLY A 380   O   100.1  87.6  54.5
REMARK 620 5 GLU A 420   OE1  82.6  97.7 126.9 174.5
REMARK 620 6 GLU A 420   OE2 107.1 152.7 121.8 118.1  56.4
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 702  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 308   OD2
REMARK 620 2 MET A 264   O   122.0
REMARK 620 3 GLY A 266   O   125.3  90.2
REMARK 620 4 GLY A 268   O    84.3 140.4  97.4
REMARK 620 5 ASP A 308   OD1  43.3  82.0 149.7 107.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 703  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 770   O
REMARK 620 2 ASP A 656   OD1  87.8
REMARK 620 3 MET A 612   O   143.8  72.0
REMARK 620 4 GLY A 616   O   103.0 102.0 110.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 704  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 452   O
REMARK 620 2 MET A 448   O   127.6
REMARK 620 3 GLY A 450   N   125.5  78.3
REMARK 620 4 ASP A 492   OD1  84.9  76.3 148.7
REMARK 620 5 GLY A 450   O    88.8 132.7  54.6 144.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 705  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A  37   O
REMARK 620 2 MET A  33   O   107.6
REMARK 620 3 GLU A  77   OE1  75.5  88.9
REMARK 620 4 GLY A  35   O   101.8 121.6 147.7
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 701
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 702
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 703
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 704
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 705
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AVC   RELATED DB: PDB
REMARK 900 1AVC IS THE NATIVE BOVINE STRUCTURE (CALCIUM-BOUND)
DBREF  1M9I A    2   673  UNP    P08133   ANXA6_HUMAN      1    672
SEQADV 1M9I ASP A  356  UNP  P08133    THR   355 ENGINEERED
SEQADV 1M9I ASP A  619  UNP  P08133    GLU   618 SEE REMARK 999
SEQRES   1 A  672  ALA LYS PRO ALA GLN GLY ALA LYS TYR ARG GLY SER ILE
SEQRES   2 A  672  HIS ASP PHE PRO GLY PHE ASP PRO ASN GLN ASP ALA GLU
SEQRES   3 A  672  ALA LEU TYR THR ALA MET LYS GLY PHE GLY SER ASP LYS
SEQRES   4 A  672  GLU ALA ILE LEU ASP ILE ILE THR SER ARG SER ASN ARG
SEQRES   5 A  672  GLN ARG GLN GLU VAL CYS GLN SER TYR LYS SER LEU TYR
SEQRES   6 A  672  GLY LYS ASP LEU ILE ALA ASP LEU LYS TYR GLU LEU THR
SEQRES   7 A  672  GLY LYS PHE GLU ARG LEU ILE VAL GLY LEU MET ARG PRO
SEQRES   8 A  672  PRO ALA TYR CYS ASP ALA LYS GLU ILE LYS ASP ALA ILE
SEQRES   9 A  672  SER GLY ILE GLY THR ASP GLU LYS CYS LEU ILE GLU ILE
SEQRES  10 A  672  LEU ALA SER ARG THR ASN GLU GLN MET HIS GLN LEU VAL
SEQRES  11 A  672  ALA ALA TYR LYS ASP ALA TYR GLU ARG ASP LEU GLU ALA
SEQRES  12 A  672  ASP ILE ILE GLY ASP THR SER GLY HIS PHE GLN LYS MET
SEQRES  13 A  672  LEU VAL VAL LEU LEU GLN GLY THR ARG GLU GLU ASP ASP
SEQRES  14 A  672  VAL VAL SER GLU ASP LEU VAL GLN GLN ASP VAL GLN ASP
SEQRES  15 A  672  LEU TYR GLU ALA GLY GLU LEU LYS TRP GLY THR ASP GLU
SEQRES  16 A  672  ALA GLN PHE ILE TYR ILE LEU GLY ASN ARG SER LYS GLN
SEQRES  17 A  672  HIS LEU ARG LEU VAL PHE ASP GLU TYR LEU LYS THR THR
SEQRES  18 A  672  GLY LYS PRO ILE GLU ALA SER ILE ARG GLY GLU LEU SER
SEQRES  19 A  672  GLY ASP PHE GLU LYS LEU MET LEU ALA VAL VAL LYS CYS
SEQRES  20 A  672  ILE ARG SER THR PRO GLU TYR PHE ALA GLU ARG LEU PHE
SEQRES  21 A  672  LYS ALA MET LYS GLY LEU GLY THR ARG ASP ASN THR LEU
SEQRES  22 A  672  ILE ARG ILE MET VAL SER ARG SER GLU LEU ASP MET LEU
SEQRES  23 A  672  ASP ILE ARG GLU ILE PHE ARG THR LYS TYR GLU LYS SER
SEQRES  24 A  672  LEU TYR SER MET ILE LYS ASN ASP THR SER GLY GLU TYR
SEQRES  25 A  672  LYS LYS THR LEU LEU LYS LEU SER GLY GLY ASP ASP ASP
SEQRES  26 A  672  ALA ALA GLY GLN PHE PHE PRO GLU ALA ALA GLN VAL ALA
SEQRES  27 A  672  TYR GLN MET TRP GLU LEU SER ALA VAL ALA ARG VAL GLU
SEQRES  28 A  672  LEU LYS GLY ASP VAL ARG PRO ALA ASN ASP PHE ASN PRO
SEQRES  29 A  672  ASP ALA ASP ALA LYS ALA LEU ARG LYS ALA MET LYS GLY
SEQRES  30 A  672  LEU GLY THR ASP GLU ASP THR ILE ILE ASP ILE ILE THR
SEQRES  31 A  672  HIS ARG SER ASN VAL GLN ARG GLN GLN ILE ARG GLN THR
SEQRES  32 A  672  PHE LYS SER HIS PHE GLY ARG ASP LEU MET THR ASP LEU
SEQRES  33 A  672  LYS SER GLU ILE SER GLY ASP LEU ALA ARG LEU ILE LEU
SEQRES  34 A  672  GLY LEU MET MET PRO PRO ALA HIS TYR ASP ALA LYS GLN
SEQRES  35 A  672  LEU LYS LYS ALA MET GLU GLY ALA GLY THR ASP GLU LYS
SEQRES  36 A  672  ALA LEU ILE GLU ILE LEU ALA THR ARG THR ASN ALA GLU
SEQRES  37 A  672  ILE ARG ALA ILE ASN GLU ALA TYR LYS GLU ASP TYR HIS
SEQRES  38 A  672  LYS SER LEU GLU ASP ALA LEU SER SER ASP THR SER GLY
SEQRES  39 A  672  HIS PHE ARG ARG ILE LEU ILE SER LEU ALA THR GLY HIS
SEQRES  40 A  672  ARG GLU GLU GLY GLY GLU ASN LEU ASP GLN ALA ARG GLU
SEQRES  41 A  672  ASP ALA GLN VAL ALA ALA GLU ILE LEU GLU ILE ALA ASP
SEQRES  42 A  672  THR PRO SER GLY ASP LYS THR SER LEU GLU THR ARG PHE
SEQRES  43 A  672  MET THR ILE LEU CYS THR ARG SER TYR PRO HIS LEU ARG
SEQRES  44 A  672  ARG VAL PHE GLN GLU PHE ILE LYS MET THR ASN TYR ASP
SEQRES  45 A  672  VAL GLU HIS THR ILE LYS LYS GLU MET SER GLY ASP VAL
SEQRES  46 A  672  ARG ASP ALA PHE VAL ALA ILE VAL GLN SER VAL LYS ASN
SEQRES  47 A  672  LYS PRO LEU PHE PHE ALA ASP LYS LEU TYR LYS SER MET
SEQRES  48 A  672  LYS GLY ALA GLY THR ASP ASP LYS THR LEU THR ARG ILE
SEQRES  49 A  672  MET VAL SER ARG SER GLU ILE ASP LEU LEU ASN ILE ARG
SEQRES  50 A  672  ARG GLU PHE ILE GLU LYS TYR ASP LYS SER LEU HIS GLN
SEQRES  51 A  672  ALA ILE GLU GLY ASP THR SER GLY ASP PHE LEU LYS ALA
SEQRES  52 A  672  LEU LEU ALA LEU CYS GLY GLY GLU ASP
HET     CA  A 701       1
HET     CA  A 702       1
HET     CA  A 703       1
HET     CA  A 704       1
HET     CA  A 705       1
HETNAM      CA CALCIUM ION
FORMUL   2   CA    5(CA 2+)
FORMUL   7  HOH   *148(H2 O)
HELIX    1   1 ASP A   21  MET A   33  1                                  13
HELIX    2   2 ASP A   39  THR A   48  1                                  10
HELIX    3   3 SER A   51  GLY A   67  1                                  17
HELIX    4   4 ASP A   69  LEU A   78  1                                  10
HELIX    5   5 THR A   79  ARG A   91  1                                  13
HELIX    6   6 PRO A   92  SER A  106  1                                  15
HELIX    7   7 ASP A  111  ARG A  122  1                                  12
HELIX    8   8 THR A  123  TYR A  138  1                                  16
HELIX    9   9 ASP A  141  THR A  150  1                                  10
HELIX   10  10 SER A  151  GLY A  164  1                                  14
HELIX   11  11 SER A  173  GLY A  188  1                                  16
HELIX   12  12 ASP A  195  ARG A  206  1                                  12
HELIX   13  13 SER A  207  THR A  222  1                                  16
HELIX   14  14 PRO A  225  ARG A  231  1                                   7
HELIX   15  15 SER A  235  ALA A  263  1                                  29
HELIX   16  16 ARG A  270  ARG A  281  1                                  12
HELIX   17  17 ASP A  285  TYR A  297  1                                  13
HELIX   18  18 SER A  300  ASN A  307  1                                   8
HELIX   19  19 SER A  310  GLY A  322  1                                  13
HELIX   20  20 PHE A  332  ALA A  349  1                                  18
HELIX   21  21 ASN A  364  LYS A  377  1                                  14
HELIX   22  22 ASP A  382  HIS A  392  1                                  11
HELIX   23  23 SER A  394  GLY A  410  1                                  17
HELIX   24  24 ASP A  412  ILE A  421  1                                  10
HELIX   25  25 GLY A  423  MET A  434  1                                  12
HELIX   26  26 PRO A  435  GLU A  449  1                                  15
HELIX   27  27 ASP A  454  ARG A  465  1                                  12
HELIX   28  28 THR A  466  HIS A  482  1                                  17
HELIX   29  29 SER A  484  THR A  493  1                                  10
HELIX   30  30 SER A  494  ALA A  505  1                                  12
HELIX   31  31 ASN A  515  GLU A  531  1                                  17
HELIX   32  32 ASP A  534  GLY A  538  5                                   5
HELIX   33  33 THR A  545  ARG A  554  1                                  10
HELIX   34  34 SER A  555  MET A  569  1                                  15
HELIX   35  35 ASP A  573  MET A  582  1                                  10
HELIX   36  36 SER A  583  MET A  612  1                                  30
HELIX   37  37 ASP A  618  ARG A  629  1                                  12
HELIX   38  38 ASP A  633  ASP A  646  1                                  14
HELIX   39  39 SER A  648  THR A  657  1                                  10
HELIX   40  40 SER A  658  CYS A  669  1                                  12
LINK        CA    CA A 701                 O   MET A 376     1555   1555  2.58
LINK        CA    CA A 701                 O   GLY A 378     1555   1555  2.95
LINK        CA    CA A 701                 O   LEU A 379     1555   1555  3.33
LINK        CA    CA A 701                 O   GLY A 380     1555   1555  2.04
LINK        CA    CA A 701                 OE1 GLU A 420     1555   1555  2.61
LINK        CA    CA A 701                 OE2 GLU A 420     1555   1555  1.80
LINK        CA    CA A 702                 OD2 ASP A 308     1555   1555  3.20
LINK        CA    CA A 702                 O   MET A 264     1555   1555  2.82
LINK        CA    CA A 702                 O   GLY A 266     1555   1555  2.07
LINK        CA    CA A 702                 O   GLY A 268     1555   1555  1.61
LINK        CA    CA A 702                 OD1 ASP A 308     1555   1555  2.28
LINK        CA    CA A 703                 O   HOH A 770     1555   1555  2.90
LINK        CA    CA A 703                 OD1 ASP A 656     1555   1555  2.40
LINK        CA    CA A 703                 O   MET A 612     1555   1555  2.75
LINK        CA    CA A 703                 O   GLY A 616     1555   1555  2.61
LINK        CA    CA A 704                 O   GLY A 452     1555   1555  2.77
LINK        CA    CA A 704                 O   MET A 448     1555   1555  1.60
LINK        CA    CA A 704                 N   GLY A 450     1555   1555  3.27
LINK        CA    CA A 704                 OD1 ASP A 492     1555   1555  2.54
LINK        CA    CA A 704                 O   GLY A 450     1555   1555  1.90
LINK        CA    CA A 705                 O   GLY A  37     1555   1555  2.79
LINK        CA    CA A 705                 O   MET A  33     1555   1555  2.41
LINK        CA    CA A 705                 OE1 GLU A  77     1555   1555  2.72
LINK        CA    CA A 705                 O   GLY A  35     1555   1555  2.14
SITE     1 AC1  5 MET A 376  GLY A 378  LEU A 379  GLY A 380
SITE     2 AC1  5 GLU A 420
SITE     1 AC2  4 MET A 264  GLY A 266  GLY A 268  ASP A 308
SITE     1 AC3  6 MET A 612  GLY A 614  ALA A 615  GLY A 616
SITE     2 AC3  6 ASP A 656  HOH A 770
SITE     1 AC4  5 MET A 448  GLU A 449  GLY A 450  GLY A 452
SITE     2 AC4  5 ASP A 492
SITE     1 AC5  5 MET A  33  LYS A  34  GLY A  35  GLY A  37
SITE     2 AC5  5 GLU A  77
CRYST1   67.970   67.970  204.600  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      0.014712  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014712  0.000000        0.00000
SCALE3      0.000000  0.000000  0.004888        0.00000
      
PROCHECK
Go to PROCHECK summary
 References