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PDBsum entry 1ain

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Calcium/phospholipid binding PDB id
1ain
Jmol
Contents
Protein chain
314 a.a.*
Metals
_CA ×6
* C-alpha coords only
HEADER    CALCIUM/PHOSPHOLIPID BINDING            03-JUN-92   1AIN
TITLE     CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS
TITLE    2 RESOLUTION
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: ANNEXIN I;
COMPND   3 CHAIN: A;
COMPND   4 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606
KEYWDS    CALCIUM/PHOSPHOLIPID BINDING
EXPDTA    X-RAY DIFFRACTION
MDLTYP    CA ATOMS ONLY, CHAIN A
AUTHOR    S.-H.KIM
REVDAT   3   24-FEB-09 1AIN    1       VERSN
REVDAT   2   01-APR-03 1AIN    1       JRNL
REVDAT   1   15-JUL-93 1AIN    0
JRNL        AUTH   X.WENG,H.LUECKE,I.S.SONG,D.S.KANG,S.H.KIM,R.HUBER
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 A
JRNL        TITL 2 RESOLUTION.
JRNL        REF    PROTEIN SCI.                  V.   2   448 1993
JRNL        REFN                   ISSN 0961-8368
JRNL        PMID   8453382
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : TNT
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : NULL
REMARK   3
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.163
REMARK   3   FREE R VALUE                     : NULL
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 314
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT
REMARK   3   BOND LENGTHS                 (A) : NULL  ; NULL  ; NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL
REMARK   3
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  RESTRAINT LIBRARIES.
REMARK   3   STEREOCHEMISTRY : NULL
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1AIN 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        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : NULL
REMARK 200  RADIATION SOURCE               : NULL
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       69.68000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       21.05500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.75000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       21.05500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       69.68000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.75000
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 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 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CA4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CA5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: CA6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF  1AIN A    6   319  UNP    P04083   ANXA1_HUMAN     32    345
SEQRES   1 A  314  GLY SER ALA VAL SER PRO TYR PRO THR PHE ASN PRO SER
SEQRES   2 A  314  SER ASP VAL ALA ALA LEU HIS LYS ALA ILE MET VAL LYS
SEQRES   3 A  314  GLY VAL ASP GLU ALA THR ILE ILE ASP ILE LEU THR LYS
SEQRES   4 A  314  ARG ASN ASN ALA GLN ARG GLN GLN ILE LYS ALA ALA TYR
SEQRES   5 A  314  LEU GLN GLU THR GLY LYS PRO LEU ASP GLU THR LEU LYS
SEQRES   6 A  314  LYS ALA LEU THR GLY HIS LEU GLU GLU VAL VAL LEU ALA
SEQRES   7 A  314  LEU LEU LYS THR PRO ALA GLN PHE ASP ALA ASP GLU LEU
SEQRES   8 A  314  ARG ALA ALA MET LYS GLY LEU GLY THR ASP GLU ASP THR
SEQRES   9 A  314  LEU ILE GLU ILE LEU ALA SER ARG THR ASN LYS GLU ILE
SEQRES  10 A  314  ARG ASP ILE ASN ARG VAL TYR ARG GLU GLU LEU LYS ARG
SEQRES  11 A  314  ASP LEU ALA LYS ASP ILE THR SER ASP THR SER GLY ASP
SEQRES  12 A  314  PHE ARG ASN ALA LEU LEU SER LEU ALA LYS GLY ASP ARG
SEQRES  13 A  314  SER GLU ASP PHE GLY VAL ASN GLU ASP LEU ALA ASP SER
SEQRES  14 A  314  ASP ALA ARG ALA LEU TYR GLU ALA GLY GLU ARG ARG LYS
SEQRES  15 A  314  GLY THR ASP VAL ASN VAL PHE ASN THR ILE LEU THR THR
SEQRES  16 A  314  ARG SER TYR PRO GLN LEU ARG ARG VAL PHE GLN LYS TYR
SEQRES  17 A  314  THR LYS TYR SER LYS HIS ASP MET ASN LYS VAL LEU ASP
SEQRES  18 A  314  LEU GLU LEU LYS GLY ASP ILE GLU LYS CYS LEU THR ALA
SEQRES  19 A  314  ILE VAL LYS CYS ALA THR SER LYS PRO ALA PHE PHE ALA
SEQRES  20 A  314  GLU LYS LEU HIS GLN ALA MET LYS GLY VAL GLY THR ARG
SEQRES  21 A  314  HIS LYS ALA LEU ILE ARG ILE MET VAL SER ARG SER GLU
SEQRES  22 A  314  ILE ASP MET ASN ASP ILE LYS ALA PHE TYR GLN LYS MET
SEQRES  23 A  314  TYR GLY ILE SER LEU CYS GLN ALA ILE LEU ASP GLU THR
SEQRES  24 A  314  LYS GLY ASP TYR GLU LYS ILE LEU VAL ALA LEU CYS GLY
SEQRES  25 A  314  GLY ASN
HET     CA  A 351       1
HET     CA  A 352       1
HET     CA  A 353       1
HET     CA  A 354       1
HET     CA  A 355       1
HET     CA  A 356       1
HETNAM      CA CALCIUM ION
FORMUL   2   CA    6(CA 2+)
HELIX    1  1A PRO A   17  VAL A   30  1                                  14
HELIX    2  1B ASP A   34  ARG A   45  1                                  12
HELIX    3  1C ASN A   46  GLY A   62  1                                  17
HELIX    4  1D PRO A   64  ALA A   72  1                                   9
HELIX    5  1E GLY A   75  LYS A   86  1                                  12
HELIX    6  2A THR A   87  MET A  100  1                                  14
HELIX    7  2B ASP A  106  ARG A  117  1                                  12
HELIX    8  2C THR A  118  LYS A  134  1                                  17
HELIX    9  2D ASP A  136  THR A  145  1                                  10
HELIX   10  2E GLY A  147  LYS A  158  1                                  12
HELIX   11  3A GLU A  169  ALA A  182  1                                  14
HELIX   12  3B ASP A  190  ARG A  201  1                                  12
HELIX   13  3C SER A  202  TYR A  216  1                                  15
HELIX   14  3D ASP A  220  LEU A  229  1                                  10
HELIX   15  3E GLY A  231  SER A  246  1                                  16
HELIX   16  4A LYS A  247  LYS A  260  1                                  14
HELIX   17  4B HIS A  266  SER A  277  1                                  12
HELIX   18  4C ASP A  280  TYR A  292  1                                  13
HELIX   19  4D SER A  295  THR A  304  1                                  10
HELIX   20  4E GLY A  306  GLY A  318  1                                  13
SITE     1 CA1  3 GLY A  32  VAL A  33  GLU A  35
SITE     1 CA2  3 LYS A  70  LEU A  73  GLU A  78
SITE     1 CA3  4 MET A 100  GLY A 102  GLY A 104  ASP A 144
SITE     1 CA4  4 GLY A 183  ARG A 186  GLY A 188  GLU A 228
SITE     1 CA5  4 MET A 259  GLY A 261  GLY A 263  GLU A 303
SITE     1 CA6  3 LEU A 301  THR A 304  GLU A 309
CRYST1  139.360   67.500   42.110  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      0.007176  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014815  0.000000        0.00000
SCALE3      0.000000  0.000000  0.023747        0.00000
      
 References