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PDBsum entry 1qls

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Top Page protein metals Protein-protein interface(s) links
Metal-binding protein/inhibitor PDB id
1qls
Jmol
Contents
Protein chains
95 a.a. *
12 a.a. *
Metals
_CA ×2
Waters ×23
* Residue conservation analysis
HEADER    METAL-BINDING PROTEIN/INHIBITOR         15-SEP-99   1QLS
TITLE     S100C (S100A11),OR CALGIZZARIN, IN COMPLEX WITH ANNEXIN
TITLE    2 I N-TERMINUS
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: S100C PROTEIN;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: CALGIZZARIN;
COMPND   5 ENGINEERED: YES;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: ANNEXIN I;
COMPND   8 CHAIN: D;
COMPND   9 FRAGMENT: N-TERMINAL;
COMPND  10 OTHER_DETAILS: N-ACETYLATED ON N-TERMINUS
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE   3 ORGANISM_COMMON: PIG;
SOURCE   4 ORGANISM_TAXID: 9823;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET23A;
SOURCE   9 MOL_ID: 2;
SOURCE  10 SYNTHETIC: YES;
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  12 ORGANISM_COMMON: HUMAN;
SOURCE  13 ORGANISM_TAXID: 9606
KEYWDS    METAL-BINDING PROTEIN/INHIBITOR, S100 FAMILY, EF-HAND
KEYWDS   2 PROTEIN, COMPLEX (LIGAND/ANNEXIN), LIGAND OF ANNEXIN II,
KEYWDS   3 CALCIUM/PHOSPHOLIPID BINDING PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.RETY,J.SOPKOVA,M.RENOUARD,D.OSTERLOH,V.GERKE,
AUTHOR   2 F.RUSSO-MARIE,A.LEWIT-BENTLEY
REVDAT   2   24-FEB-09 1QLS    1       VERSN
REVDAT   1   25-FEB-00 1QLS    0
JRNL        AUTH   S.RETY,D.OSTERLOH,J.P.ARIE,S.TABARIES,J.SEEMAN,
JRNL        AUTH 2 F.RUSSO-MARIE,V.GERKE,A.LEWIT-BENTLEY
JRNL        TITL   STRUCTURAL BASIS OF THE CA2+ DEPENDENT ASSOCIATION
JRNL        TITL 2 BETWEEN S100C (S100A11) AND ITS TARGET, THE
JRNL        TITL 3 N-TERMINAL PART OF ANNEXIN I
JRNL        REF    STRUCTURE                     V.   8   175 2000
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   10673436
JRNL        DOI    10.1016/S0969-2126(00)00093-9
REMARK   2
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.3
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7
REMARK   3   NUMBER OF REFLECTIONS             : 9333
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) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.214
REMARK   3   FREE R VALUE                     : 0.268
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.0
REMARK   3   FREE R VALUE TEST SET COUNT      : 930
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 842
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 23
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 200.109
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.217
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.1216
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.869
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA
REMARK   3    BOND LENGTH                     (A) : 0.017 ; 0.020
REMARK   3    ANGLE DISTANCE                  (A) : 0.035 ; 0.030
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.054 ; 0.05
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL
REMARK   3
REMARK   3   PLANE RESTRAINT                  (A) : 0.009 ; 0.02
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.203 ; 0.15
REMARK   3
REMARK   3   NON-BONDED CONTACT RESTRAINTS.
REMARK   3    SINGLE TORSION                  (A) : 0.206 ; 0.300
REMARK   3    MULTIPLE TORSION                (A) : 0.350 ; 0.300
REMARK   3    H-BOND (X...Y)                  (A) : 0.189 ; 0.3
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL
REMARK   3
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK   3    SPECIFIED                 (DEGREES) : 0.    ; 15.0
REMARK   3    PLANAR                    (DEGREES) : 2.1   ; 15.0
REMARK   3    STAGGERED                 (DEGREES) : 23.0  ; 15.0
REMARK   3    TRANSVERSE                (DEGREES) : 21.8  ; 20.0
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.417 ; 2.0
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.357 ; 3.0
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.480 ; 3.0
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.602 ; 4.0
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1QLS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-SEP-99.
REMARK 100 THE PDBE ID CODE IS EBI-2868.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-98
REMARK 200  TEMPERATURE           (KELVIN) : 280.0
REMARK 200  PH                             : 8.50
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : LURE
REMARK 200  BEAMLINE                       : D41A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.37
REMARK 200  MONOCHROMATOR                  : GE(111)
REMARK 200  OPTICS                         : FOCUSSING MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9310
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7
REMARK 200  DATA REDUNDANCY                : 6.600
REMARK 200  R MERGE                    (I) : 0.08000
REMARK 200  R SYM                      (I) : 0.08000
REMARK 200   FOR THE DATA SET  : 20.1000
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1BT6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS  (%): 68.2
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.9
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MG/ML PROTEIN WERE CRYSTALLIZED
REMARK 280  BY VAPOR DIFFUSION AGAINST 10% PEG 4000, 20% PEG 4000,
REMARK 280  10% 2-PROPANOL, 100MM HEPES, PH=8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+1/3
REMARK 290       3555   -X+Y,-X,Z+2/3
REMARK 290       4555   -X,-Y,Z+1/2
REMARK 290       5555   Y,-X+Y,Z+5/6
REMARK 290       6555   X-Y,X,Z+1/6
REMARK 290       7555   Y,X,-Z+1/3
REMARK 290       8555   X-Y,-Y,-Z
REMARK 290       9555   -X,-X+Y,-Z+2/3
REMARK 290      10555   -Y,-X,-Z+5/6
REMARK 290      11555   -X+Y,Y,-Z+1/2
REMARK 290      12555   X,X-Y,-Z+1/6
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.20333
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.40667
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       55.80500
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       93.00833
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       18.60167
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       37.20333
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       74.40667
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       93.00833
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       55.80500
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       18.60167
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 300
REMARK 300 DETAILS:BIOLOGICAL_UNIT: DIMERTHE DIMER IS COVALENT IN
REMARK 300  THE CRYSTAL, LINKED BY ADISULPHIDE AT CYS11.
REMARK 300 UNDER REDUCING CONDITIONS, THOUGHTHE DISULPHIDE WOULD
REMARK 300  BE REDUCED, THE DIMER SHOULD REMAININTACT.FOR
REMARK 300 THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350THE
REMARK 300 DIFFERENCE IN ACCESSIBLE SURFACE AREA PERCHAIN
REMARK 300 BETWEEN THE ISOLATED CHAIN AND THAT FOR
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      134.25126
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      111.61000
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     ARG A     4
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500
REMARK 500   SG   CYS A    11     SG   CYS A    11     8676      1.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    CYS A  11   CA  -  CB  -  SG  ANGL. DEV. =  -7.5 DEGREES
REMARK 500    ASP A  26   CB  -  CG  -  OD2 ANGL. DEV. =  12.4 DEGREES
REMARK 500    ARG A  60   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES
REMARK 500    ARG A  60   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES
REMARK 500    ASP A  66   CB  -  CG  -  OD2 ANGL. DEV. =  14.2 DEGREES
REMARK 500    ASP A  68   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES
REMARK 500    ASP A  74   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    THR A  43      -38.37   -132.16
REMARK 500    GLN A  98       65.59   -114.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    THR A   8        23.4      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 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 101  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A  23   O
REMARK 620 2 GLU A  36   OE2  74.5
REMARK 620 3 ASP A  26   OD1  99.7  72.3
REMARK 620 4 HOH A2017   O   173.9 111.3  80.7
REMARK 620 5 LYS A  31   O    98.1 121.4 160.1  80.6
REMARK 620 6 GLU A  36   OE1  96.7  46.7 108.3  88.9  78.2
REMARK 620 7 ASN A  28   O    78.0 143.7  89.7  96.0  85.4 161.9
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CA A 102  CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A  70   OD1
REMARK 620 2 GLN A  72   O    76.3
REMARK 620 3 GLU A  77   OE1 147.2  80.7
REMARK 620 4 GLU A  77   OE2 162.9 120.7  46.9
REMARK 620 5 HOH A2013   O    74.0  93.7  84.6 104.7
REMARK 620 6 ASP A  66   OD1  86.7  89.5 116.4  91.3 159.0
REMARK 620 7 ASP A  68   OD1  85.2 159.6 119.6  77.7  89.3  80.8
REMARK 620 N                    1     2     3     4     5     6
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
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 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A 102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A4P   RELATED DB: PDB
REMARK 900  P11 (S100A10), LIGAND OF ANNEXIN II CALPACTIN LIGHT CHAIN
REMARK 900 RELATED ID: 1BT6   RELATED DB: PDB
REMARK 900  P11 (S100A10), LIGAND OF ANNEXIN II IN COMPLEX WITH ANNEXIN
REMARK 900  II N-TERMINUS (HUMAN)
REMARK 900 RELATED ID: 1BO9   RELATED DB: PDB
REMARK 900  NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNIXIN I
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SYNTHETIC ANNEXIN I N-TERMINAL SEQUENCE
DBREF  1QLS A    1    99  UNP    P31950   S111_PIG         1     99
DBREF  1QLS D    1    11  UNP    P04083   ANX1_HUMAN       1     11
SEQADV 1QLS ALA D    5  UNP  P04083    GLU     5 ENGINEERED
SEQRES   1 A   99  MET ALA LYS ARG PRO THR GLU THR GLU ARG CYS ILE GLU
SEQRES   2 A   99  SER LEU ILE ALA ILE PHE GLN LYS HIS ALA GLY ARG ASP
SEQRES   3 A   99  GLY ASN ASN THR LYS ILE SER LYS THR GLU PHE LEU ILE
SEQRES   4 A   99  PHE MET ASN THR GLU LEU ALA ALA PHE THR GLN ASN GLN
SEQRES   5 A   99  LYS ASP PRO GLY VAL LEU ASP ARG MET MET LYS LYS LEU
SEQRES   6 A   99  ASP LEU ASP SER ASP GLY GLN LEU ASP PHE GLN GLU PHE
SEQRES   7 A   99  LEU ASN LEU ILE GLY GLY LEU ALA ILE ALA CYS HIS ASP
SEQRES   8 A   99  SER PHE ILE LYS SER THR GLN LYS
SEQRES   1 D   12  ACE ALA MET VAL SER ALA PHE LEU LYS GLN ALA TRP
HET     CA  A 101       1
HET     CA  A 102       1
HET    ACE  D   0       3
HETNAM      CA CALCIUM ION
HETNAM     ACE ACETYL GROUP
HETSYN      CA CA
FORMUL   3   CA    2(CA 2+)
FORMUL   5  ACE    C2 H4 O
FORMUL   6  HOH   *23(H2 O1)
HELIX    1   1 THR A    6  GLY A   24  1                                  19
HELIX    2   2 SER A   33  THR A   43  1                                  11
HELIX    3   3 ALA A   46  ASN A   51  1                                   6
HELIX    4   4 GLY A   56  LEU A   65  1                                  10
HELIX    5   5 PHE A   75  THR A   97  1                                  23
HELIX    5  1D MET D    2  GLN D    9  1                                   8
SHEET    1  S1 2 LYS A  31  SER A  33  0
SHEET    2  S1 2 GLN A  72  ASP A  74 -1  N  ILE A  32   O  LEU A 73
LINK        CA    CA A 101                 O   ALA A  23     1555   1555  2.48
LINK        CA    CA A 101                 OE2 GLU A  36     1555   1555  2.82
LINK        CA    CA A 101                 OD1 ASP A  26     1555   1555  2.54
LINK        CA    CA A 101                 O   HOH A2017     1555   1555  2.49
LINK        CA    CA A 101                 O   LYS A  31     1555   1555  2.56
LINK        CA    CA A 101                 OE1 GLU A  36     1555   1555  2.63
LINK        CA    CA A 101                 O   ASN A  28     1555   1555  2.69
LINK        CA    CA A 102                 O   GLN A  72     1555   1555  2.62
LINK        CA    CA A 102                 OE1 GLU A  77     1555   1555  2.73
LINK        CA    CA A 102                 OE2 GLU A  77     1555   1555  2.79
LINK        CA    CA A 102                 O   HOH A2013     1555   1555  2.70
LINK        CA    CA A 102                 OD1 ASP A  66     1555   1555  2.56
LINK        CA    CA A 102                 OD1 ASP A  68     1555   1555  2.60
LINK        CA    CA A 102                 OD1 ASP A  70     1555   1555  2.64
LINK         C   ACE D   0                 N   ALA D   1     1555   1555  1.33
SITE     1 AC1  6 ALA A  23  ASP A  26  ASN A  28  LYS A  31
SITE     2 AC1  6 GLU A  36  HOH A2017
SITE     1 AC2  6 ASP A  66  ASP A  68  ASP A  70  GLN A  72
SITE     2 AC2  6 GLU A  77  HOH A2013
CRYST1   77.510   77.510  111.610  90.00  90.00 120.00 P 61 2 2     12
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      0.012901  0.007449  0.000000        0.00000
SCALE2      0.000000  0.014897  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008960        0.00000
      
PROCHECK
Go to PROCHECK summary
 References