HEADER CALCIUM/PHOSPHOLIPID-BINDING PROTEIN 26-OCT-93 1ANW
TITLE THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND
TITLE 2 IMPLICATIONS FOR MEMBRANE BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANNEXIN V;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALCIUM/PHOSPHOLIPID-BINDING PROTEIN, CALCIUM-PHOSPHOLIPID-BINDING
KEYWDS 2 PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LEWIT-BENTLEY,S.MORERA,R.HUBER,G.BODO
REVDAT 3 07-FEB-24 1ANW 1 REMARK LINK
REVDAT 2 24-FEB-09 1ANW 1 VERSN
REVDAT 1 20-DEC-94 1ANW 0
JRNL AUTH A.LEWIT-BENTLEY,S.MORERA,R.HUBER,G.BODO
JRNL TITL THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V
JRNL TITL 2 AND IMPLICATIONS FOR MEMBRANE BINDING.
JRNL REF EUR.J.BIOCHEM. V. 210 73 1992
JRNL REFN ISSN 0014-2956
JRNL PMID 1446685
JRNL DOI 10.1111/J.1432-1033.1992.TB17392.X
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROLSQ
REMARK 3 AUTHORS : KONNERT,HENDRICKSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 31600
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : NULL
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 FIT/AGREEMENT OF MODEL WITH ALL DATA.
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 : 5036
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 265
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
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) : 0.043 ; 0.030
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.058 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.004 ; 0.010
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.188 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.217 ; 0.500
REMARK 3 MULTIPLE TORSION (A) : 0.246 ; 0.500
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.227 ; 0.500
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 1.800 ; 3.000
REMARK 3 STAGGERED (DEGREES) : 24.800; 15.000
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.902 ; 1.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.613 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.685 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.804 ; 2.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ANW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171045.
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 <I/SIGMA(I)> 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 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 40.45000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 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 OE1 GLN A 220 O HOH A 946 1.99
REMARK 500 NH2 ARG B 6 O HOH B 761 2.13
REMARK 500 CD ARG B 89 O HOH B 986 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL A 4 C LEU A 5 N -0.157
REMARK 500 GLN A 158 C ALA A 159 N 0.191
REMARK 500 ARG A 161 C ASP A 162 N 0.159
REMARK 500 SER A 230 C GLY A 231 N 0.159
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 LEU A 5 C - N - CA ANGL. DEV. = 17.9 DEGREES
REMARK 500 THR A 10 CB - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 ASP A 11 CB - CG - OD1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ASP A 11 CB - CG - OD2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 GLU A 36 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 THR A 43 CA - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG A 45 NH1 - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 45 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG A 50 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 63 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 67 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ASP A 92 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 GLU A 112 CG - CD - OE1 ANGL. DEV. = -12.1 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 GLU A 121 OE1 - CD - OE2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 TYR A 133 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 GLU A 138 CG - CD - OE1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 GLU A 138 CG - CD - OE2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 151 CG - CD - NE ANGL. DEV. = 14.1 DEGREES
REMARK 500 LEU A 157 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP A 211 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 211 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 SER A 230 O - C - N ANGL. DEV. = -17.8 DEGREES
REMARK 500 ARG A 245 NE - CZ - NH2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 266 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 271 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 276 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 280 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 307 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 LYS A 310 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLY A 317 C - N - CA ANGL. DEV. = 30.8 DEGREES
REMARK 500 ASP B 16 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 20 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP B 20 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LEU B 39 CB - CA - C ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG B 45 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 63 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 64 CB - CG - OD1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG B 89 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 123 CD - NE - CZ ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG B 123 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 TYR B 133 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR B 148 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG B 151 CD - NE - CZ ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASN B 160 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 ASP B 175 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 68 ANGLE DEVIATIONS.
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 THR A 105 133.56 -35.99
REMARK 500 ASN A 160 42.78 -141.59
REMARK 500 ASP A 162 153.78 -43.24
REMARK 500 SER A 217 -27.58 -154.52
REMARK 500 ASP A 226 94.84 66.98
REMARK 500 GLU A 228 -39.99 -155.80
REMARK 500 SER A 230 169.90 -12.00
REMARK 500 SER A 246 111.99 177.61
REMARK 500 ILE A 279 -72.14 -124.09
REMARK 500 GLU A 318 150.50 172.54
REMARK 500 GLN B 3 67.99 -109.49
REMARK 500 ALA B 165 -156.45 -154.58
REMARK 500 ASP B 226 -97.62 77.89
REMARK 500 ARG B 227 103.97 93.05
REMARK 500 GLU B 228 -38.27 135.91
REMARK 500 THR B 229 -134.16 -118.08
REMARK 500 SER B 230 145.30 49.70
REMARK 500 SER B 246 119.34 -162.47
REMARK 500 ASP B 265 78.82 -100.87
REMARK 500 ILE B 279 -65.36 -132.16
REMARK 500 ASP B 280 27.39 -146.95
REMARK 500 GLU B 318 140.05 177.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 50 0.11 SIDE CHAIN
REMARK 500 ARG A 201 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG A 161 19.89
REMARK 500 ARG A 227 -12.08
REMARK 500 SER A 230 -22.97
REMARK 500 ASP A 319 12.81
REMARK 500 VAL B 4 16.04
REMARK 500 ASP B 34 12.89
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 351 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 28 O
REMARK 620 2 GLY A 30 O 82.4
REMARK 620 3 GLY A 32 O 96.6 81.1
REMARK 620 4 GLU A 72 OE1 97.2 158.9 78.0
REMARK 620 5 GLU A 72 OE2 93.7 149.8 129.1 51.2
REMARK 620 6 HOH A 823 O 179.3 97.0 83.6 83.5 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 352 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 259 O
REMARK 620 2 GLY A 261 O 94.2
REMARK 620 3 GLY A 263 O 103.3 114.8
REMARK 620 4 ASP A 303 OD1 87.6 121.3 121.7
REMARK 620 5 ASP A 303 OD2 85.3 166.3 78.5 45.0
REMARK 620 6 HOH A 902 O 169.1 91.5 82.6 81.5 86.9
REMARK 620 7 HOH A 981 O 113.4 75.9 141.1 50.6 91.7 59.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 353 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 28 O
REMARK 620 2 GLY B 30 O 81.3
REMARK 620 3 GLY B 32 O 88.5 75.9
REMARK 620 4 GLU B 72 OE1 77.1 146.4 78.2
REMARK 620 5 GLU B 72 OE2 109.4 164.3 114.9 49.2
REMARK 620 6 HOH B 757 O 80.9 66.7 142.2 133.0 102.9
REMARK 620 7 HOH B 861 O 168.5 97.4 80.1 98.8 74.4 109.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 354 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 259 O
REMARK 620 2 GLY B 261 O 86.9
REMARK 620 3 GLY B 263 O 87.7 89.0
REMARK 620 4 ASP B 303 OD1 88.2 144.8 125.6
REMARK 620 5 ASP B 303 OD2 77.5 159.5 77.2 49.0
REMARK 620 6 HOH B 891 O 82.4 68.5 155.7 76.4 121.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 354
DBREF 1ANW A 2 320 UNP P08758 ANXA5_HUMAN 1 319
DBREF 1ANW B 2 320 UNP P08758 ANXA5_HUMAN 1 319
SEQRES 1 A 319 ALA GLN VAL LEU ARG GLY THR VAL THR ASP PHE PRO GLY
SEQRES 2 A 319 PHE ASP GLU ARG ALA ASP ALA GLU THR LEU ARG LYS ALA
SEQRES 3 A 319 MET LYS GLY LEU GLY THR ASP GLU GLU SER ILE LEU THR
SEQRES 4 A 319 LEU LEU THR SER ARG SER ASN ALA GLN ARG GLN GLU ILE
SEQRES 5 A 319 SER ALA ALA PHE LYS THR LEU PHE GLY ARG ASP LEU LEU
SEQRES 6 A 319 ASP ASP LEU LYS SER GLU LEU THR GLY LYS PHE GLU LYS
SEQRES 7 A 319 LEU ILE VAL ALA LEU MET LYS PRO SER ARG LEU TYR ASP
SEQRES 8 A 319 ALA TYR GLU LEU LYS HIS ALA LEU LYS GLY ALA GLY THR
SEQRES 9 A 319 ASN GLU LYS VAL LEU THR GLU ILE ILE ALA SER ARG THR
SEQRES 10 A 319 PRO GLU GLU LEU ARG ALA ILE LYS GLN VAL TYR GLU GLU
SEQRES 11 A 319 GLU TYR GLY SER SER LEU GLU ASP ASP VAL VAL GLY ASP
SEQRES 12 A 319 THR SER GLY TYR TYR GLN ARG MET LEU VAL VAL LEU LEU
SEQRES 13 A 319 GLN ALA ASN ARG ASP PRO ASP ALA GLY ILE ASP GLU ALA
SEQRES 14 A 319 GLN VAL GLU GLN ASP ALA GLN ALA LEU PHE GLN ALA GLY
SEQRES 15 A 319 GLU LEU LYS TRP GLY THR ASP GLU GLU LYS PHE ILE THR
SEQRES 16 A 319 ILE PHE GLY THR ARG SER VAL SER HIS LEU ARG LYS VAL
SEQRES 17 A 319 PHE ASP LYS TYR MET THR ILE SER GLY PHE GLN ILE GLU
SEQRES 18 A 319 GLU THR ILE ASP ARG GLU THR SER GLY ASN LEU GLU GLN
SEQRES 19 A 319 LEU LEU LEU ALA VAL VAL LYS SER ILE ARG SER ILE PRO
SEQRES 20 A 319 ALA TYR LEU ALA GLU THR LEU TYR TYR ALA MET LYS GLY
SEQRES 21 A 319 ALA GLY THR ASP ASP HIS THR LEU ILE ARG VAL MET VAL
SEQRES 22 A 319 SER ARG SER GLU ILE ASP LEU PHE ASN ILE ARG LYS GLU
SEQRES 23 A 319 PHE ARG LYS ASN PHE ALA THR SER LEU TYR SER MET ILE
SEQRES 24 A 319 LYS GLY ASP THR SER GLY ASP TYR LYS LYS ALA LEU LEU
SEQRES 25 A 319 LEU LEU CYS GLY GLU ASP ASP
SEQRES 1 B 319 ALA GLN VAL LEU ARG GLY THR VAL THR ASP PHE PRO GLY
SEQRES 2 B 319 PHE ASP GLU ARG ALA ASP ALA GLU THR LEU ARG LYS ALA
SEQRES 3 B 319 MET LYS GLY LEU GLY THR ASP GLU GLU SER ILE LEU THR
SEQRES 4 B 319 LEU LEU THR SER ARG SER ASN ALA GLN ARG GLN GLU ILE
SEQRES 5 B 319 SER ALA ALA PHE LYS THR LEU PHE GLY ARG ASP LEU LEU
SEQRES 6 B 319 ASP ASP LEU LYS SER GLU LEU THR GLY LYS PHE GLU LYS
SEQRES 7 B 319 LEU ILE VAL ALA LEU MET LYS PRO SER ARG LEU TYR ASP
SEQRES 8 B 319 ALA TYR GLU LEU LYS HIS ALA LEU LYS GLY ALA GLY THR
SEQRES 9 B 319 ASN GLU LYS VAL LEU THR GLU ILE ILE ALA SER ARG THR
SEQRES 10 B 319 PRO GLU GLU LEU ARG ALA ILE LYS GLN VAL TYR GLU GLU
SEQRES 11 B 319 GLU TYR GLY SER SER LEU GLU ASP ASP VAL VAL GLY ASP
SEQRES 12 B 319 THR SER GLY TYR TYR GLN ARG MET LEU VAL VAL LEU LEU
SEQRES 13 B 319 GLN ALA ASN ARG ASP PRO ASP ALA GLY ILE ASP GLU ALA
SEQRES 14 B 319 GLN VAL GLU GLN ASP ALA GLN ALA LEU PHE GLN ALA GLY
SEQRES 15 B 319 GLU LEU LYS TRP GLY THR ASP GLU GLU LYS PHE ILE THR
SEQRES 16 B 319 ILE PHE GLY THR ARG SER VAL SER HIS LEU ARG LYS VAL
SEQRES 17 B 319 PHE ASP LYS TYR MET THR ILE SER GLY PHE GLN ILE GLU
SEQRES 18 B 319 GLU THR ILE ASP ARG GLU THR SER GLY ASN LEU GLU GLN
SEQRES 19 B 319 LEU LEU LEU ALA VAL VAL LYS SER ILE ARG SER ILE PRO
SEQRES 20 B 319 ALA TYR LEU ALA GLU THR LEU TYR TYR ALA MET LYS GLY
SEQRES 21 B 319 ALA GLY THR ASP ASP HIS THR LEU ILE ARG VAL MET VAL
SEQRES 22 B 319 SER ARG SER GLU ILE ASP LEU PHE ASN ILE ARG LYS GLU
SEQRES 23 B 319 PHE ARG LYS ASN PHE ALA THR SER LEU TYR SER MET ILE
SEQRES 24 B 319 LYS GLY ASP THR SER GLY ASP TYR LYS LYS ALA LEU LEU
SEQRES 25 B 319 LEU LEU CYS GLY GLU ASP ASP
HET CA A 351 1
HET CA A 352 1
HET CA B 353 1
HET CA B 354 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *265(H2 O)
HELIX 1 1 ASP A 16 LYS A 29 1 14
HELIX 2 2 ASP A 34 THR A 43 1 10
HELIX 3 3 SER A 46 GLY A 62 1 17
HELIX 4 4 ASP A 64 LEU A 73 1 10
HELIX 5 5 THR A 74 LYS A 86 1 13
HELIX 6 6 PRO A 87 LEU A 100 1 14
HELIX 7 7 LYS A 101 THR A 105 5 5
HELIX 8 8 ASN A 106 ARG A 117 1 12
HELIX 9 9 THR A 118 GLY A 134 1 17
HELIX 10 10 SER A 136 THR A 145 1 10
HELIX 11 11 SER A 146 GLN A 158 1 13
HELIX 12 12 ASP A 168 LEU A 185 1 18
HELIX 13 13 ASP A 190 ARG A 201 1 12
HELIX 14 14 SER A 202 ILE A 216 1 15
HELIX 15 15 GLN A 220 ILE A 225 5 6
HELIX 16 16 GLY A 231 SER A 246 1 16
HELIX 17 17 SER A 246 ALA A 258 1 13
HELIX 18 18 ASP A 265 ARG A 276 1 12
HELIX 19 19 ASP A 280 ALA A 293 1 14
HELIX 20 20 SER A 295 THR A 304 1 10
HELIX 21 21 SER A 305 GLY A 317 1 13
HELIX 22 22 ASP B 16 LYS B 29 1 14
HELIX 23 23 ASP B 34 SER B 44 1 11
HELIX 24 24 SER B 46 GLY B 62 1 17
HELIX 25 25 ASP B 64 LEU B 73 1 10
HELIX 26 26 THR B 74 LYS B 86 1 13
HELIX 27 27 PRO B 87 HIS B 98 1 12
HELIX 28 28 LYS B 101 THR B 105 5 5
HELIX 29 29 ASN B 106 ARG B 117 1 12
HELIX 30 30 THR B 118 GLY B 134 1 17
HELIX 31 31 SER B 136 THR B 145 1 10
HELIX 32 32 SER B 146 GLN B 158 1 13
HELIX 33 33 ASP B 168 LEU B 185 1 18
HELIX 34 34 ASP B 190 ARG B 201 1 12
HELIX 35 35 SER B 202 GLY B 218 1 17
HELIX 36 36 GLN B 220 ILE B 225 5 6
HELIX 37 37 GLY B 231 SER B 246 1 16
HELIX 38 38 SER B 246 ALA B 258 1 13
HELIX 39 39 ASP B 265 SER B 277 1 13
HELIX 40 40 ASP B 280 ALA B 293 1 14
HELIX 41 41 SER B 295 THR B 304 1 10
HELIX 42 42 SER B 305 GLY B 317 1 13
LINK O MET A 28 CA CA A 351 1555 1555 2.35
LINK O GLY A 30 CA CA A 351 1555 1555 2.33
LINK O GLY A 32 CA CA A 351 1555 1555 2.40
LINK OE1 GLU A 72 CA CA A 351 1555 1555 2.70
LINK OE2 GLU A 72 CA CA A 351 1555 1555 2.34
LINK O MET A 259 CA CA A 352 1555 1555 2.20
LINK O GLY A 261 CA CA A 352 1555 1555 2.16
LINK O GLY A 263 CA CA A 352 1555 1555 2.12
LINK OD1 ASP A 303 CA CA A 352 1555 1555 2.96
LINK OD2 ASP A 303 CA CA A 352 1555 1555 2.76
LINK CA CA A 351 O HOH A 823 1555 1555 2.32
LINK CA CA A 352 O HOH A 902 1555 1555 3.04
LINK CA CA A 352 O HOH A 981 1555 1555 1.83
LINK O MET B 28 CA CA B 353 1555 1555 2.36
LINK O GLY B 30 CA CA B 353 1555 1555 2.46
LINK O GLY B 32 CA CA B 353 1555 1555 2.37
LINK OE1 GLU B 72 CA CA B 353 1555 1555 2.51
LINK OE2 GLU B 72 CA CA B 353 1555 1555 2.54
LINK O MET B 259 CA CA B 354 1555 1555 2.43
LINK O GLY B 261 CA CA B 354 1555 1555 2.37
LINK O GLY B 263 CA CA B 354 1555 1555 2.55
LINK OD1 ASP B 303 CA CA B 354 1555 1555 2.69
LINK OD2 ASP B 303 CA CA B 354 1555 1555 2.49
LINK CA CA B 353 O HOH B 757 1555 1555 2.27
LINK CA CA B 353 O HOH B 861 1555 1555 2.24
LINK CA CA B 354 O HOH B 891 1555 1555 2.68
SITE 1 AC1 5 MET A 28 GLY A 30 GLY A 32 GLU A 72
SITE 2 AC1 5 HOH A 823
SITE 1 AC2 6 MET A 259 GLY A 261 GLY A 263 ASP A 303
SITE 2 AC2 6 HOH A 902 HOH A 981
SITE 1 AC3 6 MET B 28 GLY B 30 GLY B 32 GLU B 72
SITE 2 AC3 6 HOH B 757 HOH B 861
SITE 1 AC4 5 MET B 259 GLY B 261 GLY B 263 ASP B 303
SITE 2 AC4 5 HOH B 891
CRYST1 83.900 80.900 71.400 90.00 108.70 90.00 P 1 21 1 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 0.011919 0.000000 0.004034 0.00000
SCALE2 0.000000 0.012361 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014786 0.00000
(ATOM LINES ARE NOT SHOWN.)
END