HEADER CALCIUM/PHOSPHOLIPID-BINDING PROTEIN 26-OCT-93 1ANX
TITLE THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANNEXIN V;
COMPND 3 CHAIN: A, B, C;
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 J.SOPKOVA,M.RENOUARD,A.LEWIT-BENTLEY
REVDAT 3 07-FEB-24 1ANX 1 REMARK LINK
REVDAT 2 24-FEB-09 1ANX 1 VERSN
REVDAT 1 20-DEC-94 1ANX 0
JRNL AUTH J.SOPKOVA,M.RENOUARD,A.LEWIT-BENTLEY
JRNL TITL THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN
JRNL TITL 2 V.
JRNL REF J.MOL.BIOL. V. 234 816 1993
JRNL REFN ISSN 0022-2836
JRNL PMID 8254674
JRNL DOI 10.1006/JMBI.1993.1627
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
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 : 74259
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) : 0.198
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 : 7488
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 418
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) : 0.015 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.050 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.062 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.008 ; 0.015
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.067 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.200 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.221 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : 0.241 ; 0.300
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 7.704 ; 10.000
REMARK 3 STAGGERED (DEGREES) : 21.540; 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) : 2.644 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.501 ; 1.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 3.947 ; 1.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.927 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ANX 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_1000171046.
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 (%): 48.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 ASP A 319
REMARK 465 ASP A 320
REMARK 465 ALA B 2
REMARK 465 ASP B 319
REMARK 465 ASP B 320
REMARK 465 ALA C 2
REMARK 465 ASP C 319
REMARK 465 ASP C 320
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 NH2 ARG B 123 O ALA B 159 1.94
REMARK 500 N GLN B 3 O HOH B 378 1.99
REMARK 500 NE2 GLN B 3 OE1 GLU B 121 1.99
REMARK 500 N GLN A 3 O HOH A 452 2.00
REMARK 500 NE2 GLN A 3 O SER A 116 2.02
REMARK 500 O GLN C 3 OD2 ASP C 280 2.08
REMARK 500 NE2 GLN C 3 OE1 GLU C 121 2.09
REMARK 500 O HOH A 355 O HOH A 356 2.12
REMARK 500 NH2 ARG B 18 O HOH B 371 2.12
REMARK 500 OH TYR C 91 O HOH C 361 2.15
REMARK 500 OD1 ASP A 11 OG SER A 46 2.15
REMARK 500 OD1 ASP B 11 OG SER B 46 2.15
REMARK 500 OH TYR A 91 O HOH A 354 2.15
REMARK 500 OH TYR B 91 O HOH B 339 2.16
REMARK 500 O GLN B 3 OD2 ASP B 280 2.17
REMARK 500 NE ARG A 289 O HOH A 424 2.17
REMARK 500 O GLY C 263 O HOH C 413 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 SER B 88 C ARG B 89 N -0.145
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 GLN A 3 O - C - N ANGL. DEV. = 12.1 DEGREES
REMARK 500 VAL A 4 O - C - N ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG A 6 CD - NE - CZ ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 16 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 GLU A 17 CG - CD - OE1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLU A 17 CG - CD - OE2 ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 18 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 GLY A 32 CA - C - O ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLU A 52 CG - CD - OE1 ANGL. DEV. = -15.8 DEGREES
REMARK 500 GLU A 52 CG - CD - OE2 ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR A 59 CA - CB - CG2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 PHE A 61 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP A 68 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 LEU A 69 CA - CB - CG ANGL. DEV. = 17.2 DEGREES
REMARK 500 GLU A 72 OE1 - CD - OE2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 TYR A 94 CB - CG - CD2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG A 123 CD - NE - CZ ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TYR A 129 CB - CG - CD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TYR A 148 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 TYR A 148 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 151 CD - NE - CZ ANGL. DEV. = 38.5 DEGREES
REMARK 500 ARG A 151 CD - NE - CZ ANGL. DEV. = -11.6 DEGREES
REMARK 500 ARG A 161 NH1 - CZ - NH2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG A 161 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ASP A 164 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 GLY A 166 CA - C - O ANGL. DEV. = 12.1 DEGREES
REMARK 500 ASP A 168 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 GLN A 174 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 PHE A 194 CB - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 PHE A 194 CB - CG - CD1 ANGL. DEV. = -9.5 DEGREES
REMARK 500 ARG A 201 CD - NE - CZ ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG A 201 NE - CZ - NH2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 TYR A 213 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 MET A 214 CG - SD - CE ANGL. DEV. = -12.4 DEGREES
REMARK 500 TYR A 250 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 TYR A 250 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 MET A 259 CA - CB - CG ANGL. DEV. = -10.5 DEGREES
REMARK 500 ASP A 265 O - C - N ANGL. DEV. = 11.1 DEGREES
REMARK 500 ASP A 266 CB - CG - OD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 276 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP A 280 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 154 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 VAL A 4 -161.47 -69.60
REMARK 500 LEU A 5 -70.00 122.25
REMARK 500 LYS A 101 -159.96 -112.75
REMARK 500 ALA A 103 -66.52 120.18
REMARK 500 ALA A 165 43.37 -165.96
REMARK 500 MET A 259 59.79 -110.71
REMARK 500 LYS A 260 -29.52 -149.13
REMARK 500 ILE A 279 -71.55 -120.58
REMARK 500 ASP A 280 31.63 -143.46
REMARK 500 ASN A 291 -137.23 -75.04
REMARK 500 PHE A 292 -17.43 7.68
REMARK 500 ALA A 293 97.38 42.48
REMARK 500 THR A 294 148.04 153.22
REMARK 500 LEU B 5 -77.76 137.68
REMARK 500 LEU B 31 122.11 -28.63
REMARK 500 LYS B 101 -150.50 -101.30
REMARK 500 ALA B 103 -32.94 114.55
REMARK 500 ALA B 165 30.46 -161.03
REMARK 500 SER B 246 116.43 -161.68
REMARK 500 ALA B 262 89.45 -11.38
REMARK 500 ILE B 279 -73.71 -113.46
REMARK 500 ASP B 280 27.43 -145.26
REMARK 500 LYS B 290 -71.20 -51.27
REMARK 500 PHE B 292 -18.94 37.76
REMARK 500 ALA B 293 114.99 42.92
REMARK 500 THR B 294 158.35 126.58
REMARK 500 VAL C 4 -154.58 -90.03
REMARK 500 LEU C 5 -68.67 137.55
REMARK 500 LEU C 31 123.07 -31.31
REMARK 500 ALA C 103 -57.46 128.85
REMARK 500 ALA C 165 27.17 -150.95
REMARK 500 MET C 259 58.66 -111.51
REMARK 500 LYS C 260 -27.73 -147.13
REMARK 500 ASP C 280 26.85 -143.26
REMARK 500 ASN C 291 -155.50 -83.35
REMARK 500 PHE C 292 -23.87 28.02
REMARK 500 ALA C 293 98.11 52.95
REMARK 500 THR C 294 142.84 137.17
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 6 0.10 SIDE CHAIN
REMARK 500 ARG A 45 0.27 SIDE CHAIN
REMARK 500 ARG A 63 0.15 SIDE CHAIN
REMARK 500 ARG A 161 0.08 SIDE CHAIN
REMARK 500 ARG B 25 0.11 SIDE CHAIN
REMARK 500 ARG B 45 0.25 SIDE CHAIN
REMARK 500 ARG B 50 0.10 SIDE CHAIN
REMARK 500 ARG B 63 0.10 SIDE CHAIN
REMARK 500 ARG B 117 0.09 SIDE CHAIN
REMARK 500 ARG B 151 0.15 SIDE CHAIN
REMARK 500 ARG B 161 0.10 SIDE CHAIN
REMARK 500 ARG B 276 0.08 SIDE CHAIN
REMARK 500 ARG C 25 0.16 SIDE CHAIN
REMARK 500 ARG C 45 0.34 SIDE CHAIN
REMARK 500 ARG C 63 0.19 SIDE CHAIN
REMARK 500 ARG C 117 0.11 SIDE CHAIN
REMARK 500 ARG C 123 0.26 SIDE CHAIN
REMARK 500 ARG C 151 0.27 SIDE CHAIN
REMARK 500 ARG C 161 0.09 SIDE CHAIN
REMARK 500 ARG C 227 0.14 SIDE CHAIN
REMARK 500 ARG C 285 0.10 SIDE CHAIN
REMARK 500 ARG C 289 0.29 SIDE CHAIN
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 323 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 28 O
REMARK 620 2 GLY A 30 O 80.8
REMARK 620 3 GLY A 32 O 90.3 75.6
REMARK 620 4 GLU A 72 OE1 92.3 154.5 80.0
REMARK 620 5 GLU A 72 OE2 88.9 152.2 130.6 50.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 324 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 70 O
REMARK 620 2 LEU A 73 O 92.8
REMARK 620 3 GLU A 78 OE2 90.0 88.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 321 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 183 O
REMARK 620 2 LYS A 186 O 82.0
REMARK 620 3 GLY A 188 O 101.2 74.3
REMARK 620 4 GLU A 228 OE1 85.2 153.8 85.9
REMARK 620 5 GLU A 228 OE2 80.6 149.0 134.3 48.5
REMARK 620 6 SO4 A 322 O1 149.0 129.0 88.1 65.9 72.1
REMARK 620 7 SO4 A 322 O4 154.1 76.1 86.2 120.3 112.0 54.8
REMARK 620 8 SO4 A 322 S 167.9 103.8 90.6 93.3 89.4 27.4 27.9
REMARK 620 9 HOH A 326 O 84.0 71.8 144.6 129.4 81.0 105.3 76.1 87.7
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 325 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 226 OD1
REMARK 620 2 ASP A 226 O 75.7
REMARK 620 3 THR A 229 O 129.7 78.1
REMARK 620 4 GLU A 234 OE2 53.6 102.6 92.5
REMARK 620 5 GLU A 234 OE1 91.9 129.6 73.3 40.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 323 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET B 28 O
REMARK 620 2 GLY B 30 O 74.7
REMARK 620 3 GLY B 32 O 94.3 63.5
REMARK 620 4 GLU B 72 OE1 95.2 145.1 84.6
REMARK 620 5 GLU B 72 OE2 89.7 156.9 136.2 51.6
REMARK 620 6 HOH B 441 O 173.3 102.3 89.6 90.5 91.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 324 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 70 O
REMARK 620 2 LEU B 73 O 91.3
REMARK 620 3 GLU B 78 OE2 92.1 88.2
REMARK 620 4 HOH B 455 O 88.1 67.9 156.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 321 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 183 O
REMARK 620 2 LYS B 186 O 76.2
REMARK 620 3 GLY B 188 O 96.7 71.0
REMARK 620 4 GLU B 228 OE1 89.4 149.7 84.6
REMARK 620 5 GLU B 228 OE2 83.9 145.9 139.7 55.1
REMARK 620 6 SO4 B 322 O4 155.5 128.1 89.8 67.6 76.0
REMARK 620 7 SO4 B 322 S 167.3 96.0 90.0 101.9 97.9 34.5
REMARK 620 8 SO4 B 322 O3 136.7 66.0 90.5 133.9 116.5 66.5 32.1
REMARK 620 9 HOH B 345 O 83.3 67.4 137.2 138.1 83.1 107.7 84.5 63.6
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 325 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 226 OD1
REMARK 620 2 ASP B 226 O 74.8
REMARK 620 3 THR B 229 O 134.5 79.9
REMARK 620 4 GLU B 234 OE1 97.5 128.3 69.9
REMARK 620 5 GLU B 234 OE2 57.7 102.1 92.5 41.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 323 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET C 28 O
REMARK 620 2 GLY C 30 O 73.9
REMARK 620 3 GLY C 32 O 94.7 69.5
REMARK 620 4 GLU C 72 OE1 89.1 141.4 78.0
REMARK 620 5 GLU C 72 OE2 93.8 159.3 129.3 52.3
REMARK 620 6 HOH C 385 O 174.5 100.6 82.8 95.1 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 324 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS C 70 O
REMARK 620 2 LEU C 73 O 100.9
REMARK 620 3 GLU C 78 OE2 83.8 84.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 321 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 183 O
REMARK 620 2 LYS C 186 O 82.0
REMARK 620 3 GLY C 188 O 99.7 73.3
REMARK 620 4 GLU C 228 OE1 86.0 149.9 81.7
REMARK 620 5 GLU C 228 OE2 82.5 152.4 132.1 50.5
REMARK 620 6 SO4 C 322 S 172.9 98.9 87.2 96.4 93.8
REMARK 620 7 SO4 C 322 O3 148.8 70.0 85.5 125.2 116.6 29.7
REMARK 620 8 SO4 C 322 O4 150.4 126.0 82.3 65.0 74.9 31.4 60.6
REMARK 620 9 HOH C 333 O 82.4 71.6 144.2 133.9 83.7 91.2 76.0 113.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 325 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 226 O
REMARK 620 2 ASP C 226 OD1 78.5
REMARK 620 3 THR C 229 O 81.0 137.3
REMARK 620 4 GLU C 234 OE2 106.5 55.3 96.4
REMARK 620 5 GLU C 234 OE1 131.1 95.4 71.2 41.5
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 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 325
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 321
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 322
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 323
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 324
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 325
DBREF 1ANX A 2 320 UNP P08758 ANXA5_HUMAN 1 319
DBREF 1ANX B 2 320 UNP P08758 ANXA5_HUMAN 1 319
DBREF 1ANX C 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
SEQRES 1 C 319 ALA GLN VAL LEU ARG GLY THR VAL THR ASP PHE PRO GLY
SEQRES 2 C 319 PHE ASP GLU ARG ALA ASP ALA GLU THR LEU ARG LYS ALA
SEQRES 3 C 319 MET LYS GLY LEU GLY THR ASP GLU GLU SER ILE LEU THR
SEQRES 4 C 319 LEU LEU THR SER ARG SER ASN ALA GLN ARG GLN GLU ILE
SEQRES 5 C 319 SER ALA ALA PHE LYS THR LEU PHE GLY ARG ASP LEU LEU
SEQRES 6 C 319 ASP ASP LEU LYS SER GLU LEU THR GLY LYS PHE GLU LYS
SEQRES 7 C 319 LEU ILE VAL ALA LEU MET LYS PRO SER ARG LEU TYR ASP
SEQRES 8 C 319 ALA TYR GLU LEU LYS HIS ALA LEU LYS GLY ALA GLY THR
SEQRES 9 C 319 ASN GLU LYS VAL LEU THR GLU ILE ILE ALA SER ARG THR
SEQRES 10 C 319 PRO GLU GLU LEU ARG ALA ILE LYS GLN VAL TYR GLU GLU
SEQRES 11 C 319 GLU TYR GLY SER SER LEU GLU ASP ASP VAL VAL GLY ASP
SEQRES 12 C 319 THR SER GLY TYR TYR GLN ARG MET LEU VAL VAL LEU LEU
SEQRES 13 C 319 GLN ALA ASN ARG ASP PRO ASP ALA GLY ILE ASP GLU ALA
SEQRES 14 C 319 GLN VAL GLU GLN ASP ALA GLN ALA LEU PHE GLN ALA GLY
SEQRES 15 C 319 GLU LEU LYS TRP GLY THR ASP GLU GLU LYS PHE ILE THR
SEQRES 16 C 319 ILE PHE GLY THR ARG SER VAL SER HIS LEU ARG LYS VAL
SEQRES 17 C 319 PHE ASP LYS TYR MET THR ILE SER GLY PHE GLN ILE GLU
SEQRES 18 C 319 GLU THR ILE ASP ARG GLU THR SER GLY ASN LEU GLU GLN
SEQRES 19 C 319 LEU LEU LEU ALA VAL VAL LYS SER ILE ARG SER ILE PRO
SEQRES 20 C 319 ALA TYR LEU ALA GLU THR LEU TYR TYR ALA MET LYS GLY
SEQRES 21 C 319 ALA GLY THR ASP ASP HIS THR LEU ILE ARG VAL MET VAL
SEQRES 22 C 319 SER ARG SER GLU ILE ASP LEU PHE ASN ILE ARG LYS GLU
SEQRES 23 C 319 PHE ARG LYS ASN PHE ALA THR SER LEU TYR SER MET ILE
SEQRES 24 C 319 LYS GLY ASP THR SER GLY ASP TYR LYS LYS ALA LEU LEU
SEQRES 25 C 319 LEU LEU CYS GLY GLU ASP ASP
HET CA A 321 1
HET SO4 A 322 5
HET CA A 323 1
HET CA A 324 1
HET CA A 325 1
HET CA B 321 1
HET SO4 B 322 5
HET CA B 323 1
HET CA B 324 1
HET CA B 325 1
HET CA C 321 1
HET SO4 C 322 5
HET CA C 323 1
HET CA C 324 1
HET CA C 325 1
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 4 CA 12(CA 2+)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 19 HOH *418(H2 O)
HELIX 1 1 ASP A 16 LYS A 29 1 14
HELIX 2 2 ASP A 34 SER A 44 1 11
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 LYS A 101 1 15
HELIX 7 7 ASN A 106 ARG A 117 1 12
HELIX 8 8 THR A 118 GLY A 134 1 17
HELIX 9 9 SER A 136 THR A 145 1 10
HELIX 10 10 SER A 146 GLN A 158 1 13
HELIX 11 11 ASP A 168 GLY A 183 1 16
HELIX 12 12 ASP A 190 ARG A 201 1 12
HELIX 13 13 SER A 202 GLY A 218 1 17
HELIX 14 14 GLN A 220 THR A 229 1 10
HELIX 15 15 SER A 230 SER A 246 1 17
HELIX 16 16 SER A 246 TYR A 257 1 12
HELIX 17 17 ALA A 258 LYS A 260 5 3
HELIX 18 18 ASP A 265 SER A 277 1 13
HELIX 19 19 ASP A 280 ASN A 291 1 12
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 THR B 43 1 10
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 LYS B 101 1 15
HELIX 28 28 ASN B 106 ARG B 117 1 12
HELIX 29 29 THR B 118 GLY B 134 1 17
HELIX 30 30 SER B 136 THR B 145 1 10
HELIX 31 31 SER B 146 GLN B 158 1 13
HELIX 32 32 ASP B 168 GLY B 183 1 16
HELIX 33 33 ASP B 190 ARG B 201 1 12
HELIX 34 34 SER B 202 GLY B 218 1 17
HELIX 35 35 GLN B 220 THR B 229 1 10
HELIX 36 36 SER B 230 SER B 246 1 17
HELIX 37 37 SER B 246 TYR B 257 1 12
HELIX 38 38 ASP B 265 SER B 277 1 13
HELIX 39 39 ASP B 280 ASN B 291 1 12
HELIX 40 40 SER B 295 THR B 304 1 10
HELIX 41 41 SER B 305 GLY B 317 1 13
HELIX 42 42 ASP C 16 LYS C 29 1 14
HELIX 43 43 ASP C 34 THR C 43 1 10
HELIX 44 44 SER C 46 GLY C 62 1 17
HELIX 45 45 ASP C 64 LEU C 73 1 10
HELIX 46 46 THR C 74 LYS C 86 1 13
HELIX 47 47 PRO C 87 LEU C 100 1 14
HELIX 48 48 ASN C 106 ARG C 117 1 12
HELIX 49 49 THR C 118 GLY C 134 1 17
HELIX 50 50 SER C 136 THR C 145 1 10
HELIX 51 51 SER C 146 GLN C 158 1 13
HELIX 52 52 ASP C 168 GLY C 183 1 16
HELIX 53 53 ASP C 190 ARG C 201 1 12
HELIX 54 54 SER C 202 GLY C 218 1 17
HELIX 55 55 GLN C 220 THR C 229 1 10
HELIX 56 56 SER C 230 SER C 246 1 17
HELIX 57 57 SER C 246 TYR C 257 1 12
HELIX 58 58 ASP C 265 SER C 277 1 13
HELIX 59 59 ASP C 280 ASN C 291 1 12
HELIX 60 60 SER C 295 THR C 304 1 10
HELIX 61 61 SER C 305 GLY C 317 1 13
LINK O MET A 28 CA CA A 323 1555 1555 2.19
LINK O GLY A 30 CA CA A 323 1555 1555 2.44
LINK O GLY A 32 CA CA A 323 1555 1555 2.33
LINK O LYS A 70 CA CA A 324 1555 1555 2.12
LINK OE1 GLU A 72 CA CA A 323 1555 1555 2.62
LINK OE2 GLU A 72 CA CA A 323 1555 1555 2.70
LINK O LEU A 73 CA CA A 324 1555 1555 2.30
LINK OE2 GLU A 78 CA CA A 324 1555 1555 2.65
LINK O GLY A 183 CA CA A 321 1555 1555 2.39
LINK O LYS A 186 CA CA A 321 1555 1555 2.33
LINK O GLY A 188 CA CA A 321 1555 1555 2.43
LINK OD1 ASP A 226 CA CA A 325 1555 1555 2.89
LINK O ASP A 226 CA CA A 325 1555 1555 2.51
LINK OE1 GLU A 228 CA CA A 321 1555 1555 2.54
LINK OE2 GLU A 228 CA CA A 321 1555 1555 2.67
LINK O THR A 229 CA CA A 325 1555 1555 2.86
LINK OE2 GLU A 234 CA CA A 325 1555 1555 3.38
LINK OE1 GLU A 234 CA CA A 325 1555 1555 2.89
LINK CA CA A 321 O1 SO4 A 322 1555 1555 2.70
LINK CA CA A 321 O4 SO4 A 322 1555 1555 2.71
LINK CA CA A 321 S SO4 A 322 1555 1555 3.38
LINK CA CA A 321 O HOH A 326 1555 1555 2.53
LINK O MET B 28 CA CA B 323 1555 1555 2.38
LINK O GLY B 30 CA CA B 323 1555 1555 2.73
LINK O GLY B 32 CA CA B 323 1555 1555 2.33
LINK O LYS B 70 CA CA B 324 1555 1555 2.18
LINK OE1 GLU B 72 CA CA B 323 1555 1555 2.41
LINK OE2 GLU B 72 CA CA B 323 1555 1555 2.60
LINK O LEU B 73 CA CA B 324 1555 1555 2.33
LINK OE2 GLU B 78 CA CA B 324 1555 1555 2.34
LINK O GLY B 183 CA CA B 321 1555 1555 2.16
LINK O LYS B 186 CA CA B 321 1555 1555 2.65
LINK O GLY B 188 CA CA B 321 1555 1555 2.46
LINK OD1 ASP B 226 CA CA B 325 1555 1555 3.01
LINK O ASP B 226 CA CA B 325 1555 1555 2.49
LINK OE1 GLU B 228 CA CA B 321 1555 1555 2.26
LINK OE2 GLU B 228 CA CA B 321 1555 1555 2.40
LINK O THR B 229 CA CA B 325 1555 1555 2.82
LINK OE1 GLU B 234 CA CA B 325 1555 1555 3.02
LINK OE2 GLU B 234 CA CA B 325 1555 1555 3.25
LINK CA CA B 321 O4 SO4 B 322 1555 1555 2.39
LINK CA CA B 321 S SO4 B 322 1555 1555 2.80
LINK CA CA B 321 O3 SO4 B 322 1555 1555 2.11
LINK CA CA B 321 O HOH B 345 1555 1555 2.59
LINK CA CA B 323 O HOH B 441 1555 1555 2.98
LINK CA CA B 324 O HOH B 455 1555 1555 2.85
LINK O MET C 28 CA CA C 323 1555 1555 2.18
LINK O GLY C 30 CA CA C 323 1555 1555 2.70
LINK O GLY C 32 CA CA C 323 1555 1555 2.19
LINK O LYS C 70 CA CA C 324 1555 1555 2.21
LINK OE1 GLU C 72 CA CA C 323 1555 1555 2.53
LINK OE2 GLU C 72 CA CA C 323 1555 1555 2.55
LINK O LEU C 73 CA CA C 324 1555 1555 2.20
LINK OE2 GLU C 78 CA CA C 324 1555 1555 2.67
LINK O GLY C 183 CA CA C 321 1555 1555 2.18
LINK O LYS C 186 CA CA C 321 1555 1555 2.40
LINK O GLY C 188 CA CA C 321 1555 1555 2.38
LINK O ASP C 226 CA CA C 325 1555 1555 2.41
LINK OD1 ASP C 226 CA CA C 325 1555 1555 2.76
LINK OE1 GLU C 228 CA CA C 321 1555 1555 2.54
LINK OE2 GLU C 228 CA CA C 321 1555 1555 2.51
LINK O THR C 229 CA CA C 325 1555 1555 2.87
LINK OE2 GLU C 234 CA CA C 325 1555 1555 3.20
LINK OE1 GLU C 234 CA CA C 325 1555 1555 3.04
LINK CA CA C 321 S SO4 C 322 1555 1555 3.03
LINK CA CA C 321 O3 SO4 C 322 1555 1555 2.56
LINK CA CA C 321 O4 SO4 C 322 1555 1555 2.30
LINK CA CA C 321 O HOH C 333 1555 1555 2.47
LINK CA CA C 323 O HOH C 385 1555 1555 2.75
SITE 1 AC1 6 GLY A 183 LYS A 186 GLY A 188 GLU A 228
SITE 2 AC1 6 SO4 A 322 HOH A 326
SITE 1 AC2 10 LYS A 186 TRP A 187 GLY A 188 THR A 189
SITE 2 AC2 10 GLU A 228 CA A 321 HOH A 339 HOH A 420
SITE 3 AC2 10 HOH A 449 GLN B 181
SITE 1 AC3 4 MET A 28 GLY A 30 GLY A 32 GLU A 72
SITE 1 AC4 3 LYS A 70 LEU A 73 GLU A 78
SITE 1 AC5 3 ASP A 226 THR A 229 GLU A 234
SITE 1 AC6 6 GLY B 183 LYS B 186 GLY B 188 GLU B 228
SITE 2 AC6 6 SO4 B 322 HOH B 345
SITE 1 AC7 9 LYS B 186 GLY B 188 THR B 189 GLU B 228
SITE 2 AC7 9 CA B 321 HOH B 345 HOH B 362 HOH B 382
SITE 3 AC7 9 GLN C 181
SITE 1 AC8 5 MET B 28 GLY B 30 GLY B 32 GLU B 72
SITE 2 AC8 5 HOH B 441
SITE 1 AC9 4 LYS B 70 LEU B 73 GLU B 78 HOH B 455
SITE 1 BC1 3 ASP B 226 THR B 229 GLU B 234
SITE 1 BC2 6 GLY C 183 LYS C 186 GLY C 188 GLU C 228
SITE 2 BC2 6 SO4 C 322 HOH C 333
SITE 1 BC3 8 GLN A 181 LYS C 186 TRP C 187 GLY C 188
SITE 2 BC3 8 THR C 189 GLU C 228 CA C 321 HOH C 441
SITE 1 BC4 5 MET C 28 GLY C 30 GLY C 32 GLU C 72
SITE 2 BC4 5 HOH C 385
SITE 1 BC5 3 LYS C 70 LEU C 73 GLU C 78
SITE 1 BC6 3 ASP C 226 THR C 229 GLU C 234
CRYST1 91.200 91.300 36.200 82.40 82.40 118.20 P 1 3
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 0.010965 0.005879 -0.002845 0.00000
SCALE2 0.000000 0.012428 -0.002842 0.00000
SCALE3 0.000000 0.000000 0.028589 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
