HEADER LIGASE 06-AUG-99 1CQJ
TITLE CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINYL-COA SYNTHETASE ALPHA CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: ALPHA SUBUNIT;
COMPND 5 SYNONYM: SCS-ALPHA;
COMPND 6 EC: 6.2.1.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SUCCINYL-COA SYNTHETASE BETA CHAIN;
COMPND 10 CHAIN: B, E;
COMPND 11 FRAGMENT: BETA SUBUNIT;
COMPND 12 SYNONYM: SCS-BETA;
COMPND 13 EC: 6.2.1.5;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 8 ORGANISM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ATP-GRASP FOLD, ROSSMANN FOLD, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.A.JOYCE,M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER,W.T.WOLODKO
REVDAT 4 04-OCT-17 1CQJ 1 REMARK
REVDAT 3 24-FEB-09 1CQJ 1 VERSN
REVDAT 2 01-APR-03 1CQJ 1 JRNL
REVDAT 1 10-JAN-00 1CQJ 0
JRNL AUTH M.A.JOYCE,M.E.FRASER,M.N.JAMES,W.A.BRIDGER,W.T.WOLODKO
JRNL TITL ADP-BINDING SITE OF ESCHERICHIA COLI SUCCINYL-COA SYNTHETASE
JRNL TITL 2 REVEALED BY X-RAY CRYSTALLOGRAPHY.
JRNL REF BIOCHEMISTRY V. 39 17 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10625475
JRNL DOI 10.1021/BI991696F
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER,W.T.WOLODKO
REMARK 1 TITL A DETAILED STRUCTURAL DESCRIPTION OF ESCHERICHIA COLI
REMARK 1 TITL 2 SUCCINYL-COA SYNTHETASE
REMARK 1 REF J.MOL.BIOL. V. 285 1633 1999
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1998.2324
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.T.WOLODKO,M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER
REMARK 1 TITL THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM
REMARK 1 TITL 2 ESCHERICHIA COLI AT 2.5A RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 269 10883 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 3
REMARK 1 AUTH W.T.WOLODKO,M.N.G.JAMES,W.A.BRIDGER
REMARK 1 TITL CRYSTALLIZATION OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA
REMARK 1 TITL 2 COLI
REMARK 1 REF J.BIOL.CHEM. V. 259 5316 1984
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 45002
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 11.400
REMARK 3 FREE R VALUE TEST SET COUNT : 5121
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9892
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 133
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.40
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 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD REFINEMENT IN CNS
REMARK 4
REMARK 4 1CQJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009488.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-93
REMARK 200 TEMPERATURE (KELVIN) : 283
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 6
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : FUJI
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : WEIS
REMARK 200 DATA SCALING SOFTWARE : SCALKB2, KBAPLY
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45002
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.09200
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) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.35000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: BIOMOL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, POTASSIUM PHOSPHATE,
REMARK 280 COENZYME A, PH 7.3, MICRODIALYSIS, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 202.34000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 303.51000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 101.17000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 202.34000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 101.17000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 303.51000
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: HETEROTETRAMER FORMED BY TWO ALPHA BETA-DIMERS RELATED BY A
REMARK 300 CRYSTALLOGRAPHIC TWO-FOLD AXIS.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E
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 OG1 THR D 128 OG1 THR D 173 2.16
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 CYS A 77 CB CYS A 77 SG -0.104
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 B 161 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU B 201 N - CA - C ANGL. DEV. = -16.7 DEGREES
REMARK 500 PRO D 124 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 LEU E 195 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 LEU E 201 N - CA - C ANGL. DEV. = -16.3 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
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 LEU A 3 -60.00 63.51
REMARK 500 HIS A 23 -9.21 -58.46
REMARK 500 THR A 96 130.27 -32.27
REMARK 500 TYR A 167 11.60 -68.12
REMARK 500 ASN A 186 -163.10 -111.19
REMARK 500 SER A 212 27.28 -143.01
REMARK 500 MET A 244 77.38 -101.34
REMARK 500 ASP A 278 40.02 -96.74
REMARK 500 TYR B 84 1.17 -63.50
REMARK 500 ASP B 87 -153.98 -70.29
REMARK 500 HIS B 279 37.99 -93.13
REMARK 500 ALA B 293 66.71 -66.86
REMARK 500 LEU B 366 173.79 -59.61
REMARK 500 ASN B 367 38.77 -83.01
REMARK 500 LYS B 372 79.70 -102.20
REMARK 500 ALA B 384 -7.10 -45.27
REMARK 500 LEU D 3 -56.22 58.19
REMARK 500 HIS D 23 -6.28 -59.02
REMARK 500 THR D 96 130.70 -31.10
REMARK 500 TYR D 167 10.34 -67.26
REMARK 500 SER D 172 -72.64 -71.21
REMARK 500 ASN D 186 -159.78 -105.36
REMARK 500 GLN D 199 -9.43 -54.69
REMARK 500 SER D 212 24.90 -144.15
REMARK 500 MET D 244 74.28 -103.02
REMARK 500 ASP D 278 41.19 -94.28
REMARK 500 THR D 285 30.92 -82.13
REMARK 500 TYR E 84 0.18 -65.49
REMARK 500 ASP E 87 -156.17 -70.71
REMARK 500 LEU E 255 -168.99 -129.88
REMARK 500 HIS E 279 39.81 -92.47
REMARK 500 ALA E 293 69.93 -65.90
REMARK 500 ALA E 384 -4.96 -44.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 COA B 903
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 903
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2SCU RELATED DB: PDB
REMARK 900 PHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE
REMARK 900 RELATED ID: 1CQI RELATED DB: PDB
REMARK 900 COMPLEX OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE, ADP
REMARK 900 AND MG2+
DBREF 1CQJ A 1 286 UNP P07459 SUCD_ECOLI 2 287
DBREF 1CQJ D 1 286 UNP P07459 SUCD_ECOLI 2 287
DBREF 1CQJ B 1 385 UNP P07460 SUCC_ECOLI 1 385
DBREF 1CQJ E 1 385 UNP P07460 SUCC_ECOLI 1 385
SEQRES 1 A 286 SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN
SEQRES 2 A 286 GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN
SEQRES 3 A 286 ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR
SEQRES 4 A 286 PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL
SEQRES 5 A 286 PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA
SEQRES 6 A 286 THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS
SEQRES 7 A 286 ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU
SEQRES 8 A 286 ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET
SEQRES 9 A 286 LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG
SEQRES 10 A 286 MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY
SEQRES 11 A 286 GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS
SEQRES 12 A 286 PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU
SEQRES 13 A 286 THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE
SEQRES 14 A 286 GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE
SEQRES 15 A 286 PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU
SEQRES 16 A 286 LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU
SEQRES 17 A 286 ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE
SEQRES 18 A 286 LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA
SEQRES 19 A 286 GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY HIS ALA
SEQRES 20 A 286 GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU
SEQRES 21 A 286 LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL
SEQRES 22 A 286 ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL
SEQRES 1 B 385 MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA
SEQRES 2 B 385 ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR
SEQRES 3 B 385 THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY
SEQRES 4 B 385 ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY
SEQRES 5 B 385 GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER
SEQRES 6 B 385 LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY
SEQRES 7 B 385 LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN
SEQRES 8 B 385 PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE
SEQRES 9 B 385 ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER
SEQRES 10 B 385 SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY
SEQRES 11 B 385 VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU
SEQRES 12 B 385 ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET
SEQRES 13 B 385 PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU
SEQRES 14 B 385 GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET
SEQRES 15 B 385 GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU
SEQRES 16 B 385 ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP
SEQRES 17 B 385 LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN
SEQRES 18 B 385 ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP
SEQRES 19 B 385 GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN
SEQRES 20 B 385 TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY
SEQRES 21 B 385 CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET
SEQRES 22 B 385 ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE
SEQRES 23 B 385 LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR
SEQRES 24 B 385 GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS
SEQRES 25 B 385 ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS
SEQRES 26 B 385 ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU
SEQRES 27 B 385 VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY
SEQRES 28 B 385 ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER
SEQRES 29 B 385 GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA
SEQRES 30 B 385 ALA GLN GLN VAL VAL ALA ALA VAL
SEQRES 1 D 286 SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN
SEQRES 2 D 286 GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN
SEQRES 3 D 286 ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR
SEQRES 4 D 286 PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL
SEQRES 5 D 286 PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA
SEQRES 6 D 286 THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS
SEQRES 7 D 286 ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU
SEQRES 8 D 286 ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET
SEQRES 9 D 286 LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG
SEQRES 10 D 286 MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY
SEQRES 11 D 286 GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS
SEQRES 12 D 286 PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU
SEQRES 13 D 286 THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE
SEQRES 14 D 286 GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE
SEQRES 15 D 286 PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU
SEQRES 16 D 286 LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU
SEQRES 17 D 286 ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE
SEQRES 18 D 286 LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA
SEQRES 19 D 286 GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY HIS ALA
SEQRES 20 D 286 GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU
SEQRES 21 D 286 LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL
SEQRES 22 D 286 ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL
SEQRES 1 E 385 MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA
SEQRES 2 E 385 ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR
SEQRES 3 E 385 THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY
SEQRES 4 E 385 ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY
SEQRES 5 E 385 GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER
SEQRES 6 E 385 LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY
SEQRES 7 E 385 LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN
SEQRES 8 E 385 PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE
SEQRES 9 E 385 ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER
SEQRES 10 E 385 SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY
SEQRES 11 E 385 VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU
SEQRES 12 E 385 ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET
SEQRES 13 E 385 PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU
SEQRES 14 E 385 GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET
SEQRES 15 E 385 GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU
SEQRES 16 E 385 ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP
SEQRES 17 E 385 LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN
SEQRES 18 E 385 ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP
SEQRES 19 E 385 GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN
SEQRES 20 E 385 TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY
SEQRES 21 E 385 CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET
SEQRES 22 E 385 ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE
SEQRES 23 E 385 LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR
SEQRES 24 E 385 GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS
SEQRES 25 E 385 ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS
SEQRES 26 E 385 ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU
SEQRES 27 E 385 VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY
SEQRES 28 E 385 ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER
SEQRES 29 E 385 GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA
SEQRES 30 E 385 ALA GLN GLN VAL VAL ALA ALA VAL
HET PO4 A 906 5
HET COA A 901 48
HET PO4 B 904 5
HET COA B 903 17
HET PO4 D 907 5
HET COA D 902 48
HET PO4 E 905 5
HETNAM PO4 PHOSPHATE ION
HETNAM COA COENZYME A
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 6 COA 3(C21 H36 N7 O16 P3 S)
FORMUL 12 HOH *330(H2 O)
HELIX 1 1 GLY A 17 GLY A 31 1 15
HELIX 2 2 THR A 55 GLY A 64 1 10
HELIX 3 3 PRO A 73 ALA A 87 1 15
HELIX 4 4 PRO A 100 ALA A 114 1 15
HELIX 5 5 PRO A 138 HIS A 142 5 5
HELIX 6 6 SER A 153 TYR A 167 1 15
HELIX 7 7 ASN A 186 LYS A 196 1 11
HELIX 8 8 SER A 212 VAL A 225 1 14
HELIX 9 9 THR A 257 ALA A 268 1 12
HELIX 10 10 SER A 275 ALA A 277 5 3
HELIX 11 11 ASP A 278 LYS A 284 1 7
HELIX 12 12 HIS B 4 TYR B 15 1 12
HELIX 13 13 THR B 27 GLY B 39 1 13
HELIX 14 14 SER B 65 LEU B 77 1 13
HELIX 15 15 GLU B 132 THR B 140 1 9
HELIX 16 16 MET B 156 LEU B 167 1 12
HELIX 17 17 GLY B 171 ARG B 191 1 21
HELIX 18 18 GLY B 220 ARG B 225 5 6
HELIX 19 19 GLN B 226 MET B 232 1 7
HELIX 20 20 ASP B 234 GLU B 238 5 5
HELIX 21 21 ASP B 239 TRP B 248 1 10
HELIX 22 22 GLY B 265 HIS B 279 1 15
HELIX 23 23 THR B 294 LEU B 306 1 13
HELIX 24 24 ARG B 324 GLY B 340 1 17
HELIX 25 25 ASN B 353 SER B 364 1 12
HELIX 26 26 GLY B 373 VAL B 385 1 13
HELIX 27 27 GLY D 17 TYR D 30 1 14
HELIX 28 28 THR D 55 GLY D 64 1 10
HELIX 29 29 PRO D 73 ALA D 87 1 15
HELIX 30 30 PRO D 100 ALA D 114 1 15
HELIX 31 31 PRO D 138 HIS D 142 5 5
HELIX 32 32 SER D 153 TYR D 167 1 15
HELIX 33 33 ASN D 186 LYS D 196 1 11
HELIX 34 34 SER D 212 VAL D 225 1 14
HELIX 35 35 THR D 257 ALA D 268 1 12
HELIX 36 36 SER D 275 ALA D 277 5 3
HELIX 37 37 ASP D 278 LYS D 284 1 7
HELIX 38 38 HIS E 4 TYR E 15 1 12
HELIX 39 39 THR E 27 GLY E 39 1 13
HELIX 40 40 SER E 65 LEU E 77 1 13
HELIX 41 41 GLU E 132 THR E 140 1 9
HELIX 42 42 MET E 156 LEU E 167 1 12
HELIX 43 43 GLY E 171 ARG E 191 1 21
HELIX 44 44 GLY E 220 ARG E 225 5 6
HELIX 45 45 GLN E 226 ARG E 233 1 8
HELIX 46 46 ASP E 234 GLU E 238 5 5
HELIX 47 47 ASP E 239 GLN E 247 1 9
HELIX 48 48 GLY E 265 HIS E 279 1 15
HELIX 49 49 THR E 294 LEU E 306 1 13
HELIX 50 50 ARG E 324 GLY E 340 1 17
HELIX 51 51 ASN E 353 SER E 364 1 12
HELIX 52 52 GLY E 373 ALA E 384 1 12
SHEET 1 A 7 THR A 45 HIS A 47 0
SHEET 2 A 7 LEU A 50 PHE A 53 -1 N LEU A 50 O HIS A 47
SHEET 3 A 7 LYS A 33 VAL A 38 1 O GLY A 37 N PHE A 53
SHEET 4 A 7 LYS A 9 GLN A 13 1 O VAL A 10 N VAL A 35
SHEET 5 A 7 ALA A 67 ILE A 70 1 O ALA A 67 N ILE A 11
SHEET 6 A 7 LEU A 91 THR A 94 1 O LEU A 91 N SER A 68
SHEET 7 A 7 ARG A 117 ILE A 119 1 O ARG A 117 N ILE A 92
SHEET 1 B 7 CYS A 132 GLY A 135 0
SHEET 2 B 7 GLY A 125 THR A 128 -1 N VAL A 126 O ILE A 134
SHEET 3 B 7 GLN A 171 GLY A 176 -1 N CYS A 174 O ILE A 127
SHEET 4 B 7 VAL A 147 SER A 151 1 O VAL A 147 N SER A 172
SHEET 5 B 7 ALA A 202 GLU A 208 1 O ALA A 202 N GLY A 148
SHEET 6 B 7 VAL A 229 ALA A 234 1 N VAL A 230 O ILE A 203
SHEET 7 B 7 LYS A 271 THR A 272 1 N LYS A 271 O VAL A 229
SHEET 1 C 4 GLY B 22 CYS B 25 0
SHEET 2 C 4 ILE B 96 ALA B 100 -1 O ILE B 96 N CYS B 25
SHEET 3 C 4 TRP B 43 CYS B 47 -1 N VAL B 44 O GLU B 99
SHEET 4 C 4 VAL B 60 VAL B 63 -1 O LYS B 61 N VAL B 45
SHEET 1 D 2 ARG B 80 LEU B 81 0
SHEET 2 D 2 GLN B 91 PRO B 92 -1 O GLN B 91 N LEU B 81
SHEET 1 E 5 ILE B 144 ALA B 148 0
SHEET 2 E 5 ARG B 120 SER B 126 -1 N PHE B 123 O VAL B 147
SHEET 3 E 5 ILE B 104 ASP B 115 -1 N TYR B 109 O SER B 126
SHEET 4 E 5 LEU B 193 THR B 204 -1 O ALA B 194 N VAL B 114
SHEET 5 E 5 LEU B 209 CYS B 211 -1 O ILE B 210 N VAL B 202
SHEET 1 E1 5 ILE B 144 ALA B 148 0
SHEET 2 E1 5 ARG B 120 SER B 126 -1 N PHE B 123 O VAL B 147
SHEET 3 E1 5 ILE B 104 ASP B 115 -1 N TYR B 109 O SER B 126
SHEET 4 E1 5 LEU B 193 THR B 204 -1 O ALA B 194 N VAL B 114
SHEET 5 E1 5 LYS B 215 ALA B 218 -1 O LYS B 215 N GLU B 197
SHEET 1 F 2 LEU B 250 ALA B 254 0
SHEET 2 F 2 ASN B 285 VAL B 289 -1 N PHE B 286 O VAL B 253
SHEET 1 G 4 ILE B 259 VAL B 263 0
SHEET 2 G 4 ALA B 313 PHE B 319 1 O ALA B 313 N GLY B 260
SHEET 3 G 4 VAL B 345 GLU B 350 1 O VAL B 346 N VAL B 316
SHEET 4 G 4 ILE B 368 ALA B 370 1 N ILE B 369 O VAL B 345
SHEET 1 H 7 THR D 45 HIS D 47 0
SHEET 2 H 7 LEU D 50 PHE D 53 -1 N LEU D 50 O HIS D 47
SHEET 3 H 7 LYS D 33 VAL D 38 1 O GLY D 37 N PHE D 53
SHEET 4 H 7 LYS D 9 GLN D 13 1 N VAL D 10 O LYS D 33
SHEET 5 H 7 ALA D 67 ILE D 70 1 O ALA D 67 N ILE D 11
SHEET 6 H 7 LEU D 91 THR D 94 1 O LEU D 91 N SER D 68
SHEET 7 H 7 ARG D 117 ILE D 119 1 O ARG D 117 N ILE D 92
SHEET 1 I 7 CYS D 132 GLY D 135 0
SHEET 2 I 7 GLY D 125 THR D 128 -1 N VAL D 126 O ILE D 134
SHEET 3 I 7 GLN D 171 GLY D 176 -1 N CYS D 174 O ILE D 127
SHEET 4 I 7 VAL D 147 SER D 151 1 O VAL D 147 N SER D 172
SHEET 5 I 7 ALA D 202 GLU D 208 1 O ALA D 202 N GLY D 148
SHEET 6 I 7 VAL D 229 ALA D 234 1 N VAL D 230 O ILE D 203
SHEET 7 I 7 LYS D 271 THR D 272 1 N LYS D 271 O VAL D 229
SHEET 1 J 4 GLY E 22 CYS E 25 0
SHEET 2 J 4 ILE E 96 ALA E 100 -1 O ILE E 96 N CYS E 25
SHEET 3 J 4 TRP E 43 CYS E 47 -1 N VAL E 44 O GLU E 99
SHEET 4 J 4 VAL E 60 VAL E 63 -1 O LYS E 61 N VAL E 45
SHEET 1 K 2 ARG E 80 LEU E 81 0
SHEET 2 K 2 GLN E 91 PRO E 92 -1 O GLN E 91 N LEU E 81
SHEET 1 L 5 ILE E 144 ALA E 148 0
SHEET 2 L 5 ARG E 120 SER E 126 -1 N PHE E 123 O VAL E 147
SHEET 3 L 5 ILE E 104 ASP E 115 -1 N TYR E 109 O SER E 126
SHEET 4 L 5 LEU E 193 THR E 204 -1 O ALA E 194 N VAL E 114
SHEET 5 L 5 LEU E 209 CYS E 211 -1 O ILE E 210 N VAL E 202
SHEET 1 L1 5 ILE E 144 ALA E 148 0
SHEET 2 L1 5 ARG E 120 SER E 126 -1 N PHE E 123 O VAL E 147
SHEET 3 L1 5 ILE E 104 ASP E 115 -1 N TYR E 109 O SER E 126
SHEET 4 L1 5 LEU E 193 THR E 204 -1 O ALA E 194 N VAL E 114
SHEET 5 L1 5 LYS E 215 ALA E 218 -1 O LYS E 215 N GLU E 197
SHEET 1 M 2 LEU E 250 ALA E 254 0
SHEET 2 M 2 ASN E 285 VAL E 289 -1 N PHE E 286 O VAL E 253
SHEET 1 N 4 ILE E 259 VAL E 263 0
SHEET 2 N 4 ALA E 313 PHE E 319 1 O ALA E 313 N GLY E 260
SHEET 3 N 4 VAL E 345 GLU E 350 1 O VAL E 346 N VAL E 316
SHEET 4 N 4 ILE E 368 ALA E 370 1 O ILE E 369 N VAL E 347
LINK SG CYS B 325 S1P COA B 903 1555 1555 2.03
CISPEP 1 GLY A 120 PRO A 121 0 0.04
CISPEP 2 GLY B 41 PRO B 42 0 -0.22
CISPEP 3 ASN B 199 PRO B 200 0 1.03
CISPEP 4 GLY D 120 PRO D 121 0 0.09
CISPEP 5 GLY E 41 PRO E 42 0 -0.44
CISPEP 6 ASN E 199 PRO E 200 0 0.97
SITE 1 AC1 6 GLY B 52 GLY B 53 ARG B 54 GLY B 55
SITE 2 AC1 6 LYS B 56 ASP B 213
SITE 1 AC2 7 GLY E 53 ARG E 54 GLY E 55 LYS E 56
SITE 2 AC2 7 ASP E 213 HOH E 936 HOH E 973
SITE 1 AC3 8 SER A 153 GLY A 154 THR A 155 HIS A 246
SITE 2 AC3 8 HOH A 962 GLY B 265 ALA B 266 GLY B 267
SITE 1 AC4 7 SER D 153 GLY D 154 THR D 155 HIS D 246
SITE 2 AC4 7 GLY E 265 ALA E 266 GLY E 267
SITE 1 AC5 29 GLY A 14 THR A 16 GLY A 17 SER A 18
SITE 2 AC5 29 GLN A 19 VAL A 38 PRO A 40 LYS A 42
SITE 3 AC5 29 TYR A 71 VAL A 72 PRO A 73 SER A 80
SITE 4 AC5 29 ILE A 95 THR A 96 GLU A 97 ASN A 122
SITE 5 AC5 29 CYS A 123 PRO A 124 ILE A 136 HOH A 911
SITE 6 AC5 29 HOH A 912 HOH A 913 HOH A 927 HOH A 968
SITE 7 AC5 29 ARG E 29 GLU E 33 SER E 36 LYS E 66
SITE 8 AC5 29 HOH E 991
SITE 1 AC6 26 GLU B 33 SER B 36 LYS B 66 GLY D 14
SITE 2 AC6 26 THR D 16 GLY D 17 SER D 18 GLN D 19
SITE 3 AC6 26 VAL D 38 PRO D 40 LYS D 42 TYR D 71
SITE 4 AC6 26 VAL D 72 PRO D 73 ILE D 95 THR D 96
SITE 5 AC6 26 GLU D 97 ASN D 122 CYS D 123 PRO D 124
SITE 6 AC6 26 ILE D 136 HOH D 909 HOH D 910 HOH D 923
SITE 7 AC6 26 HOH D 964 HOH D 967
SITE 1 AC7 8 GLY B 320 GLY B 321 VAL B 323 CYS B 325
SITE 2 AC7 8 GLU B 350 ASN B 352 HOH B 905 HOH B1013
CRYST1 98.820 98.820 404.680 90.00 90.00 90.00 P 43 2 2 16
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 0.010119 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002471 0.00000
(ATOM LINES ARE NOT SHOWN.)
END