HEADER LIGASE (ATP-BINDING) 18-NOV-93 1SCU
TITLE THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM ESCHERICHIA COLI
TITLE 2 AT 2.5 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINYL-COA SYNTHETASE, ALPHA SUBUNIT;
COMPND 3 CHAIN: A, D;
COMPND 4 EC: 6.2.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SUCCINYL-COA SYNTHETASE, BETA SUBUNIT;
COMPND 8 CHAIN: B, E;
COMPND 9 EC: 6.2.1.5;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 6 ORGANISM_TAXID: 562
KEYWDS LIGASE (ATP-BINDING)
EXPDTA X-RAY DIFFRACTION
AUTHOR W.T.WOLODKO,M.E.FRASER,M.N.G.JAMES,W.A.BRIDGER
REVDAT 6 14-AUG-19 1SCU 1 REMARK
REVDAT 5 17-JUL-19 1SCU 1 REMARK LINK
REVDAT 4 21-APR-09 1SCU 1 MODRES
REVDAT 3 24-FEB-09 1SCU 1 VERSN
REVDAT 2 01-APR-03 1SCU 1 JRNL
REVDAT 1 20-APR-95 1SCU 0
JRNL AUTH W.T.WOLODKO,M.E.FRASER,M.N.JAMES,W.A.BRIDGER
JRNL TITL THE CRYSTAL STRUCTURE OF SUCCINYL-COA SYNTHETASE FROM
JRNL TITL 2 ESCHERICHIA COLI AT 2.5-A RESOLUTION.
JRNL REF J.BIOL.CHEM. V. 269 10883 1994
JRNL REFN ISSN 0021-9258
JRNL PMID 8144675
REMARK 1
REMARK 1 REFERENCE 1
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. 249 5316 1984
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 67272
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9982
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SCU 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_1000176326.
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: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 200.30000
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 300.45000
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 100.15000
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 200.30000
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 100.15000
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 300.45000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 CA LEU B 189 O HOH B 408 1.27
REMARK 500 OD1 ASP B 87 N ALA B 88 1.38
REMARK 500 CA TRP B 248 O HOH B 418 1.43
REMARK 500 O HOH B 402 O HOH B 403 1.47
REMARK 500 C LEU B 189 O HOH B 408 1.54
REMARK 500 O LYS D 284 CG LYS D 288 1.59
REMARK 500 CG2 THR D 237 OD1 ASP E 274 1.65
REMARK 500 C TRP B 248 O HOH B 418 1.67
REMARK 500 N MET D 118 O HOH D 300 1.68
REMARK 500 OE1 GLU A 97 N GLY A 98 1.69
REMARK 500 N LEU B 189 O HOH B 408 1.69
REMARK 500 O HOH E 397 O HOH E 418 1.71
REMARK 500 O PRO B 42 O HOH B 390 1.78
REMARK 500 OE1 GLU D 97 N GLY D 98 1.79
REMARK 500 O ASP E 87 N ASN E 89 1.82
REMARK 500 CB MET B 270 O HOH B 419 1.88
REMARK 500 O ILE D 2 O HOH D 293 1.90
REMARK 500 C PHE B 188 O HOH B 408 1.90
REMARK 500 O ILE B 304 OG SER B 307 1.91
REMARK 500 O PHE B 188 O HOH B 408 1.93
REMARK 500 O LYS D 284 CD LYS D 288 1.93
REMARK 500 O ILE D 203 CG2 VAL D 229 1.95
REMARK 500 C ILE D 2 O HOH D 293 1.96
REMARK 500 OD1 ASP D 259 NH2 ARG D 274 2.00
REMARK 500 O GLY D 139 N ILE D 141 2.01
REMARK 500 OD2 ASP B 274 O HOH B 420 2.03
REMARK 500 O ASP E 150 O THR E 153 2.04
REMARK 500 CG ASP E 115 O HOH E 395 2.05
REMARK 500 O ASP E 326 N ILE E 328 2.05
REMARK 500 O ALA E 383 N GLU E 386 2.07
REMARK 500 O LEU B 223 NH1 ARG B 230 2.08
REMARK 500 O THR B 140 N LEU B 143 2.10
REMARK 500 O GLN A 163 N THR A 165 2.10
REMARK 500 CA MET B 270 O HOH B 419 2.13
REMARK 500 OE1 GLN D 163 O ALA D 277 2.13
REMARK 500 O LEU B 189 O HOH B 408 2.13
REMARK 500 O GLU D 266 N GLY D 269 2.13
REMARK 500 CB TRP B 248 O HOH B 418 2.14
REMARK 500 O ALA B 222 N ARG B 225 2.14
REMARK 500 O THR D 165 N GLY D 168 2.14
REMARK 500 O ASP A 197 NZ LYS A 227 2.15
REMARK 500 O SER A 212 OE1 GLU A 215 2.15
REMARK 500 OD1 ASP A 5 N ASN A 7 2.15
REMARK 500 O ILE D 203 N VAL D 230 2.15
REMARK 500 OE2 GLU B 249 NH2 ARG E 70 2.17
REMARK 500 O ALA E 246 N TRP E 248 2.17
REMARK 500 OD1 ASP B 150 N LEU B 152 2.18
REMARK 500 OD1 ASP E 239 N ARG E 241 2.18
REMARK 500 O ALA E 246 N GLU E 249 2.18
REMARK 500 OD1 ASP B 326 ND2 ASN B 353 2.19
REMARK 500
REMARK 500 THIS ENTRY HAS 51 CLOSE CONTACTS
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 GLU A 25 CD GLU A 25 OE2 0.077
REMARK 500 GLU A 58 CD GLU A 58 OE2 0.074
REMARK 500 GLU A 97 CD GLU A 97 OE2 0.086
REMARK 500 GLU A 113 CD GLU A 113 OE2 0.074
REMARK 500 GLU A 131 CD GLU A 131 OE2 0.066
REMARK 500 GLU A 159 CD GLU A 159 OE2 0.074
REMARK 500 GLU A 201 CD GLU A 201 OE1 0.069
REMARK 500 GLU A 214 CD GLU A 214 OE2 0.084
REMARK 500 GLU A 215 CD GLU A 215 OE2 0.069
REMARK 500 GLU A 216 CD GLU A 216 OE2 0.069
REMARK 500 GLU A 223 CD GLU A 223 OE1 0.090
REMARK 500 GLU A 260 CD GLU A 260 OE2 0.068
REMARK 500 GLU A 266 CD GLU A 266 OE2 0.083
REMARK 500 GLU A 281 CD GLU A 281 OE2 0.068
REMARK 500 GLU B 5 CD GLU B 5 OE2 0.083
REMARK 500 GLU B 32 CD GLU B 32 OE2 0.087
REMARK 500 GLU B 33 CD GLU B 33 OE2 0.068
REMARK 500 GLU B 74 CD GLU B 74 OE2 0.079
REMARK 500 GLU B 128 CD GLU B 128 OE1 0.072
REMARK 500 GLU B 132 CD GLU B 132 OE2 0.074
REMARK 500 GLU B 134 CD GLU B 134 OE2 0.069
REMARK 500 GLU B 138 CD GLU B 138 OE2 0.070
REMARK 500 GLU B 139 CD GLU B 139 OE2 0.075
REMARK 500 GLU B 162 CD GLU B 162 OE2 0.114
REMARK 500 GLU B 170 CD GLU B 170 OE2 0.076
REMARK 500 GLU B 190 CD GLU B 190 OE2 0.068
REMARK 500 GLU B 197 CD GLU B 197 OE2 0.082
REMARK 500 GLU B 231 CD GLU B 231 OE2 0.075
REMARK 500 GLU B 238 CD GLU B 238 OE2 0.073
REMARK 500 GLU B 242 CD GLU B 242 OE2 0.079
REMARK 500 GLU B 249 CD GLU B 249 OE2 0.083
REMARK 500 GLU B 282 CD GLU B 282 OE2 0.073
REMARK 500 GLU B 296 CD GLU B 296 OE2 0.069
REMARK 500 GLU B 300 CD GLU B 300 OE2 0.078
REMARK 500 GLU B 338 CD GLU B 338 OE2 0.083
REMARK 500 GLU B 386 CD GLU B 386 OE1 0.067
REMARK 500 GLU D 25 CD GLU D 25 OE2 0.071
REMARK 500 GLU D 58 CD GLU D 58 OE2 0.106
REMARK 500 GLU D 97 CD GLU D 97 OE1 0.076
REMARK 500 GLU D 113 CD GLU D 113 OE2 0.073
REMARK 500 GLU D 131 CD GLU D 131 OE2 0.070
REMARK 500 GLU D 159 CD GLU D 159 OE2 0.078
REMARK 500 GLU D 192 CD GLU D 192 OE2 0.083
REMARK 500 GLU D 195 CD GLU D 195 OE2 0.071
REMARK 500 GLU D 208 CD GLU D 208 OE2 0.085
REMARK 500 GLU D 215 CD GLU D 215 OE2 0.079
REMARK 500 GLU D 216 CD GLU D 216 OE2 0.068
REMARK 500 GLU D 223 CD GLU D 223 OE2 0.069
REMARK 500 GLU D 260 CD GLU D 260 OE2 0.071
REMARK 500 GLU D 266 CD GLU D 266 OE2 0.085
REMARK 500
REMARK 500 THIS ENTRY HAS 71 BOND DEVIATIONS.
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 3 C - N - CA ANGL. DEV. = -16.9 DEGREES
REMARK 500 ASP A 5 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 HIS A 23 CA - CB - CG ANGL. DEV. = -13.9 DEGREES
REMARK 500 VAL A 56 CA - CB - CG1 ANGL. DEV. = -10.6 DEGREES
REMARK 500 VAL A 69 CB - CA - C ANGL. DEV. = -12.5 DEGREES
REMARK 500 VAL A 69 CA - CB - CG2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 CYS A 77 CA - CB - SG ANGL. DEV. = -13.6 DEGREES
REMARK 500 ASP A 79 CB - CG - OD1 ANGL. DEV. = 8.8 DEGREES
REMARK 500 ASP A 79 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 THR A 101 CA - CB - CG2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 GLN A 137 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 PRO A 138 C - N - CD ANGL. DEV. = -17.3 DEGREES
REMARK 500 VAL A 150 CB - CA - C ANGL. DEV. = -11.4 DEGREES
REMARK 500 ARG A 152 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 152 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ASP A 166 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 166 CB - CG - OD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 ASP A 180 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 PRO A 183 C - N - CD ANGL. DEV. = -25.8 DEGREES
REMARK 500 ASP A 189 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 VAL A 204 CA - CB - CG1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLY A 210 C - N - CA ANGL. DEV. = -12.9 DEGREES
REMARK 500 ALA A 213 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 ALA A 219 CB - CA - C ANGL. DEV. = -10.8 DEGREES
REMARK 500 PRO A 239 C - N - CD ANGL. DEV. = -12.8 DEGREES
REMARK 500 SER A 275 N - CA - CB ANGL. DEV. = 11.2 DEGREES
REMARK 500 ASP A 278 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 278 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG B 14 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP B 68 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 68 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 VAL B 113 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 ASP B 115 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 PRO B 141 C - N - CD ANGL. DEV. = -38.5 DEGREES
REMARK 500 ASP B 150 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 GLY B 154 C - N - CA ANGL. DEV. = -13.5 DEGREES
REMARK 500 PRO B 157 C - N - CD ANGL. DEV. = -12.9 DEGREES
REMARK 500 ARG B 191 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ILE B 196 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 ASP B 213 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP B 219 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 225 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG B 225 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 230 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 PRO B 240 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASP B 256 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP B 288 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 288 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG B 297 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 131 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 ILE A 2 -51.19 -128.73
REMARK 500 PHE A 22 -75.36 -36.37
REMARK 500 PRO A 40 124.94 -37.34
REMARK 500 LEU A 48 29.02 46.88
REMARK 500 ALA A 74 -67.17 -22.45
REMARK 500 LYS A 78 -39.97 -38.99
REMARK 500 THR A 96 141.27 -35.73
REMARK 500 PRO A 121 -165.36 -100.73
REMARK 500 GLN A 137 133.46 -31.82
REMARK 500 HIS A 140 3.16 -54.62
REMARK 500 LEU A 156 -57.54 -29.06
REMARK 500 ALA A 160 -74.02 -28.92
REMARK 500 VAL A 161 -71.35 -32.94
REMARK 500 LYS A 162 -64.62 -29.86
REMARK 500 GLN A 163 -91.66 -48.06
REMARK 500 THR A 164 -40.68 -21.57
REMARK 500 SER A 172 -73.50 -77.78
REMARK 500 PHE A 187 -73.57 -39.95
REMARK 500 ILE A 188 -71.80 -36.15
REMARK 500 ASP A 189 -45.98 -21.45
REMARK 500 ALA A 213 -76.16 5.61
REMARK 500 GLU A 214 -72.93 -44.72
REMARK 500 ALA A 218 -70.19 -28.28
REMARK 500 ALA A 219 -89.04 -25.20
REMARK 500 TYR A 220 -78.86 -27.28
REMARK 500 ILE A 221 -75.66 -20.54
REMARK 500 HIS A 224 -1.88 -157.56
REMARK 500 LYS A 227 160.13 -46.53
REMARK 500 ALA A 252 -135.44 -60.04
REMARK 500 GLU A 281 -85.54 -38.82
REMARK 500 ALA A 282 -46.10 -26.87
REMARK 500 LYS A 284 -57.70 -26.15
REMARK 500 THR A 285 -90.44 -55.05
REMARK 500 VAL A 286 -22.87 -36.70
REMARK 500 ASP B 87 -130.63 -66.24
REMARK 500 ALA B 105 -70.21 -80.50
REMARK 500 LEU B 108 -164.90 -101.87
REMARK 500 LYS B 135 -79.19 -66.89
REMARK 500 VAL B 136 -57.74 -21.06
REMARK 500 GLU B 139 -2.64 -144.04
REMARK 500 THR B 140 29.87 -140.71
REMARK 500 PRO B 141 -31.64 -24.32
REMARK 500 GLN B 206 -4.56 -53.39
REMARK 500 ASP B 234 73.06 -117.44
REMARK 500 GLU B 249 40.29 38.69
REMARK 500 LEU B 255 -156.96 -119.52
REMARK 500 HIS B 279 40.20 -80.59
REMARK 500 ASN B 285 166.26 174.65
REMARK 500 ALA B 293 61.50 -54.85
REMARK 500 ASP B 309 -5.04 -54.04
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 289
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA D 289
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AMINO-TERMINAL ANALYSIS OF THE ALPHA SUBUNIT INDICATES THAT
REMARK 999 THE FIRST RESIDUE IS A SERINE (W. A. BRIDGE, ENZYMES,
REMARK 999 3RD ED. 10, 581-606 (1974)). IN THE GENE SEQUENCING
REMARK 999 PAPER, BUCK, SPENCER AND GUEST STATE THAT "[THE
REMARK 999 ASSUMPTION IS] THAT THE INITIATING FORMYLMETHIONINE IS
REMARK 999 REMOVED POSTTRANSLATIONALLY FROM THE ALPHA BUT NOT FROM
REMARK 999 THE BETA SUBUNIT" (D. BUCK, M. E. SPENCER, AND J. R. GUEST,
REMARK 999 BIOCHEMISTRY 24, 6245-6252 (1985)).
DBREF 1SCU A 1 288 UNP P07459 SUCD_ECOLI 1 288
DBREF 1SCU B 1 388 UNP P0A836 SUCC_ECOLI 1 388
DBREF 1SCU D 1 288 UNP P07459 SUCD_ECOLI 1 288
DBREF 1SCU E 1 388 UNP P0A836 SUCC_ECOLI 1 388
SEQRES 1 A 288 SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN
SEQRES 2 A 288 GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN
SEQRES 3 A 288 ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR
SEQRES 4 A 288 PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL
SEQRES 5 A 288 PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA
SEQRES 6 A 288 THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS
SEQRES 7 A 288 ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU
SEQRES 8 A 288 ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET
SEQRES 9 A 288 LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG
SEQRES 10 A 288 MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY
SEQRES 11 A 288 GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS
SEQRES 12 A 288 PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU
SEQRES 13 A 288 THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE
SEQRES 14 A 288 GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE
SEQRES 15 A 288 PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU
SEQRES 16 A 288 LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU
SEQRES 17 A 288 ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE
SEQRES 18 A 288 LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA
SEQRES 19 A 288 GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY NEP ALA
SEQRES 20 A 288 GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU
SEQRES 21 A 288 LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL
SEQRES 22 A 288 ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL
SEQRES 23 A 288 LEU LYS
SEQRES 1 B 388 MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA
SEQRES 2 B 388 ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR
SEQRES 3 B 388 THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY
SEQRES 4 B 388 ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY
SEQRES 5 B 388 GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER
SEQRES 6 B 388 LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY
SEQRES 7 B 388 LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN
SEQRES 8 B 388 PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE
SEQRES 9 B 388 ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER
SEQRES 10 B 388 SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY
SEQRES 11 B 388 VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU
SEQRES 12 B 388 ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET
SEQRES 13 B 388 PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU
SEQRES 14 B 388 GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET
SEQRES 15 B 388 GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU
SEQRES 16 B 388 ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP
SEQRES 17 B 388 LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN
SEQRES 18 B 388 ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP
SEQRES 19 B 388 GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN
SEQRES 20 B 388 TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY
SEQRES 21 B 388 CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET
SEQRES 22 B 388 ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE
SEQRES 23 B 388 LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR
SEQRES 24 B 388 GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS
SEQRES 25 B 388 ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS
SEQRES 26 B 388 ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU
SEQRES 27 B 388 VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY
SEQRES 28 B 388 ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER
SEQRES 29 B 388 GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA
SEQRES 30 B 388 ALA GLN GLN VAL VAL ALA ALA VAL GLU GLY LYS
SEQRES 1 D 288 SER ILE LEU ILE ASP LYS ASN THR LYS VAL ILE CYS GLN
SEQRES 2 D 288 GLY PHE THR GLY SER GLN GLY THR PHE HIS SER GLU GLN
SEQRES 3 D 288 ALA ILE ALA TYR GLY THR LYS MET VAL GLY GLY VAL THR
SEQRES 4 D 288 PRO GLY LYS GLY GLY THR THR HIS LEU GLY LEU PRO VAL
SEQRES 5 D 288 PHE ASN THR VAL ARG GLU ALA VAL ALA ALA THR GLY ALA
SEQRES 6 D 288 THR ALA SER VAL ILE TYR VAL PRO ALA PRO PHE CYS LYS
SEQRES 7 D 288 ASP SER ILE LEU GLU ALA ILE ASP ALA GLY ILE LYS LEU
SEQRES 8 D 288 ILE ILE THR ILE THR GLU GLY ILE PRO THR LEU ASP MET
SEQRES 9 D 288 LEU THR VAL LYS VAL LYS LEU ASP GLU ALA GLY VAL ARG
SEQRES 10 D 288 MET ILE GLY PRO ASN CYS PRO GLY VAL ILE THR PRO GLY
SEQRES 11 D 288 GLU CYS LYS ILE GLY ILE GLN PRO GLY HIS ILE HIS LYS
SEQRES 12 D 288 PRO GLY LYS VAL GLY ILE VAL SER ARG SER GLY THR LEU
SEQRES 13 D 288 THR TYR GLU ALA VAL LYS GLN THR THR ASP TYR GLY PHE
SEQRES 14 D 288 GLY GLN SER THR CYS VAL GLY ILE GLY GLY ASP PRO ILE
SEQRES 15 D 288 PRO GLY SER ASN PHE ILE ASP ILE LEU GLU MET PHE GLU
SEQRES 16 D 288 LYS ASP PRO GLN THR GLU ALA ILE VAL MET ILE GLY GLU
SEQRES 17 D 288 ILE GLY GLY SER ALA GLU GLU GLU ALA ALA ALA TYR ILE
SEQRES 18 D 288 LYS GLU HIS VAL THR LYS PRO VAL VAL GLY TYR ILE ALA
SEQRES 19 D 288 GLY VAL THR ALA PRO LYS GLY LYS ARG MET GLY NEP ALA
SEQRES 20 D 288 GLY ALA ILE ILE ALA GLY GLY LYS GLY THR ALA ASP GLU
SEQRES 21 D 288 LYS PHE ALA ALA LEU GLU ALA ALA GLY VAL LYS THR VAL
SEQRES 22 D 288 ARG SER LEU ALA ASP ILE GLY GLU ALA LEU LYS THR VAL
SEQRES 23 D 288 LEU LYS
SEQRES 1 E 388 MET ASN LEU HIS GLU TYR GLN ALA LYS GLN LEU PHE ALA
SEQRES 2 E 388 ARG TYR GLY LEU PRO ALA PRO VAL GLY TYR ALA CYS THR
SEQRES 3 E 388 THR PRO ARG GLU ALA GLU GLU ALA ALA SER LYS ILE GLY
SEQRES 4 E 388 ALA GLY PRO TRP VAL VAL LYS CYS GLN VAL HIS ALA GLY
SEQRES 5 E 388 GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL ASN SER
SEQRES 6 E 388 LYS GLU ASP ILE ARG ALA PHE ALA GLU ASN TRP LEU GLY
SEQRES 7 E 388 LYS ARG LEU VAL THR TYR GLN THR ASP ALA ASN GLY GLN
SEQRES 8 E 388 PRO VAL ASN GLN ILE LEU VAL GLU ALA ALA THR ASP ILE
SEQRES 9 E 388 ALA LYS GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG SER
SEQRES 10 E 388 SER ARG ARG VAL VAL PHE MET ALA SER THR GLU GLY GLY
SEQRES 11 E 388 VAL GLU ILE GLU LYS VAL ALA GLU GLU THR PRO HIS LEU
SEQRES 12 E 388 ILE HIS LYS VAL ALA LEU ASP PRO LEU THR GLY PRO MET
SEQRES 13 E 388 PRO TYR GLN GLY ARG GLU LEU ALA PHE LYS LEU GLY LEU
SEQRES 14 E 388 GLU GLY LYS LEU VAL GLN GLN PHE THR LYS ILE PHE MET
SEQRES 15 E 388 GLY LEU ALA THR ILE PHE LEU GLU ARG ASP LEU ALA LEU
SEQRES 16 E 388 ILE GLU ILE ASN PRO LEU VAL ILE THR LYS GLN GLY ASP
SEQRES 17 E 388 LEU ILE CYS LEU ASP GLY LYS LEU GLY ALA ASP GLY ASN
SEQRES 18 E 388 ALA LEU PHE ARG GLN PRO ASP LEU ARG GLU MET ARG ASP
SEQRES 19 E 388 GLN SER GLN GLU ASP PRO ARG GLU ALA GLN ALA ALA GLN
SEQRES 20 E 388 TRP GLU LEU ASN TYR VAL ALA LEU ASP GLY ASN ILE GLY
SEQRES 21 E 388 CYS MET VAL ASN GLY ALA GLY LEU ALA MET GLY THR MET
SEQRES 22 E 388 ASP ILE VAL LYS LEU HIS GLY GLY GLU PRO ALA ASN PHE
SEQRES 23 E 388 LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL THR
SEQRES 24 E 388 GLU ALA PHE LYS ILE ILE LEU SER ASP ASP LYS VAL LYS
SEQRES 25 E 388 ALA VAL LEU VAL ASN ILE PHE GLY GLY ILE VAL ARG CYS
SEQRES 26 E 388 ASP LEU ILE ALA ASP GLY ILE ILE GLY ALA VAL ALA GLU
SEQRES 27 E 388 VAL GLY VAL ASN VAL PRO VAL VAL VAL ARG LEU GLU GLY
SEQRES 28 E 388 ASN ASN ALA GLU LEU GLY ALA LYS LYS LEU ALA ASP SER
SEQRES 29 E 388 GLY LEU ASN ILE ILE ALA ALA LYS GLY LEU THR ASP ALA
SEQRES 30 E 388 ALA GLN GLN VAL VAL ALA ALA VAL GLU GLY LYS
MODRES 1SCU NEP A 246 HIS N1-PHOSPHONOHISTIDINE
MODRES 1SCU NEP D 246 HIS N1-PHOSPHONOHISTIDINE
HET NEP A 246 14
HET NEP D 246 14
HET COA A 289 48
HET COA D 289 48
HETNAM NEP N1-PHOSPHONOHISTIDINE
HETNAM COA COENZYME A
FORMUL 1 NEP 2(C6 H10 N3 O5 P)
FORMUL 5 COA 2(C21 H36 N7 O16 P3 S)
FORMUL 7 HOH *110(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 GLY A 88 1 16
HELIX 4 4 PRO A 100 GLY A 115 1 16
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 ASP A 197 1 12
HELIX 8 8 SER A 212 GLU A 223 1 12
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 288 1 11
HELIX 12 12 HIS B 4 GLY B 16 1 13
HELIX 13 13 THR B 27 GLY B 39 1 13
HELIX 14 14 GLY B 53 GLY B 58 1 6
HELIX 15 15 SER B 65 LEU B 77 1 13
HELIX 16 16 GLU B 132 THR B 140 1 9
HELIX 17 17 PRO B 141 ILE B 144 5 4
HELIX 18 18 PRO B 157 GLY B 168 1 12
HELIX 19 19 GLY B 171 ARG B 191 1 21
HELIX 20 20 GLY B 220 ARG B 225 5 6
HELIX 21 21 GLN B 226 MET B 232 1 7
HELIX 22 22 ARG B 233 ARG B 233 5 1
HELIX 23 23 ASP B 234 GLU B 238 5 5
HELIX 24 24 ASP B 239 GLN B 247 1 9
HELIX 25 25 GLY B 265 HIS B 279 1 15
HELIX 26 26 THR B 294 ASP B 308 1 15
HELIX 27 27 ARG B 324 GLY B 340 1 17
HELIX 28 28 ASN B 353 SER B 364 1 12
HELIX 29 29 GLY B 373 LYS B 388 1 16
SHEET 1 A 7 THR A 46 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 O VAL A 230 N MET A 205
SHEET 7 B 7 LYS A 271 THR A 272 1 O LYS A 271 N GLY A 231
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 N GLN B 91 O LEU B 81
SHEET 1 E 5 HIS B 145 ALA B 148 0
SHEET 2 E 5 ARG B 120 SER B 126 -1 O PHE B 123 N 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 N ILE B 196 O ALA B 112
SHEET 5 E 5 LEU B 209 CYS B 211 -1 O ILE B 210 N VAL B 202
SHEET 1 F 5 HIS B 145 ALA B 148 0
SHEET 2 F 5 ARG B 120 SER B 126 -1 O PHE B 123 N VAL B 147
SHEET 3 F 5 ILE B 104 ASP B 115 -1 N TYR B 109 O SER B 126
SHEET 4 F 5 LEU B 193 THR B 204 -1 N ILE B 196 O ALA B 112
SHEET 5 F 5 LEU B 216 ALA B 218 -1 O GLY B 217 N ALA B 194
SHEET 1 G 2 LEU B 250 ALA B 254 0
SHEET 2 G 2 ASN B 285 VAL B 289 -1 N PHE B 286 O VAL B 253
SHEET 1 H 4 ILE B 259 VAL B 263 0
SHEET 2 H 4 ALA B 313 ASN B 317 1 O ALA B 313 N GLY B 260
SHEET 3 H 4 VAL B 345 ARG B 348 1 O VAL B 346 N VAL B 316
SHEET 4 H 4 ILE B 368 ALA B 370 1 N ILE B 369 O VAL B 345
LINK C GLY A 245 N NEP A 246 1555 1555 1.32
LINK C NEP A 246 N ALA A 247 1555 1555 1.29
LINK C GLY D 245 N NEP D 246 1555 1555 1.30
LINK C NEP D 246 N ALA D 247 1555 1555 1.27
CISPEP 1 GLY A 120 PRO A 121 0 6.20
CISPEP 2 GLY B 41 PRO B 42 0 -3.75
CISPEP 3 ASN B 199 PRO B 200 0 11.34
CISPEP 4 GLY D 120 PRO D 121 0 0.77
CISPEP 5 GLY E 41 PRO E 42 0 -5.29
CISPEP 6 ASN E 199 PRO E 200 0 5.04
SITE 1 AC1 26 GLY A 14 THR A 16 GLY A 17 SER A 18
SITE 2 AC1 26 GLN A 19 VAL A 38 THR A 39 PRO A 40
SITE 3 AC1 26 LYS A 42 TYR A 71 VAL A 72 PRO A 73
SITE 4 AC1 26 SER A 80 ILE A 95 THR A 96 GLU A 97
SITE 5 AC1 26 ASN A 122 CYS A 123 PRO A 124 HOH A 293
SITE 6 AC1 26 HOH A 294 ARG B 161 ARG E 29 GLU E 33
SITE 7 AC1 26 SER E 36 LYS E 66
SITE 1 AC2 22 GLU B 33 SER B 36 LYS B 66 GLY D 14
SITE 2 AC2 22 THR D 16 GLY D 17 SER D 18 GLN D 19
SITE 3 AC2 22 VAL D 38 PRO D 40 LYS D 42 TYR D 71
SITE 4 AC2 22 VAL D 72 PRO D 73 SER D 80 ILE D 95
SITE 5 AC2 22 THR D 96 GLU D 97 ASN D 122 CYS D 123
SITE 6 AC2 22 HOH D 298 HOH D 303
CRYST1 98.470 98.470 400.600 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 0.010155 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010155 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002496 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
