HEADER LIGASE 16-JAN-06 2FPI
TITLE CRYSTAL STRUCTURE OF PIG GTP-SPECIFIC SUCCINYL-COA SYNTHETASE FROM
TITLE 2 POLYETHYLENE GLYCOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINYL-COA LIGASE [GDP-FORMING] ALPHA-CHAIN,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: SUCCINYL-COA SYNTHETASE, ALPHA CHAIN, SCS-ALPHA;
COMPND 6 EC: 6.2.1.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SUCCINYL-COA LIGASE [GDP-FORMING] BETA-CHAIN,
COMPND 10 MITOCHONDRIAL;
COMPND 11 CHAIN: B;
COMPND 12 SYNONYM: SUCCINYL-COA SYNTHETASE, BETAG CHAIN, SCS-BETAG, GTP-
COMPND 13 SPECIFIC SUCCINYL-COA SYNTHETASE BETA SUBUNIT, FRAGMENT;
COMPND 14 EC: 6.2.1.4;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: SUCLG1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7-7;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 13 ORGANISM_COMMON: PIG;
SOURCE 14 ORGANISM_TAXID: 9823;
SOURCE 15 GENE: SUCLG2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PT7-7
KEYWDS ACTIVE SITE PHOSPHOHISTIDINE RESIDUE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.FRASER
REVDAT 4 18-OCT-17 2FPI 1 REMARK
REVDAT 3 24-FEB-09 2FPI 1 VERSN
REVDAT 2 02-MAY-06 2FPI 1 JRNL
REVDAT 1 21-FEB-06 2FPI 0
JRNL AUTH M.E.FRASER,K.HAYAKAWA,M.S.HUME,D.G.RYAN,E.R.BROWNIE
JRNL TITL INTERACTIONS OF GTP WITH THE ATP-GRASP DOMAIN OF
JRNL TITL 2 GTP-SPECIFIC SUCCINYL-COA SYNTHETASE
JRNL REF J.BIOL.CHEM. V. 281 11058 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16481318
JRNL DOI 10.1074/JBC.M511785200
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
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) (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 22397
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.310
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1123
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 : 22
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 977
REMARK 3 BIN R VALUE (WORKING SET) : 0.3450
REMARK 3 BIN FREE R VALUE : 0.4810
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 71
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 : 5225
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12200
REMARK 3 B22 (A**2) : -0.12200
REMARK 3 B33 (A**2) : 0.24400
REMARK 3 B12 (A**2) : -10.89600
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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) : 2.000
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : 28.17
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 : PROTEIN_NEP_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FPI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : GE 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: P4K, ISOPROPANOL, AMMONIUM SULFATE AND
REMARK 280 BICINE, PH 8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.43333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.71667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 38.57500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 12.85833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 64.29167
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 LYS B 394
REMARK 465 LYS B 395
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 OH TYR B 116 OE2 GLU B 204 2.17
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 PRO A 237 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
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 ALA A 5 -1.38 -59.41
REMARK 500 LYS A 26 -18.37 -49.25
REMARK 500 ASN A 41 48.47 -71.94
REMARK 500 THR A 47 91.17 174.96
REMARK 500 GLU A 66 -86.87 -62.24
REMARK 500 ALA A 67 -25.59 -31.10
REMARK 500 LYS A 68 -73.48 -63.87
REMARK 500 GLU A 69 -75.85 -43.43
REMARK 500 ALA A 73 148.48 -8.05
REMARK 500 PRO A 81 154.87 -45.79
REMARK 500 ALA A 85 -37.79 -36.48
REMARK 500 ALA A 95 22.39 -70.46
REMARK 500 LEU A 119 -29.72 -38.09
REMARK 500 HIS A 149 -11.16 -48.66
REMARK 500 ASP A 195 -166.76 -114.53
REMARK 500 PRO A 237 -25.00 -33.35
REMARK 500 LEU B 38 -75.77 -62.36
REMARK 500 ASN B 39 86.47 94.70
REMARK 500 LYS B 91 -1.14 -54.86
REMARK 500 ALA B 108 177.32 -53.37
REMARK 500 ASN B 126 106.82 56.64
REMARK 500 GLN B 135 61.74 -102.25
REMARK 500 ASP B 139 94.03 -63.47
REMARK 500 ILE B 140 -46.74 -18.29
REMARK 500 ALA B 144 -39.13 -34.71
REMARK 500 ASN B 206 107.04 -160.15
REMARK 500 GLU B 213 5.68 -69.25
REMARK 500 GLN B 233 42.31 -147.51
REMARK 500 ASP B 256 1.38 57.25
REMARK 500 LYS B 301 121.90 -175.77
REMARK 500 GLU B 302 -39.14 -33.19
REMARK 500 ALA B 314 -86.41 -48.99
REMARK 500 ASP B 315 98.19 -39.52
REMARK 500 PRO B 316 30.65 -83.50
REMARK 500 VAL B 330 152.26 151.15
REMARK 500 CYS B 332 -8.78 -56.51
REMARK 500 GLU B 345 -6.42 -52.37
REMARK 500 GLU B 347 54.16 26.49
REMARK 500 LYS B 349 39.33 -141.35
REMARK 500 ASN B 370 58.17 -107.90
REMARK 500 LYS B 387 -70.62 -63.68
REMARK 500 SER B 391 -4.86 -48.41
REMARK 500 VAL B 392 46.41 -146.82
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 TYR B 86 0.09 SIDE CHAIN
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 SO4 A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 396
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EUC RELATED DB: PDB
REMARK 900 RELATED ID: 1EUD RELATED DB: PDB
REMARK 900 RELATED ID: 2FP4 RELATED DB: PDB
REMARK 900 RELATED ID: 2FPG RELATED DB: PDB
REMARK 900 RELATED ID: 2FPP RELATED DB: PDB
DBREF 2FPI A 3 306 UNP O19069-2 SUCA_PIG 29 332
DBREF 2FPI B 2 395 UNP P53590 SUCB2_PIG 40 433
SEQADV 2FPI SER A 2 UNP O19069-2 CLONING ARTIFACT
SEQADV 2FPI NEP A 259 UNP O19069-2 HIS 285 MODIFIED RESIDUE
SEQADV 2FPI MET B 1 UNP P53590 INITIATING METHIONINE
SEQRES 1 A 305 SER TYR THR ALA SER ARG LYS HIS LEU TYR VAL ASP LYS
SEQRES 2 A 305 ASN THR LYS VAL ILE CYS GLN GLY PHE THR GLY LYS GLN
SEQRES 3 A 305 GLY THR PHE HIS SER GLN GLN ALA LEU GLU TYR GLY THR
SEQRES 4 A 305 ASN LEU VAL GLY GLY THR THR PRO GLY LYS GLY GLY LYS
SEQRES 5 A 305 THR HIS LEU GLY LEU PRO VAL PHE ASN THR VAL LYS GLU
SEQRES 6 A 305 ALA LYS GLU GLN THR GLY ALA THR ALA SER VAL ILE TYR
SEQRES 7 A 305 VAL PRO PRO PRO PHE ALA ALA ALA ALA ILE ASN GLU ALA
SEQRES 8 A 305 ILE ASP ALA GLU VAL PRO LEU VAL VAL CYS ILE THR GLU
SEQRES 9 A 305 GLY ILE PRO GLN GLN ASP MET VAL ARG VAL LYS HIS ARG
SEQRES 10 A 305 LEU LEU ARG GLN GLY LYS THR ARG LEU ILE GLY PRO ASN
SEQRES 11 A 305 CYS PRO GLY VAL ILE ASN PRO GLY GLU CYS LYS ILE GLY
SEQRES 12 A 305 ILE MET PRO GLY HIS ILE HIS LYS LYS GLY ARG ILE GLY
SEQRES 13 A 305 ILE VAL SER ARG SER GLY THR LEU THR TYR GLU ALA VAL
SEQRES 14 A 305 HIS GLN THR THR GLN VAL GLY LEU GLY GLN SER LEU CYS
SEQRES 15 A 305 VAL GLY ILE GLY GLY ASP PRO PHE ASN GLY THR ASP PHE
SEQRES 16 A 305 THR ASP CYS LEU GLU ILE PHE LEU ASN ASP PRO ALA THR
SEQRES 17 A 305 GLU GLY ILE ILE LEU ILE GLY GLU ILE GLY GLY ASN ALA
SEQRES 18 A 305 GLU GLU ASN ALA ALA GLU PHE LEU LYS GLN HIS ASN SER
SEQRES 19 A 305 GLY PRO LYS SER LYS PRO VAL VAL SER PHE ILE ALA GLY
SEQRES 20 A 305 LEU THR ALA PRO PRO GLY ARG ARG MET GLY NEP ALA GLY
SEQRES 21 A 305 ALA ILE ILE ALA GLY GLY LYS GLY GLY ALA LYS GLU LYS
SEQRES 22 A 305 ILE THR ALA LEU GLN SER ALA GLY VAL VAL VAL SER MET
SEQRES 23 A 305 SER PRO ALA GLN LEU GLY THR THR ILE TYR LYS GLU PHE
SEQRES 24 A 305 GLU LYS ARG LYS MET LEU
SEQRES 1 B 395 MET ASN LEU GLN GLU TYR GLN SER LYS LYS LEU MET SER
SEQRES 2 B 395 ASP ASN GLY VAL LYS VAL GLN ARG PHE PHE VAL ALA ASP
SEQRES 3 B 395 THR ALA ASN GLU ALA LEU GLU ALA ALA LYS ARG LEU ASN
SEQRES 4 B 395 ALA LYS GLU ILE VAL LEU LYS ALA GLN ILE LEU ALA GLY
SEQRES 5 B 395 GLY ARG GLY LYS GLY VAL PHE SER SER GLY LEU LYS GLY
SEQRES 6 B 395 GLY VAL HIS LEU THR LYS ASP PRO GLU VAL VAL GLY GLN
SEQRES 7 B 395 LEU ALA LYS GLN MET ILE GLY TYR ASN LEU ALA THR LYS
SEQRES 8 B 395 GLN THR PRO LYS GLU GLY VAL LYS VAL ASN LYS VAL MET
SEQRES 9 B 395 VAL ALA GLU ALA LEU ASP ILE SER ARG GLU THR TYR LEU
SEQRES 10 B 395 ALA ILE LEU MET ASP ARG SER CYS ASN GLY PRO VAL LEU
SEQRES 11 B 395 VAL GLY SER PRO GLN GLY GLY VAL ASP ILE GLU GLU VAL
SEQRES 12 B 395 ALA ALA SER ASN PRO GLU LEU ILE PHE LYS GLU GLN ILE
SEQRES 13 B 395 ASP ILE ILE GLU GLY ILE LYS ASP SER GLN ALA GLN ARG
SEQRES 14 B 395 MET ALA GLU ASN LEU GLY PHE LEU GLY PRO LEU GLN ASN
SEQRES 15 B 395 GLN ALA ALA ASP GLN ILE LYS LYS LEU TYR ASN LEU PHE
SEQRES 16 B 395 LEU LYS ILE ASP ALA THR GLN VAL GLU VAL ASN PRO PHE
SEQRES 17 B 395 GLY GLU THR PRO GLU GLY GLN VAL VAL CYS PHE ASP ALA
SEQRES 18 B 395 LYS ILE ASN PHE ASP ASP ASN ALA GLU PHE ARG GLN LYS
SEQRES 19 B 395 ASP ILE PHE ALA MET ASP ASP LYS SER GLU ASN GLU PRO
SEQRES 20 B 395 ILE GLU ASN GLU ALA ALA LYS TYR ASP LEU LYS TYR ILE
SEQRES 21 B 395 GLY LEU ASP GLY ASN ILE ALA CYS PHE VAL ASN GLY ALA
SEQRES 22 B 395 GLY LEU ALA MET ALA THR CYS ASP ILE ILE PHE LEU ASN
SEQRES 23 B 395 GLY GLY LYS PRO ALA ASN PHE LEU ASP LEU GLY GLY GLY
SEQRES 24 B 395 VAL LYS GLU SER GLN VAL TYR GLN ALA PHE LYS LEU LEU
SEQRES 25 B 395 THR ALA ASP PRO LYS VAL GLU ALA ILE LEU VAL ASN ILE
SEQRES 26 B 395 PHE GLY GLY ILE VAL ASN CYS ALA ILE ILE ALA ASN GLY
SEQRES 27 B 395 ILE THR LYS ALA CYS ARG GLU LEU GLU LEU LYS VAL PRO
SEQRES 28 B 395 LEU VAL VAL ARG LEU GLU GLY THR ASN VAL HIS GLU ALA
SEQRES 29 B 395 GLN ASN ILE LEU THR ASN SER GLY LEU PRO ILE THR SER
SEQRES 30 B 395 ALA VAL ASP LEU GLU ASP ALA ALA LYS LYS ALA VAL ALA
SEQRES 31 B 395 SER VAL THR LYS LYS
MODRES 2FPI NEP A 259 HIS N1-PHOSPHONOHISTIDINE
HET NEP A 259 14
HET SO4 A 307 5
HET SO4 B 396 5
HETNAM NEP N1-PHOSPHONOHISTIDINE
HETNAM SO4 SULFATE ION
FORMUL 1 NEP C6 H10 N3 O5 P
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *64(H2 O)
HELIX 1 1 TYR A 3 TYR A 11 5 9
HELIX 2 2 GLY A 25 GLY A 39 1 15
HELIX 3 3 THR A 63 GLY A 72 1 10
HELIX 4 4 PHE A 84 ALA A 95 1 12
HELIX 5 5 PRO A 108 LEU A 120 1 13
HELIX 6 6 PRO A 147 HIS A 151 5 5
HELIX 7 7 GLY A 163 GLN A 175 1 13
HELIX 8 8 ASP A 195 ASN A 205 1 11
HELIX 9 9 ASN A 221 ASN A 234 1 14
HELIX 10 10 GLY A 270 ALA A 281 1 12
HELIX 11 11 SER A 288 ALA A 290 5 3
HELIX 12 12 GLN A 291 ARG A 303 1 13
HELIX 13 13 GLN B 4 ASN B 15 1 12
HELIX 14 14 THR B 27 ASN B 39 1 13
HELIX 15 15 ASP B 72 GLN B 82 1 11
HELIX 16 16 GLU B 142 ASN B 147 1 6
HELIX 17 17 PRO B 148 ILE B 151 5 4
HELIX 18 18 LYS B 163 GLY B 175 1 13
HELIX 19 19 LEU B 177 ASP B 199 1 23
HELIX 20 20 ASP B 227 ARG B 232 5 6
HELIX 21 21 GLN B 233 MET B 239 1 7
HELIX 22 22 GLU B 246 TYR B 255 1 10
HELIX 23 23 GLY B 272 ASN B 286 1 15
HELIX 24 24 LYS B 301 ALA B 314 1 14
HELIX 25 25 ASN B 331 GLU B 345 1 15
HELIX 26 26 ASN B 360 ASN B 370 1 11
HELIX 27 27 ASP B 380 SER B 391 1 12
SHEET 1 A 5 ASN A 41 GLY A 44 0
SHEET 2 A 5 LYS A 17 GLN A 21 1 N VAL A 18 O VAL A 43
SHEET 3 A 5 ALA A 75 ILE A 78 1 O ALA A 75 N ILE A 19
SHEET 4 A 5 LEU A 99 CYS A 102 1 O LEU A 99 N SER A 76
SHEET 5 A 5 ARG A 126 ILE A 128 1 O ARG A 126 N VAL A 100
SHEET 1 B 7 CYS A 141 GLY A 144 0
SHEET 2 B 7 GLY A 134 ASN A 137 -1 N ASN A 137 O CYS A 141
SHEET 3 B 7 GLN A 180 GLY A 185 -1 O GLY A 185 N GLY A 134
SHEET 4 B 7 LYS A 153 SER A 160 1 N ILE A 158 O VAL A 184
SHEET 5 B 7 GLY A 211 GLU A 217 1 O ILE A 215 N VAL A 159
SHEET 6 B 7 VAL A 242 ALA A 247 1 O VAL A 243 N ILE A 212
SHEET 7 B 7 VAL A 284 VAL A 285 1 O VAL A 284 N VAL A 242
SHEET 1 C 4 PHE B 22 ALA B 25 0
SHEET 2 C 4 VAL B 103 GLU B 107 -1 O VAL B 105 N PHE B 23
SHEET 3 C 4 ILE B 43 ALA B 47 -1 N VAL B 44 O ALA B 106
SHEET 4 C 4 VAL B 67 LEU B 69 -1 O HIS B 68 N LEU B 45
SHEET 1 D 3 VAL B 58 PHE B 59 0
SHEET 2 D 3 ASN B 87 ALA B 89 -1 O ALA B 89 N VAL B 58
SHEET 3 D 3 VAL B 98 LYS B 99 -1 O VAL B 98 N LEU B 88
SHEET 1 E 5 PHE B 152 GLN B 155 0
SHEET 2 E 5 PRO B 128 SER B 133 -1 N GLY B 132 O PHE B 152
SHEET 3 E 5 ARG B 113 MET B 121 -1 N TYR B 116 O SER B 133
SHEET 4 E 5 ALA B 200 GLU B 210 -1 O PHE B 208 N THR B 115
SHEET 5 E 5 VAL B 216 CYS B 218 -1 O VAL B 217 N GLY B 209
SHEET 1 F 5 PHE B 152 GLN B 155 0
SHEET 2 F 5 PRO B 128 SER B 133 -1 N GLY B 132 O PHE B 152
SHEET 3 F 5 ARG B 113 MET B 121 -1 N TYR B 116 O SER B 133
SHEET 4 F 5 ALA B 200 GLU B 210 -1 O PHE B 208 N THR B 115
SHEET 5 F 5 ALA B 221 PHE B 225 -1 O LYS B 222 N GLU B 204
SHEET 1 G 2 LYS B 258 GLY B 261 0
SHEET 2 G 2 ASN B 292 ASP B 295 -1 O ASP B 295 N LYS B 258
SHEET 1 H 3 ILE B 266 VAL B 270 0
SHEET 2 H 3 ALA B 320 PHE B 326 1 O ALA B 320 N ALA B 267
SHEET 3 H 3 LEU B 352 GLU B 357 1 O ARG B 355 N VAL B 323
LINK C GLY A 258 N NEP A 259 1555 1555 1.33
LINK C NEP A 259 N ALA A 260 1555 1555 1.32
CISPEP 1 GLY A 129 PRO A 130 0 1.17
CISPEP 2 ASN B 206 PRO B 207 0 0.62
SITE 1 AC1 4 ARG A 255 ARG A 256 ASP B 227 LYS B 258
SITE 1 AC2 4 GLY B 52 GLY B 53 ARG B 54 LYS B 222
CRYST1 135.790 135.790 77.150 90.00 90.00 120.00 P 65 6
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 0.007364 0.004252 0.000000 0.00000
SCALE2 0.000000 0.008504 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012962 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
