HEADER TRANSFERASE 23-JAN-07 2ONB
TITLE HUMAN THYMIDYLATE SYNTHASE AT LOW SALT CONDITIONS WITH PDPA BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHETASE;
COMPND 3 CHAIN: A;
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 DIPHOSPHONIC ACID, FDUMP, ZD9331, HETEROINHIBITION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.L.LOVELACE,L.M.GIBSON,L.LEBIODA
REVDAT 5 30-AUG-23 2ONB 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2ONB 1 REMARK
REVDAT 3 13-JUL-11 2ONB 1 VERSN
REVDAT 2 24-FEB-09 2ONB 1 VERSN
REVDAT 1 10-APR-07 2ONB 0
JRNL AUTH L.L.LOVELACE,L.M.GIBSON,L.LEBIODA
JRNL TITL COOPERATIVE INHIBITION OF HUMAN THYMIDYLATE SYNTHASE BY
JRNL TITL 2 MIXTURES OF ACTIVE SITE BINDING AND ALLOSTERIC INHIBITORS
JRNL REF BIOCHEMISTRY V. 46 2823 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17297914
JRNL DOI 10.1021/BI061309J
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 41.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 211861.516
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 12144
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) : 0.216
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1253
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 25
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) : 408
REMARK 3 BIN R VALUE (WORKING SET) : 0.2820
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 35
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 : 2097
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 85
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.74000
REMARK 3 B22 (A**2) : -5.74000
REMARK 3 B33 (A**2) : 11.49000
REMARK 3 B12 (A**2) : 0.76000
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) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.34
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.45
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.030
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.550 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.730 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.960 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.990 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 53.34
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_REP.PARAMHICUP
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOPHICUP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ONB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-07.
REMARK 100 THE DEPOSITION ID IS D_1000041348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97251
REMARK 200 MONOCHROMATOR : TWO PASSES, HALF DEGREE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12337
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 18.20
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
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) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 17.30
REMARK 200 R MERGE FOR SHELL (I) : 0.33400
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 MM AMMONIUM SULFATE, 30 MM 40% PEG
REMARK 280 4K, 0.1 M TRIS PH 8.5, 20 MM 2-ME, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 27.50100
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 55.00200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 55.00200
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 27.50100
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 55.00200
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 MET A 1
REMARK 465 PRO A 2
REMARK 465 VAL A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 LEU A 8
REMARK 465 PRO A 9
REMARK 465 ARG A 10
REMARK 465 ARG A 11
REMARK 465 PRO A 12
REMARK 465 LEU A 13
REMARK 465 PRO A 14
REMARK 465 PRO A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 GLN A 18
REMARK 465 GLU A 19
REMARK 465 ARG A 20
REMARK 465 ASP A 21
REMARK 465 ALA A 22
REMARK 465 GLU A 23
REMARK 465 PRO A 24
REMARK 465 ARG A 25
REMARK 465 ILE A 108
REMARK 465 TRP A 109
REMARK 465 ASP A 110
REMARK 465 ALA A 111
REMARK 465 ASN A 112
REMARK 465 GLY A 113
REMARK 465 SER A 114
REMARK 465 ARG A 115
REMARK 465 ASP A 116
REMARK 465 PHE A 117
REMARK 465 LEU A 118
REMARK 465 ASP A 119
REMARK 465 SER A 120
REMARK 465 LEU A 121
REMARK 465 GLY A 122
REMARK 465 PHE A 123
REMARK 465 SER A 124
REMARK 465 THR A 125
REMARK 465 ARG A 126
REMARK 465 GLU A 127
REMARK 465 GLU A 128
REMARK 465 MET A 311
REMARK 465 ALA A 312
REMARK 465 VAL A 313
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 42 CB CG CD NE CZ NH1 NH2
REMARK 470 ARG A 46 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS A 82 CB CG CD CE NZ
REMARK 470 LYS A 93 CB CG CD CE NZ
REMARK 470 LYS A 99 CB CG CD CE NZ
REMARK 470 LYS A 104 CB CG CD CE NZ
REMARK 470 LEU A 131 CB CG CD1 CD2
REMARK 470 TYR A 135 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR A 135 OH
REMARK 470 ARG A 147 CB CG CD NE CZ NH1 NH2
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 NH1 ARG A 215 O2 7PA A 319 2.15
REMARK 500 NH1 ARG A 215 O1 7PA A 319 2.18
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 41 82.17 -64.76
REMARK 500 ARG A 42 73.74 54.26
REMARK 500 CME A 43 56.96 -108.87
REMARK 500 GLU A 70 149.25 -170.15
REMARK 500 PRO A 72 60.00 -68.58
REMARK 500 THR A 76 2.39 -64.03
REMARK 500 VAL A 134 -156.99 -80.80
REMARK 500 MET A 149 0.09 -62.55
REMARK 500 ASN A 171 71.35 -162.19
REMARK 500 CME A 180 61.55 -155.24
REMARK 500 LEU A 192 71.52 58.94
REMARK 500 HIS A 196 -51.09 -20.40
REMARK 500 VAL A 204 136.32 -174.71
REMARK 500 SER A 206 19.40 59.09
REMARK 500 PRO A 277 -159.87 -75.88
REMARK 500 ARG A 283 164.27 176.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 42 CME A 43 61.26
REMARK 500 MET A 179 CME A 180 -140.98
REMARK 500 PRO A 194 CME A 195 121.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 CME A 43 -27.84
REMARK 500 CME A 180 -26.74
REMARK 500 CME A 195 -27.29
REMARK 500 CME A 199 -26.15
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 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7PA A 319
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YPV RELATED DB: PDB
DBREF 2ONB A 1 313 UNP Q53Y97 Q53Y97_HUMAN 1 313
SEQADV 2ONB CME A 43 UNP Q53Y97 CYS 43 MODIFIED RESIDUE
SEQADV 2ONB CME A 180 UNP Q53Y97 CYS 180 MODIFIED RESIDUE
SEQADV 2ONB CME A 195 UNP Q53Y97 CYS 195 MODIFIED RESIDUE
SEQADV 2ONB CME A 199 UNP Q53Y97 CYS 199 MODIFIED RESIDUE
SEQRES 1 A 313 MET PRO VAL ALA GLY SER GLU LEU PRO ARG ARG PRO LEU
SEQRES 2 A 313 PRO PRO ALA ALA GLN GLU ARG ASP ALA GLU PRO ARG PRO
SEQRES 3 A 313 PRO HIS GLY GLU LEU GLN TYR LEU GLY GLN ILE GLN HIS
SEQRES 4 A 313 ILE LEU ARG CME GLY VAL ARG LYS ASP ASP ARG THR GLY
SEQRES 5 A 313 THR GLY THR LEU SER VAL PHE GLY MET GLN ALA ARG TYR
SEQRES 6 A 313 SER LEU ARG ASP GLU PHE PRO LEU LEU THR THR LYS ARG
SEQRES 7 A 313 VAL PHE TRP LYS GLY VAL LEU GLU GLU LEU LEU TRP PHE
SEQRES 8 A 313 ILE LYS GLY SER THR ASN ALA LYS GLU LEU SER SER LYS
SEQRES 9 A 313 GLY VAL LYS ILE TRP ASP ALA ASN GLY SER ARG ASP PHE
SEQRES 10 A 313 LEU ASP SER LEU GLY PHE SER THR ARG GLU GLU GLY ASP
SEQRES 11 A 313 LEU GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY
SEQRES 12 A 313 ALA GLU TYR ARG ASP MET GLU SER ASP TYR SER GLY GLN
SEQRES 13 A 313 GLY VAL ASP GLN LEU GLN ARG VAL ILE ASP THR ILE LYS
SEQRES 14 A 313 THR ASN PRO ASP ASP ARG ARG ILE ILE MET CME ALA TRP
SEQRES 15 A 313 ASN PRO ARG ASP LEU PRO LEU MET ALA LEU PRO PRO CME
SEQRES 16 A 313 HIS ALA LEU CME GLN PHE TYR VAL VAL ASN SER GLU LEU
SEQRES 17 A 313 SER CYS GLN LEU TYR GLN ARG SER GLY ASP MET GLY LEU
SEQRES 18 A 313 GLY VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR
SEQRES 19 A 313 TYR MET ILE ALA HIS ILE THR GLY LEU LYS PRO GLY ASP
SEQRES 20 A 313 PHE ILE HIS THR LEU GLY ASP ALA HIS ILE TYR LEU ASN
SEQRES 21 A 313 HIS ILE GLU PRO LEU LYS ILE GLN LEU GLN ARG GLU PRO
SEQRES 22 A 313 ARG PRO PHE PRO LYS LEU ARG ILE LEU ARG LYS VAL GLU
SEQRES 23 A 313 LYS ILE ASP ASP PHE LYS ALA GLU ASP PHE GLN ILE GLU
SEQRES 24 A 313 GLY TYR ASN PRO HIS PRO THR ILE LYS MET GLU MET ALA
SEQRES 25 A 313 VAL
MODRES 2ONB CME A 43 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2ONB CME A 180 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2ONB CME A 195 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 2ONB CME A 199 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 43 10
HET CME A 180 10
HET CME A 195 10
HET CME A 199 10
HET SO4 A 316 5
HET EDO A 314 4
HET 7PA A 319 22
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 7PA PROPANE-1,3-DIYLBIS(PHOSPHONIC ACID)
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 CME 4(C5 H11 N O3 S2)
FORMUL 2 SO4 O4 S 2-
FORMUL 3 EDO C2 H6 O2
FORMUL 4 7PA C3 H10 O6 P2
FORMUL 5 HOH *85(H2 O)
HELIX 1 1 GLY A 29 LEU A 41 1 13
HELIX 2 2 PHE A 80 LYS A 93 1 14
HELIX 3 3 ASN A 97 SER A 103 1 7
HELIX 4 4 VAL A 134 HIS A 141 1 8
HELIX 5 5 ASP A 159 ASN A 171 1 13
HELIX 6 6 ARG A 185 MET A 190 1 6
HELIX 7 7 LEU A 221 THR A 241 1 21
HELIX 8 8 HIS A 261 GLN A 270 1 10
HELIX 9 9 LYS A 287 PHE A 291 5 5
SHEET 1 A 5 VAL A 45 ASP A 48 0
SHEET 2 A 5 GLY A 54 SER A 66 -1 O SER A 57 N VAL A 45
SHEET 3 A 5 LYS A 244 TYR A 258 -1 O GLY A 253 N GLY A 60
SHEET 4 A 5 GLU A 207 ASP A 218 1 N LEU A 208 O GLY A 246
SHEET 5 A 5 ALA A 197 LEU A 198 -1 N LEU A 198 O TYR A 213
SHEET 1 B 5 VAL A 45 ASP A 48 0
SHEET 2 B 5 GLY A 54 SER A 66 -1 O SER A 57 N VAL A 45
SHEET 3 B 5 LYS A 244 TYR A 258 -1 O GLY A 253 N GLY A 60
SHEET 4 B 5 GLU A 207 ASP A 218 1 N LEU A 208 O GLY A 246
SHEET 5 B 5 PHE A 201 VAL A 204 -1 N TYR A 202 O SER A 209
SHEET 1 C 2 LYS A 278 ILE A 281 0
SHEET 2 C 2 PHE A 296 GLU A 299 -1 O GLN A 297 N ARG A 280
LINK C ARG A 42 N CME A 43 1555 1555 1.33
LINK C CME A 43 N GLY A 44 1555 1555 1.32
LINK C MET A 179 N CME A 180 1555 1555 1.33
LINK C CME A 180 N ALA A 181 1555 1555 1.33
LINK C PRO A 194 N CME A 195 1555 1555 1.32
LINK C CME A 195 N HIS A 196 1555 1555 1.33
LINK C LEU A 198 N CME A 199 1555 1555 1.33
LINK C CME A 199 N GLN A 200 1555 1555 1.32
SITE 1 AC1 6 ARG A 50 ARG A 78 ARG A 176 ARG A 185
SITE 2 AC1 6 LEU A 189 THR A 306
SITE 1 AC2 6 GLN A 36 GLN A 62 ALA A 63 ILE A 227
SITE 2 AC2 6 HIS A 250 LEU A 252
SITE 1 AC3 11 ASP A 49 ARG A 50 THR A 51 ARG A 175
SITE 2 AC3 11 ASN A 183 ARG A 185 HIS A 196 ARG A 215
SITE 3 AC3 11 SER A 216 TYR A 258 HOH A 348
CRYST1 95.690 95.690 82.503 90.00 90.00 120.00 P 31 2 1 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 0.010450 0.006034 0.000000 0.00000
SCALE2 0.000000 0.012067 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012121 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
