HEADER TRANSFERASE/TRANSFERASE INHIBITOR 25-MAY-10 3N5E
TITLE CRYSTAL STRUCTURE OF HUMAN THYMIDYLATE SYNTHASE BOUND TO A PEPTIDE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TSASE, TS;
COMPND 5 EC: 2.1.1.45;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: TSASE, TS;
COMPND 11 EC: 2.1.1.45;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: SYNTHETIC PEPTIDE LR;
COMPND 15 CHAIN: D;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TYMS, TS, OK/SW-CL.29;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: TYMS, TS, OK/SW-CL.29;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 OTHER_DETAILS: SYNTHETIC PEPTIDE (8MER)
KEYWDS PEPTIDE INHIBITOR, PROTEIN-PEPTIDE COMPLEX, INTERFACE INHIBITOR,
KEYWDS 2 TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.POZZI,D.CARDINALE,G.GUAITOLI,D.TONDI,R.LUCIANI,H.MYLLYKALLIO,
AUTHOR 2 S.FERRARI,M.P.COSTI,S.MANGANI
REVDAT 3 06-SEP-23 3N5E 1 SEQADV LINK
REVDAT 2 24-JUL-13 3N5E 1 JRNL VERSN
REVDAT 1 08-JUN-11 3N5E 0
JRNL AUTH D.CARDINALE,G.GUAITOLI,D.TONDI,R.LUCIANI,S.HENRICH,
JRNL AUTH 2 O.M.SALO-AHEN,S.FERRARI,G.MARVERTI,D.GUERRIERI,A.LIGABUE,
JRNL AUTH 3 C.FRASSINETI,C.POZZI,S.MANGANI,D.FESSAS,R.GUERRINI,
JRNL AUTH 4 G.PONTERINI,R.C.WADE,M.P.COSTI
JRNL TITL PROTEIN-PROTEIN INTERFACE-BINDING PEPTIDES INHIBIT THE
JRNL TITL 2 CANCER THERAPY TARGET HUMAN THYMIDYLATE SYNTHASE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 E542 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21795601
JRNL DOI 10.1073/PNAS.1104829108
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 37678
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 + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1990
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2773
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.75
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 141
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4339
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 255
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.212
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.178
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.146
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4466 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6035 ; 1.496 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 529 ; 6.821 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 214 ;37.816 ;23.318
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 773 ;16.669 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;17.694 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 636 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3383 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2657 ; 0.802 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4293 ; 1.565 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1809 ; 2.315 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1742 ; 3.740 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4978 7.8635 0.2202
REMARK 3 T TENSOR
REMARK 3 T11: 0.2077 T22: 0.0544
REMARK 3 T33: 0.1614 T12: 0.0465
REMARK 3 T13: 0.0747 T23: 0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 1.8053 L22: 2.4460
REMARK 3 L33: 2.0267 L12: -0.5876
REMARK 3 L13: -0.1882 L23: -0.2639
REMARK 3 S TENSOR
REMARK 3 S11: 0.2729 S12: 0.2744 S13: 0.2910
REMARK 3 S21: -0.3266 S22: -0.0901 S23: -0.1716
REMARK 3 S31: -0.1080 S32: 0.1088 S33: -0.1828
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -10 B 9999
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4603 -7.9131 23.5995
REMARK 3 T TENSOR
REMARK 3 T11: 0.2122 T22: 0.0519
REMARK 3 T33: 0.1485 T12: -0.0470
REMARK 3 T13: -0.0793 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 1.7676 L22: 2.5073
REMARK 3 L33: 1.9788 L12: 0.5893
REMARK 3 L13: 0.2376 L23: -0.1691
REMARK 3 S TENSOR
REMARK 3 S11: 0.2715 S12: -0.2507 S13: -0.2930
REMARK 3 S21: 0.3391 S22: -0.0738 S23: -0.1814
REMARK 3 S31: 0.1096 S32: 0.1101 S33: -0.1978
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3N5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.947
REMARK 200 MONOCHROMATOR : SILICON (1 1 1) CHANNEL-CUT
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39745
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.260
REMARK 200 RESOLUTION RANGE LOW (A) : 83.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.30300
REMARK 200 R SYM FOR SHELL (I) : 0.30300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% SATURATED AMMONIUM SULFATE, 20MM
REMARK 280 BME, 0.1M TRIS PH8.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
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
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 27.41333
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 54.82667
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -92.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE SYNTHETIC PEPTIDE LR IS POLYPEPTIDE, A MEMBER OF INHIBITOR
REMARK 400 CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: SYNTHETIC PEPTIDE LR
REMARK 400 CHAIN: D
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 ARG A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 GLY A 11
REMARK 465 SER A 12
REMARK 465 MET A 13
REMARK 465 PRO A 14
REMARK 465 VAL A 15
REMARK 465 ALA A 16
REMARK 465 GLY A 17
REMARK 465 SER A 18
REMARK 465 GLU A 19
REMARK 465 LEU A 20
REMARK 465 PRO A 21
REMARK 465 ARG A 22
REMARK 465 ARG A 23
REMARK 465 PRO A 24
REMARK 465 LEU A 25
REMARK 465 PRO A 26
REMARK 465 PRO A 27
REMARK 465 ALA A 28
REMARK 465 ALA A 29
REMARK 465 GLN A 30
REMARK 465 GLU A 31
REMARK 465 ARG A 32
REMARK 465 ASP A 33
REMARK 465 ALA A 34
REMARK 465 GLU A 35
REMARK 465 PRO A 36
REMARK 465 ARG A 37
REMARK 465 ILE A 120
REMARK 465 TRP A 121
REMARK 465 ASP A 122
REMARK 465 ALA A 123
REMARK 465 ASN A 124
REMARK 465 GLY A 125
REMARK 465 SER A 126
REMARK 465 ARG A 127
REMARK 465 ASP A 128
REMARK 465 PHE A 129
REMARK 465 LEU A 130
REMARK 465 ASP A 131
REMARK 465 SER A 132
REMARK 465 LEU A 133
REMARK 465 GLY A 134
REMARK 465 PHE A 135
REMARK 465 SER A 136
REMARK 465 THR A 137
REMARK 465 ARG A 138
REMARK 465 GLU A 139
REMARK 465 GLU A 140
REMARK 465 GLY A 141
REMARK 465 MET A 323
REMARK 465 ALA A 324
REMARK 465 VAL A 325
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 GLY B 11
REMARK 465 SER B 12
REMARK 465 MET B 13
REMARK 465 PRO B 14
REMARK 465 VAL B 15
REMARK 465 ALA B 16
REMARK 465 GLY B 17
REMARK 465 SER B 18
REMARK 465 GLU B 19
REMARK 465 LEU B 20
REMARK 465 PRO B 21
REMARK 465 ARG B 22
REMARK 465 ARG B 23
REMARK 465 PRO B 24
REMARK 465 LEU B 25
REMARK 465 PRO B 26
REMARK 465 PRO B 27
REMARK 465 ALA B 28
REMARK 465 ALA B 29
REMARK 465 GLN B 30
REMARK 465 GLU B 31
REMARK 465 ARG B 32
REMARK 465 ASP B 33
REMARK 465 ALA B 34
REMARK 465 GLU B 35
REMARK 465 PRO B 36
REMARK 465 ARG B 37
REMARK 465 ILE B 120
REMARK 465 TRP B 121
REMARK 465 ASP B 122
REMARK 465 ALA B 123
REMARK 465 ASN B 124
REMARK 465 GLY B 125
REMARK 465 SER B 126
REMARK 465 ARG B 127
REMARK 465 ASP B 128
REMARK 465 PHE B 129
REMARK 465 LEU B 130
REMARK 465 ASP B 131
REMARK 465 SER B 132
REMARK 465 LEU B 133
REMARK 465 GLY B 134
REMARK 465 PHE B 135
REMARK 465 SER B 136
REMARK 465 THR B 137
REMARK 465 ARG B 138
REMARK 465 GLU B 139
REMARK 465 GLU B 140
REMARK 465 GLY B 141
REMARK 465 MET B 323
REMARK 465 ALA B 324
REMARK 465 VAL B 325
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 SER A 114 -82.72 -72.07
REMARK 500 LYS A 116 -49.08 -136.52
REMARK 500 VAL A 118 47.58 -102.75
REMARK 500 LEU A 143 -72.62 -90.92
REMARK 500 PRO A 145 -99.05 -129.04
REMARK 500 VAL A 146 174.46 57.77
REMARK 500 ARG A 159 -66.59 -126.66
REMARK 500 SER A 166 108.84 -57.37
REMARK 500 ASN A 183 78.41 -154.12
REMARK 500 SER A 218 18.01 58.79
REMARK 500 LEU B 143 -74.88 -91.44
REMARK 500 PRO B 145 -65.67 -128.31
REMARK 500 VAL B 146 147.33 -9.69
REMARK 500 TYR B 147 -24.69 -23.97
REMARK 500 ARG B 159 -74.32 -129.39
REMARK 500 ASN B 183 80.06 -151.76
REMARK 500 CYS D 3 146.77 150.34
REMARK 500 GLN D 4 115.87 81.79
REMARK 500 LEU D 5 153.79 -11.76
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 330
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 332
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 331
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3N5G RELATED DB: PDB
DBREF 3N5E A 13 325 UNP P04818 TYSY_HUMAN 1 313
DBREF 3N5E B 13 325 UNP P04818 TYSY_HUMAN 1 313
DBREF 3N5E D 1 8 PDB 3N5E 3N5E 1 8
SEQADV 3N5E MET A 1 UNP P04818 EXPRESSION TAG
SEQADV 3N5E ARG A 2 UNP P04818 EXPRESSION TAG
SEQADV 3N5E GLY A 3 UNP P04818 EXPRESSION TAG
SEQADV 3N5E SER A 4 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS A 5 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS A 6 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS A 7 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS A 8 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS A 9 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS A 10 UNP P04818 EXPRESSION TAG
SEQADV 3N5E GLY A 11 UNP P04818 EXPRESSION TAG
SEQADV 3N5E SER A 12 UNP P04818 EXPRESSION TAG
SEQADV 3N5E MET B 1 UNP P04818 EXPRESSION TAG
SEQADV 3N5E ARG B 2 UNP P04818 EXPRESSION TAG
SEQADV 3N5E GLY B 3 UNP P04818 EXPRESSION TAG
SEQADV 3N5E SER B 4 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS B 5 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS B 6 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS B 7 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS B 8 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS B 9 UNP P04818 EXPRESSION TAG
SEQADV 3N5E HIS B 10 UNP P04818 EXPRESSION TAG
SEQADV 3N5E GLY B 11 UNP P04818 EXPRESSION TAG
SEQADV 3N5E SER B 12 UNP P04818 EXPRESSION TAG
SEQRES 1 A 325 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 A 325 PRO VAL ALA GLY SER GLU LEU PRO ARG ARG PRO LEU PRO
SEQRES 3 A 325 PRO ALA ALA GLN GLU ARG ASP ALA GLU PRO ARG PRO PRO
SEQRES 4 A 325 HIS GLY GLU LEU GLN TYR LEU GLY GLN ILE GLN HIS ILE
SEQRES 5 A 325 LEU ARG SCH GLY VAL ARG LYS ASP ASP ARG THR GLY THR
SEQRES 6 A 325 GLY THR LEU SER VAL PHE GLY MET GLN ALA ARG TYR SER
SEQRES 7 A 325 LEU ARG ASP GLU PHE PRO LEU LEU THR THR LYS ARG VAL
SEQRES 8 A 325 PHE TRP LYS GLY VAL LEU GLU GLU LEU LEU TRP PHE ILE
SEQRES 9 A 325 LYS GLY SER THR ASN ALA LYS GLU LEU SER SER LYS GLY
SEQRES 10 A 325 VAL LYS ILE TRP ASP ALA ASN GLY SER ARG ASP PHE LEU
SEQRES 11 A 325 ASP SER LEU GLY PHE SER THR ARG GLU GLU GLY ASP LEU
SEQRES 12 A 325 GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY ALA
SEQRES 13 A 325 GLU TYR ARG ASP MET GLU SER ASP TYR SER GLY GLN GLY
SEQRES 14 A 325 VAL ASP GLN LEU GLN ARG VAL ILE ASP THR ILE LYS THR
SEQRES 15 A 325 ASN PRO ASP ASP ARG ARG ILE ILE MET SCH ALA TRP ASN
SEQRES 16 A 325 PRO ARG ASP LEU PRO LEU MET ALA LEU PRO PRO SCH HIS
SEQRES 17 A 325 ALA LEU CYS GLN PHE TYR VAL VAL ASN SER GLU LEU SER
SEQRES 18 A 325 CYS GLN LEU TYR GLN ARG SER GLY ASP MET GLY LEU GLY
SEQRES 19 A 325 VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR TYR
SEQRES 20 A 325 MET ILE ALA HIS ILE THR GLY LEU LYS PRO GLY ASP PHE
SEQRES 21 A 325 ILE HIS THR LEU GLY ASP ALA HIS ILE TYR LEU ASN HIS
SEQRES 22 A 325 ILE GLU PRO LEU LYS ILE GLN LEU GLN ARG GLU PRO ARG
SEQRES 23 A 325 PRO PHE PRO LYS LEU ARG ILE LEU ARG LYS VAL GLU LYS
SEQRES 24 A 325 ILE ASP ASP PHE LYS ALA GLU ASP PHE GLN ILE GLU GLY
SEQRES 25 A 325 TYR ASN PRO HIS PRO THR ILE LYS MET GLU MET ALA VAL
SEQRES 1 B 325 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET
SEQRES 2 B 325 PRO VAL ALA GLY SER GLU LEU PRO ARG ARG PRO LEU PRO
SEQRES 3 B 325 PRO ALA ALA GLN GLU ARG ASP ALA GLU PRO ARG PRO PRO
SEQRES 4 B 325 HIS GLY GLU LEU GLN TYR LEU GLY GLN ILE GLN HIS ILE
SEQRES 5 B 325 LEU ARG SCH GLY VAL ARG LYS ASP ASP ARG THR GLY THR
SEQRES 6 B 325 GLY THR LEU SER VAL PHE GLY MET GLN ALA ARG TYR SER
SEQRES 7 B 325 LEU ARG ASP GLU PHE PRO LEU LEU THR THR LYS ARG VAL
SEQRES 8 B 325 PHE TRP LYS GLY VAL LEU GLU GLU LEU LEU TRP PHE ILE
SEQRES 9 B 325 LYS GLY SER THR ASN ALA LYS GLU LEU SER SER LYS GLY
SEQRES 10 B 325 VAL LYS ILE TRP ASP ALA ASN GLY SER ARG ASP PHE LEU
SEQRES 11 B 325 ASP SER LEU GLY PHE SER THR ARG GLU GLU GLY ASP LEU
SEQRES 12 B 325 GLY PRO VAL TYR GLY PHE GLN TRP ARG HIS PHE GLY ALA
SEQRES 13 B 325 GLU TYR ARG ASP MET GLU SER ASP TYR SER GLY GLN GLY
SEQRES 14 B 325 VAL ASP GLN LEU GLN ARG VAL ILE ASP THR ILE LYS THR
SEQRES 15 B 325 ASN PRO ASP ASP ARG ARG ILE ILE MET CYS ALA TRP ASN
SEQRES 16 B 325 PRO ARG ASP LEU PRO LEU MET ALA LEU PRO PRO SCH HIS
SEQRES 17 B 325 ALA LEU CYS GLN PHE TYR VAL VAL ASN SER GLU LEU SER
SEQRES 18 B 325 CYS GLN LEU TYR GLN ARG SER GLY ASP MET GLY LEU GLY
SEQRES 19 B 325 VAL PRO PHE ASN ILE ALA SER TYR ALA LEU LEU THR TYR
SEQRES 20 B 325 MET ILE ALA HIS ILE THR GLY LEU LYS PRO GLY ASP PHE
SEQRES 21 B 325 ILE HIS THR LEU GLY ASP ALA HIS ILE TYR LEU ASN HIS
SEQRES 22 B 325 ILE GLU PRO LEU LYS ILE GLN LEU GLN ARG GLU PRO ARG
SEQRES 23 B 325 PRO PHE PRO LYS LEU ARG ILE LEU ARG LYS VAL GLU LYS
SEQRES 24 B 325 ILE ASP ASP PHE LYS ALA GLU ASP PHE GLN ILE GLU GLY
SEQRES 25 B 325 TYR ASN PRO HIS PRO THR ILE LYS MET GLU MET ALA VAL
SEQRES 1 D 8 LEU SER CYS GLN LEU TYR GLN ARG
MODRES 3N5E SCH A 55 CYS S-METHYL-THIO-CYSTEINE
MODRES 3N5E SCH A 192 CYS S-METHYL-THIO-CYSTEINE
MODRES 3N5E SCH A 207 CYS S-METHYL-THIO-CYSTEINE
MODRES 3N5E SCH B 55 CYS S-METHYL-THIO-CYSTEINE
MODRES 3N5E SCH B 207 CYS S-METHYL-THIO-CYSTEINE
HET SCH A 55 8
HET SCH A 192 8
HET SCH A 207 8
HET SCH B 55 8
HET SCH B 207 8
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 B 401 5
HETNAM SCH S-METHYL-THIO-CYSTEINE
HETNAM SO4 SULFATE ION
FORMUL 1 SCH 5(C4 H9 N O2 S2)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 8 HOH *255(H2 O)
HELIX 1 1 GLY A 41 GLY A 56 1 16
HELIX 2 2 PHE A 92 LYS A 105 1 14
HELIX 3 3 ASN A 109 SER A 114 5 6
HELIX 4 4 PRO A 145 PHE A 154 1 10
HELIX 5 5 ASP A 171 ASN A 183 1 13
HELIX 6 6 ASN A 195 LEU A 199 5 5
HELIX 7 7 LEU A 233 GLY A 254 1 22
HELIX 8 8 HIS A 273 LEU A 281 1 9
HELIX 9 9 LYS A 299 PHE A 303 5 5
HELIX 10 10 LYS A 304 GLU A 306 5 3
HELIX 11 11 GLY B 41 GLY B 56 1 16
HELIX 12 12 PHE B 92 LYS B 105 1 14
HELIX 13 13 ASN B 109 SER B 114 5 6
HELIX 14 14 TYR B 147 PHE B 154 1 8
HELIX 15 15 ASP B 171 ASN B 183 1 13
HELIX 16 16 ASN B 195 LEU B 199 5 5
HELIX 17 17 LEU B 233 THR B 253 1 21
HELIX 18 18 HIS B 273 LEU B 281 1 9
HELIX 19 19 LYS B 299 PHE B 303 5 5
HELIX 20 20 LYS B 304 GLU B 306 5 3
SHEET 1 A 6 VAL A 57 ASP A 60 0
SHEET 2 A 6 GLY A 66 SER A 78 -1 O SER A 69 N VAL A 57
SHEET 3 A 6 LYS A 256 TYR A 270 -1 O PHE A 260 N TYR A 77
SHEET 4 A 6 GLU A 219 ASP A 230 1 N LEU A 224 O THR A 263
SHEET 5 A 6 ALA A 209 VAL A 216 -1 N LEU A 210 O TYR A 225
SHEET 6 A 6 ILE A 190 ALA A 193 -1 N MET A 191 O CYS A 211
SHEET 1 B 2 LYS A 290 ILE A 293 0
SHEET 2 B 2 PHE A 308 GLU A 311 -1 O GLN A 309 N ARG A 292
SHEET 1 C 6 VAL B 57 ASP B 60 0
SHEET 2 C 6 GLY B 66 SER B 78 -1 O SER B 69 N VAL B 57
SHEET 3 C 6 LYS B 256 TYR B 270 -1 O PHE B 260 N TYR B 77
SHEET 4 C 6 GLU B 219 ASP B 230 1 N LEU B 224 O THR B 263
SHEET 5 C 6 ALA B 209 VAL B 216 -1 N LEU B 210 O TYR B 225
SHEET 6 C 6 ILE B 190 ALA B 193 -1 N ALA B 193 O ALA B 209
SHEET 1 D 2 LYS B 290 ILE B 293 0
SHEET 2 D 2 PHE B 308 GLU B 311 -1 O GLN B 309 N ARG B 292
SSBOND 1 CYS B 192 CYS D 3 1555 1555 2.03
LINK C ARG A 54 N SCH A 55 1555 1555 1.33
LINK C SCH A 55 N GLY A 56 1555 1555 1.33
LINK C MET A 191 N SCH A 192 1555 1555 1.33
LINK C SCH A 192 N ALA A 193 1555 1555 1.33
LINK C PRO A 206 N SCH A 207 1555 1555 1.34
LINK C SCH A 207 N HIS A 208 1555 1555 1.32
LINK C ARG B 54 N SCH B 55 1555 1555 1.33
LINK C SCH B 55 N GLY B 56 1555 1555 1.34
LINK C PRO B 206 N SCH B 207 1555 1555 1.34
LINK C SCH B 207 N HIS B 208 1555 1555 1.33
SITE 1 AC1 6 ARG A 188 ARG B 62 ARG B 90 ARG B 197
SITE 2 AC1 6 PRO B 317 THR B 318
SITE 1 AC2 7 ARG A 62 ARG A 90 ARG A 197 LEU A 201
SITE 2 AC2 7 PRO A 317 THR A 318 ARG B 188
SITE 1 AC3 5 ASN A 195 HIS A 208 ARG A 227 SER A 228
SITE 2 AC3 5 ARG B 187
SITE 1 AC4 5 ARG A 187 ASN B 195 HIS B 208 ARG B 227
SITE 2 AC4 5 SER B 228
CRYST1 96.109 96.109 82.240 90.00 90.00 120.00 P 31 3
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010405 0.006007 0.000000 0.00000
SCALE2 0.000000 0.012014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012160 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
