HEADER TRANSFERASE 07-JUN-00 1F4F
TITLE CRYSTAL STRUCTURE OF E. COLI THYMIDYLATE SYNTHASE COMPLEXED WITH SP-
TITLE 2 722
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.1.1.45;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: C2913;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTHYAWT
KEYWDS CRYSTAL STRUCTURE OF E. COLI THYMIDYLATE SYNTHASE COMPLEXED WITH SP-
KEYWDS 2 722, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.ERLANSON,A.C.BRAISTED,D.R.RAPHAEL,M.RANDAL,R.M.STROUD,E.GORDON,
AUTHOR 2 J.A.WELLS
REVDAT 9 03-NOV-21 1F4F 1 REMARK SEQADV LINK
REVDAT 8 28-FEB-18 1F4F 1 REMARK
REVDAT 7 31-JAN-18 1F4F 1 REMARK
REVDAT 6 04-OCT-17 1F4F 1 REMARK
REVDAT 5 13-JUL-11 1F4F 1 VERSN
REVDAT 4 24-FEB-09 1F4F 1 VERSN
REVDAT 3 01-APR-03 1F4F 1 JRNL
REVDAT 2 29-NOV-00 1F4F 1 JRNL
REVDAT 1 22-JUN-00 1F4F 0
JRNL AUTH D.A.ERLANSON,A.C.BRAISTED,D.R.RAPHAEL,M.RANDAL,R.M.STROUD,
JRNL AUTH 2 E.M.GORDON,J.A.WELLS
JRNL TITL SITE-DIRECTED LIGAND DISCOVERY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 97 9367 2000
JRNL REFN ISSN 0027-8424
JRNL PMID 10944209
JRNL DOI 10.1073/PNAS.97.17.9367
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 40497
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2028
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4271
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 83
REMARK 3 SOLVENT ATOMS : 473
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.200
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.160
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.000
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.007 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.027 ; 0.040
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.032 ; 0.050
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.098 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.178 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.235 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.124 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : 0.000 ; 15.000
REMARK 3 PLANAR (DEGREES) : 3.800 ; 7.000
REMARK 3 STAGGERED (DEGREES) : 14.500; 15.000
REMARK 3 TRANSVERSE (DEGREES) : 25.700; 20.000
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.100 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.900 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.100 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.900 ; 3.000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F4F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40497
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.25
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 51.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M AMMONIUM SULPHATE, 20 MM
REMARK 280 POTASSIUM PHOSPHATE, 0.2 M EDTA, PH 7.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 20.0K, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
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 0.00000
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 0.00000
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 33.40600
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 33.40600
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 33.40600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE ASYMMETRIC UNIT CONTAINS THE BIOLOGICALLY RELEVANT
REMARK 300 HOMODIMER
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: 7270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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 ALA A 263
REMARK 465 ILE A 264
REMARK 465 VAL B 262
REMARK 465 ALA B 263
REMARK 465 ILE B 264
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 LYS A 18 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG A 225 CG - CD - NE ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG A 225 CD - NE - CZ ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG B 35 CD - NE - CZ ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG B 35 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 35 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 126 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 20 -178.87 -64.29
REMARK 500 THR A 24 115.46 -36.37
REMARK 500 TYR A 94 -77.94 -7.17
REMARK 500 ALA A 100 67.38 -153.83
REMARK 500 TYR B 94 -79.11 -7.61
REMARK 500 ALA B 100 52.88 -150.48
REMARK 500 ASP B 122 59.91 -147.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH B 956
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP3 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TP3 B 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F4B RELATED DB: PDB
REMARK 900 1F4B CONTAINS THE SAME PROTEIN
REMARK 900 RELATED ID: 1F4C RELATED DB: PDB
REMARK 900 1F4C CONTAINS THE SAME PROTEIN COVALENTLY MODIFIED AT C146 WITH N-
REMARK 900 [TOSYL-D-PROLINYL]AMINO-ETHANETHIOL
REMARK 900 RELATED ID: 1F4D RELATED DB: PDB
REMARK 900 1F4D CONTAINS A MUTANT FORM OF THE SAME PROTEIN COVALENTLY MODIFIED
REMARK 900 AT C143 WITH N-[TOSYL-D-PROLINYL]AMINO-ETHANETHIOL
REMARK 900 RELATED ID: 1F4E RELATED DB: PDB
REMARK 900 1F4E CONTAINS THE SAME PROTEIN COMPLEXED WITH TOSYL-D-PROLINE
REMARK 900 RELATED ID: 1F4G RELATED DB: PDB
REMARK 900 1F4G CONTAINS THE SAME PROTEIN COMPLEXED WITH SP-876
DBREF 1F4F A 1 264 UNP P0A884 TYSY_ECOLI 1 264
DBREF 1F4F B 1 264 UNP P0A884 TYSY_ECOLI 1 264
SEQADV 1F4F CXM A 1 UNP P0A884 MET 1 ENGINEERED MUTATION
SEQADV 1F4F CXM B 1 UNP P0A884 MET 1 ENGINEERED MUTATION
SEQRES 1 A 264 CXM LYS GLN TYR LEU GLU LEU MET GLN LYS VAL LEU ASP
SEQRES 2 A 264 GLU GLY THR GLN LYS ASN ASP ARG THR GLY THR GLY THR
SEQRES 3 A 264 LEU SER ILE PHE GLY HIS GLN MET ARG PHE ASN LEU GLN
SEQRES 4 A 264 ASP GLY PHE PRO LEU VAL THR THR LYS ARG CYS HIS LEU
SEQRES 5 A 264 ARG SER ILE ILE HIS GLU LEU LEU TRP PHE LEU GLN GLY
SEQRES 6 A 264 ASP THR ASN ILE ALA TYR LEU HIS GLU ASN ASN VAL THR
SEQRES 7 A 264 ILE TRP ASP GLU TRP ALA ASP GLU ASN GLY ASP LEU GLY
SEQRES 8 A 264 PRO VAL TYR GLY LYS GLN TRP ARG ALA TRP PRO THR PRO
SEQRES 9 A 264 ASP GLY ARG HIS ILE ASP GLN ILE THR THR VAL LEU ASN
SEQRES 10 A 264 GLN LEU LYS ASN ASP PRO ASP SER ARG ARG ILE ILE VAL
SEQRES 11 A 264 SER ALA TRP ASN VAL GLY GLU LEU ASP LYS MET ALA LEU
SEQRES 12 A 264 ALA PRO CYS HIS ALA PHE PHE GLN PHE TYR VAL ALA ASP
SEQRES 13 A 264 GLY LYS LEU SER CYS GLN LEU TYR GLN ARG SER CYS ASP
SEQRES 14 A 264 VAL PHE LEU GLY LEU PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 15 A 264 LEU LEU VAL HIS MET MET ALA GLN GLN CYS ASP LEU GLU
SEQRES 16 A 264 VAL GLY ASP PHE VAL TRP THR GLY GLY ASP THR HIS LEU
SEQRES 17 A 264 TYR SER ASN HIS MET ASP GLN THR HIS LEU GLN LEU SER
SEQRES 18 A 264 ARG GLU PRO ARG PRO LEU PRO LYS LEU ILE ILE LYS ARG
SEQRES 19 A 264 LYS PRO GLU SER ILE PHE ASP TYR ARG PHE GLU ASP PHE
SEQRES 20 A 264 GLU ILE GLU GLY TYR ASP PRO HIS PRO GLY ILE LYS ALA
SEQRES 21 A 264 PRO VAL ALA ILE
SEQRES 1 B 264 CXM LYS GLN TYR LEU GLU LEU MET GLN LYS VAL LEU ASP
SEQRES 2 B 264 GLU GLY THR GLN LYS ASN ASP ARG THR GLY THR GLY THR
SEQRES 3 B 264 LEU SER ILE PHE GLY HIS GLN MET ARG PHE ASN LEU GLN
SEQRES 4 B 264 ASP GLY PHE PRO LEU VAL THR THR LYS ARG CYS HIS LEU
SEQRES 5 B 264 ARG SER ILE ILE HIS GLU LEU LEU TRP PHE LEU GLN GLY
SEQRES 6 B 264 ASP THR ASN ILE ALA TYR LEU HIS GLU ASN ASN VAL THR
SEQRES 7 B 264 ILE TRP ASP GLU TRP ALA ASP GLU ASN GLY ASP LEU GLY
SEQRES 8 B 264 PRO VAL TYR GLY LYS GLN TRP ARG ALA TRP PRO THR PRO
SEQRES 9 B 264 ASP GLY ARG HIS ILE ASP GLN ILE THR THR VAL LEU ASN
SEQRES 10 B 264 GLN LEU LYS ASN ASP PRO ASP SER ARG ARG ILE ILE VAL
SEQRES 11 B 264 SER ALA TRP ASN VAL GLY GLU LEU ASP LYS MET ALA LEU
SEQRES 12 B 264 ALA PRO CYS HIS ALA PHE PHE GLN PHE TYR VAL ALA ASP
SEQRES 13 B 264 GLY LYS LEU SER CYS GLN LEU TYR GLN ARG SER CYS ASP
SEQRES 14 B 264 VAL PHE LEU GLY LEU PRO PHE ASN ILE ALA SER TYR ALA
SEQRES 15 B 264 LEU LEU VAL HIS MET MET ALA GLN GLN CYS ASP LEU GLU
SEQRES 16 B 264 VAL GLY ASP PHE VAL TRP THR GLY GLY ASP THR HIS LEU
SEQRES 17 B 264 TYR SER ASN HIS MET ASP GLN THR HIS LEU GLN LEU SER
SEQRES 18 B 264 ARG GLU PRO ARG PRO LEU PRO LYS LEU ILE ILE LYS ARG
SEQRES 19 B 264 LYS PRO GLU SER ILE PHE ASP TYR ARG PHE GLU ASP PHE
SEQRES 20 B 264 GLU ILE GLU GLY TYR ASP PRO HIS PRO GLY ILE LYS ALA
SEQRES 21 B 264 PRO VAL ALA ILE
MODRES 1F4F CXM A 1 MET N-CARBOXYMETHIONINE
MODRES 1F4F CXM B 1 MET N-CARBOXYMETHIONINE
HET CXM A 1 11
HET CXM B 1 11
HET SO4 A 801 5
HET SO4 A 811 5
HET SO4 A 812 5
HET TP3 A 701 29
HET SO4 B 802 5
HET SO4 B 814 5
HET TP3 B 702 33
HETNAM CXM N-CARBOXYMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM TP3 4-[[GLUTAMIC ACID]-CARBONYL]-BENZENE-SULFONYL-D-PROLINE
HETSYN TP3 SP-722
FORMUL 1 CXM 2(C6 H11 N O4 S)
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 6 TP3 2(C17 H20 N2 O9 S)
FORMUL 10 HOH *473(H2 O)
HELIX 1 1 LYS A 2 GLY A 15 1 14
HELIX 2 2 GLN A 39 GLY A 41 5 3
HELIX 3 3 HIS A 51 GLY A 65 1 15
HELIX 4 4 ILE A 69 ASN A 75 1 7
HELIX 5 5 TRP A 80 ALA A 84 5 5
HELIX 6 6 VAL A 93 ALA A 100 1 8
HELIX 7 7 ASP A 110 ASP A 122 1 13
HELIX 8 8 GLU A 137 MET A 141 5 5
HELIX 9 9 GLY A 173 CYS A 192 1 20
HELIX 10 10 HIS A 212 SER A 221 1 10
HELIX 11 11 SER A 238 TYR A 242 5 5
HELIX 12 12 ARG A 243 GLU A 245 5 3
HELIX 13 13 LYS B 2 GLY B 15 1 14
HELIX 14 14 GLN B 39 GLY B 41 5 3
HELIX 15 15 HIS B 51 GLN B 64 1 14
HELIX 16 16 ILE B 69 GLU B 74 1 6
HELIX 17 17 VAL B 93 ALA B 100 1 8
HELIX 18 18 ASP B 110 ASP B 122 1 13
HELIX 19 19 ASN B 134 MET B 141 5 8
HELIX 20 20 LEU B 172 CYS B 192 1 21
HELIX 21 21 HIS B 212 SER B 221 1 10
HELIX 22 22 ARG B 243 GLU B 245 5 3
SHEET 1 A 6 THR A 16 ASN A 19 0
SHEET 2 A 6 GLY A 25 ASN A 37 -1 O THR A 26 N LYS A 18
SHEET 3 A 6 GLU A 195 TYR A 209 -1 N PHE A 199 O PHE A 36
SHEET 4 A 6 LYS A 158 ASP A 169 1 N LEU A 159 O GLU A 195
SHEET 5 A 6 HIS A 147 ALA A 155 -1 N ALA A 148 O TYR A 164
SHEET 6 A 6 ILE A 129 SER A 131 -1 O VAL A 130 N PHE A 150
SHEET 1 B 2 TRP A 101 PRO A 102 0
SHEET 2 B 2 HIS A 108 ILE A 109 -1 N ILE A 109 O TRP A 101
SHEET 1 C 2 LYS A 229 ILE A 232 0
SHEET 2 C 2 PHE A 247 GLU A 250 -1 O GLU A 248 N ILE A 231
SHEET 1 D 6 THR B 16 ASN B 19 0
SHEET 2 D 6 GLY B 25 ASN B 37 -1 O THR B 26 N LYS B 18
SHEET 3 D 6 GLU B 195 TYR B 209 -1 N PHE B 199 O PHE B 36
SHEET 4 D 6 LYS B 158 ASP B 169 1 N LEU B 159 O GLU B 195
SHEET 5 D 6 HIS B 147 ALA B 155 -1 N ALA B 148 O TYR B 164
SHEET 6 D 6 ILE B 129 SER B 131 -1 O VAL B 130 N PHE B 150
SHEET 1 E 2 TRP B 101 PRO B 102 0
SHEET 2 E 2 HIS B 108 ILE B 109 -1 N ILE B 109 O TRP B 101
SHEET 1 F 2 LYS B 229 ILE B 232 0
SHEET 2 F 2 PHE B 247 GLU B 250 -1 O GLU B 248 N ILE B 231
LINK C CXM A 1 N LYS A 2 1555 1555 1.33
LINK C CXM B 1 N LYS B 2 1555 1555 1.31
SITE 1 AC1 7 ARG A 21 ARG A 166 HOH A 869 HOH A1001
SITE 2 AC1 7 HOH A1012 ARG B 126 HOH B 953
SITE 1 AC2 5 ARG A 126 ARG B 21 ARG B 166 HOH B 936
SITE 2 AC2 5 HOH B1020
SITE 1 AC3 5 HIS A 51 LEU A 52 ARG A 53 HOH A 929
SITE 2 AC3 5 HOH A 934
SITE 1 AC4 5 GLU A 223 ARG A 225 HIS A 255 HOH A 840
SITE 2 AC4 5 HOH A 928
SITE 1 AC5 5 ARG A 243 GLY B 106 ARG B 107 HIS B 108
SITE 2 AC5 5 HOH B 868
SITE 1 AC6 16 THR A 78 ILE A 79 TRP A 80 TRP A 83
SITE 2 AC6 16 LEU A 143 CYS A 146 LEU A 172 PHE A 176
SITE 3 AC6 16 ASN A 177 HOH A 818 HOH A 851 HOH A 885
SITE 4 AC6 16 HOH A 961 HOH A 999 HOH A1042 HOH A1076
SITE 1 AC7 15 SER B 54 GLU B 58 THR B 78 ILE B 79
SITE 2 AC7 15 TRP B 80 TYR B 94 LEU B 143 CYS B 146
SITE 3 AC7 15 LEU B 172 PHE B 176 ASN B 177 HOH B 825
SITE 4 AC7 15 HOH B 910 HOH B 952 HOH B 989
CRYST1 126.140 126.140 66.812 90.00 90.00 120.00 P 63 12
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 0.007930 0.004580 0.000000 0.00000
SCALE2 0.000000 0.009150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014970 0.00000
HETATM 1 N CXM A 1 21.911 20.518 49.228 1.00 25.90 N
HETATM 2 CA CXM A 1 23.205 20.835 49.615 1.00 26.89 C
HETATM 3 CB CXM A 1 24.340 20.511 48.629 1.00 25.69 C
HETATM 4 CG CXM A 1 24.631 19.041 48.376 1.00 26.39 C
HETATM 5 SD CXM A 1 25.678 18.729 46.940 1.00 24.81 S
HETATM 6 CE CXM A 1 24.535 18.864 45.577 1.00 24.42 C
HETATM 7 C CXM A 1 23.223 22.375 49.776 1.00 27.61 C
HETATM 8 O CXM A 1 22.462 23.124 49.094 1.00 26.81 O
HETATM 9 CN CXM A 1 21.455 19.586 50.130 1.00 27.25 C
HETATM 10 ON1 CXM A 1 22.027 18.483 50.304 1.00 28.39 O
HETATM 11 ON2 CXM A 1 20.595 18.989 49.489 1.00 26.50 O
(ATOM LINES ARE NOT SHOWN.)
END
