HEADER TRANSFERASE 03-MAR-06 2G8X
TITLE ESCHERICHIA COLI Y209W APOPROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THYMIDYLATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TS, TSASE;
COMPND 5 EC: 2.1.1.45;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: THYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: CHI2913RECA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS BETA SHEET, ALPHA/BETA PROTEIN, DTT, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.T.LEE,J.S.FINER-MOORE,R.M.STROUD
REVDAT 5 30-AUG-23 2G8X 1 REMARK
REVDAT 4 20-OCT-21 2G8X 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2G8X 1 VERSN
REVDAT 2 24-FEB-09 2G8X 1 VERSN
REVDAT 1 14-MAR-06 2G8X 0
JRNL AUTH Z.NEWBY,T.T.LEE,R.J.MORSE,L.LIU,Y.LIU,P.VENKATRAMAN,
JRNL AUTH 2 D.V.SANTI,J.S.FINER-MOORE,R.M.STROUD
JRNL TITL THE ROLE OF PROTEIN DYNAMICS IN THYMIDYLATE SYNTHASE
JRNL TITL 2 CATALYSIS: VARIANTS OF CONSERVED DUMP-BINDING TYR-261
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.83 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2091436.200
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 41153
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) : 0.164
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2076
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4773
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 256
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4276
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 348
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.15000
REMARK 3 B22 (A**2) : -5.39000
REMARK 3 B33 (A**2) : 4.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 8.60000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.016
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.550
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) : 0.990 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.600 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.440 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.340 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.43
REMARK 3 BSOL : 57.54
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : PARAM.PO4
REMARK 3 PARAMETER FILE 4 : CARBONATE.PARAM
REMARK 3 PARAMETER FILE 5 : DTT_ODT_GCL.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : CARBONATE.TOPO
REMARK 3 TOPOLOGY FILE 4 : TOPO.FORMIC
REMARK 3 TOPOLOGY FILE 5 : DTT_ODT_GCL.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HIS-51 AND CYS-146 IN CHAIN A ARE IN
REMARK 3 TWO CONFORMATIONS IN THE CRYSTAL
REMARK 4
REMARK 4 2G8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036836.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-01
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41273
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 30.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: PDB CODE 1TJS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.8MG/ML PROTEIN, 25MM KPO4, PH 7.5,
REMARK 280 AND 5MM DTT EQUILIBRATED AGAINST A WELL BUFFER CONTAINING 28%
REMARK 280 PEG 4K, 100 MM TRIS-CL, PH 8.9, 200MM SODIUM ACETATE AND 5MM DTT,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.30500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.84500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.30500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.84500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: CHAINS A AND B CONSTITUTE THE BIOLOGICAL 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: 6360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 ALA B 263
REMARK 465 ILE B 264
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 B 21 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 OE2 GLU A 237 O HOH A 498 2.05
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 143 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG A 222 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 222 NE - CZ - NH2 ANGL. DEV. = -4.7 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 TYR A 94 -67.85 -27.05
REMARK 500 ALA A 100 53.89 -156.12
REMARK 500 ASP A 122 56.72 -148.23
REMARK 500 TYR B 94 -72.57 -16.05
REMARK 500 ALA B 100 51.72 -158.77
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 CO3 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 565
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 567
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G8M RELATED DB: PDB
REMARK 900 E. COLI Y209W IN COMPLEX WITH DUMP AND CB3717
REMARK 900 RELATED ID: 2G86 RELATED DB: PDB
REMARK 900 L. CASEI THYMIDYLATE SYNTHASE Y261F-DUMP
REMARK 900 RELATED ID: 2G8A RELATED DB: PDB
REMARK 900 L. CASEI THYMIDYLATE SYNTHASE Y261M-DUMP
REMARK 900 RELATED ID: 2G89 RELATED DB: PDB
REMARK 900 L. CASEI THYMIDYLATE SYNTHASE Y261A-DUMP
REMARK 900 RELATED ID: 2G8D RELATED DB: PDB
REMARK 900 L. CASEI THYMIDYLATE SYNTHASE Y261W-DUMP
REMARK 900 RELATED ID: 2G8O RELATED DB: PDB
REMARK 900 E. COLI IN COMPLEX WITH DUMP AND CB3717
DBREF 2G8X A 1 264 UNP P0A884 TYSY_ECOLI 1 264
DBREF 2G8X B 1 264 UNP P0A884 TYSY_ECOLI 1 264
SEQADV 2G8X CXM A 1 UNP P0A884 MET 1 MODIFIED RESIDUE
SEQADV 2G8X TRP A 209 UNP P0A884 TYR 209 ENGINEERED MUTATION
SEQADV 2G8X CXM B 1 UNP P0A884 MET 1 MODIFIED RESIDUE
SEQADV 2G8X TRP B 209 UNP P0A884 TYR 209 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 TRP 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 TRP 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 2G8X CXM A 1 MET N-CARBOXYMETHIONINE
MODRES 2G8X CXM B 1 MET N-CARBOXYMETHIONINE
HET CXM A 1 11
HET CXM B 1 11
HET CO3 A 803 4
HET PO4 A 565 5
HET DTT A 800 8
HET CO3 B 804 4
HET CO3 B 805 4
HET PO4 B 567 5
HET DTT B 801 8
HETNAM CXM N-CARBOXYMETHIONINE
HETNAM CO3 CARBONATE ION
HETNAM PO4 PHOSPHATE ION
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 1 CXM 2(C6 H11 N O4 S)
FORMUL 3 CO3 3(C O3 2-)
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 DTT 2(C4 H10 O2 S2)
FORMUL 10 HOH *348(H2 O)
HELIX 1 1 CXM A 1 GLY A 15 1 15
HELIX 2 2 LEU A 52 GLY A 65 1 14
HELIX 3 3 ILE A 69 ASN A 75 1 7
HELIX 4 4 VAL A 93 ALA A 100 1 8
HELIX 5 5 ASP A 110 ASP A 122 1 13
HELIX 6 6 ASN A 134 MET A 141 5 8
HELIX 7 7 LEU A 172 CYS A 192 1 21
HELIX 8 8 HIS A 212 SER A 221 1 10
HELIX 9 9 ARG A 243 GLU A 245 5 3
HELIX 10 10 CXM B 1 GLY B 15 1 15
HELIX 11 11 HIS B 51 GLY B 65 1 15
HELIX 12 12 ILE B 69 ASN B 75 1 7
HELIX 13 13 VAL B 93 ALA B 100 1 8
HELIX 14 14 ASP B 110 ASP B 122 1 13
HELIX 15 15 ASN B 134 MET B 141 5 8
HELIX 16 16 LEU B 172 CYS B 192 1 21
HELIX 17 17 HIS B 212 SER B 221 1 10
HELIX 18 18 ARG B 243 GLU B 245 5 3
SHEET 1 A 6 THR A 16 LYS A 18 0
SHEET 2 A 6 THR A 26 ASN A 37 -1 O SER A 28 N THR A 16
SHEET 3 A 6 GLU A 195 TRP A 209 -1 O PHE A 199 N PHE A 36
SHEET 4 A 6 LYS A 158 ASP A 169 1 N GLN A 165 O THR A 202
SHEET 5 A 6 HIS A 147 ALA A 155 -1 N TYR A 153 O SER A 160
SHEET 6 A 6 ILE A 128 SER A 131 -1 N VAL A 130 O 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 O ILE A 109 N 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 LYS B 18 0
SHEET 2 D 6 THR B 26 ASN B 37 -1 O THR B 26 N LYS B 18
SHEET 3 D 6 GLU B 195 TRP B 209 -1 O PHE B 199 N PHE B 36
SHEET 4 D 6 LYS B 158 ASP B 169 1 N GLN B 165 O THR B 202
SHEET 5 D 6 HIS B 147 ALA B 155 -1 N TYR B 153 O SER B 160
SHEET 6 D 6 ILE B 129 SER B 131 -1 N VAL B 130 O 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 O ILE B 109 N 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 1.32
LINK C CXM B 1 N LYS B 2 1555 1555 1.33
SITE 1 AC1 5 CYS A 50 HIS A 51 HOH A 317 HOH A 517
SITE 2 AC1 5 HOH A 655
SITE 1 AC2 4 CYS B 50 HIS B 51 HOH B 340 HOH B 532
SITE 1 AC3 8 TRP A 101 PRO A 102 PRO A 104 HOH A 291
SITE 2 AC3 8 TRP B 101 PRO B 102 ASN B 134 GLY B 136
SITE 1 AC4 5 ARG A 21 ARG A 166 SER A 167 HOH A 608
SITE 2 AC4 5 ARG B 126
SITE 1 AC5 5 ARG A 126 ARG B 166 SER B 167 HOH B 296
SITE 2 AC5 5 HOH B 512
SITE 1 AC6 7 GLU A 58 ILE A 79 TRP A 80 PHE A 176
SITE 2 AC6 7 HOH A 615 HOH A 642 HOH A 661
SITE 1 AC7 4 GLU B 58 ILE B 79 TRP B 80 HOH B 697
CRYST1 66.610 79.690 92.240 90.00 103.86 90.00 C 1 2 1 8
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 0.015013 0.000000 0.003704 0.00000
SCALE2 0.000000 0.012549 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011166 0.00000
HETATM 1 N CXM A 1 11.572 -9.469 46.695 1.00 19.23 N
HETATM 2 CA CXM A 1 12.712 -10.324 46.254 1.00 20.21 C
HETATM 3 CB CXM A 1 12.400 -11.096 44.934 1.00 20.72 C
HETATM 4 CG CXM A 1 11.214 -12.023 44.999 1.00 23.49 C
HETATM 5 SD CXM A 1 10.837 -12.696 43.356 1.00 23.37 S
HETATM 6 CE CXM A 1 10.008 -11.363 42.496 1.00 21.58 C
HETATM 7 C CXM A 1 13.897 -9.451 45.968 1.00 19.96 C
HETATM 8 O CXM A 1 13.755 -8.281 45.612 1.00 19.97 O
HETATM 9 CN CXM A 1 10.696 -9.849 47.617 1.00 19.09 C
HETATM 10 ON1 CXM A 1 9.776 -9.017 47.833 1.00 18.77 O
HETATM 11 ON2 CXM A 1 10.561 -11.057 47.923 1.00 19.07 O
(ATOM LINES ARE NOT SHOWN.)
END
