HEADER TRANSFERASE 03-AUG-12 4B5B
TITLE PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 2.7.7.74;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 208964;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23A MODIFIED
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.ALPHEY,L.PIRRIE,L.S.TORRIE,M.GARDINER,N.J.WESTWOOD,D.GRAY,
AUTHOR 2 J.H.NAISMITH
REVDAT 6 20-DEC-23 4B5B 1 REMARK
REVDAT 5 07-FEB-18 4B5B 1 JRNL
REVDAT 4 05-JUL-17 4B5B 1 REMARK
REVDAT 3 06-MAR-13 4B5B 1 JRNL
REVDAT 2 21-NOV-12 4B5B 1 AUTHOR JRNL
REVDAT 1 31-OCT-12 4B5B 0
JRNL AUTH M.S.ALPHEY,L.PIRRIE,L.S.TORRIE,W.A.BOULKEROUA,M.GARDINER,
JRNL AUTH 2 A.SARKAR,M.MARINGER,W.OEHLMANN,R.BRENK,M.S.SCHERMAN,
JRNL AUTH 3 M.MCNEIL,M.REJZEK,R.A.FIELD,M.SINGH,D.GRAY,N.J.WESTWOOD,
JRNL AUTH 4 J.H.NAISMITH
JRNL TITL ALLOSTERIC COMPETITIVE INHIBITORS OF THE GLUCOSE-1-PHOSPHATE
JRNL TITL 2 THYMIDYLYLTRANSFERASE (RMLA) FROM PSEUDOMONAS AERUGINOSA.
JRNL REF ACS CHEM. BIOL. V. 8 387 2013
JRNL REFN ESSN 1554-8937
JRNL PMID 23138692
JRNL DOI 10.1021/CB300426U
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 75264
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 3979
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) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.11
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4418
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 229
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9157
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45700
REMARK 3 B22 (A**2) : -0.11600
REMARK 3 B33 (A**2) : -0.37200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.37100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.227
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.186
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.650
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9504 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 6404 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12918 ; 1.345 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15620 ; 1.254 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1173 ; 6.012 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 431 ;33.063 ;24.385
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1577 ;15.011 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;15.812 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1403 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10638 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1913 ; 0.005 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2062 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 75 ; 0.154 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4655 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 209 ; 0.137 ; 0.200
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): 9503 ; 2.622 ; 4.165
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 6404 ; 0.730 ; 4.276
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12914 ; 3.871 ; 6.193
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3236 ; 6.196 ;12.762
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7519 ; 5.378 ;20.323
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS 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 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4B5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1290053600.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79243
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 31.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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 4ARW
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 6000, 0.1 M MES PH 6, 0.05 M
REMARK 280 MGCL2, 0.1 M NA BR, 1% BETA-MERCAPTOETHANOL
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 32.04500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 32.04500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 77.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.8 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 64.09000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 58.47951
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 134.42297
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2035 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2023 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C2029 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C2066 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D2034 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D2052 LIES ON A SPECIAL POSITION.
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 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 GLY A -4
REMARK 465 SER A -3
REMARK 465 MET A -2
REMARK 465 ALA A -1
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 GLY B -4
REMARK 465 SER B -3
REMARK 465 MET B -2
REMARK 465 ALA B -1
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 GLY C -4
REMARK 465 SER C -3
REMARK 465 MET C -2
REMARK 465 ALA C -1
REMARK 465 ARG C 194
REMARK 465 GLY C 195
REMARK 465 HIS D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 GLY D -4
REMARK 465 SER D -3
REMARK 465 MET D -2
REMARK 465 ALA D -1
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 ILE A 23 CB - CA - C ANGL. DEV. = -12.2 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 SER A 12 34.17 -97.68
REMARK 500 TYR A 31 -89.27 59.47
REMARK 500 ALA B 9 62.26 -117.51
REMARK 500 SER B 12 31.99 -98.22
REMARK 500 TYR B 31 -88.99 56.95
REMARK 500 TYR C 31 -90.50 57.64
REMARK 500 ALA D 9 68.31 -107.18
REMARK 500 TYR D 31 -89.08 57.44
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 BBE A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BBE B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BBE C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BBE D 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 1294
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FXO RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM ANDREGULATION OF
REMARK 900 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TMP COMPLEX.
REMARK 900 RELATED ID: 1FZW RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM ANDREGULATION OF
REMARK 900 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). APO ENZYME.
REMARK 900 RELATED ID: 1G0R RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM ANDREGULATION OF
REMARK 900 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). THYMIDINE/GLUCOSE-
REMARK 900 1-PHOSPHATE COMPLEX.
REMARK 900 RELATED ID: 1G1L RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM ANDREGULATION OF
REMARK 900 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-GLUCOSE
REMARK 900 COMPLEX.
REMARK 900 RELATED ID: 1G23 RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM ANDREGULATION OF
REMARK 900 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). GLUCOSE-1-
REMARK 900 PHOSPHATE COMPLEX.
REMARK 900 RELATED ID: 1G2V RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM ANDREGULATION OF
REMARK 900 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TTP COMPLEX.
REMARK 900 RELATED ID: 1G3L RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM ANDREGULATION OF
REMARK 900 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-L-RHAMNOSE
REMARK 900 COMPLEX.
REMARK 900 RELATED ID: 4B2X RELATED DB: PDB
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR
REMARK 900 RELATED ID: 4B3U RELATED DB: PDB
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR
REMARK 900 RELATED ID: 4B4B RELATED DB: PDB
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR
REMARK 900 RELATED ID: 4B4G RELATED DB: PDB
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR
REMARK 900 RELATED ID: 4B4M RELATED DB: PDB
REMARK 900 PSEUDOMONAS AERUGINOSA RMLA IN COMPLEX WITH ALLOSTERIC INHIBITOR
DBREF 4B5B A 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 4B5B B 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 4B5B C 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 4B5B D 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
SEQADV 4B5B HIS A -10 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS A -9 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS A -8 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS A -7 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS A -6 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS A -5 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B GLY A -4 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B SER A -3 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B MET A -2 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B ALA A -1 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS B -10 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS B -9 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS B -8 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS B -7 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS B -6 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS B -5 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B GLY B -4 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B SER B -3 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B MET B -2 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B ALA B -1 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS C -10 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS C -9 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS C -8 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS C -7 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS C -6 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS C -5 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B GLY C -4 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B SER C -3 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B MET C -2 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B ALA C -1 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS D -10 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS D -9 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS D -8 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS D -7 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS D -6 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B HIS D -5 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B GLY D -4 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B SER D -3 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B MET D -2 UNP Q9HU22 EXPRESSION TAG
SEQADV 4B5B ALA D -1 UNP Q9HU22 EXPRESSION TAG
SEQRES 1 A 303 HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG
SEQRES 2 A 303 LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU
SEQRES 3 A 303 HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO
SEQRES 4 A 303 VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR
SEQRES 5 A 303 LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER
SEQRES 6 A 303 THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY
SEQRES 7 A 303 ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL
SEQRES 8 A 303 GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE
SEQRES 9 A 303 GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL
SEQRES 10 A 303 LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU
SEQRES 11 A 303 LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER
SEQRES 12 A 303 VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY
SEQRES 13 A 303 VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU
SEQRES 14 A 303 GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL
SEQRES 15 A 303 THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE
SEQRES 16 A 303 ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU
SEQRES 17 A 303 ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN
SEQRES 18 A 303 LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU
SEQRES 19 A 303 ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN
SEQRES 20 A 303 PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL
SEQRES 21 A 303 ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE
SEQRES 22 A 303 ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA
SEQRES 23 A 303 LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR
SEQRES 24 A 303 GLU THR VAL TYR
SEQRES 1 B 303 HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG
SEQRES 2 B 303 LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU
SEQRES 3 B 303 HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO
SEQRES 4 B 303 VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR
SEQRES 5 B 303 LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER
SEQRES 6 B 303 THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY
SEQRES 7 B 303 ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL
SEQRES 8 B 303 GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE
SEQRES 9 B 303 GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL
SEQRES 10 B 303 LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU
SEQRES 11 B 303 LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER
SEQRES 12 B 303 VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY
SEQRES 13 B 303 VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU
SEQRES 14 B 303 GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL
SEQRES 15 B 303 THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE
SEQRES 16 B 303 ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU
SEQRES 17 B 303 ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN
SEQRES 18 B 303 LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU
SEQRES 19 B 303 ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN
SEQRES 20 B 303 PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL
SEQRES 21 B 303 ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE
SEQRES 22 B 303 ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA
SEQRES 23 B 303 LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR
SEQRES 24 B 303 GLU THR VAL TYR
SEQRES 1 C 303 HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG
SEQRES 2 C 303 LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU
SEQRES 3 C 303 HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO
SEQRES 4 C 303 VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR
SEQRES 5 C 303 LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER
SEQRES 6 C 303 THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY
SEQRES 7 C 303 ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL
SEQRES 8 C 303 GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE
SEQRES 9 C 303 GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL
SEQRES 10 C 303 LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU
SEQRES 11 C 303 LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER
SEQRES 12 C 303 VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY
SEQRES 13 C 303 VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU
SEQRES 14 C 303 GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL
SEQRES 15 C 303 THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE
SEQRES 16 C 303 ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU
SEQRES 17 C 303 ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN
SEQRES 18 C 303 LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU
SEQRES 19 C 303 ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN
SEQRES 20 C 303 PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL
SEQRES 21 C 303 ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE
SEQRES 22 C 303 ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA
SEQRES 23 C 303 LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR
SEQRES 24 C 303 GLU THR VAL TYR
SEQRES 1 D 303 HIS HIS HIS HIS HIS HIS GLY SER MET ALA MET LYS ARG
SEQRES 2 D 303 LYS GLY ILE ILE LEU ALA GLY GLY SER GLY THR ARG LEU
SEQRES 3 D 303 HIS PRO ALA THR LEU ALA ILE SER LYS GLN LEU LEU PRO
SEQRES 4 D 303 VAL TYR ASP LYS PRO MET ILE TYR TYR PRO LEU SER THR
SEQRES 5 D 303 LEU MET LEU ALA GLY ILE ARG GLU ILE LEU ILE ILE SER
SEQRES 6 D 303 THR PRO GLN ASP THR PRO ARG PHE GLN GLN LEU LEU GLY
SEQRES 7 D 303 ASP GLY SER ASN TRP GLY LEU ASP LEU GLN TYR ALA VAL
SEQRES 8 D 303 GLN PRO SER PRO ASP GLY LEU ALA GLN ALA PHE LEU ILE
SEQRES 9 D 303 GLY GLU SER PHE ILE GLY ASN ASP LEU SER ALA LEU VAL
SEQRES 10 D 303 LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP PHE HIS GLU
SEQRES 11 D 303 LEU LEU GLY SER ALA SER GLN ARG GLN THR GLY ALA SER
SEQRES 12 D 303 VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU ARG TYR GLY
SEQRES 13 D 303 VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA ILE SER LEU
SEQRES 14 D 303 GLU GLU LYS PRO LEU GLU PRO LYS SER ASN TYR ALA VAL
SEQRES 15 D 303 THR GLY LEU TYR PHE TYR ASP GLN GLN VAL VAL ASP ILE
SEQRES 16 D 303 ALA ARG ASP LEU LYS PRO SER PRO ARG GLY GLU LEU GLU
SEQRES 17 D 303 ILE THR ASP VAL ASN ARG ALA TYR LEU GLU ARG GLY GLN
SEQRES 18 D 303 LEU SER VAL GLU ILE MET GLY ARG GLY TYR ALA TRP LEU
SEQRES 19 D 303 ASP THR GLY THR HIS ASP SER LEU LEU GLU ALA GLY GLN
SEQRES 20 D 303 PHE ILE ALA THR LEU GLU ASN ARG GLN GLY LEU LYS VAL
SEQRES 21 D 303 ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN LYS TRP ILE
SEQRES 22 D 303 ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA PRO LEU ALA
SEQRES 23 D 303 LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG LEU LEU THR
SEQRES 24 D 303 GLU THR VAL TYR
HET BBE A 400 28
HET CL A1294 1
HET BBE B 400 28
HET CL B1294 1
HET BBE C 400 28
HET CL C1294 1
HET BBE D 400 28
HET CL D1294 1
HETNAM BBE N-(6-AMINO-1-BENZYL-2,4-DIOXO-1,2,3,4-
HETNAM 2 BBE TETRAHYDROPYRIMIDIN-5-YL)-N,3-
HETNAM 3 BBE DIMETHYLBENZENESULFONAMIDE
HETNAM CL CHLORIDE ION
FORMUL 5 BBE 4(C19 H20 N4 O4 S)
FORMUL 6 CL 4(CL 1-)
FORMUL 13 HOH *273(H2 O)
HELIX 1 1 SER A 24 LEU A 27 5 4
HELIX 2 2 ILE A 36 ALA A 46 1 11
HELIX 3 3 ASP A 59 GLY A 68 1 10
HELIX 4 4 GLY A 70 GLY A 74 5 5
HELIX 5 5 GLY A 87 ALA A 89 5 3
HELIX 6 6 GLN A 90 GLY A 95 1 6
HELIX 7 7 GLY A 95 GLY A 100 1 6
HELIX 8 8 ASP A 117 ARG A 128 1 12
HELIX 9 9 ASP A 141 ARG A 144 5 4
HELIX 10 10 GLN A 181 ASP A 188 1 8
HELIX 11 11 GLU A 198 ARG A 209 1 12
HELIX 12 12 THR A 228 GLY A 247 1 20
HELIX 13 13 CYS A 252 GLN A 260 1 9
HELIX 14 14 ASP A 264 ALA A 273 1 10
HELIX 15 15 PRO A 274 ALA A 276 5 3
HELIX 16 16 ASN A 278 LEU A 287 1 10
HELIX 17 17 SER B 24 LEU B 27 5 4
HELIX 18 18 ILE B 36 ALA B 46 1 11
HELIX 19 19 ASP B 59 GLY B 68 1 10
HELIX 20 20 GLY B 70 GLY B 74 5 5
HELIX 21 21 GLY B 87 ALA B 89 5 3
HELIX 22 22 GLN B 90 GLY B 95 1 6
HELIX 23 23 GLY B 95 GLY B 100 1 6
HELIX 24 24 ASP B 117 ARG B 128 1 12
HELIX 25 25 ASP B 141 ARG B 144 5 4
HELIX 26 26 GLN B 181 ASP B 188 1 8
HELIX 27 27 GLU B 198 ARG B 209 1 12
HELIX 28 28 THR B 228 GLY B 247 1 20
HELIX 29 29 CYS B 252 GLN B 260 1 9
HELIX 30 30 ASP B 264 ALA B 273 1 10
HELIX 31 31 PRO B 274 ALA B 276 5 3
HELIX 32 32 ASN B 278 LEU B 288 1 11
HELIX 33 33 PRO C 18 ILE C 23 1 6
HELIX 34 34 SER C 24 LEU C 27 5 4
HELIX 35 35 ILE C 36 ALA C 46 1 11
HELIX 36 36 ASP C 59 GLY C 68 1 10
HELIX 37 37 GLY C 70 GLY C 74 5 5
HELIX 38 38 GLY C 87 ALA C 89 5 3
HELIX 39 39 GLN C 90 GLY C 95 1 6
HELIX 40 40 GLY C 95 GLY C 100 1 6
HELIX 41 41 ASP C 117 ARG C 128 1 12
HELIX 42 42 ASP C 141 ARG C 144 5 4
HELIX 43 43 GLN C 181 ASP C 188 1 8
HELIX 44 44 GLU C 198 ARG C 209 1 12
HELIX 45 45 THR C 228 GLY C 247 1 20
HELIX 46 46 CYS C 252 GLN C 260 1 9
HELIX 47 47 ASP C 264 ALA C 273 1 10
HELIX 48 48 PRO C 274 ALA C 276 5 3
HELIX 49 49 ASN C 278 LEU C 288 1 11
HELIX 50 50 PRO D 18 ILE D 23 1 6
HELIX 51 51 SER D 24 LEU D 27 5 4
HELIX 52 52 ILE D 36 ALA D 46 1 11
HELIX 53 53 ASP D 59 GLY D 68 1 10
HELIX 54 54 GLY D 70 GLY D 74 5 5
HELIX 55 55 GLY D 87 ALA D 89 5 3
HELIX 56 56 GLN D 90 GLY D 95 1 6
HELIX 57 57 GLY D 95 GLY D 100 1 6
HELIX 58 58 ASP D 117 ARG D 128 1 12
HELIX 59 59 ASP D 141 ARG D 144 5 4
HELIX 60 60 GLN D 181 ASP D 188 1 8
HELIX 61 61 GLU D 198 ARG D 209 1 12
HELIX 62 62 THR D 228 GLY D 247 1 20
HELIX 63 63 CYS D 252 GLN D 260 1 9
HELIX 64 64 ASP D 264 ALA D 273 1 10
HELIX 65 65 PRO D 274 ALA D 276 5 3
HELIX 66 66 ASN D 278 LEU D 288 1 11
SHEET 1 AA 7 ASP A 76 VAL A 81 0
SHEET 2 AA 7 GLU A 50 SER A 55 1 O ILE A 51 N GLN A 78
SHEET 3 AA 7 ARG A 3 ALA A 9 1 O GLY A 5 N LEU A 52
SHEET 4 AA 7 LEU A 103 LEU A 108 1 O LEU A 103 N LYS A 4
SHEET 5 AA 7 TYR A 170 TYR A 178 -1 O GLY A 174 N LEU A 108
SHEET 6 AA 7 ALA A 132 HIS A 138 -1 O SER A 133 N PHE A 177
SHEET 7 AA 7 LEU A 212 ILE A 216 1 O SER A 213 N VAL A 134
SHEET 1 AB 2 PRO A 29 VAL A 30 0
SHEET 2 AB 2 LYS A 33 PRO A 34 -1 O LYS A 33 N VAL A 30
SHEET 1 AC 2 ASN A 111 TYR A 114 0
SHEET 2 AC 2 ALA A 222 ASP A 225 -1 O ALA A 222 N TYR A 114
SHEET 1 AD 2 GLY A 146 PHE A 150 0
SHEET 2 AD 2 ALA A 156 GLU A 161 -1 N ILE A 157 O GLU A 149
SHEET 1 BA 5 ASP B 76 VAL B 81 0
SHEET 2 BA 5 GLU B 50 SER B 55 1 O ILE B 51 N GLN B 78
SHEET 3 BA 5 ARG B 3 ALA B 9 1 O GLY B 5 N LEU B 52
SHEET 4 BA 5 LEU B 103 LEU B 108 1 O LEU B 103 N LYS B 4
SHEET 5 BA 5 LEU B 175 TYR B 178 -1 O TYR B 176 N LEU B 106
SHEET 1 BB 2 PRO B 29 VAL B 30 0
SHEET 2 BB 2 LYS B 33 PRO B 34 -1 O LYS B 33 N VAL B 30
SHEET 1 BC 2 LEU B 112 TYR B 114 0
SHEET 2 BC 2 ALA B 222 LEU B 224 -1 O ALA B 222 N TYR B 114
SHEET 1 BD 3 TYR B 170 VAL B 172 0
SHEET 2 BD 3 ALA B 132 HIS B 138 -1 O TYR B 137 N ALA B 171
SHEET 3 BD 3 LEU B 212 ILE B 216 1 O SER B 213 N VAL B 134
SHEET 1 BE 2 GLY B 146 PHE B 150 0
SHEET 2 BE 2 ALA B 156 GLU B 161 -1 N ILE B 157 O GLU B 149
SHEET 1 CA 7 ASP C 76 VAL C 81 0
SHEET 2 CA 7 GLU C 50 SER C 55 1 O ILE C 51 N GLN C 78
SHEET 3 CA 7 ARG C 3 LEU C 8 1 O GLY C 5 N LEU C 52
SHEET 4 CA 7 LEU C 103 LEU C 108 1 O LEU C 103 N LYS C 4
SHEET 5 CA 7 TYR C 170 TYR C 178 -1 O GLY C 174 N LEU C 108
SHEET 6 CA 7 ALA C 132 HIS C 138 -1 O SER C 133 N PHE C 177
SHEET 7 CA 7 LEU C 212 ILE C 216 1 O SER C 213 N VAL C 134
SHEET 1 CB 2 PRO C 29 VAL C 30 0
SHEET 2 CB 2 LYS C 33 PRO C 34 -1 O LYS C 33 N VAL C 30
SHEET 1 CC 2 ASN C 111 TYR C 114 0
SHEET 2 CC 2 ALA C 222 ASP C 225 -1 O ALA C 222 N TYR C 114
SHEET 1 CD 2 GLY C 146 PHE C 150 0
SHEET 2 CD 2 ALA C 156 GLU C 161 -1 N ILE C 157 O GLU C 149
SHEET 1 DA 5 ASP D 76 VAL D 81 0
SHEET 2 DA 5 GLU D 50 SER D 55 1 O ILE D 51 N GLN D 78
SHEET 3 DA 5 ARG D 3 ALA D 9 1 O GLY D 5 N LEU D 52
SHEET 4 DA 5 LEU D 103 LEU D 108 1 O LEU D 103 N LYS D 4
SHEET 5 DA 5 LEU D 175 TYR D 178 -1 O TYR D 176 N LEU D 106
SHEET 1 DB 2 PRO D 29 VAL D 30 0
SHEET 2 DB 2 LYS D 33 PRO D 34 -1 O LYS D 33 N VAL D 30
SHEET 1 DC 2 ASN D 111 TYR D 114 0
SHEET 2 DC 2 ALA D 222 ASP D 225 -1 O ALA D 222 N TYR D 114
SHEET 1 DD 3 TYR D 170 VAL D 172 0
SHEET 2 DD 3 ALA D 132 HIS D 138 -1 O TYR D 137 N ALA D 171
SHEET 3 DD 3 LEU D 212 ILE D 216 1 O SER D 213 N VAL D 134
SHEET 1 DE 2 GLY D 146 PHE D 150 0
SHEET 2 DE 2 ALA D 156 GLU D 161 -1 N ILE D 157 O GLU D 149
CISPEP 1 HIS A 17 PRO A 18 0 6.95
CISPEP 2 HIS B 17 PRO B 18 0 6.77
CISPEP 3 HIS C 17 PRO C 18 0 4.90
CISPEP 4 HIS D 17 PRO D 18 0 4.48
SITE 1 AC1 14 SER A 41 THR A 42 LEU A 45 TYR A 113
SITE 2 AC1 14 TYR A 114 GLY A 115 PHE A 118 VAL A 250
SITE 3 AC1 14 ALA A 251 GLU A 255 ILE A 256 HOH A2037
SITE 4 AC1 14 HOH A2070 HOH A2076
SITE 1 AC2 13 SER B 41 THR B 42 LEU B 45 TYR B 113
SITE 2 AC2 13 GLY B 115 HIS B 119 ARG B 219 VAL B 250
SITE 3 AC2 13 ALA B 251 GLU B 255 ILE B 256 HOH B2024
SITE 4 AC2 13 HOH B2053
SITE 1 AC3 15 SER C 41 LEU C 45 TYR C 113 TYR C 114
SITE 2 AC3 15 GLY C 115 PHE C 118 ARG C 219 VAL C 250
SITE 3 AC3 15 ALA C 251 GLU C 255 ILE C 256 HOH C2028
SITE 4 AC3 15 HOH C2031 HOH C2068 HOH C2075
SITE 1 AC4 15 SER D 41 LEU D 45 TYR D 113 TYR D 114
SITE 2 AC4 15 GLY D 115 PHE D 118 ARG D 219 VAL D 250
SITE 3 AC4 15 ALA D 251 GLU D 255 ILE D 256 HOH D2015
SITE 4 AC4 15 HOH D2035 HOH D2055 HOH D2064
SITE 1 AC5 3 HIS C 116 GLY C 220 HOH C2030
SITE 1 AC6 2 HIS A 116 GLY A 220
SITE 1 AC7 4 HIS B 116 GLY B 218 ARG B 219 GLY B 220
SITE 1 AC8 3 HIS D 116 ARG D 219 GLY D 220
CRYST1 64.090 154.400 134.540 90.00 92.39 90.00 C 1 2 1 16
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 0.015603 0.000000 0.000651 0.00000
SCALE2 0.000000 0.006477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007439 0.00000
MTRIX1 1 -0.935700 0.009294 -0.352700 62.30000 1
MTRIX2 1 -0.004804 -0.999900 -0.013600 -36.12000 1
MTRIX3 1 -0.352800 -0.011030 0.935600 10.93000 1
MTRIX1 2 0.999200 -0.006606 -0.040200 5.42400 1
MTRIX2 2 -0.006024 -0.999900 0.014580 -17.51000 1
MTRIX3 2 -0.040290 -0.014330 -0.999100 68.07000 1
MTRIX1 3 -0.955000 0.010410 0.296400 39.87000 1
MTRIX2 3 0.014040 0.999800 0.010140 -20.64000 1
MTRIX3 3 -0.296200 0.013850 -0.955000 72.52000 1
(ATOM LINES ARE NOT SHOWN.)
END
