HEADER TRANSFERASE 24-OCT-00 1G3L
TITLE THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF
TITLE 2 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). TDP-L-RHAMNOSE
TITLE 3 COMPLEX.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA);
COMPND 5 EC: 2.7.7.24;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(LAMBDA DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET23A(+)
KEYWDS L-RHAMNOSE, NUCLEOTIDYLTRANSFERASE, PYROPHOSPHORYLASE,
KEYWDS 2 THYMIDYLYLTRANSFERASE, ALLOSTERY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH
REVDAT 5 09-AUG-23 1G3L 1 REMARK
REVDAT 4 07-MAR-18 1G3L 1 REMARK
REVDAT 3 24-FEB-09 1G3L 1 VERSN
REVDAT 2 01-APR-03 1G3L 1 JRNL
REVDAT 1 27-DEC-00 1G3L 0
JRNL AUTH W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH
JRNL TITL THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND
JRNL TITL 2 REGULATION OF GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE
JRNL TITL 3 (RMLA).
JRNL REF EMBO J. V. 19 6652 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 11118200
JRNL DOI 10.1093/EMBOJ/19.24.6652
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.BLANKENFELDT,M.F.GIRAUD,G.LEONARD,R.RAHIM,C.CREUZENET,
REMARK 1 AUTH 2 J.S.LAM,J.H.NAISMITH
REMARK 1 TITL THE PURIFICATION, CRYSTALLISATION AND PRELIMINARY STRUCTURAL
REMARK 1 TITL 2 CHARACTERISATION OF GLUCOSE-1-PHOSPHATE
REMARK 1 TITL 3 THYMIDYLYLTRANSFERASE (RMLA), THE FIRST ENZYME OF THE
REMARK 1 TITL 4 DTDP-L-RHAMNOSE SYNTHESIS PATHWAY FROM PSEUDOMONAS
REMARK 1 TITL 5 AERUGINOSA
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1501 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900010040
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.MELO,L.GLASER
REMARK 1 TITL THE NUCLEOTIDE SPECIFICITY AND FEEDBACK CONTROL OF THYMIDINE
REMARK 1 TITL 2 DIPHOSPHATE D-GLUCOSE PYROPHOSPHORYLASE.
REMARK 1 REF J.BIOL.CHEM. V. 240 398 1965
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.70 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 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 34462
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1815
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9148
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 305
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.11
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.07000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -1.08000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.470
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.410
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G3L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.0
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
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
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36311
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 49.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.8
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.26600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1G1L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 % (W/V) PEG 6000, 0.2 M LI-SULFATE,
REMARK 280 0.1 M NA-CITRATE PH 4.0; PROTEIN INCUBATED WITH 10 MM DTDP-L-
REMARK 280 RHAMNOSE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 35.54350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.83800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.27850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.83800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.54350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.27850
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: THE BIOLOGICAL ASSEMBLY IS A TETRAMER CONSISTING OF TWO
REMARK 300 DIMERS.
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: 21980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 MET B 1
REMARK 465 MET C 1
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 OD1 ASP D 69 OG SER D 71 2.06
REMARK 500 OD1 ASP A 69 OG SER A 71 2.15
REMARK 500 OD2 ASP A 110 O3' TRH A 500 2.16
REMARK 500 OE1 GLN A 237 NE2 GLN B 237 2.17
REMARK 500 OG SER D 24 OD2 ASP D 59 2.17
REMARK 500 OD1 ASP B 69 OG SER B 71 2.18
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 ASP A 184 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 201 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 225 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 59 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 102 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 GLN B 152 CA - CB - CG ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP C 59 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP C 110 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 GLN C 152 CA - CB - CG ANGL. DEV. = -14.9 DEGREES
REMARK 500 ASP C 184 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP D 59 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP D 117 CB - CG - OD2 ANGL. DEV. = 5.8 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 LEU A 16 12.89 -67.74
REMARK 500 TYR A 31 -80.73 69.99
REMARK 500 THR A 289 25.89 -144.01
REMARK 500 LEU B 16 13.82 -65.74
REMARK 500 TYR B 31 -85.85 59.58
REMARK 500 THR B 226 64.96 -100.57
REMARK 500 ALA C 9 51.55 -118.16
REMARK 500 SER C 12 -154.54 -75.15
REMARK 500 ARG C 15 -89.46 -38.55
REMARK 500 LEU C 16 0.95 -51.88
REMARK 500 HIS C 17 151.55 -49.70
REMARK 500 ILE C 23 136.84 -174.48
REMARK 500 TYR C 31 -85.43 67.92
REMARK 500 THR C 226 62.31 -105.44
REMARK 500 ARG D 15 -72.18 -44.92
REMARK 500 HIS D 17 150.56 -49.66
REMARK 500 TYR D 31 -81.30 71.48
REMARK 500 ARG D 219 -7.63 -58.72
REMARK 500 LYS D 277 0.73 -66.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 HIS A 17 0.10 SIDE CHAIN
REMARK 500 HIS A 119 0.09 SIDE CHAIN
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 B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH C 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH D 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRH D 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G23 RELATED DB: PDB
REMARK 900 1G23 IS RMLA IN COMPLEX WITH GLUCOSE-1-PHOSPHATE
REMARK 900 RELATED ID: 1FXO RELATED DB: PDB
REMARK 900 1FXO IS RMLA IN COMPLEX WITH DTMP
REMARK 900 RELATED ID: 1FZW RELATED DB: PDB
REMARK 900 1FZW IS RMLA APO ENZYME
REMARK 900 RELATED ID: 1G2V RELATED DB: PDB
REMARK 900 1G2V IS RMLA IN COMPLEX WITH DTTP
REMARK 900 RELATED ID: 1G0R RELATED DB: PDB
REMARK 900 1G0R IS RMLA IN COMPLEX WITH GLUCOSE-1-PHOSPHATE AND THYMIDINE
REMARK 900 RELATED ID: 1G1L RELATED DB: PDB
REMARK 900 1G1L IS RMLA IN COMPLEX WITH DTDP-D-GLUCOSE
DBREF 1G3L A 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1G3L B 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1G3L C 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1G3L D 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
SEQRES 1 A 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 A 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 A 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 A 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 A 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 A 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 A 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 A 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 A 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 A 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 A 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 A 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 A 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 A 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 A 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 A 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 A 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 A 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 A 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 A 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 A 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 A 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 A 293 LEU LEU THR GLU THR VAL TYR
SEQRES 1 B 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 B 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 B 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 B 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 B 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 B 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 B 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 B 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 B 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 B 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 B 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 B 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 B 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 B 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 B 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 B 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 B 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 B 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 B 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 B 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 B 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 B 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 B 293 LEU LEU THR GLU THR VAL TYR
SEQRES 1 C 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 C 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 C 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 C 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 C 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 C 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 C 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 C 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 C 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 C 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 C 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 C 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 C 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 C 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 C 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 C 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 C 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 C 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 C 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 C 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 C 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 C 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 C 293 LEU LEU THR GLU THR VAL TYR
SEQRES 1 D 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 D 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 D 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 D 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 D 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 D 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 D 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 D 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 D 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 D 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 D 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 D 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 D 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 D 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 D 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 D 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 D 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 D 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 D 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 D 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 D 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 D 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 D 293 LEU LEU THR GLU THR VAL TYR
HET SO4 A 701 5
HET TRH A 500 35
HET TRH A 501 35
HET SO4 B 700 5
HET SO4 B 702 5
HET TRH B 502 35
HET TRH B 503 35
HET SO4 C 703 5
HET TRH C 504 35
HET TRH C 505 35
HET SO4 D 704 5
HET TRH D 506 35
HET TRH D 507 35
HETNAM SO4 SULFATE ION
HETNAM TRH 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 6 TRH 8(C16 H26 N2 O15 P2)
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 ALA A 89 GLY A 95 1 7
HELIX 6 6 GLY A 95 GLY A 100 1 6
HELIX 7 7 ASP A 117 ARG A 128 1 12
HELIX 8 8 ASP A 141 ARG A 144 5 4
HELIX 9 9 GLN A 181 ASP A 188 1 8
HELIX 10 10 GLU A 198 ARG A 209 1 12
HELIX 11 11 THR A 228 GLY A 247 1 20
HELIX 12 12 CYS A 252 GLN A 260 1 9
HELIX 13 13 ASP A 264 ALA A 273 1 10
HELIX 14 14 PRO A 274 ALA A 276 5 3
HELIX 15 15 ASN A 278 LEU A 288 1 11
HELIX 16 16 SER B 24 LEU B 27 5 4
HELIX 17 17 ILE B 36 ALA B 46 1 11
HELIX 18 18 ASP B 59 GLY B 68 1 10
HELIX 19 19 GLY B 70 GLY B 74 5 5
HELIX 20 20 ALA B 89 GLY B 95 1 7
HELIX 21 21 GLY B 95 GLY B 100 1 6
HELIX 22 22 ASP B 117 ARG B 128 1 12
HELIX 23 23 ASP B 141 ARG B 144 5 4
HELIX 24 24 GLN B 181 ASP B 188 1 8
HELIX 25 25 GLU B 198 ARG B 209 1 12
HELIX 26 26 THR B 228 GLY B 247 1 20
HELIX 27 27 CYS B 252 GLN B 260 1 9
HELIX 28 28 ASP B 264 ALA B 273 1 10
HELIX 29 29 PRO B 274 ALA B 276 5 3
HELIX 30 30 ASN B 278 LEU B 288 1 11
HELIX 31 31 SER C 24 LEU C 27 5 4
HELIX 32 32 ILE C 36 ALA C 46 1 11
HELIX 33 33 ASP C 59 GLY C 68 1 10
HELIX 34 34 GLY C 70 GLY C 74 5 5
HELIX 35 35 ALA C 89 GLY C 95 1 7
HELIX 36 36 GLY C 95 GLY C 100 1 6
HELIX 37 37 ASP C 117 GLN C 127 1 11
HELIX 38 38 ASP C 141 ARG C 144 5 4
HELIX 39 39 GLN C 181 ASP C 188 1 8
HELIX 40 40 GLU C 198 GLU C 208 1 11
HELIX 41 41 THR C 228 GLY C 247 1 20
HELIX 42 42 CYS C 252 GLN C 260 1 9
HELIX 43 43 ASP C 264 ALA C 273 1 10
HELIX 44 44 PRO C 274 ALA C 276 5 3
HELIX 45 45 ASN C 278 LEU C 288 1 11
HELIX 46 46 PRO D 18 ALA D 22 5 5
HELIX 47 47 SER D 24 LEU D 27 5 4
HELIX 48 48 ILE D 36 ALA D 46 1 11
HELIX 49 49 ASP D 59 GLY D 68 1 10
HELIX 50 50 GLY D 70 GLY D 74 5 5
HELIX 51 51 ALA D 89 GLY D 95 1 7
HELIX 52 52 GLY D 95 GLY D 100 1 6
HELIX 53 53 ASP D 117 ARG D 128 1 12
HELIX 54 54 ASP D 141 ARG D 144 5 4
HELIX 55 55 GLN D 181 ASP D 188 1 8
HELIX 56 56 GLU D 198 GLU D 208 1 11
HELIX 57 57 THR D 228 GLY D 247 1 20
HELIX 58 58 CYS D 252 GLN D 260 1 9
HELIX 59 59 ASP D 264 ALA D 273 1 10
HELIX 60 60 PRO D 274 ALA D 276 5 3
HELIX 61 61 ASN D 278 LEU D 288 1 11
SHEET 1 A 5 ASP A 76 VAL A 81 0
SHEET 2 A 5 GLU A 50 SER A 55 1 O ILE A 51 N GLN A 78
SHEET 3 A 5 ARG A 3 LEU A 8 1 O GLY A 5 N LEU A 52
SHEET 4 A 5 LEU A 103 LEU A 108 1 O LEU A 103 N LYS A 4
SHEET 5 A 5 LEU A 175 TYR A 178 -1 O TYR A 176 N LEU A 106
SHEET 1 B 2 PRO A 29 VAL A 30 0
SHEET 2 B 2 LYS A 33 PRO A 34 -1 O LYS A 33 N VAL A 30
SHEET 1 C 2 ASN A 111 TYR A 114 0
SHEET 2 C 2 ALA A 222 ASP A 225 -1 N ALA A 222 O TYR A 114
SHEET 1 D 3 TYR A 170 VAL A 172 0
SHEET 2 D 3 ALA A 132 HIS A 138 -1 O TYR A 137 N ALA A 171
SHEET 3 D 3 LEU A 212 ILE A 216 1 N SER A 213 O ALA A 132
SHEET 1 E 2 GLY A 146 PHE A 150 0
SHEET 2 E 2 ALA A 156 GLU A 161 -1 N ILE A 157 O GLU A 149
SHEET 1 F 7 ASP B 76 VAL B 81 0
SHEET 2 F 7 GLU B 50 SER B 55 1 O ILE B 51 N GLN B 78
SHEET 3 F 7 ARG B 3 ALA B 9 1 O GLY B 5 N LEU B 52
SHEET 4 F 7 LEU B 103 LEU B 108 1 O LEU B 103 N LYS B 4
SHEET 5 F 7 TYR B 170 TYR B 178 -1 O GLY B 174 N LEU B 108
SHEET 6 F 7 ALA B 132 HIS B 138 -1 N SER B 133 O PHE B 177
SHEET 7 F 7 LEU B 212 ILE B 216 1 O SER B 213 N VAL B 134
SHEET 1 G 2 PRO B 29 VAL B 30 0
SHEET 2 G 2 LYS B 33 PRO B 34 -1 O LYS B 33 N VAL B 30
SHEET 1 H 2 ASN B 111 TYR B 114 0
SHEET 2 H 2 ALA B 222 ASP B 225 -1 N ALA B 222 O TYR B 114
SHEET 1 I 2 GLY B 146 PHE B 150 0
SHEET 2 I 2 ALA B 156 GLU B 161 -1 N ILE B 157 O GLU B 149
SHEET 1 J 5 ASP C 76 VAL C 81 0
SHEET 2 J 5 GLU C 50 SER C 55 1 O ILE C 51 N GLN C 78
SHEET 3 J 5 ARG C 3 ALA C 9 1 O GLY C 5 N LEU C 52
SHEET 4 J 5 LEU C 103 LEU C 108 1 O LEU C 103 N LYS C 4
SHEET 5 J 5 LEU C 175 TYR C 178 -1 N TYR C 176 O LEU C 106
SHEET 1 K 2 PRO C 29 VAL C 30 0
SHEET 2 K 2 LYS C 33 PRO C 34 -1 O LYS C 33 N VAL C 30
SHEET 1 L 2 ASN C 111 TYR C 114 0
SHEET 2 L 2 ALA C 222 ASP C 225 -1 N ALA C 222 O TYR C 114
SHEET 1 M 3 TYR C 170 VAL C 172 0
SHEET 2 M 3 ALA C 132 HIS C 138 -1 N TYR C 137 O ALA C 171
SHEET 3 M 3 LEU C 212 ILE C 216 1 O SER C 213 N VAL C 134
SHEET 1 N 2 GLY C 146 PHE C 150 0
SHEET 2 N 2 ALA C 156 GLU C 161 -1 N ILE C 157 O GLU C 149
SHEET 1 O 5 ASP D 76 VAL D 81 0
SHEET 2 O 5 GLU D 50 SER D 55 1 O ILE D 51 N GLN D 78
SHEET 3 O 5 ARG D 3 LEU D 8 1 O GLY D 5 N LEU D 52
SHEET 4 O 5 LEU D 103 LEU D 108 1 O LEU D 103 N LYS D 4
SHEET 5 O 5 LEU D 175 TYR D 178 -1 N TYR D 176 O LEU D 106
SHEET 1 P 2 PRO D 29 VAL D 30 0
SHEET 2 P 2 LYS D 33 PRO D 34 -1 O LYS D 33 N VAL D 30
SHEET 1 Q 2 ASN D 111 TYR D 114 0
SHEET 2 Q 2 ALA D 222 ASP D 225 -1 N ALA D 222 O TYR D 114
SHEET 1 R 3 TYR D 170 VAL D 172 0
SHEET 2 R 3 ALA D 132 HIS D 138 -1 N TYR D 137 O ALA D 171
SHEET 3 R 3 LEU D 212 ILE D 216 1 O SER D 213 N VAL D 134
SHEET 1 S 2 GLY D 146 PHE D 150 0
SHEET 2 S 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 -3.94
CISPEP 2 HIS B 17 PRO B 18 0 -6.58
CISPEP 3 HIS C 17 PRO C 18 0 0.73
CISPEP 4 HIS D 17 PRO D 18 0 -3.51
SITE 1 AC1 3 ARG A 62 PRO B 61 ARG B 62
SITE 1 AC2 4 ARG A 128 GLU A 215 ASP D 151 GLN D 152
SITE 1 AC3 4 ARG B 128 GLU B 215 ASP C 151 GLN C 152
SITE 1 AC4 3 ARG C 128 GLN C 129 THR C 130
SITE 1 AC5 3 ARG D 128 GLN D 129 THR D 130
SITE 1 AC6 20 LEU A 8 ALA A 9 GLY A 10 GLY A 11
SITE 2 AC6 20 GLN A 82 PRO A 85 ASP A 86 GLY A 87
SITE 3 AC6 20 ASP A 110 TYR A 145 GLY A 146 GLU A 161
SITE 4 AC6 20 LYS A 162 VAL A 172 THR A 173 GLY A 174
SITE 5 AC6 20 TYR A 176 ARG A 194 GLU A 196 THR A 200
SITE 1 AC7 16 TYR A 114 GLY A 115 HIS A 116 ASP A 117
SITE 2 AC7 16 PHE A 118 HIS A 119 GLU A 120 VAL A 250
SITE 3 AC7 16 ALA A 251 GLU A 255 ILE A 256 ARG A 259
SITE 4 AC7 16 TYR A 293 GLY C 218 ARG C 219 GLY C 220
SITE 1 AC8 18 LEU B 8 GLY B 10 GLY B 11 GLN B 82
SITE 2 AC8 18 PRO B 85 ASP B 86 GLY B 87 ASP B 110
SITE 3 AC8 18 TYR B 145 GLY B 146 GLU B 161 LYS B 162
SITE 4 AC8 18 VAL B 172 THR B 173 TYR B 176 ARG B 194
SITE 5 AC8 18 GLU B 196 THR B 200
SITE 1 AC9 15 LEU B 45 TYR B 114 GLY B 115 HIS B 116
SITE 2 AC9 15 ASP B 117 PHE B 118 HIS B 119 GLU B 120
SITE 3 AC9 15 ALA B 251 GLU B 255 ILE B 256 ARG B 259
SITE 4 AC9 15 GLY D 218 ARG D 219 GLY D 220
SITE 1 BC1 18 LEU C 8 GLY C 10 GLY C 11 GLN C 82
SITE 2 BC1 18 PRO C 85 ASP C 86 GLY C 87 LEU C 108
SITE 3 BC1 18 ASP C 110 TYR C 145 GLY C 146 GLU C 161
SITE 4 BC1 18 LYS C 162 VAL C 172 TYR C 176 ARG C 194
SITE 5 BC1 18 GLU C 196 THR C 200
SITE 1 BC2 16 GLY A 218 ARG A 219 GLY A 220 LEU C 45
SITE 2 BC2 16 TYR C 114 GLY C 115 HIS C 116 ASP C 117
SITE 3 BC2 16 PHE C 118 HIS C 119 GLU C 120 VAL C 250
SITE 4 BC2 16 ALA C 251 GLU C 255 ARG C 259 TYR C 293
SITE 1 BC3 18 LEU D 8 GLY D 10 GLY D 11 GLN D 26
SITE 2 BC3 18 GLN D 82 PRO D 85 ASP D 86 GLY D 87
SITE 3 BC3 18 ASP D 110 GLY D 146 GLU D 161 LYS D 162
SITE 4 BC3 18 VAL D 172 THR D 173 TYR D 176 ARG D 194
SITE 5 BC3 18 GLU D 196 THR D 200
SITE 1 BC4 16 ILE B 216 GLY B 218 ARG B 219 GLY B 220
SITE 2 BC4 16 LEU D 45 TYR D 114 GLY D 115 HIS D 116
SITE 3 BC4 16 ASP D 117 PHE D 118 HIS D 119 ALA D 251
SITE 4 BC4 16 GLU D 255 ILE D 256 ARG D 259 TYR D 293
CRYST1 71.087 138.557 139.676 90.00 90.00 90.00 P 21 21 21 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 0.014067 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007217 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007159 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
