HEADER TRANSFERASE 04-OCT-00 1FZW
TITLE THE STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND REGULATION OF
TITLE 2 GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE (RMLA). APO ENZYME.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE-1-PHOSPHATE THYMIDYLYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
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_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET23A(+)
KEYWDS RHAMNOSE, NUCLEOTIDYLTRANSFERASE, PYROPHOSPHORYLASE,
KEYWDS 2 THYMIDYLYLTRANSFERASE, ALLOSTERY, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.BLANKENFELDT,M.ASUNCION,J.S.LAM,J.H.NAISMITH
REVDAT 4 07-FEB-24 1FZW 1 REMARK
REVDAT 3 24-FEB-09 1FZW 1 VERSN
REVDAT 2 01-APR-03 1FZW 1 JRNL
REVDAT 1 27-DEC-00 1FZW 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. 1.90 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 190758
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.176
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 : 10141
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12512
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.80
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : 623
REMARK 3 BIN FREE R VALUE : 0.4500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18296
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 100
REMARK 3 SOLVENT ATOMS : 2478
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : -0.10000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : -0.19000
REMARK 3 B13 (A**2) : -0.13000
REMARK 3 B23 (A**2) : -0.09000
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): 0.220
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.180
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.570
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 1FZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012058.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 202988
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 72.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.28600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA-CITRATE, 0.5 M LI-SULFATE, 9
REMARK 280 -11% (W/V) PEG 6000, PH 4.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER THAT CAN BE DESCRIBED
REMARK 300 AS A DIMER OF 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: 14130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -179.0 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 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: 14640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43530 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -213.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 D 1
REMARK 465 MET E 1
REMARK 465 MET G 1
REMARK 465 MET H 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 O GLY C 13 O HOH C 5196 1.92
REMARK 500 O HOH G 4974 O HOH G 5200 1.92
REMARK 500 O HOH A 3792 O HOH A 3828 1.92
REMARK 500 O HOH D 3856 O HOH D 3939 1.95
REMARK 500 O HOH B 3945 O HOH B 3969 1.97
REMARK 500 OE2 GLU F 269 O HOH F 4984 1.97
REMARK 500 O HOH A 3921 O HOH C 5044 1.99
REMARK 500 OG SER C 55 O HOH C 5263 2.00
REMARK 500 O HOH H 6285 O HOH H 6378 2.01
REMARK 500 O HOH G 5102 O HOH G 5182 2.02
REMARK 500 N PHE E 98 O HOH E 6239 2.02
REMARK 500 O HOH G 5090 O HOH G 5200 2.02
REMARK 500 O HOH G 4968 O HOH G 5041 2.03
REMARK 500 O HOH F 4745 O HOH F 4946 2.04
REMARK 500 N GLY E 227 O HOH E 6150 2.04
REMARK 500 O HOH C 5115 O HOH C 5233 2.04
REMARK 500 O HOH C 5111 O HOH C 5153 2.04
REMARK 500 OD1 ASP B 141 O HOH B 3954 2.07
REMARK 500 O HOH C 5146 O HOH C 5255 2.07
REMARK 500 O HOH B 3781 O HOH B 3835 2.08
REMARK 500 OE1 GLN G 127 O HOH G 5199 2.09
REMARK 500 OE1 GLN G 152 O HOH G 5042 2.09
REMARK 500 OE2 GLU B 149 O HOH B 3960 2.09
REMARK 500 N LYS H 2 O HOH H 6268 2.09
REMARK 500 O HOH D 3966 O HOH D 4034 2.09
REMARK 500 NE2 GLN E 26 O HOH E 6286 2.09
REMARK 500 O HOH C 5044 O HOH C 5204 2.10
REMARK 500 O HOH G 4930 O HOH G 5071 2.11
REMARK 500 O GLN E 26 O HOH E 6299 2.11
REMARK 500 OE2 GLU C 234 O HOH C 5256 2.11
REMARK 500 O HOH E 6146 O HOH E 6284 2.11
REMARK 500 OD2 ASP F 141 NH2 ARG F 144 2.12
REMARK 500 NH2 ARG F 15 O HOH F 4951 2.12
REMARK 500 OD1 ASP A 141 O HOH A 3913 2.12
REMARK 500 O HOH G 5261 O HOH H 6148 2.12
REMARK 500 O HOH D 3855 O HOH D 3992 2.13
REMARK 500 CD2 HIS C 119 O HOH C 5244 2.13
REMARK 500 O HOH H 6257 O HOH H 6320 2.14
REMARK 500 O HOH F 4803 O HOH F 5013 2.14
REMARK 500 O HOH B 3798 O HOH B 3981 2.14
REMARK 500 NE2 HIS B 17 O HOH B 3873 2.14
REMARK 500 O HOH A 3871 O HOH A 3875 2.14
REMARK 500 NH1 ARG B 128 O HOH B 3973 2.15
REMARK 500 NH2 ARG E 128 OE2 GLU E 215 2.15
REMARK 500 O HOH G 5178 O HOH G 5192 2.15
REMARK 500 NE2 GLN E 260 O HOH E 6211 2.15
REMARK 500 OE1 GLN A 90 O HOH A 3877 2.15
REMARK 500 NE2 GLN E 260 O HOH E 6211 2.16
REMARK 500 NH1 ARG E 128 OG SER E 133 2.16
REMARK 500 O HOH C 5100 O HOH C 5111 2.16
REMARK 500
REMARK 500 THIS ENTRY HAS 69 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER G 84 O HOH F 4852 1655 1.25
REMARK 500 O HOH A 3776 O HOH F 4954 1566 1.99
REMARK 500 O HOH F 4955 O HOH G 5148 1455 2.06
REMARK 500 O HOH G 5209 O HOH H 6340 1565 2.09
REMARK 500 O HOH F 4950 O HOH G 4974 1455 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 38 CE1 TYR A 38 CZ 0.085
REMARK 500 ARG A 128 CZ ARG A 128 NH2 -0.131
REMARK 500 VAL A 148 CB VAL A 148 CG1 -0.128
REMARK 500 SER A 213 CB SER A 213 OG 0.086
REMARK 500 TYR A 221 CE2 TYR A 221 CD2 0.092
REMARK 500 LYS A 249 CE LYS A 249 NZ 0.166
REMARK 500 MET B 35 CG MET B 35 SD -0.176
REMARK 500 TYR B 114 CE2 TYR B 114 CD2 -0.109
REMARK 500 PHE B 135 CZ PHE B 135 CE2 -0.128
REMARK 500 TYR B 145 CE1 TYR B 145 CZ -0.084
REMARK 500 TYR B 178 CD1 TYR B 178 CE1 0.098
REMARK 500 GLN B 180 CG GLN B 180 CD 0.155
REMARK 500 ARG B 245 CG ARG B 245 CD -0.167
REMARK 500 PHE C 92 CE1 PHE C 92 CZ -0.138
REMARK 500 TYR C 137 CZ TYR C 137 CE2 -0.082
REMARK 500 TYR C 206 CG TYR C 206 CD1 -0.097
REMARK 500 ALA C 222 CA ALA C 222 CB -0.129
REMARK 500 ALA C 257 CA ALA C 257 CB -0.136
REMARK 500 MET D 35 CG MET D 35 SD -0.248
REMARK 500 PHE D 92 CB PHE D 92 CG -0.106
REMARK 500 GLU D 120 CD GLU D 120 OE1 0.078
REMARK 500 GLU D 120 CD GLU D 120 OE2 0.075
REMARK 500 TYR D 137 CE2 TYR D 137 CD2 0.107
REMARK 500 TYR D 206 CE2 TYR D 206 CD2 -0.095
REMARK 500 TYR E 38 CG TYR E 38 CD1 0.080
REMARK 500 GLU E 120 CD GLU E 120 OE1 0.074
REMARK 500 TYR E 137 CE2 TYR E 137 CD2 0.103
REMARK 500 LYS E 249 CD LYS E 249 CE 0.206
REMARK 500 TYR E 280 CD1 TYR E 280 CE1 0.104
REMARK 500 ILE F 51 N ILE F 51 CA -0.125
REMARK 500 TYR F 79 CE1 TYR F 79 CZ 0.094
REMARK 500 SER F 124 CB SER F 124 OG 0.083
REMARK 500 TYR F 137 CG TYR F 137 CD2 -0.103
REMARK 500 ARG F 144 CG ARG F 144 CD 0.154
REMARK 500 VAL F 172 CB VAL F 172 CG1 0.136
REMARK 500 LYS F 249 CD LYS F 249 CE 0.153
REMARK 500 ALA F 251 CA ALA F 251 CB 0.167
REMARK 500 ARG F 286 CG ARG F 286 CD 0.166
REMARK 500 ALA G 105 CA ALA G 105 CB -0.145
REMARK 500 PHE G 118 CG PHE G 118 CD1 -0.111
REMARK 500 PHE G 118 CE1 PHE G 118 CZ -0.116
REMARK 500 PHE G 118 CZ PHE G 118 CE2 0.117
REMARK 500 GLU G 120 CD GLU G 120 OE1 0.068
REMARK 500 SER G 124 CB SER G 124 OG 0.095
REMARK 500 ARG G 128 CB ARG G 128 CG -0.166
REMARK 500 VAL G 148 CB VAL G 148 CG1 -0.161
REMARK 500 GLU G 149 CD GLU G 149 OE2 -0.069
REMARK 500 TYR G 178 CZ TYR G 178 CE2 0.081
REMARK 500 VAL G 214 CB VAL G 214 CG2 -0.138
REMARK 500 TRP G 223 CB TRP G 223 CG 0.124
REMARK 500
REMARK 500 THIS ENTRY HAS 63 BOND DEVIATIONS.
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 102 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 117 CB - CG - OD2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 128 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ASP A 201 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 209 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG A 286 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 MET B 35 CG - SD - CE ANGL. DEV. = 10.5 DEGREES
REMARK 500 ASP B 69 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 76 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP B 86 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP B 102 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP B 117 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 LEU B 121 CB - CG - CD1 ANGL. DEV. = -12.1 DEGREES
REMARK 500 ASP B 151 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP B 188 CB - CG - OD2 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP B 201 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 209 NE - CZ - NH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG B 219 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 245 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 286 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP C 69 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP C 86 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 PHE C 118 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP C 141 CB - CG - OD1 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG C 144 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 144 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP C 151 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 GLY C 154 N - CA - C ANGL. DEV. = 15.8 DEGREES
REMARK 500 THR C 226 OG1 - CB - CG2 ANGL. DEV. = -14.8 DEGREES
REMARK 500 LEU C 232 CB - CG - CD1 ANGL. DEV. = 13.3 DEGREES
REMARK 500 CYS C 252 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG C 259 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 259 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP C 264 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP D 69 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP D 76 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP D 86 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP D 141 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ASP D 188 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU E 88 CA - CB - CG ANGL. DEV. = 20.4 DEGREES
REMARK 500 LEU E 88 CB - CG - CD2 ANGL. DEV. = 11.5 DEGREES
REMARK 500 ARG E 144 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG E 144 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP E 151 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP E 188 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP F 59 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP F 69 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP F 86 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 74 ANGLE DEVIATIONS.
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 31 -90.17 64.03
REMARK 500 PRO A 85 73.90 -67.35
REMARK 500 ASN A 101 48.25 -108.26
REMARK 500 ASP A 179 -164.81 -79.89
REMARK 500 THR A 226 41.99 -101.38
REMARK 500 ALA B 9 55.46 -116.05
REMARK 500 SER B 24 154.60 -45.29
REMARK 500 TYR B 31 -81.03 65.35
REMARK 500 ASN B 101 41.24 -106.16
REMARK 500 TYR C 31 -94.22 64.48
REMARK 500 SER C 192 -178.34 -60.41
REMARK 500 ARG C 194 16.12 -67.46
REMARK 500 THR C 226 42.43 -99.25
REMARK 500 THR D 14 -58.01 -20.99
REMARK 500 TYR D 31 -82.00 73.55
REMARK 500 ALA D 273 -70.27 -39.72
REMARK 500 THR E 14 -59.35 -7.06
REMARK 500 TYR E 31 -86.38 58.41
REMARK 500 PRO E 191 103.71 -47.23
REMARK 500 SER E 192 162.18 -33.07
REMARK 500 THR F 14 -39.21 -32.37
REMARK 500 ARG F 15 -77.67 -55.43
REMARK 500 LEU F 16 2.57 -62.35
REMARK 500 ALA F 19 -39.98 -38.81
REMARK 500 TYR F 31 -87.57 61.05
REMARK 500 LEU G 16 41.49 -102.31
REMARK 500 LEU G 21 -38.08 -37.13
REMARK 500 TYR G 31 -82.56 67.18
REMARK 500 ASP G 86 30.78 -99.65
REMARK 500 ASN G 101 50.51 -107.36
REMARK 500 TYR H 31 -85.19 59.81
REMARK 500 THR H 226 40.27 -107.80
REMARK 500 LEU H 287 -19.34 -49.76
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 C 119 0.09 SIDE CHAIN
REMARK 500 HIS G 17 0.07 SIDE CHAIN
REMARK 500 HIS G 138 0.08 SIDE CHAIN
REMARK 500 HIS H 17 0.07 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 C 3600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 3604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 3605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 3606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 3607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3701
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 3800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 4700
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 4900
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 3704
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 5000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 6100
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 6101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FXO RELATED DB: PDB
REMARK 900 1FXO IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-5'-MONOPHOSPHATE
REMARK 900 (TMP)
REMARK 900 RELATED ID: 1G0R RELATED DB: PDB
REMARK 900 1G0R IS RMLA IN COMPLEX WITH 2'-DEOXY-THIMIDINE (THM) AND ALPHA-D-
REMARK 900 GLUCOSE-1-PHOSPHATE (G1P)
REMARK 900 RELATED ID: 1G1L RELATED DB: PDB
REMARK 900 1G1L IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-ALPHA-D-GLUCOSE
REMARK 900 (TDG)
REMARK 900 RELATED ID: 1G23 RELATED DB: PDB
REMARK 900 1G23 IS RMLA IN COMPLEX WITH ALPHA-D-GLUCOSE-1-PHOSPHATE (G1P)
REMARK 900 RELATED ID: 1G2V RELATED DB: PDB
REMARK 900 1G2V IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-5'-TRIPHOSPHATE
REMARK 900 (TTP)
REMARK 900 RELATED ID: 1G31 RELATED DB: PDB
REMARK 900 1G31 IS RMLA IN COMPLEX WITH 2'-DEOXY-THYMIDINE-BETA-L-RHAMNOSE
REMARK 900 (TDR)
DBREF 1FZW A 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1FZW B 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1FZW C 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1FZW D 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1FZW E 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1FZW F 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1FZW G 1 293 UNP Q9HU22 Q9HU22_PSEAE 1 293
DBREF 1FZW H 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
SEQRES 1 E 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 E 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 E 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 E 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 E 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 E 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 E 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 E 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 E 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 E 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 E 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 E 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 E 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 E 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 E 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 E 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 E 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 E 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 E 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 E 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 E 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 E 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 E 293 LEU LEU THR GLU THR VAL TYR
SEQRES 1 F 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 F 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 F 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 F 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 F 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 F 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 F 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 F 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 F 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 F 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 F 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 F 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 F 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 F 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 F 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 F 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 F 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 F 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 F 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 F 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 F 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 F 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 F 293 LEU LEU THR GLU THR VAL TYR
SEQRES 1 G 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 G 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 G 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 G 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 G 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 G 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 G 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 G 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 G 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 G 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 G 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 G 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 G 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 G 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 G 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 G 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 G 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 G 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 G 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 G 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 G 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 G 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 G 293 LEU LEU THR GLU THR VAL TYR
SEQRES 1 H 293 MET LYS ARG LYS GLY ILE ILE LEU ALA GLY GLY SER GLY
SEQRES 2 H 293 THR ARG LEU HIS PRO ALA THR LEU ALA ILE SER LYS GLN
SEQRES 3 H 293 LEU LEU PRO VAL TYR ASP LYS PRO MET ILE TYR TYR PRO
SEQRES 4 H 293 LEU SER THR LEU MET LEU ALA GLY ILE ARG GLU ILE LEU
SEQRES 5 H 293 ILE ILE SER THR PRO GLN ASP THR PRO ARG PHE GLN GLN
SEQRES 6 H 293 LEU LEU GLY ASP GLY SER ASN TRP GLY LEU ASP LEU GLN
SEQRES 7 H 293 TYR ALA VAL GLN PRO SER PRO ASP GLY LEU ALA GLN ALA
SEQRES 8 H 293 PHE LEU ILE GLY GLU SER PHE ILE GLY ASN ASP LEU SER
SEQRES 9 H 293 ALA LEU VAL LEU GLY ASP ASN LEU TYR TYR GLY HIS ASP
SEQRES 10 H 293 PHE HIS GLU LEU LEU GLY SER ALA SER GLN ARG GLN THR
SEQRES 11 H 293 GLY ALA SER VAL PHE ALA TYR HIS VAL LEU ASP PRO GLU
SEQRES 12 H 293 ARG TYR GLY VAL VAL GLU PHE ASP GLN GLY GLY LYS ALA
SEQRES 13 H 293 ILE SER LEU GLU GLU LYS PRO LEU GLU PRO LYS SER ASN
SEQRES 14 H 293 TYR ALA VAL THR GLY LEU TYR PHE TYR ASP GLN GLN VAL
SEQRES 15 H 293 VAL ASP ILE ALA ARG ASP LEU LYS PRO SER PRO ARG GLY
SEQRES 16 H 293 GLU LEU GLU ILE THR ASP VAL ASN ARG ALA TYR LEU GLU
SEQRES 17 H 293 ARG GLY GLN LEU SER VAL GLU ILE MET GLY ARG GLY TYR
SEQRES 18 H 293 ALA TRP LEU ASP THR GLY THR HIS ASP SER LEU LEU GLU
SEQRES 19 H 293 ALA GLY GLN PHE ILE ALA THR LEU GLU ASN ARG GLN GLY
SEQRES 20 H 293 LEU LYS VAL ALA CYS PRO GLU GLU ILE ALA TYR ARG GLN
SEQRES 21 H 293 LYS TRP ILE ASP ALA ALA GLN LEU GLU LYS LEU ALA ALA
SEQRES 22 H 293 PRO LEU ALA LYS ASN GLY TYR GLY GLN TYR LEU LYS ARG
SEQRES 23 H 293 LEU LEU THR GLU THR VAL TYR
HET SO4 A3602 5
HET SO4 A3700 5
HET SO4 B3603 5
HET SO4 B3701 5
HET SO4 C3600 5
HET SO4 C3702 5
HET SO4 C5000 5
HET SO4 D3601 5
HET SO4 D3703 5
HET SO4 D3800 5
HET SO4 E3607 5
HET SO4 E5001 5
HET SO4 E6100 5
HET SO4 F3606 5
HET SO4 F4700 5
HET SO4 G3605 5
HET SO4 G4900 5
HET SO4 G3704 5
HET SO4 H3604 5
HET SO4 H6101 5
HETNAM SO4 SULFATE ION
FORMUL 9 SO4 20(O4 S 2-)
FORMUL 29 HOH *2478(H2 O)
HELIX 1 1 GLY A 13 HIS A 17 5 5
HELIX 2 2 PRO A 18 ILE A 23 1 6
HELIX 3 3 SER A 24 LEU A 27 5 4
HELIX 4 4 ILE A 36 ALA A 46 1 11
HELIX 5 5 ASP A 59 GLY A 68 1 10
HELIX 6 6 GLY A 70 GLY A 74 5 5
HELIX 7 7 GLY A 87 ALA A 89 5 3
HELIX 8 8 GLN A 90 GLY A 95 1 6
HELIX 9 9 GLY A 95 GLY A 100 1 6
HELIX 10 10 ASP A 117 ARG A 128 1 12
HELIX 11 11 ASP A 141 ARG A 144 5 4
HELIX 12 12 GLN A 181 ASP A 188 1 8
HELIX 13 13 GLU A 198 ARG A 209 1 12
HELIX 14 14 THR A 228 GLY A 247 1 20
HELIX 15 15 CYS A 252 GLN A 260 1 9
HELIX 16 16 ASP A 264 ALA A 273 1 10
HELIX 17 17 PRO A 274 ALA A 276 5 3
HELIX 18 18 ASN A 278 GLU A 290 1 13
HELIX 19 19 GLY B 13 HIS B 17 5 5
HELIX 20 20 SER B 24 LEU B 27 5 4
HELIX 21 21 ILE B 36 ALA B 46 1 11
HELIX 22 22 ASP B 59 GLY B 68 1 10
HELIX 23 23 GLY B 70 GLY B 74 5 5
HELIX 24 24 GLY B 87 ALA B 89 5 3
HELIX 25 25 GLN B 90 GLY B 95 1 6
HELIX 26 26 GLY B 95 GLY B 100 1 6
HELIX 27 27 ASP B 117 ARG B 128 1 12
HELIX 28 28 ASP B 141 ARG B 144 5 4
HELIX 29 29 GLN B 181 LEU B 189 1 9
HELIX 30 30 GLU B 198 ARG B 209 1 12
HELIX 31 31 THR B 228 GLY B 247 1 20
HELIX 32 32 CYS B 252 GLN B 260 1 9
HELIX 33 33 ASP B 264 ALA B 273 1 10
HELIX 34 34 PRO B 274 ALA B 276 5 3
HELIX 35 35 ASN B 278 GLU B 290 1 13
HELIX 36 36 GLY C 13 HIS C 17 5 5
HELIX 37 37 PRO C 18 ALA C 22 5 5
HELIX 38 38 SER C 24 LEU C 27 5 4
HELIX 39 39 ILE C 36 ALA C 46 1 11
HELIX 40 40 ASP C 59 GLY C 68 1 10
HELIX 41 41 GLY C 70 GLY C 74 5 5
HELIX 42 42 GLY C 87 ALA C 89 5 3
HELIX 43 43 GLN C 90 GLY C 95 1 6
HELIX 44 44 GLY C 95 GLY C 100 1 6
HELIX 45 45 ASP C 117 ARG C 128 1 12
HELIX 46 46 ASP C 141 ARG C 144 5 4
HELIX 47 47 GLN C 181 LEU C 189 1 9
HELIX 48 48 GLU C 198 GLU C 208 1 11
HELIX 49 49 THR C 228 GLY C 247 1 20
HELIX 50 50 CYS C 252 GLN C 260 1 9
HELIX 51 51 ASP C 264 ALA C 273 1 10
HELIX 52 52 PRO C 274 ALA C 276 5 3
HELIX 53 53 ASN C 278 GLU C 290 1 13
HELIX 54 54 GLY D 13 HIS D 17 5 5
HELIX 55 55 SER D 24 LEU D 27 5 4
HELIX 56 56 ILE D 36 ALA D 46 1 11
HELIX 57 57 ASP D 59 GLY D 68 1 10
HELIX 58 58 GLY D 70 GLY D 74 5 5
HELIX 59 59 GLY D 87 ALA D 89 5 3
HELIX 60 60 GLN D 90 GLY D 95 1 6
HELIX 61 61 GLY D 95 GLY D 100 1 6
HELIX 62 62 ASP D 117 GLN D 127 1 11
HELIX 63 63 ASP D 141 ARG D 144 5 4
HELIX 64 64 GLN D 181 ASP D 188 1 8
HELIX 65 65 GLU D 198 GLU D 208 1 11
HELIX 66 66 THR D 228 GLY D 247 1 20
HELIX 67 67 CYS D 252 GLN D 260 1 9
HELIX 68 68 ASP D 264 ALA D 273 1 10
HELIX 69 69 PRO D 274 ALA D 276 5 3
HELIX 70 70 ASN D 278 GLU D 290 1 13
HELIX 71 71 GLY E 13 HIS E 17 5 5
HELIX 72 72 SER E 24 LEU E 27 5 4
HELIX 73 73 ILE E 36 ALA E 46 1 11
HELIX 74 74 ASP E 59 GLY E 68 1 10
HELIX 75 75 GLY E 70 GLY E 74 5 5
HELIX 76 76 GLY E 87 ALA E 89 5 3
HELIX 77 77 GLN E 90 GLY E 95 1 6
HELIX 78 78 GLY E 95 GLY E 100 1 6
HELIX 79 79 ASP E 117 ARG E 128 1 12
HELIX 80 80 ASP E 141 ARG E 144 5 4
HELIX 81 81 GLN E 181 ASP E 188 1 8
HELIX 82 82 GLU E 198 GLU E 208 1 11
HELIX 83 83 THR E 228 GLY E 247 1 20
HELIX 84 84 CYS E 252 GLN E 260 1 9
HELIX 85 85 ASP E 264 ALA E 273 1 10
HELIX 86 86 PRO E 274 ALA E 276 5 3
HELIX 87 87 ASN E 278 LEU E 287 1 10
HELIX 88 88 SER F 24 LEU F 27 5 4
HELIX 89 89 ILE F 36 ALA F 46 1 11
HELIX 90 90 ASP F 59 GLY F 68 1 10
HELIX 91 91 GLY F 70 GLY F 74 5 5
HELIX 92 92 ALA F 89 GLY F 95 1 7
HELIX 93 93 GLY F 95 GLY F 100 1 6
HELIX 94 94 ASP F 117 ARG F 128 1 12
HELIX 95 95 ASP F 141 ARG F 144 5 4
HELIX 96 96 GLN F 181 ASP F 188 1 8
HELIX 97 97 GLU F 198 GLU F 208 1 11
HELIX 98 98 THR F 228 GLY F 247 1 20
HELIX 99 99 CYS F 252 GLN F 260 1 9
HELIX 100 100 ASP F 264 ALA F 273 1 10
HELIX 101 101 PRO F 274 ALA F 276 5 3
HELIX 102 102 ASN F 278 LEU F 287 1 10
HELIX 103 103 GLY G 13 HIS G 17 5 5
HELIX 104 104 SER G 24 LEU G 27 5 4
HELIX 105 105 ILE G 36 ALA G 46 1 11
HELIX 106 106 ASP G 59 GLY G 68 1 10
HELIX 107 107 GLY G 70 GLY G 74 5 5
HELIX 108 108 GLY G 87 ALA G 89 5 3
HELIX 109 109 GLN G 90 GLY G 95 1 6
HELIX 110 110 GLY G 95 GLY G 100 1 6
HELIX 111 111 ASP G 117 ARG G 128 1 12
HELIX 112 112 ASP G 141 ARG G 144 5 4
HELIX 113 113 GLN G 181 ASP G 188 1 8
HELIX 114 114 GLU G 198 ARG G 209 1 12
HELIX 115 115 THR G 228 GLY G 247 1 20
HELIX 116 116 CYS G 252 GLN G 260 1 9
HELIX 117 117 ASP G 264 ALA G 273 1 10
HELIX 118 118 PRO G 274 ALA G 276 5 3
HELIX 119 119 ASN G 278 THR G 289 1 12
HELIX 120 120 GLY H 13 HIS H 17 5 5
HELIX 121 121 SER H 24 LEU H 27 5 4
HELIX 122 122 ILE H 36 ALA H 46 1 11
HELIX 123 123 ASP H 59 GLY H 68 1 10
HELIX 124 124 GLY H 70 GLY H 74 5 5
HELIX 125 125 GLY H 87 ALA H 89 5 3
HELIX 126 126 GLN H 90 GLY H 95 1 6
HELIX 127 127 GLY H 95 GLY H 100 1 6
HELIX 128 128 ASP H 117 ARG H 128 1 12
HELIX 129 129 ASP H 141 ARG H 144 5 4
HELIX 130 130 GLN H 181 LEU H 189 1 9
HELIX 131 131 GLU H 198 ARG H 209 1 12
HELIX 132 132 THR H 228 GLY H 247 1 20
HELIX 133 133 CYS H 252 GLN H 260 1 9
HELIX 134 134 ASP H 264 ALA H 273 1 10
HELIX 135 135 PRO H 274 ALA H 276 5 3
HELIX 136 136 ASN H 278 LEU H 287 1 10
HELIX 137 137 LEU H 288 GLU H 290 5 3
SHEET 1 A 7 ASP A 76 VAL A 81 0
SHEET 2 A 7 GLU A 50 SER A 55 1 N ILE A 51 O ASP A 76
SHEET 3 A 7 ARG A 3 LEU A 8 1 O GLY A 5 N LEU A 52
SHEET 4 A 7 LEU A 103 LEU A 108 1 O LEU A 103 N LYS A 4
SHEET 5 A 7 TYR A 170 TYR A 178 -1 O GLY A 174 N LEU A 108
SHEET 6 A 7 ALA A 132 HIS A 138 -1 O SER A 133 N PHE A 177
SHEET 7 A 7 LEU A 212 ILE A 216 1 N SER A 213 O ALA A 132
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 O ALA A 222 N TYR A 114
SHEET 1 D 2 GLY A 146 PHE A 150 0
SHEET 2 D 2 ALA A 156 GLU A 161 -1 N ILE A 157 O GLU A 149
SHEET 1 E 7 ASP B 76 VAL B 81 0
SHEET 2 E 7 GLU B 50 SER B 55 1 O ILE B 51 N GLN B 78
SHEET 3 E 7 ARG B 3 LEU B 8 1 N GLY B 5 O GLU B 50
SHEET 4 E 7 LEU B 103 LEU B 108 1 O LEU B 103 N LYS B 4
SHEET 5 E 7 TYR B 170 TYR B 178 -1 O GLY B 174 N LEU B 108
SHEET 6 E 7 ALA B 132 HIS B 138 -1 O SER B 133 N PHE B 177
SHEET 7 E 7 LEU B 212 ILE B 216 1 N SER B 213 O ALA B 132
SHEET 1 F 2 PRO B 29 VAL B 30 0
SHEET 2 F 2 LYS B 33 PRO B 34 -1 O LYS B 33 N VAL B 30
SHEET 1 G 2 ASN B 111 TYR B 114 0
SHEET 2 G 2 ALA B 222 ASP B 225 -1 N ALA B 222 O TYR B 114
SHEET 1 H 2 GLY B 146 PHE B 150 0
SHEET 2 H 2 ALA B 156 GLU B 161 -1 N ILE B 157 O GLU B 149
SHEET 1 I 7 ASP C 76 VAL C 81 0
SHEET 2 I 7 GLU C 50 SER C 55 1 O ILE C 51 N GLN C 78
SHEET 3 I 7 ARG C 3 LEU C 8 1 N GLY C 5 O GLU C 50
SHEET 4 I 7 LEU C 103 LEU C 108 1 O LEU C 103 N LYS C 4
SHEET 5 I 7 TYR C 170 TYR C 178 -1 O GLY C 174 N LEU C 108
SHEET 6 I 7 ALA C 132 HIS C 138 -1 N SER C 133 O PHE C 177
SHEET 7 I 7 LEU C 212 ILE C 216 1 N SER C 213 O ALA C 132
SHEET 1 J 2 PRO C 29 VAL C 30 0
SHEET 2 J 2 LYS C 33 PRO C 34 -1 O LYS C 33 N VAL C 30
SHEET 1 K 2 ASN C 111 TYR C 114 0
SHEET 2 K 2 ALA C 222 ASP C 225 -1 N ALA C 222 O TYR C 114
SHEET 1 L 2 GLY C 146 PHE C 150 0
SHEET 2 L 2 ALA C 156 GLU C 161 -1 N ILE C 157 O GLU C 149
SHEET 1 M 7 ASP D 76 VAL D 81 0
SHEET 2 M 7 GLU D 50 SER D 55 1 O ILE D 51 N GLN D 78
SHEET 3 M 7 ARG D 3 LEU D 8 1 O GLY D 5 N LEU D 52
SHEET 4 M 7 LEU D 103 LEU D 108 1 O LEU D 103 N LYS D 4
SHEET 5 M 7 TYR D 170 TYR D 178 -1 O GLY D 174 N LEU D 108
SHEET 6 M 7 ALA D 132 HIS D 138 -1 O SER D 133 N PHE D 177
SHEET 7 M 7 LEU D 212 ILE D 216 1 N SER D 213 O ALA D 132
SHEET 1 N 2 PRO D 29 VAL D 30 0
SHEET 2 N 2 LYS D 33 PRO D 34 -1 O LYS D 33 N VAL D 30
SHEET 1 O 2 ASN D 111 TYR D 114 0
SHEET 2 O 2 ALA D 222 ASP D 225 -1 N ALA D 222 O TYR D 114
SHEET 1 P 2 GLY D 146 PHE D 150 0
SHEET 2 P 2 ALA D 156 GLU D 161 -1 N ILE D 157 O GLU D 149
SHEET 1 Q 7 ASP E 76 VAL E 81 0
SHEET 2 Q 7 GLU E 50 SER E 55 1 O ILE E 51 N GLN E 78
SHEET 3 Q 7 ARG E 3 LEU E 8 1 O GLY E 5 N LEU E 52
SHEET 4 Q 7 LEU E 103 LEU E 108 1 O LEU E 103 N LYS E 4
SHEET 5 Q 7 TYR E 170 TYR E 178 -1 O GLY E 174 N LEU E 108
SHEET 6 Q 7 ALA E 132 HIS E 138 -1 O SER E 133 N PHE E 177
SHEET 7 Q 7 LEU E 212 ILE E 216 1 N SER E 213 O ALA E 132
SHEET 1 R 2 PRO E 29 VAL E 30 0
SHEET 2 R 2 LYS E 33 PRO E 34 -1 O LYS E 33 N VAL E 30
SHEET 1 S 2 ASN E 111 TYR E 114 0
SHEET 2 S 2 ALA E 222 ASP E 225 -1 O ALA E 222 N TYR E 114
SHEET 1 T 2 GLY E 146 PHE E 150 0
SHEET 2 T 2 ALA E 156 GLU E 161 -1 N ILE E 157 O GLU E 149
SHEET 1 U 7 ASP F 76 VAL F 81 0
SHEET 2 U 7 GLU F 50 SER F 55 1 O ILE F 51 N GLN F 78
SHEET 3 U 7 ARG F 3 LEU F 8 1 N GLY F 5 O GLU F 50
SHEET 4 U 7 LEU F 103 LEU F 108 1 O LEU F 103 N LYS F 4
SHEET 5 U 7 TYR F 170 TYR F 178 -1 O GLY F 174 N LEU F 108
SHEET 6 U 7 ALA F 132 HIS F 138 -1 O SER F 133 N PHE F 177
SHEET 7 U 7 LEU F 212 ILE F 216 1 N SER F 213 O ALA F 132
SHEET 1 V 2 PRO F 29 VAL F 30 0
SHEET 2 V 2 LYS F 33 PRO F 34 -1 O LYS F 33 N VAL F 30
SHEET 1 W 2 ASN F 111 TYR F 114 0
SHEET 2 W 2 ALA F 222 ASP F 225 -1 N ALA F 222 O TYR F 114
SHEET 1 X 2 GLY F 146 PHE F 150 0
SHEET 2 X 2 ALA F 156 GLU F 161 -1 N ILE F 157 O GLU F 149
SHEET 1 Y 3 LEU G 212 ILE G 216 0
SHEET 2 Y 3 ALA G 132 HIS G 138 1 O ALA G 132 N SER G 213
SHEET 3 Y 3 TYR G 170 VAL G 172 -1 O ALA G 171 N TYR G 137
SHEET 1 Z 7 LEU G 212 ILE G 216 0
SHEET 2 Z 7 ALA G 132 HIS G 138 1 O ALA G 132 N SER G 213
SHEET 3 Z 7 LEU G 175 TYR G 178 -1 N PHE G 177 O SER G 133
SHEET 4 Z 7 LEU G 103 LEU G 108 -1 O SER G 104 N TYR G 178
SHEET 5 Z 7 ARG G 3 ALA G 9 1 N LYS G 4 O LEU G 103
SHEET 6 Z 7 GLU G 50 SER G 55 1 O GLU G 50 N GLY G 5
SHEET 7 Z 7 ASP G 76 VAL G 81 1 O ASP G 76 N ILE G 51
SHEET 1 AA 2 PRO G 29 VAL G 30 0
SHEET 2 AA 2 LYS G 33 PRO G 34 -1 O LYS G 33 N VAL G 30
SHEET 1 AB 2 ASN G 111 TYR G 114 0
SHEET 2 AB 2 ALA G 222 ASP G 225 -1 N ALA G 222 O TYR G 114
SHEET 1 AC 2 GLY G 146 PHE G 150 0
SHEET 2 AC 2 ALA G 156 GLU G 161 -1 N ILE G 157 O GLU G 149
SHEET 1 AD 7 ASP H 76 VAL H 81 0
SHEET 2 AD 7 GLU H 50 SER H 55 1 N ILE H 51 O ASP H 76
SHEET 3 AD 7 ARG H 3 LEU H 8 1 O GLY H 5 N LEU H 52
SHEET 4 AD 7 LEU H 103 LEU H 108 1 O LEU H 103 N LYS H 4
SHEET 5 AD 7 TYR H 170 TYR H 178 -1 O GLY H 174 N LEU H 108
SHEET 6 AD 7 ALA H 132 HIS H 138 -1 O SER H 133 N PHE H 177
SHEET 7 AD 7 LEU H 212 ILE H 216 1 N SER H 213 O ALA H 132
SHEET 1 AE 2 PRO H 29 VAL H 30 0
SHEET 2 AE 2 LYS H 33 PRO H 34 -1 O LYS H 33 N VAL H 30
SHEET 1 AF 2 ASN H 111 TYR H 114 0
SHEET 2 AF 2 ALA H 222 ASP H 225 -1 N ALA H 222 O TYR H 114
SHEET 1 AG 2 GLY H 146 PHE H 150 0
SHEET 2 AG 2 ALA H 156 GLU H 161 -1 N ILE H 157 O GLU H 149
CISPEP 1 HIS A 17 PRO A 18 0 -0.20
CISPEP 2 HIS B 17 PRO B 18 0 -1.24
CISPEP 3 HIS C 17 PRO C 18 0 5.67
CISPEP 4 HIS D 17 PRO D 18 0 -1.17
CISPEP 5 HIS E 17 PRO E 18 0 1.97
CISPEP 6 HIS F 17 PRO F 18 0 -4.95
CISPEP 7 HIS G 17 PRO G 18 0 1.33
CISPEP 8 HIS H 17 PRO H 18 0 -0.56
SITE 1 AC1 9 HIS A 116 ASP A 117 GLY C 218 ARG C 219
SITE 2 AC1 9 GLY C 220 HOH C5007 HOH C5064 HOH C5229
SITE 3 AC1 9 HOH C5240
SITE 1 AC2 9 HIS B 116 ASP B 117 HOH B3735 HOH B3800
SITE 2 AC2 9 GLY D 218 ARG D 219 GLY D 220 HOH D3923
SITE 3 AC2 9 HOH D3941
SITE 1 AC3 10 GLY A 218 ARG A 219 GLY A 220 HOH A3723
SITE 2 AC3 10 HOH A3761 HOH A3839 HIS C 116 ASP C 117
SITE 3 AC3 10 HOH C5022 HOH C5197
SITE 1 AC4 11 GLY B 218 ARG B 219 GLY B 220 HOH B3765
SITE 2 AC4 11 HOH B3771 HOH B3792 HIS D 116 ASP D 117
SITE 3 AC4 11 HOH D3806 HOH D3895 HOH D4030
SITE 1 AC5 11 HIS E 116 ASP E 117 HIS E 119 HOH E6110
SITE 2 AC5 11 HOH E6270 GLY H 218 ARG H 219 GLY H 220
SITE 3 AC5 11 HOH H6106 HOH H6174 HOH H6365
SITE 1 AC6 11 HIS F 116 ASP F 117 HOH F4712 HOH F4898
SITE 2 AC6 11 HOH F4928 GLY G 218 ARG G 219 GLY G 220
SITE 3 AC6 11 HOH G4991 HOH G5003 HOH G5027
SITE 1 AC7 9 GLY F 218 ARG F 219 GLY F 220 HOH F4765
SITE 2 AC7 9 HOH F4867 HOH F4874 HIS G 116 ASP G 117
SITE 3 AC7 9 HOH G4913
SITE 1 AC8 10 GLY E 218 ARG E 219 GLY E 220 HOH E6161
SITE 2 AC8 10 HOH E6177 HOH E6202 HIS H 116 ASP H 117
SITE 3 AC8 10 HOH H6142 HOH H6222
SITE 1 AC9 7 ARG A 128 GLU A 215 HOH A3801 ASP F 151
SITE 2 AC9 7 GLN F 152 HOH F4877 HOH F4938
SITE 1 BC1 6 ARG B 128 GLU B 215 HOH B3986 HOH B4011
SITE 2 BC1 6 ASP E 151 GLN E 152
SITE 1 BC2 3 ARG C 128 GLN C 129 THR C 130
SITE 1 BC3 2 GLN D 129 THR D 130
SITE 1 BC4 6 ASP D 151 GLN D 152 ARG H 128 GLU H 215
SITE 2 BC4 6 HOH H6192 HOH H6269
SITE 1 BC5 3 ARG F 128 GLN F 129 THR F 130
SITE 1 BC6 4 ARG G 62 HOH G5186 ARG H 62 GLN H 65
SITE 1 BC7 6 ASP C 151 GLN C 152 ARG G 128 GLU G 215
SITE 2 BC7 6 HOH G5068 HOH G5204
SITE 1 BC8 2 ARG C 62 ARG D 62
SITE 1 BC9 3 ARG E 62 HOH E6355 ARG F 62
SITE 1 CC1 5 GLN E 127 ARG E 128 GLN E 129 THR E 130
SITE 2 CC1 5 HOH E6265
SITE 1 CC2 4 SER H 12 GLY H 13 THR H 14 ARG H 15
CRYST1 71.656 73.656 134.469 89.98 80.91 80.91 P 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 0.013956 -0.002233 -0.002291 0.00000
SCALE2 0.000000 0.013749 0.000348 0.00000
SCALE3 0.000000 0.000000 0.007534 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
