HEADER PROTEIN BINDING 23-DEC-04 1YDG
TITLE CRYSTAL STRUCTURE OF TRP REPRESSOR BINDING PROTEIN WRBA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRP REPRESSOR BINDING PROTEIN WRBA;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 GENE: DRA0214;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TETRAMER, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NEW
KEYWDS 2 YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC, PROTEIN
KEYWDS 3 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.GORMAN,L.SHAPIRO,S.K.BURLEY,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 6 14-FEB-24 1YDG 1 REMARK
REVDAT 5 03-FEB-21 1YDG 1 AUTHOR REMARK SEQADV
REVDAT 4 24-FEB-09 1YDG 1 VERSN
REVDAT 3 28-FEB-06 1YDG 1 JRNL
REVDAT 2 25-JAN-05 1YDG 1 AUTHOR KEYWDS REMARK
REVDAT 1 04-JAN-05 1YDG 0
JRNL AUTH J.GORMAN,L.SHAPIRO
JRNL TITL CRYSTAL STRUCTURES OF THE TRYPTOPHAN REPRESSOR BINDING
JRNL TITL 2 PROTEIN WRBA AND COMPLEXES WITH FLAVIN MONONUCLEOTIDE.
JRNL REF PROTEIN SCI. V. 14 3004 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16322580
JRNL DOI 10.1110/PS.051680805
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 116506
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5845
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8192
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 436
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12056
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 1293
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.25000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : -0.37000
REMARK 3 B12 (A**2) : 0.12000
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): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.169
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.132
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.890
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12336 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 11075 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16771 ; 1.182 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25735 ; 0.767 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1608 ; 5.869 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 512 ;40.610 ;24.531
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1945 ;13.830 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;15.580 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1879 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14008 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2416 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2869 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 10961 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6138 ; 0.173 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 6415 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1087 ; 0.168 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.087 ; 0.200
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): 20 ; 0.273 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 86 ; 0.212 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 31 ; 0.194 ; 0.200
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): 10262 ; 1.053 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3336 ; 0.128 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12726 ; 1.155 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5070 ; 1.546 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4045 ; 2.376 ; 4.500
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1YDG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : .9793
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116736
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.6M AMSULFATE, 20% GLYCEROL, PH 4.5,
REMARK 280 VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 138.62200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.31100
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.31100
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 138.62200
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 UNIT IS A TETRAMER, THERE ARE TWO IN THE
REMARK 300 ASYMMETRIC UNIT. 1: CHAINS A, B, C, D 2: CHAINS E, F, G, H
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: 11530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -157.0 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: 11540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 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 SER A 0
REMARK 465 LEU A 1
REMARK 465 THR A 2
REMARK 465 HIS A 204
REMARK 465 HIS A 205
REMARK 465 HIS A 206
REMARK 465 HIS A 207
REMARK 465 HIS A 208
REMARK 465 HIS A 209
REMARK 465 MET B -1
REMARK 465 SER B 0
REMARK 465 LEU B 1
REMARK 465 HIS B 204
REMARK 465 HIS B 205
REMARK 465 HIS B 206
REMARK 465 HIS B 207
REMARK 465 HIS B 208
REMARK 465 HIS B 209
REMARK 465 MET C -1
REMARK 465 SER C 0
REMARK 465 LEU C 1
REMARK 465 HIS C 204
REMARK 465 HIS C 205
REMARK 465 HIS C 206
REMARK 465 HIS C 207
REMARK 465 HIS C 208
REMARK 465 HIS C 209
REMARK 465 MET D -1
REMARK 465 SER D 0
REMARK 465 LEU D 1
REMARK 465 HIS D 204
REMARK 465 HIS D 205
REMARK 465 HIS D 206
REMARK 465 HIS D 207
REMARK 465 HIS D 208
REMARK 465 HIS D 209
REMARK 465 MET E -1
REMARK 465 HIS E 204
REMARK 465 HIS E 205
REMARK 465 HIS E 206
REMARK 465 HIS E 207
REMARK 465 HIS E 208
REMARK 465 HIS E 209
REMARK 465 MET F -1
REMARK 465 SER F 0
REMARK 465 LEU F 1
REMARK 465 THR F 2
REMARK 465 HIS F 204
REMARK 465 HIS F 205
REMARK 465 HIS F 206
REMARK 465 HIS F 207
REMARK 465 HIS F 208
REMARK 465 HIS F 209
REMARK 465 MET G -1
REMARK 465 SER G 0
REMARK 465 LEU G 1
REMARK 465 HIS G 204
REMARK 465 HIS G 205
REMARK 465 HIS G 206
REMARK 465 HIS G 207
REMARK 465 HIS G 208
REMARK 465 HIS G 209
REMARK 465 MET H -1
REMARK 465 SER H 0
REMARK 465 LEU H 1
REMARK 465 HIS H 204
REMARK 465 HIS H 205
REMARK 465 HIS H 206
REMARK 465 HIS H 207
REMARK 465 HIS H 208
REMARK 465 HIS H 209
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 OD2 ASP H 51 OD2 ASP H 51 6555 2.08
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 ASN D 113 -5.95 76.21
REMARK 500 TYR D 152 40.06 -109.49
REMARK 500 ALA F 122 133.41 -175.46
REMARK 500 SER G 14 -66.13 -90.05
REMARK 500 ASN G 172 57.74 -149.68
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 H 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 1308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 1309
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1310
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-T1617 RELATED DB: TARGETDB
DBREF 1YDG A 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
DBREF 1YDG B 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
DBREF 1YDG C 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
DBREF 1YDG D 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
DBREF 1YDG E 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
DBREF 1YDG F 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
DBREF 1YDG G 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
DBREF 1YDG H 2 201 UNP Q9RYU4 Q9RYU4_DEIRA 2 200
SEQADV 1YDG MET A -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER A 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU A 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU A 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY A 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER A 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS A 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS A 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS A 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS A 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS A 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS A 209 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG MET B -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER B 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU B 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU B 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY B 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER B 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS B 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS B 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS B 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS B 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS B 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS B 209 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG MET C -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER C 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU C 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU C 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY C 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER C 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS C 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS C 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS C 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS C 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS C 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS C 209 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG MET D -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER D 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU D 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU D 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY D 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER D 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS D 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS D 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS D 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS D 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS D 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS D 209 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG MET E -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER E 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU E 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU E 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY E 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER E 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS E 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS E 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS E 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS E 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS E 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS E 209 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG MET F -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER F 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU F 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU F 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY F 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER F 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS F 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS F 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS F 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS F 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS F 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS F 209 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG MET G -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER G 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU G 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU G 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY G 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER G 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS G 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS G 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS G 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS G 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS G 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS G 209 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG MET H -1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER H 0 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG LEU H 1 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLU H 200 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG GLY H 202 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG SER H 203 UNP Q9RYU4 CLONING ARTIFACT
SEQADV 1YDG HIS H 204 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS H 205 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS H 206 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS H 207 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS H 208 UNP Q9RYU4 EXPRESSION TAG
SEQADV 1YDG HIS H 209 UNP Q9RYU4 EXPRESSION TAG
SEQRES 1 A 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 A 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 A 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 A 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 A 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 A 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 A 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 A 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 A 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 A 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 A 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 A 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 A 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 A 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 A 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 A 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 A 211 HIS HIS HIS
SEQRES 1 B 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 B 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 B 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 B 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 B 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 B 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 B 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 B 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 B 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 B 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 B 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 B 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 B 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 B 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 B 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 B 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 B 211 HIS HIS HIS
SEQRES 1 C 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 C 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 C 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 C 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 C 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 C 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 C 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 C 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 C 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 C 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 C 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 C 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 C 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 C 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 C 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 C 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 C 211 HIS HIS HIS
SEQRES 1 D 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 D 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 D 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 D 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 D 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 D 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 D 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 D 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 D 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 D 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 D 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 D 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 D 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 D 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 D 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 D 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 D 211 HIS HIS HIS
SEQRES 1 E 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 E 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 E 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 E 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 E 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 E 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 E 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 E 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 E 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 E 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 E 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 E 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 E 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 E 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 E 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 E 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 E 211 HIS HIS HIS
SEQRES 1 F 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 F 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 F 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 F 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 F 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 F 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 F 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 F 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 F 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 F 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 F 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 F 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 F 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 F 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 F 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 F 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 F 211 HIS HIS HIS
SEQRES 1 G 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 G 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 G 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 G 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 G 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 G 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 G 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 G 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 G 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 G 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 G 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 G 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 G 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 G 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 G 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 G 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 G 211 HIS HIS HIS
SEQRES 1 H 211 MET SER LEU THR ALA PRO VAL LYS LEU ALA ILE VAL PHE
SEQRES 2 H 211 TYR SER SER THR GLY THR GLY TYR ALA MET ALA GLN GLU
SEQRES 3 H 211 ALA ALA GLU ALA GLY ARG ALA ALA GLY ALA GLU VAL ARG
SEQRES 4 H 211 LEU LEU LYS VAL ARG GLU THR ALA PRO GLN ASP VAL ILE
SEQRES 5 H 211 ASP GLY GLN ASP ALA TRP LYS ALA ASN ILE GLU ALA MET
SEQRES 6 H 211 LYS ASP VAL PRO GLU ALA THR PRO ALA ASP LEU GLU TRP
SEQRES 7 H 211 ALA GLU ALA ILE VAL PHE SER SER PRO THR ARG PHE GLY
SEQRES 8 H 211 GLY ALA THR SER GLN MET ARG ALA PHE ILE ASP THR LEU
SEQRES 9 H 211 GLY GLY LEU TRP SER SER GLY LYS LEU ALA ASN LYS THR
SEQRES 10 H 211 PHE SER ALA MET THR SER ALA GLN ASN VAL ASN GLY GLY
SEQRES 11 H 211 GLN GLU THR THR LEU GLN THR LEU TYR MET THR ALA MET
SEQRES 12 H 211 HIS TRP GLY ALA VAL LEU THR PRO PRO GLY TYR THR ASP
SEQRES 13 H 211 GLU VAL ILE PHE LYS SER GLY GLY ASN PRO TYR GLY ALA
SEQRES 14 H 211 SER VAL THR ALA ASN GLY GLN PRO LEU LEU GLU ASN ASP
SEQRES 15 H 211 ARG ALA SER ILE ARG HIS GLN VAL ARG ARG GLN VAL GLU
SEQRES 16 H 211 LEU THR ALA LYS LEU LEU GLU GLY GLY SER HIS HIS HIS
SEQRES 17 H 211 HIS HIS HIS
HET SO4 A1302 5
HET SO4 B1303 5
HET SO4 C1304 5
HET SO4 D1305 5
HET SO4 D1310 5
HET SO4 E1306 5
HET SO4 F1307 5
HET SO4 G1308 5
HET SO4 H1301 5
HET SO4 H1309 5
HETNAM SO4 SULFATE ION
FORMUL 9 SO4 10(O4 S 2-)
FORMUL 19 HOH *1293(H2 O)
HELIX 1 1 GLY A 16 ALA A 32 1 17
HELIX 2 2 PRO A 46 ASP A 51 1 6
HELIX 3 3 GLN A 53 MET A 63 1 11
HELIX 4 4 THR A 70 ALA A 77 1 8
HELIX 5 5 THR A 92 THR A 101 1 10
HELIX 6 6 LEU A 102 SER A 108 1 7
HELIX 7 7 GLU A 130 HIS A 142 1 13
HELIX 8 8 ASP A 154 SER A 160 1 7
HELIX 9 9 LEU A 177 GLY A 202 1 26
HELIX 10 10 GLY B 16 ALA B 32 1 17
HELIX 11 11 PRO B 46 ASP B 51 1 6
HELIX 12 12 GLN B 53 MET B 63 1 11
HELIX 13 13 THR B 70 ALA B 77 1 8
HELIX 14 14 THR B 92 THR B 101 1 10
HELIX 15 15 LEU B 102 SER B 108 1 7
HELIX 16 16 GLY B 128 TRP B 143 1 16
HELIX 17 17 ASP B 154 GLY B 161 1 8
HELIX 18 18 LEU B 177 SER B 203 1 27
HELIX 19 19 GLY C 16 ALA C 32 1 17
HELIX 20 20 PRO C 46 ASP C 51 1 6
HELIX 21 21 GLN C 53 MET C 63 1 11
HELIX 22 22 THR C 70 ALA C 77 1 8
HELIX 23 23 THR C 92 ASP C 100 1 9
HELIX 24 24 LEU C 102 SER C 108 1 7
HELIX 25 25 GLU C 130 TRP C 143 1 14
HELIX 26 26 ASP C 154 SER C 160 1 7
HELIX 27 27 LEU C 177 GLY C 202 1 26
HELIX 28 28 GLY D 16 ALA D 32 1 17
HELIX 29 29 PRO D 46 ASP D 51 1 6
HELIX 30 30 GLN D 53 MET D 63 1 11
HELIX 31 31 THR D 70 ALA D 77 1 8
HELIX 32 32 THR D 92 ASP D 100 1 9
HELIX 33 33 LEU D 102 SER D 108 1 7
HELIX 34 34 GLY D 128 TRP D 143 1 16
HELIX 35 35 ASP D 154 SER D 160 1 7
HELIX 36 36 LEU D 177 SER D 203 1 27
HELIX 37 37 GLY E 16 ALA E 32 1 17
HELIX 38 38 PRO E 46 GLN E 53 1 8
HELIX 39 39 GLN E 53 MET E 63 1 11
HELIX 40 40 THR E 70 ALA E 77 1 8
HELIX 41 41 THR E 92 THR E 101 1 10
HELIX 42 42 LEU E 102 SER E 108 1 7
HELIX 43 43 GLU E 130 HIS E 142 1 13
HELIX 44 44 ASP E 154 SER E 160 1 7
HELIX 45 45 LEU E 177 GLY E 202 1 26
HELIX 46 46 GLY F 16 ALA F 32 1 17
HELIX 47 47 PRO F 46 ASP F 51 1 6
HELIX 48 48 GLN F 53 MET F 63 1 11
HELIX 49 49 THR F 70 ALA F 77 1 8
HELIX 50 50 THR F 92 THR F 101 1 10
HELIX 51 51 LEU F 102 SER F 108 1 7
HELIX 52 52 GLY F 128 TRP F 143 1 16
HELIX 53 53 ASP F 154 SER F 160 1 7
HELIX 54 54 LEU F 177 SER F 203 1 27
HELIX 55 55 GLY G 16 ALA G 32 1 17
HELIX 56 56 PRO G 46 GLY G 52 1 7
HELIX 57 57 GLN G 53 LYS G 64 1 12
HELIX 58 58 THR G 70 ALA G 77 1 8
HELIX 59 59 THR G 92 THR G 101 1 10
HELIX 60 60 LEU G 102 SER G 108 1 7
HELIX 61 61 GLY G 128 TRP G 143 1 16
HELIX 62 62 ASP G 154 SER G 160 1 7
HELIX 63 63 LEU G 177 SER G 203 1 27
HELIX 64 64 GLY H 16 ALA H 32 1 17
HELIX 65 65 PRO H 46 ASP H 51 1 6
HELIX 66 66 GLN H 53 MET H 63 1 11
HELIX 67 67 THR H 70 ALA H 77 1 8
HELIX 68 68 THR H 92 ASP H 100 1 9
HELIX 69 69 LEU H 102 SER H 108 1 7
HELIX 70 70 GLU H 130 HIS H 142 1 13
HELIX 71 71 ASP H 154 SER H 160 1 7
HELIX 72 72 LEU H 177 GLY H 202 1 26
SHEET 1 A 5 GLU A 35 LYS A 40 0
SHEET 2 A 5 LYS A 6 PHE A 11 1 N ILE A 9 O LEU A 39
SHEET 3 A 5 ALA A 79 ARG A 87 1 O VAL A 81 N VAL A 10
SHEET 4 A 5 THR A 115 ALA A 122 1 O THR A 115 N ILE A 80
SHEET 5 A 5 VAL A 146 LEU A 147 1 O VAL A 146 N PHE A 116
SHEET 1 B 4 GLY A 90 ALA A 91 0
SHEET 2 B 4 ALA A 79 ARG A 87 -1 N ARG A 87 O GLY A 90
SHEET 3 B 4 THR A 115 ALA A 122 1 O THR A 115 N ILE A 80
SHEET 4 B 4 SER A 168 THR A 170 1 O VAL A 169 N ALA A 122
SHEET 1 C 5 GLU B 35 LYS B 40 0
SHEET 2 C 5 LYS B 6 PHE B 11 1 N ILE B 9 O ARG B 37
SHEET 3 C 5 ALA B 79 ARG B 87 1 O VAL B 81 N VAL B 10
SHEET 4 C 5 THR B 115 ALA B 122 1 O SER B 121 N THR B 86
SHEET 5 C 5 VAL B 146 LEU B 147 1 O VAL B 146 N PHE B 116
SHEET 1 D 4 GLY B 90 ALA B 91 0
SHEET 2 D 4 ALA B 79 ARG B 87 -1 N ARG B 87 O GLY B 90
SHEET 3 D 4 THR B 115 ALA B 122 1 O SER B 121 N THR B 86
SHEET 4 D 4 SER B 168 THR B 170 1 O VAL B 169 N ALA B 122
SHEET 1 E 5 GLU C 35 LYS C 40 0
SHEET 2 E 5 LYS C 6 PHE C 11 1 N LEU C 7 O GLU C 35
SHEET 3 E 5 ALA C 79 ARG C 87 1 O VAL C 81 N VAL C 10
SHEET 4 E 5 THR C 115 ALA C 122 1 O SER C 121 N THR C 86
SHEET 5 E 5 VAL C 146 LEU C 147 1 O VAL C 146 N PHE C 116
SHEET 1 F 4 GLY C 90 ALA C 91 0
SHEET 2 F 4 ALA C 79 ARG C 87 -1 N ARG C 87 O GLY C 90
SHEET 3 F 4 THR C 115 ALA C 122 1 O SER C 121 N THR C 86
SHEET 4 F 4 ALA C 167 THR C 170 1 O ALA C 167 N THR C 120
SHEET 1 G 5 GLU D 35 LYS D 40 0
SHEET 2 G 5 LYS D 6 PHE D 11 1 N LEU D 7 O GLU D 35
SHEET 3 G 5 ALA D 79 ARG D 87 1 O VAL D 81 N VAL D 10
SHEET 4 G 5 THR D 115 ALA D 122 1 O SER D 121 N THR D 86
SHEET 5 G 5 VAL D 146 LEU D 147 1 O VAL D 146 N PHE D 116
SHEET 1 H 4 GLY D 90 ALA D 91 0
SHEET 2 H 4 ALA D 79 ARG D 87 -1 N ARG D 87 O GLY D 90
SHEET 3 H 4 THR D 115 ALA D 122 1 O SER D 121 N THR D 86
SHEET 4 H 4 SER D 168 THR D 170 1 O VAL D 169 N THR D 120
SHEET 1 I 5 GLU E 35 LYS E 40 0
SHEET 2 I 5 LYS E 6 PHE E 11 1 N ILE E 9 O LEU E 39
SHEET 3 I 5 ALA E 79 ARG E 87 1 O ALA E 79 N ALA E 8
SHEET 4 I 5 THR E 115 ALA E 122 1 O SER E 121 N THR E 86
SHEET 5 I 5 VAL E 146 LEU E 147 1 O VAL E 146 N PHE E 116
SHEET 1 J 4 GLY E 90 ALA E 91 0
SHEET 2 J 4 ALA E 79 ARG E 87 -1 N ARG E 87 O GLY E 90
SHEET 3 J 4 THR E 115 ALA E 122 1 O SER E 121 N THR E 86
SHEET 4 J 4 SER E 168 THR E 170 1 O VAL E 169 N THR E 120
SHEET 1 K 5 GLU F 35 LYS F 40 0
SHEET 2 K 5 LYS F 6 PHE F 11 1 N LEU F 7 O GLU F 35
SHEET 3 K 5 ALA F 79 ARG F 87 1 O VAL F 81 N VAL F 10
SHEET 4 K 5 THR F 115 ALA F 122 1 O SER F 121 N THR F 86
SHEET 5 K 5 VAL F 146 LEU F 147 1 O VAL F 146 N PHE F 116
SHEET 1 L 4 GLY F 90 ALA F 91 0
SHEET 2 L 4 ALA F 79 ARG F 87 -1 N ARG F 87 O GLY F 90
SHEET 3 L 4 THR F 115 ALA F 122 1 O SER F 121 N THR F 86
SHEET 4 L 4 SER F 168 THR F 170 1 O VAL F 169 N THR F 120
SHEET 1 M 5 GLU G 35 LYS G 40 0
SHEET 2 M 5 LYS G 6 PHE G 11 1 N ILE G 9 O ARG G 37
SHEET 3 M 5 ALA G 79 ARG G 87 1 O VAL G 81 N VAL G 10
SHEET 4 M 5 THR G 115 ALA G 122 1 O THR G 115 N ILE G 80
SHEET 5 M 5 VAL G 146 LEU G 147 1 O VAL G 146 N PHE G 116
SHEET 1 N 4 GLY G 90 ALA G 91 0
SHEET 2 N 4 ALA G 79 ARG G 87 -1 N ARG G 87 O GLY G 90
SHEET 3 N 4 THR G 115 ALA G 122 1 O THR G 115 N ILE G 80
SHEET 4 N 4 SER G 168 THR G 170 1 O VAL G 169 N ALA G 122
SHEET 1 O 5 GLU H 35 LYS H 40 0
SHEET 2 O 5 LYS H 6 PHE H 11 1 N ILE H 9 O ARG H 37
SHEET 3 O 5 ALA H 79 PRO H 85 1 O VAL H 81 N VAL H 10
SHEET 4 O 5 THR H 115 ALA H 122 1 O THR H 115 N ILE H 80
SHEET 5 O 5 VAL H 146 LEU H 147 1 O VAL H 146 N PHE H 116
SHEET 1 P 5 GLU H 35 LYS H 40 0
SHEET 2 P 5 LYS H 6 PHE H 11 1 N ILE H 9 O ARG H 37
SHEET 3 P 5 ALA H 79 PRO H 85 1 O VAL H 81 N VAL H 10
SHEET 4 P 5 THR H 115 ALA H 122 1 O THR H 115 N ILE H 80
SHEET 5 P 5 SER H 168 THR H 170 1 O VAL H 169 N THR H 120
SITE 1 AC1 9 SER H 13 SER H 14 THR H 15 GLY H 16
SITE 2 AC1 9 THR H 17 GLY H 18 PRO H 85 SER H 121
SITE 3 AC1 9 HOH H1331
SITE 1 AC2 9 SER A 13 SER A 14 THR A 15 GLY A 16
SITE 2 AC2 9 THR A 17 GLY A 18 PRO A 85 SER A 121
SITE 3 AC2 9 HOH A1349
SITE 1 AC3 10 SER B 13 SER B 14 THR B 15 GLY B 16
SITE 2 AC3 10 THR B 17 GLY B 18 PRO B 85 SER B 121
SITE 3 AC3 10 HOH B1318 HOH B1322
SITE 1 AC4 11 SER C 13 SER C 14 THR C 15 GLY C 16
SITE 2 AC4 11 THR C 17 GLY C 18 PRO C 85 SER C 121
SITE 3 AC4 11 HOH C1332 HOH C1333 HOH C1403
SITE 1 AC5 9 SER D 13 SER D 14 THR D 15 GLY D 16
SITE 2 AC5 9 THR D 17 GLY D 18 PRO D 85 SER D 121
SITE 3 AC5 9 HOH D1386
SITE 1 AC6 10 SER E 13 SER E 14 THR E 15 GLY E 16
SITE 2 AC6 10 THR E 17 GLY E 18 PRO E 85 SER E 121
SITE 3 AC6 10 HOH E1392 HOH E1403
SITE 1 AC7 9 SER F 13 SER F 14 THR F 15 GLY F 16
SITE 2 AC7 9 THR F 17 GLY F 18 PRO F 85 SER F 121
SITE 3 AC7 9 HOH F1323
SITE 1 AC8 9 SER G 13 SER G 14 THR G 15 GLY G 16
SITE 2 AC8 9 THR G 17 GLY G 18 PRO G 85 SER G 121
SITE 3 AC8 9 HOH G1320
SITE 1 AC9 4 LYS A 110 ARG H 185 ARG H 189 HOH H1363
SITE 1 BC1 5 LYS B 110 ARG D 185 ARG D 189 HOH D1410
SITE 2 BC1 5 HOH D1461
CRYST1 121.611 121.611 207.933 90.00 90.00 120.00 P 32 2 1 48
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 0.008223 0.004748 0.000000 0.00000
SCALE2 0.000000 0.009495 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004809 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
