HEADER TRANSFERASE 03-SEP-09 2WS2
TITLE THE 2 ANGSTROM STRUCTURE OF A NU-CLASS GST FROM HAEMONCHUS CONTORTUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTATHIONE S-TRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NU-CLASS GST;
COMPND 5 EC: 2.5.1.18;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMONCHUS CONTORTUS;
SOURCE 3 ORGANISM_TAXID: 6289;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET23D
KEYWDS PARASITE, NEMATODE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.LINE,M.N.ISUPOV,A.J.VANROSSUM,P.M.BROPHY,J.A.LITTLECHILD
REVDAT 2 20-DEC-23 2WS2 1 REMARK
REVDAT 1 29-SEP-10 2WS2 0
JRNL AUTH K.LINE,M.N.ISUPOV,A.J.VANROSSUM,P.M.BROPHY,J.A.LITTLECHILD
JRNL TITL THE 2 ANGSTROM STRUCTURE OF A NU-CLASS GST FROM HAEMONCHUS
JRNL TITL 2 CONTORTUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0088
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) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 26940
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) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1383
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1863
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3323
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 178
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -26.41000
REMARK 3 B22 (A**2) : 35.27000
REMARK 3 B33 (A**2) : -8.86000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.18000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.053
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.046
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.233
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.617
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3435 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4642 ; 1.891 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 411 ; 8.466 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 164 ;36.236 ;23.841
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 608 ;22.104 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;17.254 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 488 ; 0.151 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2621 ; 0.008 ; 0.021
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): 2044 ; 0.943 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3295 ; 1.533 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1391 ; 2.303 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1344 ; 2.864 ; 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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H,K,L
REMARK 3 TWIN FRACTION : 0.599
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : L,-K,H
REMARK 3 TWIN FRACTION : 0.401
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 81 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3710 3.4550 11.4510
REMARK 3 T TENSOR
REMARK 3 T11: 0.3503 T22: 0.0446
REMARK 3 T33: 0.4213 T12: -0.0331
REMARK 3 T13: 0.0315 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 11.0809 L22: 0.2910
REMARK 3 L33: 8.4257 L12: 0.1284
REMARK 3 L13: 2.2782 L23: 0.9022
REMARK 3 S TENSOR
REMARK 3 S11: 0.1278 S12: 0.0927 S13: -0.0198
REMARK 3 S21: -0.1346 S22: -0.0224 S23: 0.1510
REMARK 3 S31: 0.1141 S32: -0.4814 S33: -0.1054
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 81 B 100
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5830 17.3670 16.1480
REMARK 3 T TENSOR
REMARK 3 T11: 0.3425 T22: 0.1104
REMARK 3 T33: 0.3561 T12: 0.0379
REMARK 3 T13: 0.0397 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 2.2979 L22: 3.8618
REMARK 3 L33: 6.9863 L12: -1.5332
REMARK 3 L13: 0.6953 L23: -2.4565
REMARK 3 S TENSOR
REMARK 3 S11: 0.3349 S12: 0.3476 S13: -0.2692
REMARK 3 S21: 0.0047 S22: 0.0912 S23: 0.3233
REMARK 3 S31: -0.0874 S32: -0.1962 S33: -0.4260
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. TLS AND TWIN REFINEMENT USED. ATOM RECORD CONTAINS
REMARK 3 SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF
REMARK 3 TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2WS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1290041022.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
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 : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28361
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 14.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.690
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 124.3900
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) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.440
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1TW9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS HCL, PH 8.5, 50 MM CACL2,
REMARK 280 30% (W/V) PEG 10000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 50.69100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 HOH A 2009 O HOH A 2016 1.61
REMARK 500 O HOH A 2012 O HOH A 2013 1.70
REMARK 500 O HOH B 2013 O HOH B 2044 1.70
REMARK 500 O HOH B 2019 O HOH B 2022 1.87
REMARK 500 O PRO B 104 O HOH B 2067 1.90
REMARK 500 CB HIS A 42 O HOH A 2017 1.96
REMARK 500 O HOH B 2018 O HOH B 2056 2.04
REMARK 500 O MET B 163 N PHE B 165 2.07
REMARK 500 OD2 ASP B 157 O HOH B 2086 2.09
REMARK 500 NE2 HIS A 42 O HOH A 2019 2.10
REMARK 500 O HOH B 2014 O HOH B 2015 2.10
REMARK 500 O GLY A 175 O HOH A 2070 2.17
REMARK 500 OE1 GLU B 55 O HOH B 2042 2.19
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 O HOH B 2008 O HOH B 2072 1655 2.01
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 PRO A 47 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 93 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 PRO B 47 C - N - CA ANGL. DEV. = 11.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ARG A 12 -78.79 -87.24
REMARK 500 ASP A 57 53.64 17.46
REMARK 500 GLN A 63 126.82 88.83
REMARK 500 VAL A 108 2.03 -51.65
REMARK 500 LEU A 110 -144.43 -67.49
REMARK 500 MET A 112 -81.92 176.41
REMARK 500 GLN A 114 67.02 -116.07
REMARK 500 VAL A 124 -64.73 -125.85
REMARK 500 LYS A 144 17.38 50.28
REMARK 500 ASP A 151 33.11 -148.03
REMARK 500 MET A 163 7.38 -64.55
REMARK 500 THR A 166 41.06 -107.80
REMARK 500 GLU A 167 8.26 -65.23
REMARK 500 LYS A 171 33.24 -94.63
REMARK 500 TYR A 173 55.89 -101.84
REMARK 500 ASP A 174 -77.61 -59.80
REMARK 500 GLN B 63 102.31 83.71
REMARK 500 PHE B 106 85.05 -55.10
REMARK 500 VAL B 108 -143.03 33.54
REMARK 500 LEU B 110 21.41 -76.59
REMARK 500 ASP B 113 -70.59 -24.02
REMARK 500 GLN B 114 80.13 -49.08
REMARK 500 LYS B 118 30.95 176.93
REMARK 500 VAL B 124 -55.61 -122.70
REMARK 500 THR B 145 -3.38 -140.61
REMARK 500 GLU B 167 21.75 44.43
REMARK 500 TYR B 169 104.44 -162.12
REMARK 500 LEU B 172 149.87 -37.40
REMARK 500 ARG B 187 33.48 -75.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP B 116 LEU B 117 -144.83
REMARK 500 GLY B 164 PHE B 165 -149.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B2011 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH B2022 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B2023 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH B2048 DISTANCE = 7.14 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE ARE CONFLICTS BETWEEN SEQUENCE MODELLED IN THE
REMARK 999 STRUCTURE AND THE SEQUENCE DEPOSITED. WE HAVE MODELLED
REMARK 999 OUR SEQUENCE BASED ON THE DENSITY OBSERVED
DBREF 2WS2 A 1 164 UNP Q9NAW7 Q9NAW7_HAECO 1 164
DBREF 2WS2 A 165 204 UNP Q9NAW7 Q9NAW7_HAECO 166 205
DBREF 2WS2 B 1 164 UNP Q9NAW7 Q9NAW7_HAECO 1 164
DBREF 2WS2 B 165 204 UNP Q9NAW7 Q9NAW7_HAECO 166 205
SEQADV 2WS2 GLY A 164 UNP Q9NAW7 THR 164 SEE REMARK 999
SEQADV 2WS2 GLY B 164 UNP Q9NAW7 THR 164 SEE REMARK 999
SEQRES 1 A 204 MET VAL HIS TYR LYS LEU THR TYR PHE ASN GLY ARG GLY
SEQRES 2 A 204 ALA ALA GLU ILE ILE ARG GLN VAL PHE VAL LEU ALA GLY
SEQRES 3 A 204 GLN ASP TYR GLU ASP VAL ARG LEU THR HIS GLU GLU TRP
SEQRES 4 A 204 PRO LYS HIS LYS ALA SER MET PRO PHE GLY GLN LEU PRO
SEQRES 5 A 204 VAL LEU GLU VAL ASP GLY LYS GLN LEU PRO GLN SER VAL
SEQRES 6 A 204 ALA ILE VAL ARG TYR LEU ALA ARG LYS PHE GLY TYR ALA
SEQRES 7 A 204 GLY LYS SER ALA TRP GLU GLU ALA VAL VAL ASP SER ILE
SEQRES 8 A 204 ALA ASP GLN PHE LYS ASP PHE LEU ASN GLU VAL ARG PRO
SEQRES 9 A 204 TYR PHE LYS VAL LEU LEU GLY MET ASP GLN GLY ASP LEU
SEQRES 10 A 204 LYS ALA LEU GLU LYS ASP VAL PHE GLU PRO ALA ARG GLN
SEQRES 11 A 204 LYS PHE PHE THR ILE VAL THR LYS ILE LEU LYS GLU ASN
SEQRES 12 A 204 LYS THR GLY TYR LEU VAL GLY ASP SER LEU THR PHE ALA
SEQRES 13 A 204 ASP LEU TYR VAL ALA GLU MET GLY PHE THR GLU HIS TYR
SEQRES 14 A 204 PRO LYS LEU TYR ASP GLY PHE PRO GLU VAL LYS ALA HIS
SEQRES 15 A 204 ALA GLU LYS VAL ARG SER ASN PRO LYS LEU LYS LYS TRP
SEQRES 16 A 204 ILE GLU THR ARG PRO ALA SER LYS PHE
SEQRES 1 B 204 MET VAL HIS TYR LYS LEU THR TYR PHE ASN GLY ARG GLY
SEQRES 2 B 204 ALA ALA GLU ILE ILE ARG GLN VAL PHE VAL LEU ALA GLY
SEQRES 3 B 204 GLN ASP TYR GLU ASP VAL ARG LEU THR HIS GLU GLU TRP
SEQRES 4 B 204 PRO LYS HIS LYS ALA SER MET PRO PHE GLY GLN LEU PRO
SEQRES 5 B 204 VAL LEU GLU VAL ASP GLY LYS GLN LEU PRO GLN SER VAL
SEQRES 6 B 204 ALA ILE VAL ARG TYR LEU ALA ARG LYS PHE GLY TYR ALA
SEQRES 7 B 204 GLY LYS SER ALA TRP GLU GLU ALA VAL VAL ASP SER ILE
SEQRES 8 B 204 ALA ASP GLN PHE LYS ASP PHE LEU ASN GLU VAL ARG PRO
SEQRES 9 B 204 TYR PHE LYS VAL LEU LEU GLY MET ASP GLN GLY ASP LEU
SEQRES 10 B 204 LYS ALA LEU GLU LYS ASP VAL PHE GLU PRO ALA ARG GLN
SEQRES 11 B 204 LYS PHE PHE THR ILE VAL THR LYS ILE LEU LYS GLU ASN
SEQRES 12 B 204 LYS THR GLY TYR LEU VAL GLY ASP SER LEU THR PHE ALA
SEQRES 13 B 204 ASP LEU TYR VAL ALA GLU MET GLY PHE THR GLU HIS TYR
SEQRES 14 B 204 PRO LYS LEU TYR ASP GLY PHE PRO GLU VAL LYS ALA HIS
SEQRES 15 B 204 ALA GLU LYS VAL ARG SER ASN PRO LYS LEU LYS LYS TRP
SEQRES 16 B 204 ILE GLU THR ARG PRO ALA SER LYS PHE
FORMUL 3 HOH *178(H2 O)
HELIX 1 1 ALA A 15 ALA A 25 1 11
HELIX 2 2 GLU A 38 HIS A 42 5 5
HELIX 3 3 HIS A 42 MET A 46 5 5
HELIX 4 4 GLN A 63 PHE A 75 1 13
HELIX 5 5 SER A 81 GLU A 101 1 21
HELIX 6 6 VAL A 102 VAL A 108 1 7
HELIX 7 7 LEU A 117 LYS A 122 1 6
HELIX 8 8 PHE A 125 LYS A 144 1 20
HELIX 9 9 THR A 154 MET A 163 1 10
HELIX 10 10 PHE A 176 ARG A 187 1 12
HELIX 11 11 ASN A 189 ARG A 199 1 11
HELIX 12 12 ALA B 15 ALA B 25 1 11
HELIX 13 13 GLU B 38 HIS B 42 5 5
HELIX 14 14 HIS B 42 MET B 46 5 5
HELIX 15 15 GLN B 63 PHE B 75 1 13
HELIX 16 16 SER B 81 ARG B 103 1 23
HELIX 17 17 PRO B 104 PHE B 106 5 3
HELIX 18 18 ALA B 119 VAL B 124 1 6
HELIX 19 19 VAL B 124 LYS B 144 1 21
HELIX 20 20 THR B 154 GLU B 162 1 9
HELIX 21 21 PHE B 176 ARG B 187 1 12
HELIX 22 22 ASN B 189 ARG B 199 1 11
SHEET 1 AA 4 GLU A 30 LEU A 34 0
SHEET 2 AA 4 TYR A 4 PHE A 9 1 O TYR A 4 N GLU A 30
SHEET 3 AA 4 VAL A 53 VAL A 56 -1 O VAL A 53 N THR A 7
SHEET 4 AA 4 GLN A 60 PRO A 62 -1 O LEU A 61 N LEU A 54
SHEET 1 BA 4 GLU B 30 LEU B 34 0
SHEET 2 BA 4 TYR B 4 PHE B 9 1 O TYR B 4 N GLU B 30
SHEET 3 BA 4 VAL B 53 VAL B 56 -1 O VAL B 53 N THR B 7
SHEET 4 BA 4 GLN B 60 PRO B 62 -1 O LEU B 61 N LEU B 54
CISPEP 1 LEU A 51 PRO A 52 0 6.15
CISPEP 2 LEU B 51 PRO B 52 0 -0.95
CRYST1 47.216 101.382 47.170 90.00 100.46 90.00 P 1 21 1 4
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 0.021179 0.000000 0.003910 0.00000
SCALE2 0.000000 0.009864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021558 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
