HEADER ELECTRON TRANSPORT 17-SEP-04 1W89
TITLE STRUCTURE OF THE REDUCED FORM OF HUMAN THIOREDOXIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: ACTIVE SITE, RESIDUES 60-166;
COMPND 5 SYNONYM: MITOCHONDRIAL PRECURSOR, MT-TRX, THIOREDOXIN 2, HUMAN
COMPND 6 THIOREDOXIN 2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: M15 (PREP4);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PQE30
KEYWDS ANTIOXIDANT ENZYME, MITOCHONDRION, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SMEETS,C.EVRARD,J.P.DECLERCQ
REVDAT 6 13-DEC-23 1W89 1 REMARK
REVDAT 5 24-JUL-19 1W89 1 REMARK
REVDAT 4 13-JUL-11 1W89 1 VERSN
REVDAT 3 09-JUN-09 1W89 1 HEADER KEYWDS REMARK
REVDAT 2 24-FEB-09 1W89 1 VERSN
REVDAT 1 05-OCT-05 1W89 0
JRNL AUTH A.SMEETS,C.EVRARD,M.LANDTMETERS,C.MARCHAND,B.KNOOPS,
JRNL AUTH 2 J.P.DECLERCQ
JRNL TITL CRYSTAL STRUCTURES OF OXIDIZED AND REDUCED FORMS OF HUMAN
JRNL TITL 2 MITOCHONDRIAL THIOREDOXIN 2.
JRNL REF PROTEIN SCI. V. 14 2610 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16195549
JRNL DOI 10.1110/PS.051632905
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.E.DAMDIMOPOULOS,A.MIRANDA-VIZUETE,M.PELTO-HUIKKOS,
REMARK 1 AUTH 2 J.A.GUSTAFSSON,G.SPYROU
REMARK 1 TITL HUMAN MITOCHONDRIAL THIOREDOXIN
REMARK 1 REF J.BIOL.CHEM. V. 277 33249 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 12080052
REMARK 1 DOI 10.1074/JBC.M203036200
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) : 19.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 46290
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2442
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) : 3452
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 170
REMARK 3 BIN FREE R VALUE : 0.3570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 498
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : UNVERIFIED
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.04000
REMARK 3 B12 (A**2) : 0.15000
REMARK 3 B13 (A**2) : 0.16000
REMARK 3 B23 (A**2) : -0.11000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.215
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.203
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.171
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.824
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5167 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6999 ; 2.324 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 648 ; 8.109 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 231 ;37.744 ;26.234
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 920 ;18.749 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;18.161 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 806 ; 0.155 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3864 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2413 ; 0.059 ; 0.100
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3323 ; 0.283 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 568 ; 0.217 ; 0.500
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): 86 ; 0.037 ; 0.100
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 44 ; 0.257 ; 0.500
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): 3406 ; 3.086 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5292 ; 4.034 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2020 ; 6.445 ; 4.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1707 ; 8.338 ; 6.000
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 : 6
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 98 A 107
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9360 14.4370 53.5970
REMARK 3 T TENSOR
REMARK 3 T11: -0.1980 T22: -0.1770
REMARK 3 T33: -0.2073 T12: 0.0049
REMARK 3 T13: 0.0106 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 2.1375 L22: 1.5696
REMARK 3 L33: 4.6174 L12: 0.2481
REMARK 3 L13: -0.3602 L23: -0.1300
REMARK 3 S TENSOR
REMARK 3 S11: -0.0184 S12: -0.0896 S13: 0.0504
REMARK 3 S21: -0.0998 S22: 0.0022 S23: 0.0480
REMARK 3 S31: 0.1599 S32: -0.0822 S33: 0.0162
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 98 B 107
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6960 12.6970 21.9870
REMARK 3 T TENSOR
REMARK 3 T11: -0.1581 T22: -0.1986
REMARK 3 T33: -0.2097 T12: -0.0030
REMARK 3 T13: 0.0152 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 1.9981 L22: 1.6151
REMARK 3 L33: 4.7317 L12: 0.0120
REMARK 3 L13: -0.3795 L23: -0.9609
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: -0.0708 S13: -0.0713
REMARK 3 S21: -0.1204 S22: 0.0112 S23: 0.0258
REMARK 3 S31: 0.0280 S32: 0.2257 S33: -0.0163
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 101 C 107
REMARK 3 ORIGIN FOR THE GROUP (A): 39.6450 38.4950 6.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.0097 T22: -0.1073
REMARK 3 T33: -0.0508 T12: 0.0130
REMARK 3 T13: 0.0229 T23: 0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 1.1851 L22: 5.6888
REMARK 3 L33: 0.8489 L12: 0.8424
REMARK 3 L13: -0.3588 L23: 1.0107
REMARK 3 S TENSOR
REMARK 3 S11: 0.0481 S12: 0.2534 S13: 0.2714
REMARK 3 S21: -0.1355 S22: 0.0037 S23: 0.0367
REMARK 3 S31: -0.2944 S32: -0.1730 S33: -0.0517
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 99 D 107
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7900 38.4830 35.9070
REMARK 3 T TENSOR
REMARK 3 T11: 0.0811 T22: -0.0562
REMARK 3 T33: 0.0434 T12: -0.0608
REMARK 3 T13: -0.0523 T23: 0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 0.6365 L22: 3.3838
REMARK 3 L33: 9.6174 L12: -0.1590
REMARK 3 L13: 1.2695 L23: -0.2893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0710 S12: 0.2077 S13: 0.2254
REMARK 3 S21: -0.0615 S22: -0.1961 S23: -0.0182
REMARK 3 S31: -0.4105 S32: 0.3768 S33: 0.1251
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 98 E 107
REMARK 3 ORIGIN FOR THE GROUP (A): 15.3450 11.8370 39.2280
REMARK 3 T TENSOR
REMARK 3 T11: -0.0877 T22: 0.0491
REMARK 3 T33: -0.1071 T12: -0.0062
REMARK 3 T13: 0.0194 T23: -0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 3.0885 L22: 0.3312
REMARK 3 L33: 4.2652 L12: 0.0033
REMARK 3 L13: -1.1469 L23: -0.3269
REMARK 3 S TENSOR
REMARK 3 S11: -0.0302 S12: -0.0582 S13: 0.0385
REMARK 3 S21: 0.0147 S22: -0.0197 S23: -0.0249
REMARK 3 S31: 0.0456 S32: 0.0661 S33: 0.0499
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 100 F 107
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5900 20.3090 69.3720
REMARK 3 T TENSOR
REMARK 3 T11: -0.1286 T22: -0.0191
REMARK 3 T33: -0.1815 T12: 0.0213
REMARK 3 T13: 0.0308 T23: -0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 4.6227 L22: 0.6425
REMARK 3 L33: 0.9831 L12: -0.0628
REMARK 3 L13: -0.0590 L23: -0.0030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0684 S12: -0.1856 S13: 0.1165
REMARK 3 S21: 0.1087 S22: 0.0111 S23: -0.0641
REMARK 3 S31: -0.0976 S32: 0.0177 S33: -0.0795
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 1W89 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1290021079.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL FOCUSSING
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50114
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 19.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 2.680
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4200
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) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.53
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.290
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1UVZ
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: PEG 3350 22% (W/V), NA ACETATE 0.1M
REMARK 280 (PH 4.6), AMMONIUM SULFATE 0.2M, DTT 1MM. SOACKING IN A
REMARK 280 TRISHYDROXIMETHYLPHOSPHINE SOLUTION 10MM, PH 4.60
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, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 MET B -11
REMARK 465 ARG B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 MET C -11
REMARK 465 ARG C -10
REMARK 465 GLY C -9
REMARK 465 SER C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET D -11
REMARK 465 ARG D -10
REMARK 465 GLY D -9
REMARK 465 SER D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 MET E -11
REMARK 465 ARG E -10
REMARK 465 GLY E -9
REMARK 465 SER E -8
REMARK 465 HIS E -7
REMARK 465 HIS E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 MET F -11
REMARK 465 ARG F -10
REMARK 465 GLY F -9
REMARK 465 SER F -8
REMARK 465 HIS F -7
REMARK 465 HIS F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 GLY F -1
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 VAL A 22 CB VAL A 22 CG2 -0.129
REMARK 500 VAL A 23 CB VAL A 23 CG1 -0.132
REMARK 500 CYS B 34 CB CYS B 34 SG -0.097
REMARK 500 VAL B 77 CB VAL B 77 CG1 0.127
REMARK 500 VAL D 23 CB VAL D 23 CG1 -0.127
REMARK 500 VAL D 74 CB VAL D 74 CG2 -0.126
REMARK 500 VAL F 74 CB VAL F 74 CG2 -0.135
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 25 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 94 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP B 94 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP C 94 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP E 25 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP F 58 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP F 94 CB - CG - OD1 ANGL. DEV. = 6.7 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 HIS A 62 58.41 -144.28
REMARK 500 VAL B 15 -66.14 -107.61
REMARK 500 HIS C 62 56.91 -140.03
REMARK 500 PRO D 33 -33.24 -35.35
REMARK 500 LEU D 65 -34.49 -160.73
REMARK 500 ASP D 94 -158.95 -74.19
REMARK 500 VAL E 15 -62.59 -122.39
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 D 64 LEU D 65 146.86
REMARK 500 LYS D 88 PHE D 89 149.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UVZ RELATED DB: PDB
REMARK 900 STRUCTURE OF HUMAN THIOREDOXIN 2
REMARK 900 RELATED ID: 1W4V RELATED DB: PDB
REMARK 900 STRUCTURE OF THE OXIDISED FORM OF HUMAN THIOREDOXIN 2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THR1 CORRESPONDS TO THR60 IN Q99757
DBREF 1W89 A 1 107 UNP Q99757 THIOM_HUMAN 60 166
DBREF 1W89 B 1 107 UNP Q99757 THIOM_HUMAN 60 166
DBREF 1W89 C 1 107 UNP Q99757 THIOM_HUMAN 60 166
DBREF 1W89 D 1 107 UNP Q99757 THIOM_HUMAN 60 166
DBREF 1W89 E 1 107 UNP Q99757 THIOM_HUMAN 60 166
DBREF 1W89 F 1 107 UNP Q99757 THIOM_HUMAN 60 166
SEQADV 1W89 MET A -11 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 ARG A -10 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY A -9 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER A -8 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS A -7 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS A -6 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS A -5 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS A -4 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS A -3 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS A -2 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY A -1 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER A 0 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 MET B -11 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 ARG B -10 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY B -9 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER B -8 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS B -7 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS B -6 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS B -5 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS B -4 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS B -3 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS B -2 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY B -1 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER B 0 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 MET C -11 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 ARG C -10 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY C -9 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER C -8 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS C -7 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS C -6 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS C -5 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS C -4 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS C -3 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS C -2 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY C -1 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER C 0 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 MET D -11 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 ARG D -10 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY D -9 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER D -8 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS D -7 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS D -6 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS D -5 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS D -4 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS D -3 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS D -2 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY D -1 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER D 0 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 MET E -11 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 ARG E -10 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY E -9 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER E -8 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS E -7 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS E -6 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS E -5 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS E -4 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS E -3 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS E -2 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY E -1 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER E 0 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 MET F -11 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 ARG F -10 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY F -9 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER F -8 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS F -7 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS F -6 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS F -5 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS F -4 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS F -3 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 HIS F -2 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 GLY F -1 UNP Q99757 EXPRESSION TAG
SEQADV 1W89 SER F 0 UNP Q99757 EXPRESSION TAG
SEQRES 1 A 119 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER THR
SEQRES 2 A 119 THR PHE ASN ILE GLN ASP GLY PRO ASP PHE GLN ASP ARG
SEQRES 3 A 119 VAL VAL ASN SER GLU THR PRO VAL VAL VAL ASP PHE HIS
SEQRES 4 A 119 ALA GLN TRP CYS GLY PRO CYS LYS ILE LEU GLY PRO ARG
SEQRES 5 A 119 LEU GLU LYS MET VAL ALA LYS GLN HIS GLY LYS VAL VAL
SEQRES 6 A 119 MET ALA LYS VAL ASP ILE ASP ASP HIS THR ASP LEU ALA
SEQRES 7 A 119 ILE GLU TYR GLU VAL SER ALA VAL PRO THR VAL LEU ALA
SEQRES 8 A 119 MET LYS ASN GLY ASP VAL VAL ASP LYS PHE VAL GLY ILE
SEQRES 9 A 119 LYS ASP GLU ASP GLN LEU GLU ALA PHE LEU LYS LYS LEU
SEQRES 10 A 119 ILE GLY
SEQRES 1 B 119 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER THR
SEQRES 2 B 119 THR PHE ASN ILE GLN ASP GLY PRO ASP PHE GLN ASP ARG
SEQRES 3 B 119 VAL VAL ASN SER GLU THR PRO VAL VAL VAL ASP PHE HIS
SEQRES 4 B 119 ALA GLN TRP CYS GLY PRO CYS LYS ILE LEU GLY PRO ARG
SEQRES 5 B 119 LEU GLU LYS MET VAL ALA LYS GLN HIS GLY LYS VAL VAL
SEQRES 6 B 119 MET ALA LYS VAL ASP ILE ASP ASP HIS THR ASP LEU ALA
SEQRES 7 B 119 ILE GLU TYR GLU VAL SER ALA VAL PRO THR VAL LEU ALA
SEQRES 8 B 119 MET LYS ASN GLY ASP VAL VAL ASP LYS PHE VAL GLY ILE
SEQRES 9 B 119 LYS ASP GLU ASP GLN LEU GLU ALA PHE LEU LYS LYS LEU
SEQRES 10 B 119 ILE GLY
SEQRES 1 C 119 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER THR
SEQRES 2 C 119 THR PHE ASN ILE GLN ASP GLY PRO ASP PHE GLN ASP ARG
SEQRES 3 C 119 VAL VAL ASN SER GLU THR PRO VAL VAL VAL ASP PHE HIS
SEQRES 4 C 119 ALA GLN TRP CYS GLY PRO CYS LYS ILE LEU GLY PRO ARG
SEQRES 5 C 119 LEU GLU LYS MET VAL ALA LYS GLN HIS GLY LYS VAL VAL
SEQRES 6 C 119 MET ALA LYS VAL ASP ILE ASP ASP HIS THR ASP LEU ALA
SEQRES 7 C 119 ILE GLU TYR GLU VAL SER ALA VAL PRO THR VAL LEU ALA
SEQRES 8 C 119 MET LYS ASN GLY ASP VAL VAL ASP LYS PHE VAL GLY ILE
SEQRES 9 C 119 LYS ASP GLU ASP GLN LEU GLU ALA PHE LEU LYS LYS LEU
SEQRES 10 C 119 ILE GLY
SEQRES 1 D 119 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER THR
SEQRES 2 D 119 THR PHE ASN ILE GLN ASP GLY PRO ASP PHE GLN ASP ARG
SEQRES 3 D 119 VAL VAL ASN SER GLU THR PRO VAL VAL VAL ASP PHE HIS
SEQRES 4 D 119 ALA GLN TRP CYS GLY PRO CYS LYS ILE LEU GLY PRO ARG
SEQRES 5 D 119 LEU GLU LYS MET VAL ALA LYS GLN HIS GLY LYS VAL VAL
SEQRES 6 D 119 MET ALA LYS VAL ASP ILE ASP ASP HIS THR ASP LEU ALA
SEQRES 7 D 119 ILE GLU TYR GLU VAL SER ALA VAL PRO THR VAL LEU ALA
SEQRES 8 D 119 MET LYS ASN GLY ASP VAL VAL ASP LYS PHE VAL GLY ILE
SEQRES 9 D 119 LYS ASP GLU ASP GLN LEU GLU ALA PHE LEU LYS LYS LEU
SEQRES 10 D 119 ILE GLY
SEQRES 1 E 119 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER THR
SEQRES 2 E 119 THR PHE ASN ILE GLN ASP GLY PRO ASP PHE GLN ASP ARG
SEQRES 3 E 119 VAL VAL ASN SER GLU THR PRO VAL VAL VAL ASP PHE HIS
SEQRES 4 E 119 ALA GLN TRP CYS GLY PRO CYS LYS ILE LEU GLY PRO ARG
SEQRES 5 E 119 LEU GLU LYS MET VAL ALA LYS GLN HIS GLY LYS VAL VAL
SEQRES 6 E 119 MET ALA LYS VAL ASP ILE ASP ASP HIS THR ASP LEU ALA
SEQRES 7 E 119 ILE GLU TYR GLU VAL SER ALA VAL PRO THR VAL LEU ALA
SEQRES 8 E 119 MET LYS ASN GLY ASP VAL VAL ASP LYS PHE VAL GLY ILE
SEQRES 9 E 119 LYS ASP GLU ASP GLN LEU GLU ALA PHE LEU LYS LYS LEU
SEQRES 10 E 119 ILE GLY
SEQRES 1 F 119 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER THR
SEQRES 2 F 119 THR PHE ASN ILE GLN ASP GLY PRO ASP PHE GLN ASP ARG
SEQRES 3 F 119 VAL VAL ASN SER GLU THR PRO VAL VAL VAL ASP PHE HIS
SEQRES 4 F 119 ALA GLN TRP CYS GLY PRO CYS LYS ILE LEU GLY PRO ARG
SEQRES 5 F 119 LEU GLU LYS MET VAL ALA LYS GLN HIS GLY LYS VAL VAL
SEQRES 6 F 119 MET ALA LYS VAL ASP ILE ASP ASP HIS THR ASP LEU ALA
SEQRES 7 F 119 ILE GLU TYR GLU VAL SER ALA VAL PRO THR VAL LEU ALA
SEQRES 8 F 119 MET LYS ASN GLY ASP VAL VAL ASP LYS PHE VAL GLY ILE
SEQRES 9 F 119 LYS ASP GLU ASP GLN LEU GLU ALA PHE LEU LYS LYS LEU
SEQRES 10 F 119 ILE GLY
FORMUL 7 HOH *498(H2 O)
HELIX 1 1 ASP A 7 VAL A 15 1 9
HELIX 2 2 CYS A 31 GLN A 48 1 18
HELIX 3 3 HIS A 62 TYR A 69 1 8
HELIX 4 4 ASP A 94 GLY A 107 1 14
HELIX 5 5 ASP B 7 VAL B 15 1 9
HELIX 6 6 PRO B 33 LYS B 47 1 15
HELIX 7 7 HIS B 62 TYR B 69 1 8
HELIX 8 8 ASP B 94 GLY B 107 1 14
HELIX 9 9 ASP C 7 VAL C 15 1 9
HELIX 10 10 PRO C 33 GLN C 48 1 16
HELIX 11 11 HIS C 62 TYR C 69 1 8
HELIX 12 12 ASP C 94 GLY C 107 1 14
HELIX 13 13 ASP D 7 ARG D 14 1 8
HELIX 14 14 CYS D 31 LYS D 47 1 17
HELIX 15 15 HIS D 62 ILE D 67 1 6
HELIX 16 16 ASP D 94 GLY D 107 1 14
HELIX 17 17 ASP E 7 VAL E 15 1 9
HELIX 18 18 CYS E 31 LYS E 47 1 17
HELIX 19 19 HIS E 62 TYR E 69 1 8
HELIX 20 20 ASP E 94 GLY E 107 1 14
HELIX 21 21 ASP F 7 VAL F 15 1 9
HELIX 22 22 PRO F 33 LYS F 47 1 15
HELIX 23 23 HIS F 62 TYR F 69 1 8
HELIX 24 24 ASP F 94 GLY F 107 1 14
SHEET 1 AA 5 THR A 2 ASN A 4 0
SHEET 2 AA 5 VAL A 53 ASP A 58 1 O MET A 54 N PHE A 3
SHEET 3 AA 5 VAL A 22 HIS A 27 1 O VAL A 23 N ALA A 55
SHEET 4 AA 5 THR A 76 LYS A 81 -1 O THR A 76 N PHE A 26
SHEET 5 AA 5 ASP A 84 VAL A 90 -1 O ASP A 84 N LYS A 81
SHEET 1 BA 5 THR B 2 ASN B 4 0
SHEET 2 BA 5 VAL B 53 ASP B 58 1 O MET B 54 N PHE B 3
SHEET 3 BA 5 VAL B 22 HIS B 27 1 O VAL B 23 N ALA B 55
SHEET 4 BA 5 THR B 76 LYS B 81 -1 O THR B 76 N PHE B 26
SHEET 5 BA 5 ASP B 84 VAL B 90 -1 O ASP B 84 N LYS B 81
SHEET 1 CA 5 THR C 2 ASN C 4 0
SHEET 2 CA 5 VAL C 53 ASP C 58 1 O MET C 54 N PHE C 3
SHEET 3 CA 5 VAL C 22 HIS C 27 1 O VAL C 23 N ALA C 55
SHEET 4 CA 5 THR C 76 LYS C 81 -1 O THR C 76 N PHE C 26
SHEET 5 CA 5 ASP C 84 VAL C 90 -1 O ASP C 84 N LYS C 81
SHEET 1 DA 5 THR D 2 ASN D 4 0
SHEET 2 DA 5 VAL D 53 ASP D 58 1 O MET D 54 N PHE D 3
SHEET 3 DA 5 VAL D 22 HIS D 27 1 O VAL D 23 N ALA D 55
SHEET 4 DA 5 THR D 76 LYS D 81 -1 O THR D 76 N PHE D 26
SHEET 5 DA 5 ASP D 84 VAL D 90 -1 O ASP D 84 N LYS D 81
SHEET 1 EA 5 THR E 2 ASN E 4 0
SHEET 2 EA 5 VAL E 53 ASP E 58 1 O MET E 54 N PHE E 3
SHEET 3 EA 5 VAL E 22 HIS E 27 1 O VAL E 23 N ALA E 55
SHEET 4 EA 5 THR E 76 LYS E 81 -1 O THR E 76 N PHE E 26
SHEET 5 EA 5 ASP E 84 VAL E 90 -1 O ASP E 84 N LYS E 81
SHEET 1 FA 5 THR F 2 ASN F 4 0
SHEET 2 FA 5 VAL F 53 ASP F 58 1 O MET F 54 N PHE F 3
SHEET 3 FA 5 VAL F 22 HIS F 27 1 O VAL F 23 N ALA F 55
SHEET 4 FA 5 THR F 76 LYS F 81 -1 O THR F 76 N PHE F 26
SHEET 5 FA 5 ASP F 84 VAL F 90 -1 O ASP F 84 N LYS F 81
CISPEP 1 VAL A 74 PRO A 75 0 -6.56
CISPEP 2 VAL B 74 PRO B 75 0 -8.68
CISPEP 3 VAL C 74 PRO C 75 0 -5.35
CISPEP 4 VAL D 74 PRO D 75 0 -4.96
CISPEP 5 VAL E 74 PRO E 75 0 -1.85
CISPEP 6 VAL F 74 PRO F 75 0 -13.38
CRYST1 49.580 49.610 80.020 87.77 82.30 79.31 P 1 6
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 0.020169 -0.003807 -0.002672 0.00000
SCALE2 0.000000 0.020513 -0.000296 0.00000
SCALE3 0.000000 0.000000 0.012612 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
