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HEADER HYDROLASE 17-DEC-21 7QJQ
TITLE CRYSTAL STRUCTURE OF A CUTINASE ENZYME FROM THERMOBIFIDA FUSCA NTU22
TITLE 2 (702)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLXYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_TAXID: 2021;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS PLASTIC DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZAHN,R.S.GILL,L.AVILAN,G.T.BECKHAM,J.E.MCGEEHAN
REVDAT 1 28-DEC-22 7QJQ 0
JRNL AUTH E.ERICKSON,J.E.GADO,L.AVILAN,F.BRATTI,R.K.BRIZENDINE,
JRNL AUTH 2 P.A.COX,R.GILL,R.GRAHAM,D.J.KIM,G.KONIG,W.E.MICHENER,
JRNL AUTH 3 S.POUDEL,K.J.RAMIREZ,T.J.SHAKESPEARE,M.ZAHN,E.S.BOYD,
JRNL AUTH 4 C.M.PAYNE,J.L.DUBOIS,A.R.PICKFORD,G.T.BECKHAM,J.E.MCGEEHAN
JRNL TITL SOURCING THERMOTOLERANT POLY(ETHYLENE TEREPHTHALATE)
JRNL TITL 2 HYDROLASE SCAFFOLDS FROM NATURAL DIVERSITY
JRNL REF NAT COMMUN V. 13 7850 2022
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-022-35237-X
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 119.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.6
REMARK 3 NUMBER OF REFLECTIONS : 133556
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 6780
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) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.68
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1424
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 11.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 81
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11924
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 1515
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : 0.06000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : -0.05000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.879
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12383 ; 0.013 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 11422 ; 0.001 ; 0.014
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16927 ; 1.632 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 26365 ; 1.483 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1598 ; 6.762 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 607 ;31.190 ;21.087
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1859 ;10.925 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 91 ;18.874 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1680 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14149 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2873 ; 0.001 ; 0.020
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 15
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 263 B 2 263 8836 0.070 0.050
REMARK 3 2 A 2 262 C 2 262 8903 0.060 0.050
REMARK 3 3 A 2 262 D 2 262 8833 0.070 0.050
REMARK 3 4 A 2 262 E 2 262 8855 0.060 0.050
REMARK 3 5 A 2 261 F 2 261 8777 0.070 0.050
REMARK 3 6 B 1 263 C 1 263 8757 0.070 0.050
REMARK 3 7 B 1 261 D 1 261 8960 0.040 0.050
REMARK 3 8 B 1 261 E 1 261 8921 0.050 0.050
REMARK 3 9 B 1 262 F 1 262 8755 0.070 0.050
REMARK 3 10 C 1 262 D 1 262 8776 0.080 0.050
REMARK 3 11 C 1 262 E 1 262 8774 0.080 0.050
REMARK 3 12 C 1 262 F 1 262 8763 0.070 0.050
REMARK 3 13 D 1 262 E 1 262 9006 0.060 0.050
REMARK 3 14 D 1 262 F 1 262 8764 0.070 0.050
REMARK 3 15 E 1 262 F 1 262 8826 0.060 0.050
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 2 A 301
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0846 -0.2966 -0.2708
REMARK 3 T TENSOR
REMARK 3 T11: 0.0117 T22: 0.0266
REMARK 3 T33: 0.0382 T12: -0.0008
REMARK 3 T13: -0.0077 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.1647 L22: 0.3188
REMARK 3 L33: 0.4088 L12: -0.1304
REMARK 3 L13: -0.0419 L23: -0.0465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0323 S12: -0.0417 S13: -0.0188
REMARK 3 S21: -0.0430 S22: -0.0198 S23: 0.0257
REMARK 3 S31: 0.0038 S32: 0.0482 S33: -0.0125
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 1 B 301
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2703 37.3602 10.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.0166 T22: 0.0046
REMARK 3 T33: 0.0509 T12: 0.0010
REMARK 3 T13: 0.0063 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.1126 L22: 0.4664
REMARK 3 L33: 0.3210 L12: 0.0031
REMARK 3 L13: -0.0147 L23: 0.0078
REMARK 3 S TENSOR
REMARK 3 S11: 0.0217 S12: 0.0087 S13: 0.0171
REMARK 3 S21: 0.0246 S22: -0.0374 S23: -0.0043
REMARK 3 S31: -0.0153 S32: -0.0149 S33: 0.0157
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 1 C 301
REMARK 3 ORIGIN FOR THE GROUP (A): -28.3315 39.5255 -26.9003
REMARK 3 T TENSOR
REMARK 3 T11: 0.0127 T22: 0.0184
REMARK 3 T33: 0.0460 T12: 0.0089
REMARK 3 T13: 0.0028 T23: 0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.1240 L22: 0.4075
REMARK 3 L33: 0.5383 L12: 0.2084
REMARK 3 L13: -0.0185 L23: 0.1289
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: 0.0185 S13: 0.0113
REMARK 3 S21: 0.0462 S22: 0.0084 S23: -0.0043
REMARK 3 S31: 0.0269 S32: -0.0514 S33: -0.0357
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 1 D 301
REMARK 3 ORIGIN FOR THE GROUP (A): -16.0716 -2.6828 -37.7414
REMARK 3 T TENSOR
REMARK 3 T11: 0.0086 T22: 0.0317
REMARK 3 T33: 0.0268 T12: 0.0017
REMARK 3 T13: -0.0083 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.0513 L22: 0.4523
REMARK 3 L33: 0.7556 L12: -0.0449
REMARK 3 L13: -0.1349 L23: -0.0843
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: 0.0212 S13: -0.0184
REMARK 3 S21: 0.0181 S22: -0.0585 S23: 0.0397
REMARK 3 S31: -0.0614 S32: 0.0366 S33: 0.0423
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 1 E 301
REMARK 3 ORIGIN FOR THE GROUP (A): -43.3355 48.2072 -64.5142
REMARK 3 T TENSOR
REMARK 3 T11: 0.0256 T22: 0.0207
REMARK 3 T33: 0.0300 T12: 0.0061
REMARK 3 T13: -0.0140 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.2640 L22: 0.2941
REMARK 3 L33: 0.5014 L12: 0.0295
REMARK 3 L13: 0.1804 L23: -0.1989
REMARK 3 S TENSOR
REMARK 3 S11: 0.0461 S12: -0.0219 S13: -0.0351
REMARK 3 S21: -0.0427 S22: -0.0122 S23: 0.0082
REMARK 3 S31: 0.0287 S32: -0.0144 S33: -0.0339
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 1 F 301
REMARK 3 ORIGIN FOR THE GROUP (A): -28.6393 80.0254 -83.0245
REMARK 3 T TENSOR
REMARK 3 T11: 0.0471 T22: 0.0621
REMARK 3 T33: 0.0564 T12: -0.0271
REMARK 3 T13: 0.0137 T23: 0.0378
REMARK 3 L TENSOR
REMARK 3 L11: 0.6709 L22: 0.1063
REMARK 3 L33: 1.3191 L12: 0.0009
REMARK 3 L13: 0.9164 L23: 0.0857
REMARK 3 S TENSOR
REMARK 3 S11: 0.1443 S12: -0.1393 S13: -0.0644
REMARK 3 S21: -0.0431 S22: -0.0126 S23: -0.0715
REMARK 3 S31: 0.1449 S32: -0.2077 S33: -0.1317
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 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 7QJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-21.
REMARK 100 THE DEPOSITION ID IS D_1292119750.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-21
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 140392
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.637
REMARK 200 RESOLUTION RANGE LOW (A) : 119.804
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 53.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.77200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
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: 5ZOA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 0.2 M SODIUM SULFATE,
REMARK 280 0.1 M BIS-TRIS PROPANE PH 6.5, VAPOR DIFFUSION, HANGING 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, 3, 4, 5, 6
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 0
REMARK 465 ALA A 1
REMARK 465 GLY A 248
REMARK 465 LEU A 249
REMARK 465 PHE A 250
REMARK 465 GLY A 251
REMARK 465 GLU A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 MET B 0
REMARK 465 GLU B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 MET C 0
REMARK 465 GLY C 248
REMARK 465 LEU C 249
REMARK 465 PHE C 250
REMARK 465 GLY C 251
REMARK 465 GLU C 264
REMARK 465 HIS C 265
REMARK 465 HIS C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 MET D 0
REMARK 465 LEU D 263
REMARK 465 GLU D 264
REMARK 465 HIS D 265
REMARK 465 HIS D 266
REMARK 465 HIS D 267
REMARK 465 HIS D 268
REMARK 465 HIS D 269
REMARK 465 HIS D 270
REMARK 465 MET E 0
REMARK 465 LEU E 263
REMARK 465 GLU E 264
REMARK 465 HIS E 265
REMARK 465 HIS E 266
REMARK 465 HIS E 267
REMARK 465 HIS E 268
REMARK 465 HIS E 269
REMARK 465 HIS E 270
REMARK 465 MET F 0
REMARK 465 ASP F 247
REMARK 465 GLY F 248
REMARK 465 LEU F 249
REMARK 465 PHE F 250
REMARK 465 GLY F 251
REMARK 465 LEU F 263
REMARK 465 GLU F 264
REMARK 465 HIS F 265
REMARK 465 HIS F 266
REMARK 465 HIS F 267
REMARK 465 HIS F 268
REMARK 465 HIS F 269
REMARK 465 HIS F 270
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 517 O HOH A 560 1.73
REMARK 500 O HOH D 416 O HOH D 504 1.82
REMARK 500 O HOH B 552 O HOH B 656 1.92
REMARK 500 O HOH C 463 O HOH C 521 1.92
REMARK 500 O HOH A 613 O HOH A 665 1.97
REMARK 500 O HOH E 415 O HOH E 547 1.97
REMARK 500 O HOH B 438 O HOH B 585 1.98
REMARK 500 O HOH E 511 O HOH E 612 1.99
REMARK 500 O HOH A 657 O HOH B 402 1.99
REMARK 500 O HOH D 472 O HOH D 551 2.00
REMARK 500 O HOH C 427 O HOH C 459 2.01
REMARK 500 O HOH F 417 O HOH F 489 2.01
REMARK 500 O HOH B 588 O HOH B 666 2.02
REMARK 500 O HOH A 403 O HOH A 593 2.02
REMARK 500 O HOH C 363 O HOH C 518 2.03
REMARK 500 O HOH B 416 O HOH B 501 2.04
REMARK 500 O HOH D 565 O HOH D 620 2.06
REMARK 500 OD1 ASP D 146 O HOH D 401 2.08
REMARK 500 O HOH C 303 O HOH C 519 2.09
REMARK 500 O HOH A 446 O HOH A 660 2.09
REMARK 500 OD1 ASP E 146 O HOH E 401 2.10
REMARK 500 O CYS F 260 O HOH F 401 2.13
REMARK 500 O HOH B 509 O HOH B 649 2.13
REMARK 500 O HOH E 489 O HOH E 572 2.15
REMARK 500 O HOH A 590 O HOH A 614 2.15
REMARK 500 O HOH E 570 O HOH E 622 2.15
REMARK 500 O HOH A 623 O HOH A 649 2.15
REMARK 500 O HOH A 576 O HOH A 635 2.16
REMARK 500 NE2 GLN E 93 O HOH E 402 2.16
REMARK 500 O HOH B 656 O HOH C 546 2.16
REMARK 500 NH1 ARG D 32 O ILE D 88 2.16
REMARK 500 O HOH E 433 O HOH E 617 2.16
REMARK 500 O HOH A 631 O HOH A 656 2.17
REMARK 500 OG1 THR F 51 O HOH F 402 2.17
REMARK 500 OG SER A 123 O HOH A 401 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 677 O HOH C 559 1655 1.98
REMARK 500 NH1 ARG C 19 OG SER C 163 1455 2.08
REMARK 500 NH1 ARG A 19 OG SER A 163 1655 2.13
REMARK 500 O HOH B 676 O HOH C 504 1655 2.16
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 ARG A 19 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 74 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG C 74 CB - CG - CD ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG C 74 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG C 74 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG D 32 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 74 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG F 74 NE - CZ - NH2 ANGL. DEV. = -3.9 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 THR A 62 -10.21 71.57
REMARK 500 SER A 131 -115.88 63.73
REMARK 500 THR A 154 59.01 34.30
REMARK 500 HIS A 185 -86.65 -123.25
REMARK 500 ASN B 50 175.52 177.05
REMARK 500 THR B 62 -8.27 71.98
REMARK 500 SER B 131 -115.80 62.98
REMARK 500 THR B 154 57.30 34.75
REMARK 500 HIS B 185 -84.63 -121.78
REMARK 500 GLU B 252 -56.69 -132.02
REMARK 500 ASN C 50 174.28 178.50
REMARK 500 THR C 62 -9.58 71.47
REMARK 500 SER C 131 -114.60 62.04
REMARK 500 THR C 154 59.79 34.95
REMARK 500 HIS C 185 -85.94 -122.92
REMARK 500 ASN D 50 176.57 175.97
REMARK 500 THR D 62 -7.80 72.35
REMARK 500 SER D 131 -114.56 63.37
REMARK 500 THR D 154 57.53 36.10
REMARK 500 HIS D 185 -85.97 -123.06
REMARK 500 GLU D 252 -51.92 -131.67
REMARK 500 ASN E 50 176.79 176.99
REMARK 500 THR E 62 -10.51 72.55
REMARK 500 SER E 131 -114.47 62.20
REMARK 500 THR E 154 58.80 35.41
REMARK 500 HIS E 185 -85.75 -123.41
REMARK 500 GLU E 252 -54.88 -132.29
REMARK 500 ASN F 50 178.14 177.62
REMARK 500 THR F 62 -8.39 71.62
REMARK 500 SER F 131 -115.72 62.96
REMARK 500 THR F 154 59.25 35.19
REMARK 500 HIS F 185 -86.81 -121.93
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 ASN A 213 0.08 SIDE CHAIN
REMARK 500 ASN C 213 0.07 SIDE CHAIN
REMARK 500 ASN F 213 0.07 SIDE CHAIN
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 A 677 DISTANCE = 9.62 ANGSTROMS
REMARK 525 HOH E 636 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH E 637 DISTANCE = 6.24 ANGSTROMS
DBREF 7QJQ A 1 262 UNP E0Z5H1 E0Z5H1_THEFU 1 262
DBREF 7QJQ B 1 262 UNP E0Z5H1 E0Z5H1_THEFU 1 262
DBREF 7QJQ C 1 262 UNP E0Z5H1 E0Z5H1_THEFU 1 262
DBREF 7QJQ D 1 262 UNP E0Z5H1 E0Z5H1_THEFU 1 262
DBREF 7QJQ E 1 262 UNP E0Z5H1 E0Z5H1_THEFU 1 262
DBREF 7QJQ F 1 262 UNP E0Z5H1 E0Z5H1_THEFU 1 262
SEQADV 7QJQ MET A 0 UNP E0Z5H1 INITIATING METHIONINE
SEQADV 7QJQ LEU A 263 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ GLU A 264 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS A 265 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS A 266 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS A 267 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS A 268 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS A 269 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS A 270 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ MET B 0 UNP E0Z5H1 INITIATING METHIONINE
SEQADV 7QJQ LEU B 263 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ GLU B 264 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS B 265 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS B 266 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS B 267 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS B 268 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS B 269 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS B 270 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ MET C 0 UNP E0Z5H1 INITIATING METHIONINE
SEQADV 7QJQ LEU C 263 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ GLU C 264 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS C 265 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS C 266 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS C 267 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS C 268 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS C 269 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS C 270 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ MET D 0 UNP E0Z5H1 INITIATING METHIONINE
SEQADV 7QJQ LEU D 263 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ GLU D 264 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS D 265 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS D 266 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS D 267 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS D 268 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS D 269 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS D 270 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ MET E 0 UNP E0Z5H1 INITIATING METHIONINE
SEQADV 7QJQ LEU E 263 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ GLU E 264 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS E 265 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS E 266 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS E 267 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS E 268 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS E 269 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS E 270 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ MET F 0 UNP E0Z5H1 INITIATING METHIONINE
SEQADV 7QJQ LEU F 263 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ GLU F 264 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS F 265 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS F 266 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS F 267 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS F 268 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS F 269 UNP E0Z5H1 EXPRESSION TAG
SEQADV 7QJQ HIS F 270 UNP E0Z5H1 EXPRESSION TAG
SEQRES 1 A 271 MET ALA ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR
SEQRES 2 A 271 ASP ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL
SEQRES 3 A 271 SER GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE
SEQRES 4 A 271 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU SER ASN THR
SEQRES 5 A 271 TYR GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR
SEQRES 6 A 271 GLU ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER
SEQRES 7 A 271 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR
SEQRES 8 A 271 LEU ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA
SEQRES 9 A 271 ALA LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL
SEQRES 10 A 271 ARG SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY
SEQRES 11 A 271 HIS SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER
SEQRES 12 A 271 GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 A 271 TRP HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO
SEQRES 14 A 271 THR LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO
SEQRES 15 A 271 VAL ALA THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO
SEQRES 16 A 271 SER SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA
SEQRES 17 A 271 THR HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY
SEQRES 18 A 271 LYS TYR SER VAL ALA TRP LEU LYS TRP PHE VAL ASP ASN
SEQRES 19 A 271 ASP THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG
SEQRES 20 A 271 ASP GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR
SEQRES 21 A 271 CYS PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 271 MET ALA ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR
SEQRES 2 B 271 ASP ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL
SEQRES 3 B 271 SER GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE
SEQRES 4 B 271 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU SER ASN THR
SEQRES 5 B 271 TYR GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR
SEQRES 6 B 271 GLU ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER
SEQRES 7 B 271 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR
SEQRES 8 B 271 LEU ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA
SEQRES 9 B 271 ALA LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL
SEQRES 10 B 271 ARG SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY
SEQRES 11 B 271 HIS SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER
SEQRES 12 B 271 GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 B 271 TRP HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO
SEQRES 14 B 271 THR LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO
SEQRES 15 B 271 VAL ALA THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO
SEQRES 16 B 271 SER SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA
SEQRES 17 B 271 THR HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY
SEQRES 18 B 271 LYS TYR SER VAL ALA TRP LEU LYS TRP PHE VAL ASP ASN
SEQRES 19 B 271 ASP THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG
SEQRES 20 B 271 ASP GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR
SEQRES 21 B 271 CYS PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 271 MET ALA ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR
SEQRES 2 C 271 ASP ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL
SEQRES 3 C 271 SER GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE
SEQRES 4 C 271 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU SER ASN THR
SEQRES 5 C 271 TYR GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR
SEQRES 6 C 271 GLU ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER
SEQRES 7 C 271 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR
SEQRES 8 C 271 LEU ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA
SEQRES 9 C 271 ALA LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL
SEQRES 10 C 271 ARG SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY
SEQRES 11 C 271 HIS SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER
SEQRES 12 C 271 GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 C 271 TRP HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO
SEQRES 14 C 271 THR LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO
SEQRES 15 C 271 VAL ALA THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO
SEQRES 16 C 271 SER SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA
SEQRES 17 C 271 THR HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY
SEQRES 18 C 271 LYS TYR SER VAL ALA TRP LEU LYS TRP PHE VAL ASP ASN
SEQRES 19 C 271 ASP THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG
SEQRES 20 C 271 ASP GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR
SEQRES 21 C 271 CYS PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 271 MET ALA ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR
SEQRES 2 D 271 ASP ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL
SEQRES 3 D 271 SER GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE
SEQRES 4 D 271 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU SER ASN THR
SEQRES 5 D 271 TYR GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR
SEQRES 6 D 271 GLU ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER
SEQRES 7 D 271 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR
SEQRES 8 D 271 LEU ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA
SEQRES 9 D 271 ALA LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL
SEQRES 10 D 271 ARG SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY
SEQRES 11 D 271 HIS SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER
SEQRES 12 D 271 GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 D 271 TRP HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO
SEQRES 14 D 271 THR LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO
SEQRES 15 D 271 VAL ALA THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO
SEQRES 16 D 271 SER SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA
SEQRES 17 D 271 THR HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY
SEQRES 18 D 271 LYS TYR SER VAL ALA TRP LEU LYS TRP PHE VAL ASP ASN
SEQRES 19 D 271 ASP THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG
SEQRES 20 D 271 ASP GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR
SEQRES 21 D 271 CYS PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 271 MET ALA ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR
SEQRES 2 E 271 ASP ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL
SEQRES 3 E 271 SER GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE
SEQRES 4 E 271 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU SER ASN THR
SEQRES 5 E 271 TYR GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR
SEQRES 6 E 271 GLU ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER
SEQRES 7 E 271 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR
SEQRES 8 E 271 LEU ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA
SEQRES 9 E 271 ALA LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL
SEQRES 10 E 271 ARG SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY
SEQRES 11 E 271 HIS SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER
SEQRES 12 E 271 GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 E 271 TRP HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO
SEQRES 14 E 271 THR LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO
SEQRES 15 E 271 VAL ALA THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO
SEQRES 16 E 271 SER SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA
SEQRES 17 E 271 THR HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY
SEQRES 18 E 271 LYS TYR SER VAL ALA TRP LEU LYS TRP PHE VAL ASP ASN
SEQRES 19 E 271 ASP THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG
SEQRES 20 E 271 ASP GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR
SEQRES 21 E 271 CYS PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 F 271 MET ALA ALA ASN PRO TYR GLU ARG GLY PRO ASN PRO THR
SEQRES 2 F 271 ASP ALA LEU LEU GLU ALA ARG SER GLY PRO PHE SER VAL
SEQRES 3 F 271 SER GLU GLU ASN VAL SER ARG LEU SER ALA SER GLY PHE
SEQRES 4 F 271 GLY GLY GLY THR ILE TYR TYR PRO ARG GLU SER ASN THR
SEQRES 5 F 271 TYR GLY ALA VAL ALA ILE SER PRO GLY TYR THR GLY THR
SEQRES 6 F 271 GLU ALA SER ILE ALA TRP LEU GLY GLU ARG ILE ALA SER
SEQRES 7 F 271 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ILE THR THR
SEQRES 8 F 271 LEU ASP GLN PRO ASP SER ARG ALA GLU GLN LEU ASN ALA
SEQRES 9 F 271 ALA LEU ASN HIS MET ILE ASN ARG ALA SER SER THR VAL
SEQRES 10 F 271 ARG SER ARG ILE ASP SER SER ARG LEU ALA VAL MET GLY
SEQRES 11 F 271 HIS SER MET GLY GLY GLY GLY THR LEU ARG LEU ALA SER
SEQRES 12 F 271 GLN ARG PRO ASP LEU LYS ALA ALA ILE PRO LEU THR PRO
SEQRES 13 F 271 TRP HIS LEU ASN LYS ASN TRP SER SER VAL THR VAL PRO
SEQRES 14 F 271 THR LEU ILE ILE GLY ALA ASP LEU ASP THR ILE ALA PRO
SEQRES 15 F 271 VAL ALA THR HIS ALA LYS PRO PHE TYR ASN SER LEU PRO
SEQRES 16 F 271 SER SER ILE SER LYS ALA TYR LEU GLU LEU ASP GLY ALA
SEQRES 17 F 271 THR HIS PHE ALA PRO ASN ILE PRO ASN LYS ILE ILE GLY
SEQRES 18 F 271 LYS TYR SER VAL ALA TRP LEU LYS TRP PHE VAL ASP ASN
SEQRES 19 F 271 ASP THR ARG TYR THR GLN PHE LEU CYS PRO GLY PRO ARG
SEQRES 20 F 271 ASP GLY LEU PHE GLY GLU VAL GLU GLU TYR ARG SER THR
SEQRES 21 F 271 CYS PRO PHE LEU GLU HIS HIS HIS HIS HIS HIS
HET PEG A 301 7
HET PEG B 301 7
HET PEG D 301 7
HET PEG E 301 7
HET PEG E 302 7
HET PEG F 301 7
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 7 PEG 6(C4 H10 O3)
FORMUL 13 HOH *1515(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 THR A 64 SER A 67 5 4
HELIX 3 AA3 ILE A 68 SER A 77 1 10
HELIX 4 AA4 GLN A 93 ARG A 111 1 19
HELIX 5 AA5 SER A 113 SER A 118 1 6
HELIX 6 AA6 SER A 131 ARG A 144 1 14
HELIX 7 AA7 HIS A 185 LEU A 193 1 9
HELIX 8 AA8 PHE A 210 ILE A 214 5 5
HELIX 9 AA9 ASN A 216 ASN A 233 1 18
HELIX 10 AB1 ASP A 234 ARG A 236 5 3
HELIX 11 AB2 TYR A 237 CYS A 242 1 6
HELIX 12 AB3 THR B 12 ALA B 18 1 7
HELIX 13 AB4 THR B 64 SER B 67 5 4
HELIX 14 AB5 ILE B 68 SER B 77 1 10
HELIX 15 AB6 GLN B 93 ARG B 111 1 19
HELIX 16 AB7 SER B 113 SER B 118 1 6
HELIX 17 AB8 SER B 131 ARG B 144 1 14
HELIX 18 AB9 HIS B 185 LEU B 193 1 9
HELIX 19 AC1 PHE B 210 ILE B 214 5 5
HELIX 20 AC2 ASN B 216 ASN B 233 1 18
HELIX 21 AC3 ASP B 234 ARG B 236 5 3
HELIX 22 AC4 TYR B 237 CYS B 242 1 6
HELIX 23 AC5 THR C 12 ALA C 18 1 7
HELIX 24 AC6 THR C 64 SER C 67 5 4
HELIX 25 AC7 ILE C 68 SER C 77 1 10
HELIX 26 AC8 GLN C 93 ARG C 111 1 19
HELIX 27 AC9 SER C 113 SER C 118 1 6
HELIX 28 AD1 SER C 131 ARG C 144 1 14
HELIX 29 AD2 HIS C 185 LEU C 193 1 9
HELIX 30 AD3 PHE C 210 ILE C 214 5 5
HELIX 31 AD4 ASN C 216 ASN C 233 1 18
HELIX 32 AD5 ASP C 234 ARG C 236 5 3
HELIX 33 AD6 TYR C 237 CYS C 242 1 6
HELIX 34 AD7 THR D 12 ALA D 18 1 7
HELIX 35 AD8 THR D 64 SER D 67 5 4
HELIX 36 AD9 ILE D 68 SER D 77 1 10
HELIX 37 AE1 GLN D 93 ARG D 111 1 19
HELIX 38 AE2 SER D 113 SER D 118 1 6
HELIX 39 AE3 SER D 131 ARG D 144 1 14
HELIX 40 AE4 HIS D 185 LEU D 193 1 9
HELIX 41 AE5 PHE D 210 ILE D 214 5 5
HELIX 42 AE6 ASN D 216 ASN D 233 1 18
HELIX 43 AE7 ASP D 234 ARG D 236 5 3
HELIX 44 AE8 TYR D 237 CYS D 242 1 6
HELIX 45 AE9 THR E 12 ALA E 18 1 7
HELIX 46 AF1 THR E 64 SER E 67 5 4
HELIX 47 AF2 ILE E 68 SER E 77 1 10
HELIX 48 AF3 GLN E 93 ARG E 111 1 19
HELIX 49 AF4 SER E 113 SER E 118 1 6
HELIX 50 AF5 SER E 131 ARG E 144 1 14
HELIX 51 AF6 HIS E 185 LEU E 193 1 9
HELIX 52 AF7 PHE E 210 ILE E 214 5 5
HELIX 53 AF8 ASN E 216 ASN E 233 1 18
HELIX 54 AF9 ASP E 234 ARG E 236 5 3
HELIX 55 AG1 TYR E 237 CYS E 242 1 6
HELIX 56 AG2 THR F 12 ALA F 18 1 7
HELIX 57 AG3 THR F 64 SER F 67 5 4
HELIX 58 AG4 ILE F 68 SER F 77 1 10
HELIX 59 AG5 GLN F 93 ARG F 111 1 19
HELIX 60 AG6 SER F 113 SER F 118 1 6
HELIX 61 AG7 SER F 131 ARG F 144 1 14
HELIX 62 AG8 HIS F 185 LEU F 193 1 9
HELIX 63 AG9 PHE F 210 ILE F 214 5 5
HELIX 64 AH1 ASN F 216 ASN F 233 1 18
HELIX 65 AH2 ASP F 234 ARG F 236 5 3
HELIX 66 AH3 TYR F 237 CYS F 242 1 6
SHEET 1 AA1 6 VAL A 25 VAL A 30 0
SHEET 2 AA1 6 GLY A 41 PRO A 46 -1 O GLY A 41 N VAL A 30
SHEET 3 AA1 6 VAL A 81 ILE A 85 -1 O VAL A 82 N TYR A 44
SHEET 4 AA1 6 TYR A 52 SER A 58 1 N VAL A 55 O ILE A 83
SHEET 5 AA1 6 ILE A 120 HIS A 130 1 O ASP A 121 N TYR A 52
SHEET 6 AA1 6 ALA A 149 LEU A 153 1 O LEU A 153 N GLY A 129
SHEET 1 AA2 3 THR A 169 ALA A 174 0
SHEET 2 AA2 3 LYS A 199 LEU A 204 1 O LEU A 204 N GLY A 173
SHEET 3 AA2 3 VAL A 253 SER A 258 -1 O GLU A 255 N GLU A 203
SHEET 1 AA3 6 VAL B 25 VAL B 30 0
SHEET 2 AA3 6 GLY B 41 PRO B 46 -1 O GLY B 41 N VAL B 30
SHEET 3 AA3 6 VAL B 81 ILE B 85 -1 O VAL B 82 N TYR B 44
SHEET 4 AA3 6 TYR B 52 SER B 58 1 N ILE B 57 O ILE B 85
SHEET 5 AA3 6 ILE B 120 HIS B 130 1 O ASP B 121 N TYR B 52
SHEET 6 AA3 6 ALA B 149 LEU B 153 1 O LEU B 153 N GLY B 129
SHEET 1 AA4 3 THR B 169 ALA B 174 0
SHEET 2 AA4 3 LYS B 199 LEU B 204 1 O LEU B 204 N GLY B 173
SHEET 3 AA4 3 VAL B 253 SER B 258 -1 O GLU B 255 N GLU B 203
SHEET 1 AA5 6 VAL C 25 VAL C 30 0
SHEET 2 AA5 6 GLY C 41 PRO C 46 -1 O GLY C 41 N VAL C 30
SHEET 3 AA5 6 VAL C 81 ILE C 85 -1 O VAL C 82 N TYR C 44
SHEET 4 AA5 6 TYR C 52 SER C 58 1 N VAL C 55 O ILE C 83
SHEET 5 AA5 6 ILE C 120 HIS C 130 1 O ASP C 121 N TYR C 52
SHEET 6 AA5 6 ALA C 149 LEU C 153 1 O LEU C 153 N GLY C 129
SHEET 1 AA6 3 THR C 169 ALA C 174 0
SHEET 2 AA6 3 LYS C 199 LEU C 204 1 O LEU C 204 N GLY C 173
SHEET 3 AA6 3 VAL C 253 SER C 258 -1 O GLU C 255 N GLU C 203
SHEET 1 AA7 6 VAL D 25 VAL D 30 0
SHEET 2 AA7 6 GLY D 41 PRO D 46 -1 O ILE D 43 N GLU D 28
SHEET 3 AA7 6 VAL D 81 ILE D 85 -1 O VAL D 82 N TYR D 44
SHEET 4 AA7 6 TYR D 52 SER D 58 1 N VAL D 55 O VAL D 81
SHEET 5 AA7 6 ILE D 120 HIS D 130 1 O ASP D 121 N TYR D 52
SHEET 6 AA7 6 ALA D 149 LEU D 153 1 O LEU D 153 N GLY D 129
SHEET 1 AA8 3 THR D 169 ALA D 174 0
SHEET 2 AA8 3 LYS D 199 LEU D 204 1 O LEU D 204 N GLY D 173
SHEET 3 AA8 3 VAL D 253 SER D 258 -1 O GLU D 255 N GLU D 203
SHEET 1 AA9 6 VAL E 25 VAL E 30 0
SHEET 2 AA9 6 GLY E 41 PRO E 46 -1 O ILE E 43 N GLU E 28
SHEET 3 AA9 6 PHE E 80 ILE E 85 -1 O VAL E 82 N TYR E 44
SHEET 4 AA9 6 TYR E 52 SER E 58 1 N VAL E 55 O ILE E 83
SHEET 5 AA9 6 ILE E 120 HIS E 130 1 O ASP E 121 N TYR E 52
SHEET 6 AA9 6 ALA E 149 LEU E 153 1 O LEU E 153 N GLY E 129
SHEET 1 AB1 3 THR E 169 ALA E 174 0
SHEET 2 AB1 3 LYS E 199 LEU E 204 1 O LEU E 204 N GLY E 173
SHEET 3 AB1 3 VAL E 253 SER E 258 -1 O GLU E 255 N GLU E 203
SHEET 1 AB2 6 VAL F 25 VAL F 30 0
SHEET 2 AB2 6 GLY F 41 PRO F 46 -1 O GLY F 41 N VAL F 30
SHEET 3 AB2 6 VAL F 81 ILE F 85 -1 O VAL F 82 N TYR F 44
SHEET 4 AB2 6 TYR F 52 SER F 58 1 N VAL F 55 O ILE F 83
SHEET 5 AB2 6 ILE F 120 HIS F 130 1 O ASP F 121 N TYR F 52
SHEET 6 AB2 6 ALA F 149 LEU F 153 1 O LEU F 153 N GLY F 129
SHEET 1 AB3 3 THR F 169 ALA F 174 0
SHEET 2 AB3 3 LYS F 199 LEU F 204 1 O LEU F 204 N GLY F 173
SHEET 3 AB3 3 VAL F 253 SER F 258 -1 O GLU F 255 N GLU F 203
SSBOND 1 CYS A 242 CYS A 260 1555 1555 2.05
SSBOND 2 CYS B 242 CYS B 260 1555 1555 2.02
SSBOND 3 CYS C 242 CYS C 260 1555 1555 2.07
SSBOND 4 CYS D 242 CYS D 260 1555 1555 2.07
SSBOND 5 CYS E 242 CYS E 260 1555 1555 2.05
SSBOND 6 CYS F 242 CYS F 260 1555 1555 2.08
CISPEP 1 CYS A 242 PRO A 243 0 0.15
CISPEP 2 CYS A 260 PRO A 261 0 -4.80
CISPEP 3 CYS B 242 PRO B 243 0 -2.11
CISPEP 4 CYS B 260 PRO B 261 0 -4.40
CISPEP 5 CYS C 242 PRO C 243 0 -1.15
CISPEP 6 CYS C 260 PRO C 261 0 -5.80
CISPEP 7 CYS D 242 PRO D 243 0 -1.59
CISPEP 8 CYS D 260 PRO D 261 0 -5.71
CISPEP 9 CYS E 242 PRO E 243 0 -1.52
CISPEP 10 CYS E 260 PRO E 261 0 -3.12
CISPEP 11 CYS F 242 PRO F 243 0 -2.86
CISPEP 12 CYS F 260 PRO F 261 0 -5.08
CRYST1 40.346 79.753 120.133 86.28 87.94 89.50 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 0.024786 -0.000215 -0.000880 0.00000
SCALE2 0.000000 0.012539 -0.000813 0.00000
SCALE3 0.000000 0.000000 0.008347 0.00000
TER 1994 LEU A 263
TER 4008 LEU B 263
TER 6001 LEU C 263
TER 8010 PHE D 262
TER 10035 PHE E 262
TER 12012 PHE F 262
MASTER 629 0 6 66 54 0 0 613481 6 54 126
END |