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HEADER HYDROLASE 27-MAY-15 5BOV
TITLE CRYSTAL STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE (KPN_01808) FROM
TITLE 2 KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH 78578 AT 1.60 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE EPOXIDE HYDROLASE PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE (STRAIN
SOURCE 3 ATCC 700721 / MGH 78578);
SOURCE 4 ORGANISM_TAXID: 272620;
SOURCE 5 STRAIN: ATCC 700721 / MGH 78578;
SOURCE 6 GENE: KPN_01808;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS PUTATIVE EPOXIDE HYDROLASE, STRUCTURAL GENOMICS, JOINT CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 3 BIOLOGY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 10-JUN-15 5BOV 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A PUTATIVE EPOXIDE HYDROLASE
JRNL TITL 2 (KPN_01808) FROM KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH
JRNL TITL 3 78578 AT 1.60 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 146328
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.174
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7372
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10164
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 529
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9395
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.78
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.17000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : -0.49000
REMARK 3 B13 (A**2) : -0.51000
REMARK 3 B23 (A**2) : 0.04000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.085
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.449
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9843 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9140 ; 0.013 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13485 ; 1.785 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20967 ; 1.910 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1241 ; 6.056 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 480 ;36.868 ;23.354
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1415 ;10.562 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 75 ;16.128 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1408 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11495 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2454 ; 0.011 ; 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): 4838 ; 0.882 ; 1.043
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4837 ; 0.881 ; 1.043
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6052 ; 1.397 ; 1.561
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 38 A 338
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9308 -7.5371 40.4715
REMARK 3 T TENSOR
REMARK 3 T11: 0.0103 T22: 0.0223
REMARK 3 T33: 0.0087 T12: 0.0057
REMARK 3 T13: 0.0004 T23: -0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.4018 L22: 0.3028
REMARK 3 L33: 0.5315 L12: 0.2096
REMARK 3 L13: 0.2425 L23: -0.0327
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.0470 S13: -0.0443
REMARK 3 S21: 0.0110 S22: 0.0350 S23: -0.0197
REMARK 3 S31: -0.0267 S32: 0.0460 S33: -0.0305
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 37 B 338
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9272 -35.6327 -0.7875
REMARK 3 T TENSOR
REMARK 3 T11: 0.0147 T22: 0.0078
REMARK 3 T33: 0.0069 T12: 0.0042
REMARK 3 T13: -0.0091 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 0.2983 L22: 0.3135
REMARK 3 L33: 0.4148 L12: 0.0982
REMARK 3 L13: 0.0750 L23: -0.0871
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: -0.0004 S13: 0.0138
REMARK 3 S21: 0.0052 S22: 0.0344 S23: -0.0134
REMARK 3 S31: -0.0107 S32: -0.0016 S33: 0.0028
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 41 C 338
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2354 5.4567 1.8599
REMARK 3 T TENSOR
REMARK 3 T11: 0.0094 T22: 0.0093
REMARK 3 T33: 0.0081 T12: -0.0008
REMARK 3 T13: 0.0029 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.2391 L22: 0.4925
REMARK 3 L33: 0.7209 L12: -0.0369
REMARK 3 L13: 0.2353 L23: -0.4051
REMARK 3 S TENSOR
REMARK 3 S11: 0.0314 S12: -0.0091 S13: 0.0145
REMARK 3 S21: -0.0004 S22: 0.0081 S23: 0.0525
REMARK 3 S31: 0.0377 S32: -0.0043 S33: -0.0395
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 41 D 338
REMARK 3 ORIGIN FOR THE GROUP (A): 34.9545 -47.0996 43.2845
REMARK 3 T TENSOR
REMARK 3 T11: 0.0167 T22: 0.0263
REMARK 3 T33: 0.0311 T12: -0.0082
REMARK 3 T13: -0.0161 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 0.4593 L22: 1.2296
REMARK 3 L33: 1.0845 L12: 0.4477
REMARK 3 L13: 0.3771 L23: -0.3009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: -0.0584 S13: 0.0952
REMARK 3 S21: -0.0880 S22: 0.0288 S23: 0.1628
REMARK 3 S31: 0.0976 S32: -0.1211 S33: -0.0153
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: 1. A MET-INHIBITION PROTOCOL WAS USED
REMARK 3 FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION.
REMARK 3 THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 2. THE MAD PHASES WERE USED AS RESTRAINTS DURING
REMARK 3 REFINEMENT. 3. HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. 4. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS.
REMARK 4
REMARK 4 5BOV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210294.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-15
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 : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97907
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : VERTICAL FOCUSING MIRROR; DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, XSCALE NOVEMBER 3, 2014
REMARK 200 BUILT=20141118
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146333
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 42.848
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.916
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.6600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.65500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, SHARP, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BICINE PH 9, 30% POLYETHYLENE
REMARK 280 GLYCOL 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -44.19900
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -18.05761
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 22.47589
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -83.05400
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 GLY A 0
REMARK 465 ALA A 36
REMARK 465 GLU A 37
REMARK 465 GLY B 0
REMARK 465 ALA B 36
REMARK 465 GLY C 0
REMARK 465 ALA C 36
REMARK 465 GLU C 37
REMARK 465 ASP C 38
REMARK 465 ALA C 39
REMARK 465 GLY C 40
REMARK 465 GLY D 0
REMARK 465 ALA D 36
REMARK 465 GLU D 37
REMARK 465 ASP D 38
REMARK 465 ALA D 39
REMARK 465 GLY D 40
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU B 37 CG CD OE1 OE2
REMARK 470 ARG B 136 CD NE CZ NH1 NH2
REMARK 470 LYS C 44 CD CE NZ
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 LEU A 312 O HOH A 401 2.04
REMARK 500 OE2 GLU A 258 O HOH A 402 2.15
REMARK 500 NH1 ARG C 160 O HOH C 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 A 694 O HOH A 776 1655 2.19
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 310 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 310 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 160 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 236 CG - CD - NE ANGL. DEV. = -13.6 DEGREES
REMARK 500 ARG B 254 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG C 49 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 49 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP C 151 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 160 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG C 160 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG C 254 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG C 310 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG D 310 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG D 337 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG D 337 NE - CZ - NH2 ANGL. DEV. = -4.0 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 ASP A 144 -128.94 54.21
REMARK 500 GLN A 225 59.95 -90.51
REMARK 500 PRO B 75 74.07 -100.07
REMARK 500 ASP B 144 -128.47 54.11
REMARK 500 GLN B 225 59.39 -90.42
REMARK 500 PRO C 75 75.14 -101.67
REMARK 500 ASP C 144 -130.50 56.18
REMARK 500 ASP D 144 -126.76 55.38
REMARK 500 ASN D 240 131.49 -39.64
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 911 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH A 912 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH A 913 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH B 915 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B 916 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH B 917 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 918 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B 919 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B 920 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH C 854 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH C 855 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH C 856 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH C 857 DISTANCE = 6.74 ANGSTROMS
REMARK 525 HOH D 789 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH D 790 DISTANCE = 6.73 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-420280 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT (36-338) WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 5BOV A 36 338 UNP A6T9G8 A6T9G8_KLEP7 36 338
DBREF 5BOV B 36 338 UNP A6T9G8 A6T9G8_KLEP7 36 338
DBREF 5BOV C 36 338 UNP A6T9G8 A6T9G8_KLEP7 36 338
DBREF 5BOV D 36 338 UNP A6T9G8 A6T9G8_KLEP7 36 338
SEQADV 5BOV GLY A 0 UNP A6T9G8 LEADER SEQUENCE
SEQADV 5BOV GLY B 0 UNP A6T9G8 LEADER SEQUENCE
SEQADV 5BOV GLY C 0 UNP A6T9G8 LEADER SEQUENCE
SEQADV 5BOV GLY D 0 UNP A6T9G8 LEADER SEQUENCE
SEQRES 1 A 304 GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN
SEQRES 2 A 304 ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE
SEQRES 3 A 304 GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY
SEQRES 4 A 304 TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO
SEQRES 5 A 304 ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR
SEQRES 6 A 304 LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER
SEQRES 7 A 304 THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP
SEQRES 8 A 304 ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA
SEQRES 9 A 304 ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP
SEQRES 10 A 304 ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU
SEQRES 11 A 304 VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE
SEQRES 12 A 304 GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP
SEQRES 13 A 304 TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA
SEQRES 14 A 304 GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE
SEQRES 15 A 304 TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA
SEQRES 16 A 304 THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP
SEQRES 17 A 304 HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU
SEQRES 18 A 304 GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU
SEQRES 19 A 304 GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR
SEQRES 20 A 304 ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO
SEQRES 21 A 304 ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR
SEQRES 22 A 304 GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO
SEQRES 23 A 304 PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL
SEQRES 24 A 304 ASP ALA ASP ARG LEU
SEQRES 1 B 304 GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN
SEQRES 2 B 304 ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE
SEQRES 3 B 304 GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY
SEQRES 4 B 304 TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO
SEQRES 5 B 304 ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR
SEQRES 6 B 304 LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER
SEQRES 7 B 304 THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP
SEQRES 8 B 304 ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA
SEQRES 9 B 304 ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP
SEQRES 10 B 304 ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU
SEQRES 11 B 304 VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE
SEQRES 12 B 304 GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP
SEQRES 13 B 304 TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA
SEQRES 14 B 304 GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE
SEQRES 15 B 304 TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA
SEQRES 16 B 304 THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP
SEQRES 17 B 304 HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU
SEQRES 18 B 304 GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU
SEQRES 19 B 304 GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR
SEQRES 20 B 304 ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO
SEQRES 21 B 304 ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR
SEQRES 22 B 304 GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO
SEQRES 23 B 304 PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL
SEQRES 24 B 304 ASP ALA ASP ARG LEU
SEQRES 1 C 304 GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN
SEQRES 2 C 304 ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE
SEQRES 3 C 304 GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY
SEQRES 4 C 304 TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO
SEQRES 5 C 304 ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR
SEQRES 6 C 304 LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER
SEQRES 7 C 304 THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP
SEQRES 8 C 304 ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA
SEQRES 9 C 304 ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP
SEQRES 10 C 304 ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU
SEQRES 11 C 304 VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE
SEQRES 12 C 304 GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP
SEQRES 13 C 304 TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA
SEQRES 14 C 304 GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE
SEQRES 15 C 304 TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA
SEQRES 16 C 304 THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP
SEQRES 17 C 304 HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU
SEQRES 18 C 304 GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU
SEQRES 19 C 304 GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR
SEQRES 20 C 304 ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO
SEQRES 21 C 304 ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR
SEQRES 22 C 304 GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO
SEQRES 23 C 304 PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL
SEQRES 24 C 304 ASP ALA ASP ARG LEU
SEQRES 1 D 304 GLY ALA GLU ASP ALA GLY ALA PHE ASP LYS ILE GLN GLN
SEQRES 2 D 304 ILE ARG ALA GLY ASP LEU ASN ILE GLY TYR VAL ASP ILE
SEQRES 3 D 304 GLY PRO ARG ASP GLY GLN PRO VAL ILE LEU LEU HIS GLY
SEQRES 4 D 304 TRP PRO TYR ASP ILE GLN SER TYR ALA GLN VAL ALA PRO
SEQRES 5 D 304 ALA LEU ALA GLN LYS GLY TYR ARG VAL ILE VAL PRO TYR
SEQRES 6 D 304 LEU ARG GLY TYR GLY THR THR ARG PHE LEU SER ALA SER
SEQRES 7 D 304 THR PRO ARG ASN GLY GLN PRO SER ALA MSE ALA ALA ASP
SEQRES 8 D 304 ILE VAL HIS LEU MSE ASP ALA LEU ASN ILE ARG GLN ALA
SEQRES 9 D 304 ASP LEU ALA GLY PHE ASP TRP GLY ALA ARG THR ALA ASP
SEQRES 10 D 304 ILE VAL ALA ALA LEU TRP PRO GLN ARG VAL LYS SER LEU
SEQRES 11 D 304 VAL SER VAL SER GLY TYR LEU ILE SER SER GLN GLN ILE
SEQRES 12 D 304 GLY GLU LYS PRO LEU PRO PRO GLN ALA GLU LEU SER TRP
SEQRES 13 D 304 TRP TYR GLN PHE TYR PHE ALA THR PRO ARG GLY GLU ALA
SEQRES 14 D 304 GLY TYR ARG GLN ASN THR HIS ASP PHE ALA LYS PHE ILE
SEQRES 15 D 304 TRP HIS GLN ALA SER PRO GLN TRP GLN PHE SER ASP ALA
SEQRES 16 D 304 THR PHE ALA LYS THR ALA ARG ALA LEU ASP ASN PRO ASP
SEQRES 17 D 304 HIS VAL ALA ILE THR ILE SER ASN TYR ARG TRP ARG LEU
SEQRES 18 D 304 GLY LEU GLU LYS GLY GLU ALA LYS TYR ALA GLY TYR GLU
SEQRES 19 D 304 GLN ARG LEU ALA ALA LEU PRO PRO ILE THR VAL PRO THR
SEQRES 20 D 304 ILE THR LEU GLU GLY ALA ASN ASN GLY ALA PRO HIS PRO
SEQRES 21 D 304 ALA PRO ALA SER TYR ARG ALA LYS PHE THR GLY LYS TYR
SEQRES 22 D 304 GLU HIS ARG ASP LEU PRO GLY ALA VAL GLY HIS ASN PRO
SEQRES 23 D 304 PRO GLN GLU ASP PRO THR ALA PHE VAL GLN ALA VAL VAL
SEQRES 24 D 304 ASP ALA ASP ARG LEU
MODRES 5BOV MSE A 122 MET MODIFIED RESIDUE
MODRES 5BOV MSE A 130 MET MODIFIED RESIDUE
MODRES 5BOV MSE B 122 MET MODIFIED RESIDUE
MODRES 5BOV MSE B 130 MET MODIFIED RESIDUE
MODRES 5BOV MSE C 122 MET MODIFIED RESIDUE
MODRES 5BOV MSE C 130 MET MODIFIED RESIDUE
MODRES 5BOV MSE D 122 MET MODIFIED RESIDUE
MODRES 5BOV MSE D 130 MET MODIFIED RESIDUE
HET MSE A 122 8
HET MSE A 130 8
HET MSE B 122 8
HET MSE B 130 8
HET MSE C 122 8
HET MSE C 130 8
HET MSE D 122 8
HET MSE D 130 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 5 HOH *1880(H2 O)
HELIX 1 AA1 GLY A 40 LYS A 44 5 5
HELIX 2 AA2 ASP A 77 ALA A 82 5 6
HELIX 3 AA3 GLN A 83 LYS A 91 1 9
HELIX 4 AA4 GLN A 118 LEU A 133 1 16
HELIX 5 AA5 ASP A 144 TRP A 157 1 14
HELIX 6 AA6 SER A 174 GLU A 179 1 6
HELIX 7 AA7 PRO A 183 TRP A 190 1 8
HELIX 8 AA8 TRP A 190 ALA A 197 1 8
HELIX 9 AA9 THR A 198 ASN A 208 1 11
HELIX 10 AB1 ASN A 208 SER A 221 1 14
HELIX 11 AB2 SER A 227 ARG A 236 1 10
HELIX 12 AB3 ALA A 237 ASN A 240 5 4
HELIX 13 AB4 ASP A 242 LEU A 255 1 14
HELIX 14 AB5 GLU A 261 LYS A 263 5 3
HELIX 15 AB6 TYR A 264 ALA A 273 1 10
HELIX 16 AB7 ALA A 295 ARG A 300 1 6
HELIX 17 AB8 ALA A 301 PHE A 303 5 3
HELIX 18 AB9 ASN A 319 ASP A 324 1 6
HELIX 19 AC1 ASP A 324 LEU A 338 1 15
HELIX 20 AC2 GLY B 40 LYS B 44 5 5
HELIX 21 AC3 ASP B 77 ALA B 82 5 6
HELIX 22 AC4 GLN B 83 LYS B 91 1 9
HELIX 23 AC5 GLN B 118 LEU B 133 1 16
HELIX 24 AC6 ASP B 144 TRP B 157 1 14
HELIX 25 AC7 SER B 174 GLU B 179 1 6
HELIX 26 AC8 PRO B 183 TRP B 190 1 8
HELIX 27 AC9 TRP B 190 ALA B 197 1 8
HELIX 28 AD1 THR B 198 ASN B 208 1 11
HELIX 29 AD2 ASN B 208 SER B 221 1 14
HELIX 30 AD3 SER B 227 LEU B 238 1 12
HELIX 31 AD4 ASP B 242 LEU B 255 1 14
HELIX 32 AD5 GLU B 261 LYS B 263 5 3
HELIX 33 AD6 TYR B 264 ALA B 273 1 10
HELIX 34 AD7 ALA B 295 ARG B 300 1 6
HELIX 35 AD8 ALA B 301 PHE B 303 5 3
HELIX 36 AD9 ASN B 319 ASP B 324 1 6
HELIX 37 AE1 ASP B 324 LEU B 338 1 15
HELIX 38 AE2 ASP C 77 ALA C 82 5 6
HELIX 39 AE3 GLN C 83 LYS C 91 1 9
HELIX 40 AE4 GLN C 118 LEU C 133 1 16
HELIX 41 AE5 ASP C 144 TRP C 157 1 14
HELIX 42 AE6 SER C 174 GLU C 179 1 6
HELIX 43 AE7 PRO C 183 TRP C 190 1 8
HELIX 44 AE8 TRP C 190 ALA C 197 1 8
HELIX 45 AE9 THR C 198 ASN C 208 1 11
HELIX 46 AF1 ASN C 208 SER C 221 1 14
HELIX 47 AF2 SER C 227 ASP C 239 1 13
HELIX 48 AF3 ASP C 242 LEU C 255 1 14
HELIX 49 AF4 GLU C 261 LYS C 263 5 3
HELIX 50 AF5 TYR C 264 ALA C 273 1 10
HELIX 51 AF6 ALA C 295 ARG C 300 1 6
HELIX 52 AF7 ALA C 301 PHE C 303 5 3
HELIX 53 AF8 ASN C 319 ASP C 324 1 6
HELIX 54 AF9 ASP C 324 LEU C 338 1 15
HELIX 55 AG1 ASP D 77 ALA D 82 5 6
HELIX 56 AG2 GLN D 83 LYS D 91 1 9
HELIX 57 AG3 GLN D 118 LEU D 133 1 16
HELIX 58 AG4 ASP D 144 TRP D 157 1 14
HELIX 59 AG5 SER D 174 GLU D 179 1 6
HELIX 60 AG6 PRO D 183 TRP D 190 1 8
HELIX 61 AG7 TRP D 190 ALA D 197 1 8
HELIX 62 AG8 THR D 198 ASN D 208 1 11
HELIX 63 AG9 ASN D 208 SER D 221 1 14
HELIX 64 AH1 SER D 227 ASP D 239 1 13
HELIX 65 AH2 ASP D 242 LEU D 255 1 14
HELIX 66 AH3 GLU D 261 LYS D 263 5 3
HELIX 67 AH4 TYR D 264 ALA D 273 1 10
HELIX 68 AH5 ALA D 295 PHE D 303 5 9
HELIX 69 AH6 ASN D 319 ASP D 324 1 6
HELIX 70 AH7 ASP D 324 LEU D 338 1 15
SHEET 1 AA1 3 GLN A 46 ALA A 50 0
SHEET 2 AA1 3 LEU A 53 ILE A 60 -1 O TYR A 57 N GLN A 46
SHEET 3 AA1 3 ARG A 107 PHE A 108 -1 O ARG A 107 N ASN A 54
SHEET 1 AA2 8 GLN A 46 ALA A 50 0
SHEET 2 AA2 8 LEU A 53 ILE A 60 -1 O TYR A 57 N GLN A 46
SHEET 3 AA2 8 TYR A 93 PRO A 98 -1 O VAL A 95 N ILE A 60
SHEET 4 AA2 8 GLN A 66 LEU A 71 1 N VAL A 68 O ILE A 96
SHEET 5 AA2 8 ALA A 138 GLY A 142 1 O ALA A 141 N LEU A 71
SHEET 6 AA2 8 VAL A 161 VAL A 167 1 O SER A 163 N LEU A 140
SHEET 7 AA2 8 THR A 281 GLY A 286 1 O ILE A 282 N LEU A 164
SHEET 8 AA2 8 TYR A 307 LEU A 312 1 O LEU A 312 N GLU A 285
SHEET 1 AA3 3 GLN B 46 ALA B 50 0
SHEET 2 AA3 3 LEU B 53 ILE B 60 -1 O TYR B 57 N GLN B 46
SHEET 3 AA3 3 ARG B 107 PHE B 108 -1 O ARG B 107 N ASN B 54
SHEET 1 AA4 8 GLN B 46 ALA B 50 0
SHEET 2 AA4 8 LEU B 53 ILE B 60 -1 O TYR B 57 N GLN B 46
SHEET 3 AA4 8 ARG B 94 PRO B 98 -1 O VAL B 95 N ILE B 60
SHEET 4 AA4 8 PRO B 67 LEU B 71 1 N VAL B 68 O ILE B 96
SHEET 5 AA4 8 ALA B 138 GLY B 142 1 O ALA B 141 N LEU B 71
SHEET 6 AA4 8 VAL B 161 VAL B 167 1 O SER B 163 N LEU B 140
SHEET 7 AA4 8 THR B 281 GLY B 286 1 O ILE B 282 N LEU B 164
SHEET 8 AA4 8 TYR B 307 LEU B 312 1 O LEU B 312 N GLU B 285
SHEET 1 AA5 3 GLN C 46 ALA C 50 0
SHEET 2 AA5 3 LEU C 53 ILE C 60 -1 O TYR C 57 N GLN C 46
SHEET 3 AA5 3 ARG C 107 PHE C 108 -1 O ARG C 107 N ASN C 54
SHEET 1 AA6 8 GLN C 46 ALA C 50 0
SHEET 2 AA6 8 LEU C 53 ILE C 60 -1 O TYR C 57 N GLN C 46
SHEET 3 AA6 8 ARG C 94 PRO C 98 -1 O VAL C 95 N ILE C 60
SHEET 4 AA6 8 PRO C 67 LEU C 71 1 N VAL C 68 O ILE C 96
SHEET 5 AA6 8 ALA C 138 GLY C 142 1 O ALA C 141 N LEU C 71
SHEET 6 AA6 8 VAL C 161 VAL C 167 1 O SER C 163 N LEU C 140
SHEET 7 AA6 8 THR C 281 GLY C 286 1 O ILE C 282 N LEU C 164
SHEET 8 AA6 8 TYR C 307 LEU C 312 1 O LEU C 312 N GLU C 285
SHEET 1 AA7 3 GLN D 46 ALA D 50 0
SHEET 2 AA7 3 LEU D 53 ILE D 60 -1 O TYR D 57 N GLN D 46
SHEET 3 AA7 3 ARG D 107 PHE D 108 -1 O ARG D 107 N ASN D 54
SHEET 1 AA8 8 GLN D 46 ALA D 50 0
SHEET 2 AA8 8 LEU D 53 ILE D 60 -1 O TYR D 57 N GLN D 46
SHEET 3 AA8 8 ARG D 94 PRO D 98 -1 O VAL D 95 N ILE D 60
SHEET 4 AA8 8 PRO D 67 LEU D 71 1 N VAL D 68 O ILE D 96
SHEET 5 AA8 8 ALA D 138 GLY D 142 1 O ALA D 141 N LEU D 71
SHEET 6 AA8 8 VAL D 161 VAL D 167 1 O SER D 163 N LEU D 140
SHEET 7 AA8 8 THR D 281 GLY D 286 1 O ILE D 282 N LEU D 164
SHEET 8 AA8 8 TYR D 307 LEU D 312 1 O LEU D 312 N GLU D 285
LINK C ALA A 121 N MSE A 122 1555 1555 1.33
LINK C MSE A 122 N ALA A 123 1555 1555 1.34
LINK C LEU A 129 N MSE A 130 1555 1555 1.33
LINK C MSE A 130 N ASP A 131 1555 1555 1.33
LINK C ALA B 121 N MSE B 122 1555 1555 1.35
LINK C MSE B 122 N ALA B 123 1555 1555 1.34
LINK C LEU B 129 N MSE B 130 1555 1555 1.32
LINK C MSE B 130 N ASP B 131 1555 1555 1.33
LINK C ALA C 121 N MSE C 122 1555 1555 1.34
LINK C MSE C 122 N ALA C 123 1555 1555 1.34
LINK C LEU C 129 N MSE C 130 1555 1555 1.33
LINK C MSE C 130 N ASP C 131 1555 1555 1.33
LINK C ALA D 121 N MSE D 122 1555 1555 1.35
LINK C MSE D 122 N ALA D 123 1555 1555 1.32
LINK C LEU D 129 N MSE D 130 1555 1555 1.33
LINK C MSE D 130 N ASP D 131 1555 1555 1.32
CISPEP 1 TRP A 74 PRO A 75 0 -9.30
CISPEP 2 TRP B 74 PRO B 75 0 -9.93
CISPEP 3 TRP C 74 PRO C 75 0 -4.45
CISPEP 4 TRP D 74 PRO D 75 0 -10.83
CRYST1 44.199 81.866 89.925 101.00 106.90 100.84 P 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 0.022625 0.004332 0.008295 0.00000
SCALE2 0.000000 0.012437 0.003365 0.00000
SCALE3 0.000000 0.000000 0.012040 0.00000
TER 2408 LEU A 338
TER 4805 LEU B 338
TER 7155 LEU C 338
TER 9531 LEU D 338
MASTER 511 0 8 70 44 0 0 611275 4 80 96
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