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HEADER HYDROLASE 11-JUN-14 4QLA
TITLE CRYSTAL STRUCTURE OF JUVENILE HORMONE EPOXIDE HYDROLASE FROM THE
TITLE 2 SILKWORM BOMBYX MORI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: JUVENILE HORMONE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 23-461;
COMPND 5 SYNONYM: BOMMO-JHEH;
COMPND 6 EC: 3.3.2.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOMBYX MORI;
SOURCE 3 ORGANISM_COMMON: SILK MOTH, SILKWORM;
SOURCE 4 ORGANISM_TAXID: 7091;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET29A
KEYWDS ALPHA/BETA HYDROLASE, EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.ZHOU,N.JIA,C.HU,Y.L.JIANG,J.P.YANG,Y.CHEN,S.LI,C.Z.ZHOU
REVDAT 1 03-SEP-14 4QLA 0
JRNL AUTH K.ZHOU,N.JIA,C.HU,Y.L.JIANG,J.P.YANG,Y.CHEN,S.LI,W.F.LI,
JRNL AUTH 2 C.Z.ZHOU
JRNL TITL CRYSTAL STRUCTURE OF JUVENILE HORMONE EPOXIDE HYDROLASE FROM
JRNL TITL 2 THE SILKWORM BOMBYX MORI
JRNL REF PROTEINS 2014
JRNL REFN ESSN 1097-0134
JRNL PMID 25143157
JRNL DOI 10.1002/PROT.24676
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 36297
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1907
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2406
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE SET COUNT : 131
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6491
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.76000
REMARK 3 B22 (A**2) : -2.64000
REMARK 3 B33 (A**2) : 5.24000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 4.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.400
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.253
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.193
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.974
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6712 ; 0.006 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9087 ; 1.067 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 800 ; 5.439 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 288 ;37.805 ;23.785
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1153 ;16.767 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;12.561 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 970 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5036 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4QLA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-JUN-14.
REMARK 100 THE RCSB ID CODE IS RCSB086197.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38204
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : 0.10800
REMARK 200 FOR THE DATA SET : 11.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : 0.50000
REMARK 200 FOR SHELL : 2.880
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: 1QO7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, PH 8.0, 19%
REMARK 280 POLYETHYLENE GLYCOL 2000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 80.70200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.73300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 80.70200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.73300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 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 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 GLY A 22
REMARK 465 VAL A 23
REMARK 465 LEU A 24
REMARK 465 LYS A 25
REMARK 465 SER A 26
REMARK 465 PRO A 27
REMARK 465 PRO A 28
REMARK 465 PRO A 29
REMARK 465 MET A 30
REMARK 465 PRO A 31
REMARK 465 LYS A 32
REMARK 465 VAL A 457
REMARK 465 LYS A 458
REMARK 465 THR A 459
REMARK 465 GLU A 460
REMARK 465 LEU A 461
REMARK 465 MET B 15
REMARK 465 HIS B 16
REMARK 465 HIS B 17
REMARK 465 HIS B 18
REMARK 465 HIS B 19
REMARK 465 HIS B 20
REMARK 465 HIS B 21
REMARK 465 GLY B 22
REMARK 465 VAL B 23
REMARK 465 LEU B 24
REMARK 465 LYS B 25
REMARK 465 SER B 26
REMARK 465 PRO B 27
REMARK 465 PRO B 28
REMARK 465 PRO B 29
REMARK 465 MET B 30
REMARK 465 PRO B 31
REMARK 465 LYS B 32
REMARK 465 LEU B 253
REMARK 465 THR B 254
REMARK 465 LEU B 255
REMARK 465 SER B 256
REMARK 465 PRO B 257
REMARK 465 ALA B 258
REMARK 465 ALA B 259
REMARK 465 THR B 260
REMARK 465 PHE B 261
REMARK 465 LEU B 262
REMARK 465 GLU B 263
REMARK 465 PHE B 264
REMARK 465 VAL B 265
REMARK 465 GLY B 266
REMARK 465 ALA B 267
REMARK 465 LEU B 268
REMARK 465 PHE B 269
REMARK 465 PRO B 270
REMARK 465 SER B 271
REMARK 465 LEU B 272
REMARK 465 ILE B 273
REMARK 465 VAL B 274
REMARK 465 GLU B 275
REMARK 465 PRO B 276
REMARK 465 GLU B 277
REMARK 465 LEU B 278
REMARK 465 ALA B 279
REMARK 465 ASN B 280
REMARK 465 ARG B 281
REMARK 465 LEU B 282
REMARK 465 TYR B 283
REMARK 465 PRO B 284
REMARK 465 LEU B 285
REMARK 465 SER B 286
REMARK 465 GLU B 287
REMARK 465 LYS B 288
REMARK 465 TYR B 289
REMARK 465 SER B 290
REMARK 465 ASP B 383
REMARK 465 LEU B 384
REMARK 465 LYS B 385
REMARK 465 LEU B 386
REMARK 465 ASP B 387
REMARK 465 GLU B 388
REMARK 465 VAL B 457
REMARK 465 LYS B 458
REMARK 465 THR B 459
REMARK 465 GLU B 460
REMARK 465 LEU B 461
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 LYS A 73 38.25 -89.21
REMARK 500 PRO A 155 46.90 -96.99
REMARK 500 SER A 157 -173.84 -172.64
REMARK 500 GLU A 160 -39.32 -39.56
REMARK 500 LYS A 173 -17.21 93.04
REMARK 500 ASP A 227 -121.62 51.64
REMARK 500 MET A 251 53.88 -145.79
REMARK 500 LEU A 255 48.84 -107.45
REMARK 500 SER A 271 2.32 -64.29
REMARK 500 GLU B 37 129.46 -36.83
REMARK 500 LYS B 47 32.48 -89.68
REMARK 500 PRO B 155 49.70 -98.17
REMARK 500 SER B 157 -177.92 -175.92
REMARK 500 ASP B 227 -134.65 58.73
REMARK 500 SER B 329 -71.72 -73.79
REMARK 500 ASN B 333 109.27 -166.69
REMARK 500 ARG B 347 -41.36 -130.53
REMARK 500 PHE B 377 36.00 -96.74
REMARK 500 GLN B 392 32.32 -99.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 501
DBREF 4QLA A 23 461 UNP H9JWL6 H9JWL6_BOMMO 23 461
DBREF 4QLA B 23 461 UNP H9JWL6 H9JWL6_BOMMO 23 461
SEQADV 4QLA MET A 15 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS A 16 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS A 17 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS A 18 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS A 19 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS A 20 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS A 21 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA GLY A 22 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA GLY A 142 UNP H9JWL6 ASP 142 ENGINEERED MUTATION
SEQADV 4QLA LEU A 336 UNP H9JWL6 PHE 336 ENGINEERED MUTATION
SEQADV 4QLA HIS A 402 UNP H9JWL6 TYR 402 ENGINEERED MUTATION
SEQADV 4QLA MET A 414 UNP H9JWL6 LEU 414 ENGINEERED MUTATION
SEQADV 4QLA ALA A 433 UNP H9JWL6 SER 433 ENGINEERED MUTATION
SEQADV 4QLA MET B 15 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS B 16 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS B 17 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS B 18 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS B 19 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS B 20 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA HIS B 21 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA GLY B 22 UNP H9JWL6 EXPRESSION TAG
SEQADV 4QLA GLY B 142 UNP H9JWL6 ASP 142 ENGINEERED MUTATION
SEQADV 4QLA LEU B 336 UNP H9JWL6 PHE 336 ENGINEERED MUTATION
SEQADV 4QLA HIS B 402 UNP H9JWL6 TYR 402 ENGINEERED MUTATION
SEQADV 4QLA MET B 414 UNP H9JWL6 LEU 414 ENGINEERED MUTATION
SEQADV 4QLA ALA B 433 UNP H9JWL6 SER 433 ENGINEERED MUTATION
SEQRES 1 A 447 MET HIS HIS HIS HIS HIS HIS GLY VAL LEU LYS SER PRO
SEQRES 2 A 447 PRO PRO MET PRO LYS LEU ASP LEU GLU GLU TRP TRP GLY
SEQRES 3 A 447 PRO PRO GLU LEU LYS GLN LYS GLN ASP THR SER ILE LYS
SEQRES 4 A 447 PRO PHE GLU ILE THR PHE SER GLU THR MET VAL LYS GLU
SEQRES 5 A 447 LEU LYS GLU ARG ILE LYS LYS ARG ARG PRO PHE ALA PRO
SEQRES 6 A 447 PRO LEU GLU GLY VAL GLY PHE LYS TYR GLY PHE ASN SER
SEQRES 7 A 447 LYS GLN LEU ASP SER TRP LEU LYS TYR TRP ALA GLU GLU
SEQRES 8 A 447 TYR PRO PHE ALA GLU ARG GLN LYS PHE LEU ASN GLN TYR
SEQRES 9 A 447 PRO HIS PHE LYS THR ASN ILE GLN GLY LEU ASN ILE HIS
SEQRES 10 A 447 PHE MET ARG ILE THR PRO LYS VAL PRO LYS GLY VAL GLU
SEQRES 11 A 447 ILE VAL PRO LEU LEU LEU LEU HIS GLY TRP PRO GLY SER
SEQRES 12 A 447 VAL ARG GLU PHE TYR GLU ALA ILE PRO HIS LEU THR ALA
SEQRES 13 A 447 VAL SER LYS ASP ARG ASN PHE ALA LEU GLU ILE ILE ALA
SEQRES 14 A 447 PRO SER LEU PRO GLY TYR GLY PHE SER ASP ALA ALA VAL
SEQRES 15 A 447 ARG PRO GLY LEU ALA ALA ALA GLU VAL ALA VAL ILE PHE
SEQRES 16 A 447 LYS ASN LEU MET ALA ARG LEU GLY TYR LYS GLN TYR TYR
SEQRES 17 A 447 VAL GLN GLY GLY ASP TRP GLY ALA LEU ILE GLY SER ALA
SEQRES 18 A 447 MET ALA THR PHE PHE PRO LYS GLU ILE ILE GLY PHE HIS
SEQRES 19 A 447 SER ASN MET ALA LEU THR LEU SER PRO ALA ALA THR PHE
SEQRES 20 A 447 LEU GLU PHE VAL GLY ALA LEU PHE PRO SER LEU ILE VAL
SEQRES 21 A 447 GLU PRO GLU LEU ALA ASN ARG LEU TYR PRO LEU SER GLU
SEQRES 22 A 447 LYS TYR SER THR LEU LEU GLU GLU LEU GLY TYR MET HIS
SEQRES 23 A 447 ILE GLN ALA THR LYS PRO ASP THR VAL GLY ILE GLY LEU
SEQRES 24 A 447 THR ASP SER PRO ALA GLY LEU LEU ALA TYR ILE LEU GLU
SEQRES 25 A 447 LYS PHE SER THR TRP THR ASN PRO ASP LEU ARG SER LYS
SEQRES 26 A 447 GLU ASP GLY GLY LEU SER TYR ARG TRP THR LYS ASP GLN
SEQRES 27 A 447 LEU ILE ASP ASN LEU MET LEU TYR TRP SER THR LYS SER
SEQRES 28 A 447 ILE VAL THR SER MET ARG LEU TYR ALA GLU SER PHE SER
SEQRES 29 A 447 SER ARG HIS PHE ASP LEU LYS LEU ASP GLU ILE GLN VAL
SEQRES 30 A 447 GLN VAL PRO THR TRP VAL LEU GLN ALA LYS HIS GLU LEU
SEQRES 31 A 447 ALA TYR GLN PRO PRO CYS ILE LEU LYS MET LYS TYR PRO
SEQRES 32 A 447 LYS LEU VAL ASN ALA SER VAL ILE GLU ASP GLY GLY HIS
SEQRES 33 A 447 PHE LEU ALA PHE GLU LEU PRO GLU ILE PHE ALA LYS ASP
SEQRES 34 A 447 VAL LEU LYS ALA ILE GLY GLU PHE ARG LYS LEU LYS ASN
SEQRES 35 A 447 VAL LYS THR GLU LEU
SEQRES 1 B 447 MET HIS HIS HIS HIS HIS HIS GLY VAL LEU LYS SER PRO
SEQRES 2 B 447 PRO PRO MET PRO LYS LEU ASP LEU GLU GLU TRP TRP GLY
SEQRES 3 B 447 PRO PRO GLU LEU LYS GLN LYS GLN ASP THR SER ILE LYS
SEQRES 4 B 447 PRO PHE GLU ILE THR PHE SER GLU THR MET VAL LYS GLU
SEQRES 5 B 447 LEU LYS GLU ARG ILE LYS LYS ARG ARG PRO PHE ALA PRO
SEQRES 6 B 447 PRO LEU GLU GLY VAL GLY PHE LYS TYR GLY PHE ASN SER
SEQRES 7 B 447 LYS GLN LEU ASP SER TRP LEU LYS TYR TRP ALA GLU GLU
SEQRES 8 B 447 TYR PRO PHE ALA GLU ARG GLN LYS PHE LEU ASN GLN TYR
SEQRES 9 B 447 PRO HIS PHE LYS THR ASN ILE GLN GLY LEU ASN ILE HIS
SEQRES 10 B 447 PHE MET ARG ILE THR PRO LYS VAL PRO LYS GLY VAL GLU
SEQRES 11 B 447 ILE VAL PRO LEU LEU LEU LEU HIS GLY TRP PRO GLY SER
SEQRES 12 B 447 VAL ARG GLU PHE TYR GLU ALA ILE PRO HIS LEU THR ALA
SEQRES 13 B 447 VAL SER LYS ASP ARG ASN PHE ALA LEU GLU ILE ILE ALA
SEQRES 14 B 447 PRO SER LEU PRO GLY TYR GLY PHE SER ASP ALA ALA VAL
SEQRES 15 B 447 ARG PRO GLY LEU ALA ALA ALA GLU VAL ALA VAL ILE PHE
SEQRES 16 B 447 LYS ASN LEU MET ALA ARG LEU GLY TYR LYS GLN TYR TYR
SEQRES 17 B 447 VAL GLN GLY GLY ASP TRP GLY ALA LEU ILE GLY SER ALA
SEQRES 18 B 447 MET ALA THR PHE PHE PRO LYS GLU ILE ILE GLY PHE HIS
SEQRES 19 B 447 SER ASN MET ALA LEU THR LEU SER PRO ALA ALA THR PHE
SEQRES 20 B 447 LEU GLU PHE VAL GLY ALA LEU PHE PRO SER LEU ILE VAL
SEQRES 21 B 447 GLU PRO GLU LEU ALA ASN ARG LEU TYR PRO LEU SER GLU
SEQRES 22 B 447 LYS TYR SER THR LEU LEU GLU GLU LEU GLY TYR MET HIS
SEQRES 23 B 447 ILE GLN ALA THR LYS PRO ASP THR VAL GLY ILE GLY LEU
SEQRES 24 B 447 THR ASP SER PRO ALA GLY LEU LEU ALA TYR ILE LEU GLU
SEQRES 25 B 447 LYS PHE SER THR TRP THR ASN PRO ASP LEU ARG SER LYS
SEQRES 26 B 447 GLU ASP GLY GLY LEU SER TYR ARG TRP THR LYS ASP GLN
SEQRES 27 B 447 LEU ILE ASP ASN LEU MET LEU TYR TRP SER THR LYS SER
SEQRES 28 B 447 ILE VAL THR SER MET ARG LEU TYR ALA GLU SER PHE SER
SEQRES 29 B 447 SER ARG HIS PHE ASP LEU LYS LEU ASP GLU ILE GLN VAL
SEQRES 30 B 447 GLN VAL PRO THR TRP VAL LEU GLN ALA LYS HIS GLU LEU
SEQRES 31 B 447 ALA TYR GLN PRO PRO CYS ILE LEU LYS MET LYS TYR PRO
SEQRES 32 B 447 LYS LEU VAL ASN ALA SER VAL ILE GLU ASP GLY GLY HIS
SEQRES 33 B 447 PHE LEU ALA PHE GLU LEU PRO GLU ILE PHE ALA LYS ASP
SEQRES 34 B 447 VAL LEU LYS ALA ILE GLY GLU PHE ARG LYS LEU LYS ASN
SEQRES 35 B 447 VAL LYS THR GLU LEU
HET 1PE A 501 16
HET 1PE B 501 16
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 1PE 2(C10 H22 O6)
FORMUL 5 HOH *159(H2 O)
HELIX 1 1 PRO A 41 LYS A 47 5 7
HELIX 2 2 SER A 60 LYS A 73 1 14
HELIX 3 3 ASN A 91 LYS A 93 5 3
HELIX 4 4 GLN A 94 GLU A 105 1 12
HELIX 5 5 PRO A 107 ASN A 116 1 10
HELIX 6 6 SER A 157 GLU A 163 5 7
HELIX 7 7 ALA A 164 THR A 169 1 6
HELIX 8 8 ALA A 201 GLY A 217 1 17
HELIX 9 9 ASP A 227 PHE A 240 1 14
HELIX 10 10 SER A 256 PHE A 269 1 14
HELIX 11 11 PRO A 270 ILE A 273 5 4
HELIX 12 12 LEU A 278 LEU A 282 5 5
HELIX 13 13 PRO A 284 LEU A 296 1 13
HELIX 14 14 LEU A 296 LYS A 305 1 10
HELIX 15 15 LYS A 305 SER A 316 1 12
HELIX 16 16 SER A 316 TRP A 331 1 16
HELIX 17 17 ASN A 333 LYS A 339 5 7
HELIX 18 18 THR A 349 SER A 362 1 14
HELIX 19 19 SER A 365 PHE A 377 1 13
HELIX 20 20 SER A 378 ASP A 383 1 6
HELIX 21 21 PRO A 408 TYR A 416 1 9
HELIX 22 22 PHE A 431 LEU A 436 1 6
HELIX 23 23 LEU A 436 LYS A 455 1 20
HELIX 24 24 PRO B 41 LYS B 45 5 5
HELIX 25 25 SER B 60 LYS B 73 1 14
HELIX 26 26 ASN B 91 LYS B 93 5 3
HELIX 27 27 GLN B 94 GLU B 105 1 12
HELIX 28 28 PRO B 107 ASN B 116 1 10
HELIX 29 29 SER B 157 TYR B 162 5 6
HELIX 30 30 ALA B 164 THR B 169 1 6
HELIX 31 31 ALA B 201 LEU B 216 1 16
HELIX 32 32 ASP B 227 PHE B 240 1 14
HELIX 33 33 LEU B 292 GLU B 295 5 4
HELIX 34 34 LEU B 296 ALA B 303 1 8
HELIX 35 35 LYS B 305 SER B 316 1 12
HELIX 36 36 SER B 316 TRP B 331 1 16
HELIX 37 37 ASN B 333 LYS B 339 5 7
HELIX 38 38 THR B 349 SER B 362 1 14
HELIX 39 39 SER B 365 PHE B 377 1 13
HELIX 40 40 PRO B 408 TYR B 416 1 9
HELIX 41 41 PHE B 431 LEU B 436 1 6
HELIX 42 42 LEU B 436 LYS B 455 1 20
SHEET 1 A 9 LYS A 53 PHE A 55 0
SHEET 2 A 9 HIS A 120 ILE A 125 -1 O LYS A 122 N LYS A 53
SHEET 3 A 9 LEU A 128 ILE A 135 -1 O LEU A 128 N ILE A 125
SHEET 4 A 9 PHE A 177 PRO A 184 -1 O ALA A 183 N MET A 133
SHEET 5 A 9 GLU A 144 LEU A 151 1 N VAL A 146 O ALA A 178
SHEET 6 A 9 TYR A 221 GLY A 225 1 O TYR A 222 N LEU A 149
SHEET 7 A 9 ILE A 244 SER A 249 1 O HIS A 248 N VAL A 223
SHEET 8 A 9 THR A 395 GLN A 399 1 O LEU A 398 N SER A 249
SHEET 9 A 9 LEU A 419 VAL A 424 1 O VAL A 420 N THR A 395
SHEET 1 B 9 LYS B 53 PHE B 55 0
SHEET 2 B 9 HIS B 120 ILE B 125 -1 O HIS B 120 N PHE B 55
SHEET 3 B 9 LEU B 128 ILE B 135 -1 O LEU B 128 N ILE B 125
SHEET 4 B 9 PHE B 177 PRO B 184 -1 O ALA B 183 N MET B 133
SHEET 5 B 9 GLU B 144 LEU B 151 1 N LEU B 148 O GLU B 180
SHEET 6 B 9 TYR B 221 GLY B 225 1 O TYR B 222 N LEU B 149
SHEET 7 B 9 ILE B 244 SER B 249 1 O HIS B 248 N VAL B 223
SHEET 8 B 9 THR B 395 ALA B 400 1 O TRP B 396 N SER B 249
SHEET 9 B 9 LEU B 419 ILE B 425 1 O VAL B 420 N THR B 395
CISPEP 1 TRP A 154 PRO A 155 0 1.47
CISPEP 2 TYR A 283 PRO A 284 0 -0.76
CISPEP 3 GLY A 342 GLY A 343 0 -16.80
CISPEP 4 TRP B 154 PRO B 155 0 4.46
CISPEP 5 GLY B 342 GLY B 343 0 -20.93
SITE 1 AC1 3 HIS A 300 PHE A 377 SER A 379
SITE 1 AC2 3 THR B 304 SER B 378 SER B 379
CRYST1 161.404 51.466 124.449 90.00 122.68 90.00 C 1 2 1 8
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 0.006196 0.000000 0.003974 0.00000
SCALE2 0.000000 0.019430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009547 0.00000
TER 3420 ASN A 456
TER 6493 ASN B 456
MASTER 381 0 2 42 18 0 2 6 6682 2 32 70
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