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HEADER HYDROLASE 04-AUG-10 3O9M
TITLE CO-CRYSTALLIZATION STUDIES OF FULL LENGTH RECOMBINANT BCHE WITH
TITLE 2 COCAINE OFFERS INSIGHTS INTO COCAINE DETOXIFICATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,
COMPND 5 BUTYRYLCHOLINE ESTERASE, PSEUDOCHOLINESTERASE;
COMPND 6 EC: 3.1.1.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCHE, CHE1;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS CHOLINESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR O.A.ASOJO,M.N.NGAMELUE,K.HOMMA,O.LOCKRIDGE
REVDAT 1 13-APR-11 3O9M 0
JRNL AUTH O.A.ASOJO,M.N.NGAMELUE,K.HOMMA,O.LOCKRIDGE
JRNL TITL COCRYSTALLIZATION STUDIES OF FULL-LENGTH RECOMBINANT
JRNL TITL 2 BUTYRYLCHOLINESTERASE (BCHE) WITH COCAINE
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 67 434 2011
JRNL REFN ESSN 1744-3091
JRNL DOI 10.1107/S1744309111004805
REMARK 2
REMARK 2 RESOLUTION. 2.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 142.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 32219
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1720
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) : 2.98
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2336
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8452
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 2
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.408
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.284
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.761
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8714 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11834 ; 1.761 ; 1.945
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1060 ; 7.010 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 406 ;37.556 ;24.089
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1412 ;20.290 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;21.487 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1254 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6732 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5286 ; 0.799 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8528 ; 1.551 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3428 ; 1.910 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3306 ; 3.310 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A -99999 A 99999 1
REMARK 3 1 B -99999 B 99999 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4236 ; 0.09 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 4236 ; 0.14 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O9M COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-AUG-10.
REMARK 100 THE RCSB ID CODE IS RCSB060838.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34043
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.980
REMARK 200 RESOLUTION RANGE LOW (A) : 31.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 75.19600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 75.19600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 75.19600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 75.19600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 75.19600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 75.19600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 75.19600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 75.19600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
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 BIOMT1 2 -1.000000 0.000000 0.000000 150.39200
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 BIOMT1 3 0.000000 -1.000000 0.000000 75.19600
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -75.19600
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 75.19600
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 75.19600
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
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 BIOMT1 2 -1.000000 0.000000 0.000000 150.39200
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 BIOMT1 3 0.000000 -1.000000 0.000000 75.19600
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -75.19600
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 75.19600
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 75.19600
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 29450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 156350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 150.39200
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 BIOMT1 3 0.000000 -1.000000 0.000000 75.19600
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -75.19600
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 75.19600
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 75.19600
REMARK 350 BIOMT3 4 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 GLU A 1
REMARK 465 ASP A 2
REMARK 465 ASP A 3
REMARK 465 ASN A 535
REMARK 465 ILE A 536
REMARK 465 ASP A 537
REMARK 465 GLU A 538
REMARK 465 ALA A 539
REMARK 465 GLU A 540
REMARK 465 TRP A 541
REMARK 465 GLU A 542
REMARK 465 TRP A 543
REMARK 465 LYS A 544
REMARK 465 ALA A 545
REMARK 465 GLY A 546
REMARK 465 PHE A 547
REMARK 465 HIS A 548
REMARK 465 ARG A 549
REMARK 465 TRP A 550
REMARK 465 ASN A 551
REMARK 465 ASN A 552
REMARK 465 TYR A 553
REMARK 465 MET A 554
REMARK 465 MET A 555
REMARK 465 ASP A 556
REMARK 465 TRP A 557
REMARK 465 LYS A 558
REMARK 465 ASN A 559
REMARK 465 GLN A 560
REMARK 465 PHE A 561
REMARK 465 ASN A 562
REMARK 465 ASP A 563
REMARK 465 TYR A 564
REMARK 465 THR A 565
REMARK 465 SER A 566
REMARK 465 LYS A 567
REMARK 465 LYS A 568
REMARK 465 GLU A 569
REMARK 465 SER A 570
REMARK 465 CYS A 571
REMARK 465 VAL A 572
REMARK 465 GLY A 573
REMARK 465 LEU A 574
REMARK 465 GLU B 1
REMARK 465 ASP B 2
REMARK 465 ASP B 3
REMARK 465 ASN B 535
REMARK 465 ILE B 536
REMARK 465 ASP B 537
REMARK 465 GLU B 538
REMARK 465 ALA B 539
REMARK 465 GLU B 540
REMARK 465 TRP B 541
REMARK 465 GLU B 542
REMARK 465 TRP B 543
REMARK 465 LYS B 544
REMARK 465 ALA B 545
REMARK 465 GLY B 546
REMARK 465 PHE B 547
REMARK 465 HIS B 548
REMARK 465 ARG B 549
REMARK 465 TRP B 550
REMARK 465 ASN B 551
REMARK 465 ASN B 552
REMARK 465 TYR B 553
REMARK 465 MET B 554
REMARK 465 MET B 555
REMARK 465 ASP B 556
REMARK 465 TRP B 557
REMARK 465 LYS B 558
REMARK 465 ASN B 559
REMARK 465 GLN B 560
REMARK 465 PHE B 561
REMARK 465 ASN B 562
REMARK 465 ASP B 563
REMARK 465 TYR B 564
REMARK 465 THR B 565
REMARK 465 SER B 566
REMARK 465 LYS B 567
REMARK 465 LYS B 568
REMARK 465 GLU B 569
REMARK 465 SER B 570
REMARK 465 CYS B 571
REMARK 465 VAL B 572
REMARK 465 GLY B 573
REMARK 465 LEU B 574
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 40 CZ ARG A 40 NH2 0.094
REMARK 500 CYS A 92 CB CYS A 92 SG -0.111
REMARK 500 PHE A 364 CB PHE A 364 CG -0.133
REMARK 500 LYS B 105 CD LYS B 105 CE 0.176
REMARK 500 PHE B 364 CB PHE B 364 CG -0.119
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 102 C - N - CA ANGL. DEV. = -22.2 DEGREES
REMARK 500 LYS A 105 CB - CA - C ANGL. DEV. = 14.1 DEGREES
REMARK 500 CYS A 263 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 MET A 302 CG - SD - CE ANGL. DEV. = 11.5 DEGREES
REMARK 500 PHE A 364 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 465 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LYS B 105 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 CYS B 263 CA - CB - SG ANGL. DEV. = 9.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 37 47.19 -73.34
REMARK 500 PHE A 43 -6.89 78.15
REMARK 500 ASP A 54 -144.38 -103.85
REMARK 500 LYS A 103 125.35 -29.60
REMARK 500 LYS A 105 -61.37 -107.19
REMARK 500 PHE A 118 -2.02 69.61
REMARK 500 PRO A 157 108.51 -44.10
REMARK 500 SER A 198 -102.34 39.23
REMARK 500 ARG A 254 -154.05 -135.07
REMARK 500 GLU A 255 -73.35 -120.71
REMARK 500 ASP A 297 -76.11 -100.40
REMARK 500 ARG A 347 -38.35 -30.29
REMARK 500 ASP A 379 11.80 32.90
REMARK 500 PHE A 398 -59.51 -131.93
REMARK 500 ASN A 455 46.63 -100.60
REMARK 500 THR A 488 101.94 61.12
REMARK 500 GLN A 498 61.63 61.95
REMARK 500 GLU A 506 -105.55 -80.50
REMARK 500 THR A 508 81.53 50.17
REMARK 500 LYS A 513 78.48 37.84
REMARK 500 PRO B 37 48.15 -77.49
REMARK 500 PHE B 43 -6.42 72.85
REMARK 500 ASP B 54 -144.73 -107.27
REMARK 500 LEU B 93 80.58 -67.36
REMARK 500 LYS B 103 125.80 -31.02
REMARK 500 LYS B 105 -137.46 76.36
REMARK 500 PHE B 118 -3.82 70.50
REMARK 500 PRO B 160 -9.72 -58.85
REMARK 500 ALA B 162 76.80 -152.35
REMARK 500 SER B 198 -104.62 42.71
REMARK 500 GLU B 255 -75.79 -113.31
REMARK 500 ASP B 297 -69.72 -107.16
REMARK 500 TYR B 332 42.50 -106.97
REMARK 500 ASP B 379 11.96 34.55
REMARK 500 PHE B 398 -62.73 -128.36
REMARK 500 ASN B 455 42.45 -100.30
REMARK 500 PRO B 480 46.29 -82.90
REMARK 500 THR B 483 27.34 -79.17
REMARK 500 GLN B 484 -64.75 -122.97
REMARK 500 THR B 488 101.38 60.93
REMARK 500 GLU B 506 -110.92 -78.54
REMARK 500 THR B 508 79.75 54.48
REMARK 500 LYS B 513 81.05 31.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO B 104 LYS B 105 45.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ALA A 101 22.5 L L OUTSIDE RANGE
REMARK 500 ASN A 106 20.8 L L OUTSIDE RANGE
REMARK 500 ASN B 106 22.5 L L OUTSIDE RANGE
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 BEZ A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEZ B 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PM8 RELATED DB: PDB
REMARK 900 RELATED ID: 2P0P RELATED DB: PDB
REMARK 900 RELATED ID: 2WSL RELATED DB: PDB
DBREF 3O9M A 1 574 UNP P06276 CHLE_HUMAN 29 602
DBREF 3O9M B 1 574 UNP P06276 CHLE_HUMAN 29 602
SEQRES 1 A 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 A 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 A 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 A 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 A 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 A 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 A 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 A 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 A 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 A 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 A 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 A 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 A 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 A 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 A 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 A 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 A 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 A 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 A 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 A 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 A 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 A 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 A 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 A 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 A 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 A 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 A 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 A 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 A 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 A 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 A 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 A 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 A 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 A 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 A 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 A 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 A 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 A 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 A 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 A 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 A 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 A 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 A 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 A 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 A 574 GLY LEU
SEQRES 1 B 574 GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL
SEQRES 2 B 574 ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR
SEQRES 3 B 574 ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY
SEQRES 4 B 574 ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP
SEQRES 5 B 574 SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS
SEQRES 6 B 574 CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY
SEQRES 7 B 574 SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP
SEQRES 8 B 574 CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO
SEQRES 9 B 574 LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY
SEQRES 10 B 574 PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY
SEQRES 11 B 574 LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER
SEQRES 12 B 574 MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU
SEQRES 13 B 574 PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE
SEQRES 14 B 574 ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE
SEQRES 15 B 574 ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE
SEQRES 16 B 574 GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU
SEQRES 17 B 574 LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE
SEQRES 18 B 574 LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR
SEQRES 19 B 574 SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA
SEQRES 20 B 574 LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE
SEQRES 21 B 574 ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU
SEQRES 22 B 574 LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU
SEQRES 23 B 574 SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU
SEQRES 24 B 574 THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE
SEQRES 25 B 574 LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU
SEQRES 26 B 574 GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER
SEQRES 27 B 574 LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN
SEQRES 28 B 574 GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE
SEQRES 29 B 574 GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL
SEQRES 30 B 574 ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY
SEQRES 31 B 574 ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU
SEQRES 32 B 574 GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA
SEQRES 33 B 574 PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO
SEQRES 34 B 574 TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE
SEQRES 35 B 574 GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN
SEQRES 36 B 574 TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL
SEQRES 37 B 574 LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN
SEQRES 38 B 574 GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS
SEQRES 39 B 574 SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER
SEQRES 40 B 574 THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG
SEQRES 41 B 574 PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR
SEQRES 42 B 574 GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY
SEQRES 43 B 574 PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN
SEQRES 44 B 574 GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL
SEQRES 45 B 574 GLY LEU
HET BEZ A 999 9
HET BEZ B 999 9
HETNAM BEZ BENZOIC ACID
FORMUL 3 BEZ 2(C7 H6 O2)
FORMUL 5 HOH *2(H2 O)
HELIX 1 1 LEU A 38 ARG A 42 5 5
HELIX 2 2 PHE A 76 MET A 81 1 6
HELIX 3 3 LEU A 125 ASP A 129 5 5
HELIX 4 4 GLY A 130 ARG A 138 1 9
HELIX 5 5 VAL A 148 LEU A 154 1 7
HELIX 6 6 ASN A 165 ILE A 182 1 18
HELIX 7 7 ALA A 183 PHE A 185 5 3
HELIX 8 8 SER A 198 SER A 210 1 13
HELIX 9 9 SER A 235 THR A 250 1 16
HELIX 10 10 ASN A 256 ARG A 265 1 10
HELIX 11 11 ASP A 268 ALA A 277 1 10
HELIX 12 12 MET A 302 LEU A 309 1 8
HELIX 13 13 GLY A 326 VAL A 331 1 6
HELIX 14 14 THR A 346 PHE A 358 1 13
HELIX 15 15 SER A 362 ASP A 375 1 14
HELIX 16 16 GLU A 383 PHE A 398 1 16
HELIX 17 17 PHE A 398 GLU A 411 1 14
HELIX 18 18 PRO A 431 GLY A 435 5 5
HELIX 19 19 GLU A 441 PHE A 446 1 6
HELIX 20 20 GLY A 447 GLU A 451 5 5
HELIX 21 21 THR A 457 GLY A 478 1 22
HELIX 22 22 ARG A 515 SER A 524 1 10
HELIX 23 23 SER A 524 THR A 533 1 10
HELIX 24 24 LEU B 38 ARG B 42 5 5
HELIX 25 25 PHE B 76 MET B 81 1 6
HELIX 26 26 LEU B 125 ASP B 129 5 5
HELIX 27 27 GLY B 130 ARG B 138 1 9
HELIX 28 28 GLY B 149 LEU B 154 1 6
HELIX 29 29 ASN B 165 ILE B 182 1 18
HELIX 30 30 ALA B 183 PHE B 185 5 3
HELIX 31 31 SER B 198 SER B 210 1 13
HELIX 32 32 PRO B 211 HIS B 214 5 4
HELIX 33 33 SER B 235 THR B 250 1 16
HELIX 34 34 ASN B 256 ARG B 265 1 10
HELIX 35 35 ASP B 268 ALA B 277 1 10
HELIX 36 36 MET B 302 LEU B 309 1 8
HELIX 37 37 GLY B 326 GLY B 333 5 8
HELIX 38 38 THR B 346 PHE B 358 1 13
HELIX 39 39 SER B 362 ASP B 375 1 14
HELIX 40 40 GLU B 383 PHE B 398 1 16
HELIX 41 41 PHE B 398 GLU B 411 1 14
HELIX 42 42 PRO B 431 GLY B 435 5 5
HELIX 43 43 GLU B 441 PHE B 446 1 6
HELIX 44 44 GLY B 447 GLU B 451 5 5
HELIX 45 45 THR B 457 GLY B 478 1 22
HELIX 46 46 ARG B 515 SER B 524 1 10
HELIX 47 47 SER B 524 THR B 533 1 10
SHEET 1 A 3 ILE A 5 THR A 8 0
SHEET 2 A 3 GLY A 11 ARG A 14 -1 O VAL A 13 N ILE A 6
SHEET 3 A 3 ILE A 55 ASN A 57 1 O TRP A 56 N ARG A 14
SHEET 1 B 4 MET A 16 VAL A 20 0
SHEET 2 B 4 GLY A 23 ALA A 27 -1 O VAL A 25 N LEU A 18
SHEET 3 B 4 TYR A 94 ILE A 99 -1 O ILE A 99 N THR A 26
SHEET 4 B 4 ILE A 31 PRO A 32 -1 N ILE A 31 O LEU A 95
SHEET 1 C11 MET A 16 VAL A 20 0
SHEET 2 C11 GLY A 23 ALA A 27 -1 O VAL A 25 N LEU A 18
SHEET 3 C11 TYR A 94 ILE A 99 -1 O ILE A 99 N THR A 26
SHEET 4 C11 ILE A 140 MET A 144 -1 O SER A 143 N ASN A 96
SHEET 5 C11 ALA A 107 ILE A 113 1 N LEU A 110 O VAL A 142
SHEET 6 C11 GLY A 187 GLU A 197 1 O ASN A 188 N ALA A 107
SHEET 7 C11 ARG A 219 GLN A 223 1 O ILE A 221 N LEU A 194
SHEET 8 C11 ILE A 317 ASN A 322 1 O LEU A 318 N LEU A 222
SHEET 9 C11 ALA A 416 PHE A 421 1 O PHE A 417 N VAL A 319
SHEET 10 C11 LYS A 499 LEU A 503 1 O LEU A 503 N TYR A 420
SHEET 11 C11 ILE A 510 THR A 512 -1 O MET A 511 N TYR A 500
SHEET 1 D 3 ILE B 5 THR B 8 0
SHEET 2 D 3 GLY B 11 ARG B 14 -1 O VAL B 13 N ILE B 6
SHEET 3 D 3 ILE B 55 ASN B 57 1 O TRP B 56 N ARG B 14
SHEET 1 E 4 MET B 16 VAL B 20 0
SHEET 2 E 4 GLY B 23 ALA B 27 -1 O VAL B 25 N LEU B 18
SHEET 3 E 4 TYR B 94 PRO B 100 -1 O ILE B 99 N THR B 26
SHEET 4 E 4 ILE B 31 PRO B 32 -1 N ILE B 31 O LEU B 95
SHEET 1 F11 MET B 16 VAL B 20 0
SHEET 2 F11 GLY B 23 ALA B 27 -1 O VAL B 25 N LEU B 18
SHEET 3 F11 TYR B 94 PRO B 100 -1 O ILE B 99 N THR B 26
SHEET 4 F11 ILE B 140 MET B 144 -1 O VAL B 141 N TRP B 98
SHEET 5 F11 ALA B 107 ILE B 113 1 N LEU B 110 O VAL B 142
SHEET 6 F11 GLY B 187 GLU B 197 1 O ASN B 188 N ALA B 107
SHEET 7 F11 ARG B 219 GLN B 223 1 O ILE B 221 N LEU B 194
SHEET 8 F11 ILE B 317 ASN B 322 1 O LEU B 318 N LEU B 222
SHEET 9 F11 ALA B 416 PHE B 421 1 O PHE B 417 N VAL B 319
SHEET 10 F11 LYS B 499 LEU B 503 1 O LEU B 501 N PHE B 418
SHEET 11 F11 ILE B 510 THR B 512 -1 O MET B 511 N TYR B 500
SHEET 1 G 2 SER B 64 CYS B 65 0
SHEET 2 G 2 LEU B 88 SER B 89 1 O SER B 89 N SER B 64
SSBOND 1 CYS A 65 CYS A 92 1555 1555 2.02
SSBOND 2 CYS A 252 CYS A 263 1555 1555 2.07
SSBOND 3 CYS A 400 CYS A 519 1555 1555 2.11
SSBOND 4 CYS B 65 CYS B 92 1555 1555 2.07
SSBOND 5 CYS B 252 CYS B 263 1555 1555 2.08
SSBOND 6 CYS B 400 CYS B 519 1555 1555 2.09
CISPEP 1 ALA B 101 PRO B 102 0 6.48
SITE 1 AC1 5 GLY A 116 GLY A 117 SER A 198 LEU A 286
SITE 2 AC1 5 HIS A 438
SITE 1 AC2 4 GLY B 116 GLY B 117 SER B 198 HIS B 438
CRYST1 150.392 150.392 142.448 90.00 90.00 90.00 P 4 21 2 16
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 0.006649 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006649 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007020 0.00000
TER 4227 GLY A 534
TER 8454 GLY B 534
MASTER 549 0 2 47 38 0 3 6 8472 2 30 90
END |