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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 17-SEP-99 1QLW
TITLE THE ATOMIC RESOLUTION STRUCTURE OF A NOVEL BACTERIAL
TITLE 2 ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: ALPHA/BETA HYDROLASE FOLD
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALCALIGENES SP.;
SOURCE 3 EXPRESSION_SYSTEM: AGROBACTERIUM SP.
KEYWDS ESTERASE, ANISOTROPIC REFINEMENT, ATOMIC RESOLUTION,
KEYWDS 2 ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD
REVDAT 1 10-FEB-00 1QLW 0
JRNL AUTH P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD
JRNL TITL THE ATOMIC RESOLUTION STRUCTURE OF A NOVEL
JRNL TITL 2 BACTERIAL ESTERASE
JRNL REF STRUCTURE (LONDON) V. 8 143 2000
JRNL REFN ASTM STRUE6 UK ISSN 0969-2126
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.C.BOURNE,M.N.ISUPOV,J.A.LITTLECHILD
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY DIFFRACTION
REMARK 1 TITL 2 STUDIES OF A NOVEL BACTERIAL ESTERASE
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 55 915 1999
REMARK 1 REFN ASTM ABCRE6 DK ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 1.1 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 272934
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.158
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.5
REMARK 3 FREE R VALUE TEST SET COUNT : 1356
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4869
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 715
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.4
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.72
REMARK 3 B22 (A**2) : -2.25
REMARK 3 B33 (A**2) : -3.70
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.02
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.025
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.025
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.015
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.296
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.009 ; 0.02
REMARK 3 ANGLE DISTANCE (A) : 0.027 ; 0.04
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.033 ; 0.05
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : 0.024 ; 0.025
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.114 ; 0.150
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : 0.164 ; 0.300
REMARK 3 MULTIPLE TORSION (A) : 0.250 ; 0.300
REMARK 3 H-BOND (X...Y) (A) : 0.110 ; 0.300
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : 5.6 ; 7.0
REMARK 3 STAGGERED (DEGREES) : 12.7 ; 15.0
REMARK 3 TRANSVERSE (DEGREES) : 38.1 ; 20.0
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.6 ; 2.0
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.3 ; 3.0
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.3 ; 2.0
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.2 ; 3.0
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE C-TERMINAL RESIDUE WAS NOT
REMARK 3 SEEN IN THE DENSITY MAPS
REMARK 4
REMARK 4 1QLW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 17-SEP-1999.
REMARK 100 THE EBI ID CODE IS EBI-4098.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-1997
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG BEAMLINE BW7B
REMARK 200 BEAMLINE : BW7B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8373
REMARK 200 MONOCHROMATOR : HAMBURG
REMARK 200 OPTICS : BENT MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH MAR345
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 274290
REMARK 200 RESOLUTION RANGE HIGH (A) : 28.
REMARK 200 RESOLUTION RANGE LOW (A) : 1.09
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.8
REMARK 200 R MERGE (I) : 0.094
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.36
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.3
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: SHELX, MLPHARE, DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+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 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 67.36500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.36500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 27.80000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 SSS
REMARK 295 M 1 A 5 .. 322 X ..
REMARK 295
REMARK 295 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 BIOLOGICAL_UNIT: HOMODIMER
REMARK 300
REMARK 300 FOR THE HOMO-ASSEMBLY DESCRIBED BY REMARK 350
REMARK 300 THE DIFFERENCE IN ACCESSIBLE SURFACE AREA PER
REMARK 300 CHAIN BETWEEN THE ISOLATED CHAIN AND THAT FOR
REMARK 300 THE CHAIN IN THE COMPLEX IS 3076.5 ANGSTROM**2
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 ALA A 1
REMARK 465 PRO A 2
REMARK 465 PRO A 3
REMARK 465 PRO A 4
REMARK 465 LYS A 323
REMARK 465 PRO A 324
REMARK 465 ALA A 325
REMARK 465 HIS A 326
REMARK 465 GLY A 327
REMARK 465 ARG A 328
REMARK 465 ALA B 1
REMARK 465 PRO B 2
REMARK 465 PRO B 3
REMARK 465 PRO B 4
REMARK 465 ALA B 322
REMARK 465 LYS B 323
REMARK 465 PRO B 324
REMARK 465 ALA B 325
REMARK 465 HIS B 326
REMARK 465 GLY B 327
REMARK 465 ARG B 328
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 LYS A 7 CG CD CE NZ
REMARK 470 SER A 36 OG
REMARK 470 LYS A 156 CG CD CE NZ
REMARK 470 LYS B 7 CG CD CE NZ
REMARK 470 SER B 36 OG
REMARK 470 LYS B 156 CG CD CE NZ
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 59 NH1 - CZ - NH2 ANGL. DEV. = 19.0 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 24.8 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH2 ANGL. DEV. = -44.8 DEGREES
REMARK 500 GLU A 257 CG - CD - OE2 ANGL. DEV. = 14.3 DEGREES
REMARK 500 GLN B 18 CA - CB - CG ANGL. DEV. = 13.3 DEGREES
REMARK 500 LEU B 35 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG B 53 NH1 - CZ - NH2 ANGL. DEV. = 14.2 DEGREES
REMARK 500 THR B 215 OG1 - CB - CG2 ANGL. DEV. = 14.1 DEGREES
REMARK 500 GLU B 257 CB - CG - CD ANGL. DEV. = 22.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 180 SD MET A 180 CE -0.163
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
REMARK 500 NH1 ARG A 59 O HOH U 108 1656 2.18
REMARK 500 NH2 ARG A 59 O HOH U 108 1656 1.87
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500
REMARK 500 SER A 206 56.74 -115.77
REMARK 500 SER B 206 53.66 -111.78
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A U
REMARK 525 B V
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CS1
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CS2
REMARK 800 SITE_DESCRIPTION: CATALYTIC SITE
REMARK 800
DBREF 1QLW A 1 328 PDB 1QLW 1QLW 1 328
DBREF 1QLW B 1 328 PDB 1QLW 1QLW 1 328
SEQRES 1 A 328 ALA PRO PRO PRO VAL PRO LYS THR PRO ALA GLY PRO LEU
SEQRES 2 A 328 THR LEU SER GLY GLN GLY SER PHE PHE VAL GLY GLY ARG
SEQRES 3 A 328 ASP VAL THR SER GLU THR LEU SER LEU SER PRO LYS TYR
SEQRES 4 A 328 ASP ALA HIS GLY THR VAL THR VAL ASP GLN MET TYR VAL
SEQRES 5 A 328 ARG TYR GLN ILE PRO GLN ARG ALA LYS ARG TYR PRO ILE
SEQRES 6 A 328 THR LEU ILE HIS GLY CYS CYS LEU THR GLY MET THR TRP
SEQRES 7 A 328 GLU THR THR PRO ASP GLY ARG MET GLY TRP ASP GLU TYR
SEQRES 8 A 328 PHE LEU ARG LYS GLY TYR SER THR TYR VAL ILE ASP GLN
SEQRES 9 A 328 SER GLY ARG GLY ARG SER ALA THR ASP ILE SER ALA ILE
SEQRES 10 A 328 ASN ALA VAL LYS LEU GLY LYS ALA PRO ALA SER SER LEU
SEQRES 11 A 328 PRO ASP LEU PHE ALA ALA GLY HIS GLU ALA ALA TRP ALA
SEQRES 12 A 328 ILE PHE ARG PHE GLY PRO ARG TYR PRO ASP ALA PHE LYS
SEQRES 13 A 328 ASP THR GLN PHE PRO VAL GLN ALA GLN ALA GLU LEU TRP
SEQRES 14 A 328 GLN GLN MET VAL PRO ASP TRP LEU GLY SER MET PRO THR
SEQRES 15 A 328 PRO ASN PRO THR VAL ALA ASN LEU SER LYS LEU ALA ILE
SEQRES 16 A 328 LYS LEU ASP GLY THR VAL LEU LEU SER HIS SER GLN SER
SEQRES 17 A 328 GLY ILE TYR PRO PHE GLN THR ALA ALA MET ASN PRO LYS
SEQRES 18 A 328 GLY ILE THR ALA ILE VAL SER VAL GLU PRO GLY GLU CYS
SEQRES 19 A 328 PRO LYS PRO GLU ASP VAL LYS PRO LEU THR SER ILE PRO
SEQRES 20 A 328 VAL LEU VAL VAL PHE GLY ASP HIS ILE GLU GLU PHE PRO
SEQRES 21 A 328 ARG TRP ALA PRO ARG LEU LYS ALA CYS HIS ALA PHE ILE
SEQRES 22 A 328 ASP ALA LEU ASN ALA ALA GLY GLY LYS GLY GLN LEU MET
SEQRES 23 A 328 SER LEU PRO ALA LEU GLY VAL HIS GLY ASN SER HIS MET
SEQRES 24 A 328 MET MET GLN ASP ARG ASN ASN LEU GLN VAL ALA ASP LEU
SEQRES 25 A 328 ILE LEU ASP TRP ILE GLY ARG ASN THR ALA LYS PRO ALA
SEQRES 26 A 328 HIS GLY ARG
SEQRES 1 B 328 ALA PRO PRO PRO VAL PRO LYS THR PRO ALA GLY PRO LEU
SEQRES 2 B 328 THR LEU SER GLY GLN GLY SER PHE PHE VAL GLY GLY ARG
SEQRES 3 B 328 ASP VAL THR SER GLU THR LEU SER LEU ALA PRO LYS TYR
SEQRES 4 B 328 ASP ALA HIS GLY THR VAL THR VAL ASP GLN MET TYR VAL
SEQRES 5 B 328 ARG TYR GLN ILE PRO GLN ARG ALA LYS ARG TYR PRO ILE
SEQRES 6 B 328 THR LEU ILE HIS GLY CYS CYS LEU THR GLY MET THR TRP
SEQRES 7 B 328 GLU THR THR PRO ASP GLY ARG MET GLY TRP ASP GLU TYR
SEQRES 8 B 328 PHE LEU ARG LYS GLY TYR SER THR TYR VAL ILE ASP GLN
SEQRES 9 B 328 SER GLY ARG GLY ARG SER ALA THR ASP ILE SER ALA ILE
SEQRES 10 B 328 ASN ALA VAL LYS LEU GLY LYS ALA PRO ALA SER SER LEU
SEQRES 11 B 328 PRO ASP LEU PHE ALA ALA GLY HIS GLU ALA ALA TRP ALA
SEQRES 12 B 328 ILE PHE ARG PHE GLY PRO ARG TYR PRO ASP ALA PHE LYS
SEQRES 13 B 328 ASP THR GLN PHE PRO VAL GLN ALA GLN ALA GLU LEU TRP
SEQRES 14 B 328 GLN GLN MET VAL PRO ASP TRP LEU GLY SER MET PRO THR
SEQRES 15 B 328 PRO ASN PRO THR VAL ALA ASN LEU SER LYS LEU ALA ILE
SEQRES 16 B 328 LYS LEU ASP GLY THR VAL LEU LEU SER HIS SER GLN SER
SEQRES 17 B 328 GLY ILE TYR PRO PHE GLN THR ALA ALA MET ASN PRO LYS
SEQRES 18 B 328 GLY ILE THR ALA ILE VAL SER VAL GLU PRO GLY GLU CYS
SEQRES 19 B 328 PRO LYS PRO GLU ASP VAL LYS PRO LEU THR SER ILE PRO
SEQRES 20 B 328 VAL LEU VAL VAL PHE GLY ASP HIS ILE GLU GLU PHE PRO
SEQRES 21 B 328 ARG TRP ALA PRO ARG LEU LYS ALA CYS HIS ALA PHE ILE
SEQRES 22 B 328 ASP ALA LEU ASN ALA ALA GLY GLY LYS GLY GLN LEU MET
SEQRES 23 B 328 SER LEU PRO ALA LEU GLY VAL HIS GLY ASN SER HIS MET
SEQRES 24 B 328 MET MET GLN ASP ARG ASN ASN LEU GLN VAL ALA ASP LEU
SEQRES 25 B 328 ILE LEU ASP TRP ILE GLY ARG ASN THR ALA LYS PRO ALA
SEQRES 26 B 328 HIS GLY ARG
HET SO4 A 575 5
HET SO4 B 575 5
HET SO4 A 576 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 3(O4 S1 2-)
FORMUL 4 HOH *715(H2 O1)
HELIX 1 1 THR A 74 GLU A 79 5 6
HELIX 2 2 GLY A 87 LYS A 95 1 9
HELIX 3 3 PRO A 126 LEU A 130 5 5
HELIX 4 4 GLY A 137 PHE A 145 1 9
HELIX 5 5 PRO A 161 GLN A 163 5 3
HELIX 6 6 ALA A 164 MET A 172 1 9
HELIX 7 7 TRP A 176 MET A 180 5 5
HELIX 8 8 LEU A 190 ASP A 198 1 9
HELIX 9 9 GLN A 207 GLY A 209 5 3
HELIX 10 10 ILE A 210 MET A 218 1 9
HELIX 11 11 LYS A 236 VAL A 240 5 5
HELIX 12 12 VAL A 240 THR A 244 5 5
HELIX 13 13 TRP A 262 LEU A 276 1 15
HELIX 14 14 PRO A 289 GLY A 292 5 4
HELIX 15 15 MET A 299 ASP A 303 5 5
HELIX 16 16 LEU A 307 ARG A 319 1 13
HELIX 17 17 THR B 74 GLU B 79 5 6
HELIX 18 18 GLY B 87 LYS B 95 1 9
HELIX 19 19 PRO B 126 LEU B 130 5 5
HELIX 20 20 GLY B 137 PHE B 145 1 9
HELIX 21 21 PRO B 161 GLN B 163 5 3
HELIX 22 22 ALA B 164 MET B 172 1 9
HELIX 23 23 TRP B 176 MET B 180 5 5
HELIX 24 24 LEU B 190 ASP B 198 1 9
HELIX 25 25 GLN B 207 GLY B 209 5 3
HELIX 26 26 ILE B 210 MET B 218 1 9
HELIX 27 27 LYS B 236 VAL B 240 5 5
HELIX 28 28 VAL B 240 THR B 244 5 5
HELIX 29 29 TRP B 262 LEU B 276 1 15
HELIX 30 30 PRO B 289 GLY B 292 5 4
HELIX 31 31 MET B 299 ASP B 303 5 5
HELIX 32 32 LEU B 307 ARG B 319 1 13
SHEET 1 A 2 ARG A 26 SER A 30 0
SHEET 2 A 2 GLY A 43 VAL A 47 -1 N VAL A 47 O ARG A 26
SHEET 1 B 8 GLY A 283 SER A 287 0
SHEET 2 B 8 PRO A 247 PHE A 252 1 N VAL A 248 O GLN A 284
SHEET 3 B 8 ILE A 223 VAL A 229 1 N ILE A 226 O PRO A 247
SHEET 4 B 8 THR A 200 HIS A 205 1 N THR A 200 O THR A 224
SHEET 5 B 8 PRO A 64 ILE A 68 1 N PRO A 64 O VAL A 201
SHEET 6 B 8 THR A 99 ASP A 103 1 N TYR A 100 O ILE A 65
SHEET 7 B 8 MET A 50 PRO A 57 -1 N GLN A 55 O THR A 99
SHEET 8 B 8 LEU A 15 VAL A 23 -1 N VAL A 23 O MET A 50
SHEET 1 C 2 ARG B 26 SER B 30 0
SHEET 2 C 2 GLY B 43 VAL B 47 -1 N VAL B 47 O ARG B 26
SHEET 1 D 8 GLY B 283 SER B 287 0
SHEET 2 D 8 PRO B 247 PHE B 252 1 N VAL B 248 O GLN B 284
SHEET 3 D 8 ILE B 223 VAL B 229 1 N ILE B 226 O PRO B 247
SHEET 4 D 8 THR B 200 HIS B 205 1 N THR B 200 O THR B 224
SHEET 5 D 8 PRO B 64 ILE B 68 1 N PRO B 64 O VAL B 201
SHEET 6 D 8 THR B 99 ASP B 103 1 N TYR B 100 O ILE B 65
SHEET 7 D 8 MET B 50 PRO B 57 -1 N GLN B 55 O THR B 99
SHEET 8 D 8 LEU B 15 VAL B 23 -1 N VAL B 23 O MET B 50
SSBOND 1 CYS A 71 CYS A 72
SSBOND 2 CYS A 234 CYS A 269
SSBOND 3 CYS B 71 CYS B 72
SSBOND 5 CYS B 234 CYS B 269
CISPEP 1 TYR A 151 PRO A 152 0 -0.23
CISPEP 2 THR A 182 PRO A 183 0 -0.96
CISPEP 3 TYR B 151 PRO B 152 0 -6.48
CISPEP 4 THR B 182 PRO B 183 0 -1.71
SITE 1 CS1 3 SER A 206 GLU A 230 HIS A 298
SITE 1 CS2 3 SER B 206 GLU B 230 HIS B 298
CRYST1 134.730 55.600 110.200 90.00 125.06 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 0.007422 0.000000 0.005209 0.00000
SCALE2 0.000000 0.017986 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011086 0.00000
MTRIX1 1 -0.992340 -0.021820 0.121580 51.80933 1
MTRIX2 1 -0.012180 -0.962200 -0.272070 5.28295 1
MTRIX3 1 0.122920 -0.271470 0.954570 -2.50379 1
END |