HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 20-MAR-08 3CLW
TITLE CRYSTAL STRUCTURE OF CONSERVED EXPORTED PROTEIN FROM BACTEROIDES
TITLE 2 FRAGILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED EXPORTED PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 FRAGMENT: RESIDUES 27-522;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES FRAGILIS;
SOURCE 3 ORGANISM_TAXID: 272559;
SOURCE 4 STRAIN: NCTC 9343;
SOURCE 5 ATCC: 25285;
SOURCE 6 GENE: BF1510;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26
KEYWDS STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.BONANNO,M.RUTTER,K.T.BAIN,S.CHANG,K.OZYURT,D.SMITH,S.WASSERMAN,
AUTHOR 2 J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR
AUTHOR 3 STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 9 21-FEB-24 3CLW 1 REMARK
REVDAT 8 03-FEB-21 3CLW 1 AUTHOR JRNL SEQADV
REVDAT 7 14-NOV-18 3CLW 1 AUTHOR
REVDAT 6 25-OCT-17 3CLW 1 REMARK
REVDAT 5 13-JUL-11 3CLW 1 VERSN
REVDAT 4 09-JUN-09 3CLW 1 REVDAT
REVDAT 3 24-FEB-09 3CLW 1 VERSN
REVDAT 2 23-DEC-08 3CLW 1 AUTHOR KEYWDS
REVDAT 1 29-APR-08 3CLW 0
JRNL AUTH J.B.BONANNO,M.RUTTER,K.T.BAIN,S.CHANG,K.OZYURT,D.SMITH,
JRNL AUTH 2 S.WASSERMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF CONSERVED EXPORTED PROTEIN FROM
JRNL TITL 2 BACTEROIDES FRAGILIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.5
REMARK 3 NUMBER OF REFLECTIONS : 172302
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8668
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11103
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 592
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23409
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 944
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.24000
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : -0.44000
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): 0.286
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.751
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 24003 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32580 ; 1.412 ; 1.933
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2953 ; 6.960 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1167 ;37.379 ;24.713
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3992 ;15.892 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 112 ;13.347 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3536 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18438 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 11330 ; 0.206 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 16337 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1336 ; 0.146 ; 0.200
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): 27 ; 0.144 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.292 ; 0.200
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): 15183 ; 0.825 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23665 ; 1.257 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 10356 ; 1.959 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8910 ; 3.013 ; 4.500
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3CLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-08.
REMARK 100 THE DEPOSITION ID IS D_1000046933.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-08
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 : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97958
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 172557
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.199
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.5
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.55100
REMARK 200 R SYM FOR SHELL (I) : 0.55100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM SODIUM SULFATE, 20% PEG 3350, PH
REMARK 280 7.0, VAPOR DIFFUSION, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 43.76500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 196.67500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 58.12900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 196.67500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.76500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 58.12900
REMARK 290 SMTRY3 4 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 300 REMARK: AUTHORS STATE THAT THE MONOMERIC ASSEMBLY OF THE BIOLOGICAL
REMARK 300 UNIT THAT IS SHOWN IN REMARK 350 IS PUTATIVE AT THE TIME OF
REMARK 300 DEPOSITION.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 24
REMARK 465 SER A 25
REMARK 465 LEU A 26
REMARK 465 ASN A 27
REMARK 465 GLU A 520
REMARK 465 ASP A 521
REMARK 465 ASN A 522
REMARK 465 GLU A 523
REMARK 465 GLY A 524
REMARK 465 HIS A 525
REMARK 465 HIS A 526
REMARK 465 HIS A 527
REMARK 465 HIS A 528
REMARK 465 HIS A 529
REMARK 465 HIS A 530
REMARK 465 MET B 24
REMARK 465 SER B 25
REMARK 465 LEU B 26
REMARK 465 ASN B 27
REMARK 465 GLU B 520
REMARK 465 ASP B 521
REMARK 465 ASN B 522
REMARK 465 GLU B 523
REMARK 465 GLY B 524
REMARK 465 HIS B 525
REMARK 465 HIS B 526
REMARK 465 HIS B 527
REMARK 465 HIS B 528
REMARK 465 HIS B 529
REMARK 465 HIS B 530
REMARK 465 MET C 24
REMARK 465 SER C 25
REMARK 465 LEU C 26
REMARK 465 ASN C 27
REMARK 465 LYS C 28
REMARK 465 GLU C 520
REMARK 465 ASP C 521
REMARK 465 ASN C 522
REMARK 465 GLU C 523
REMARK 465 GLY C 524
REMARK 465 HIS C 525
REMARK 465 HIS C 526
REMARK 465 HIS C 527
REMARK 465 HIS C 528
REMARK 465 HIS C 529
REMARK 465 HIS C 530
REMARK 465 MET D 24
REMARK 465 SER D 25
REMARK 465 LEU D 26
REMARK 465 ASN D 27
REMARK 465 LYS D 28
REMARK 465 GLU D 520
REMARK 465 ASP D 521
REMARK 465 ASN D 522
REMARK 465 GLU D 523
REMARK 465 GLY D 524
REMARK 465 HIS D 525
REMARK 465 HIS D 526
REMARK 465 HIS D 527
REMARK 465 HIS D 528
REMARK 465 HIS D 529
REMARK 465 HIS D 530
REMARK 465 MET E 24
REMARK 465 SER E 25
REMARK 465 LEU E 26
REMARK 465 ASN E 27
REMARK 465 LYS E 28
REMARK 465 GLU E 520
REMARK 465 ASP E 521
REMARK 465 ASN E 522
REMARK 465 GLU E 523
REMARK 465 GLY E 524
REMARK 465 HIS E 525
REMARK 465 HIS E 526
REMARK 465 HIS E 527
REMARK 465 HIS E 528
REMARK 465 HIS E 529
REMARK 465 HIS E 530
REMARK 465 MET F 24
REMARK 465 SER F 25
REMARK 465 LEU F 26
REMARK 465 ASN F 27
REMARK 465 GLU F 520
REMARK 465 ASP F 521
REMARK 465 ASN F 522
REMARK 465 GLU F 523
REMARK 465 GLY F 524
REMARK 465 HIS F 525
REMARK 465 HIS F 526
REMARK 465 HIS F 527
REMARK 465 HIS F 528
REMARK 465 HIS F 529
REMARK 465 HIS F 530
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 A 79 CG CD OE1 OE2
REMARK 470 LYS A 80 CG CD CE NZ
REMARK 470 LYS A 138 CG CD CE NZ
REMARK 470 LYS A 436 CG CD CE NZ
REMARK 470 TYR A 439 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 440 CG CD CE NZ
REMARK 470 ILE A 441 CG1 CG2 CD1
REMARK 470 GLU A 471 CG CD OE1 OE2
REMARK 470 GLN A 473 CG CD OE1 NE2
REMARK 470 SER A 476 OG
REMARK 470 GLN A 483 CG CD OE1 NE2
REMARK 470 LYS A 505 CG CD CE NZ
REMARK 470 LYS A 506 CG CD CE NZ
REMARK 470 GLN A 508 CG CD OE1 NE2
REMARK 470 GLU B 79 CG CD OE1 OE2
REMARK 470 LYS B 138 CG CD CE NZ
REMARK 470 LYS B 341 CG CD CE NZ
REMARK 470 LYS B 436 CG CD CE NZ
REMARK 470 TYR B 439 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 440 CG CD CE NZ
REMARK 470 ILE B 441 CG1 CG2 CD1
REMARK 470 GLU B 445 CG CD OE1 OE2
REMARK 470 LYS B 459 CG CD CE NZ
REMARK 470 GLU B 471 CG CD OE1 OE2
REMARK 470 SER B 476 OG
REMARK 470 ASP B 480 CG OD1 OD2
REMARK 470 HIS B 481 CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 483 CG CD OE1 NE2
REMARK 470 ARG B 497 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 505 CG CD CE NZ
REMARK 470 LYS B 506 CG CD CE NZ
REMARK 470 GLN B 508 CG CD OE1 NE2
REMARK 470 LYS C 29 CG CD CE NZ
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 LYS C 80 CG CD CE NZ
REMARK 470 LYS C 138 CG CD CE NZ
REMARK 470 LYS C 436 CG CD CE NZ
REMARK 470 TYR C 439 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 440 CG CD CE NZ
REMARK 470 ILE C 441 CG1 CG2 CD1
REMARK 470 SER C 442 OG
REMARK 470 GLU C 445 CG CD OE1 OE2
REMARK 470 LYS C 459 CG CD CE NZ
REMARK 470 GLN C 473 CG CD OE1 NE2
REMARK 470 SER C 476 OG
REMARK 470 ASP C 480 CG OD1 OD2
REMARK 470 GLN C 483 CG CD OE1 NE2
REMARK 470 LYS C 505 CG CD CE NZ
REMARK 470 LYS C 506 CG CD CE NZ
REMARK 470 GLN C 508 CG CD OE1 NE2
REMARK 470 LYS D 29 CG CD CE NZ
REMARK 470 GLU D 79 CG CD OE1 OE2
REMARK 470 LYS D 80 CG CD CE NZ
REMARK 470 LYS D 138 CG CD CE NZ
REMARK 470 LYS D 436 CG CD CE NZ
REMARK 470 TYR D 439 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS D 440 CG CD CE NZ
REMARK 470 ILE D 441 CG1 CG2 CD1
REMARK 470 GLU D 445 CG CD OE1 OE2
REMARK 470 GLU D 471 CG CD OE1 OE2
REMARK 470 GLN D 473 CG CD OE1 NE2
REMARK 470 SER D 476 OG
REMARK 470 ASP D 480 CG OD1 OD2
REMARK 470 HIS D 481 CG ND1 CD2 CE1 NE2
REMARK 470 GLN D 483 CG CD OE1 NE2
REMARK 470 LYS D 505 CG CD CE NZ
REMARK 470 LYS D 506 CG CD CE NZ
REMARK 470 GLN D 508 CG CD OE1 NE2
REMARK 470 GLU E 79 CG CD OE1 OE2
REMARK 470 LYS E 80 CG CD CE NZ
REMARK 470 LYS E 138 CG CD CE NZ
REMARK 470 LYS E 436 CG CD CE NZ
REMARK 470 TYR E 439 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS E 440 CG CD CE NZ
REMARK 470 ILE E 441 CG1 CG2 CD1
REMARK 470 SER E 442 OG
REMARK 470 GLU E 445 CG CD OE1 OE2
REMARK 470 LYS E 459 CG CD CE NZ
REMARK 470 GLU E 471 CG CD OE1 OE2
REMARK 470 GLN E 473 CG CD OE1 NE2
REMARK 470 SER E 476 OG
REMARK 470 GLN E 483 CG CD OE1 NE2
REMARK 470 ARG E 497 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 505 CG CD CE NZ
REMARK 470 LYS E 506 CG CD CE NZ
REMARK 470 GLN E 508 CG CD OE1 NE2
REMARK 470 GLU F 79 CG CD OE1 OE2
REMARK 470 LYS F 436 CG CD CE NZ
REMARK 470 TYR F 439 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS F 440 CG CD CE NZ
REMARK 470 ILE F 441 CG1 CG2 CD1
REMARK 470 GLU F 445 CG CD OE1 OE2
REMARK 470 LYS F 459 CG CD CE NZ
REMARK 470 SER F 476 OG
REMARK 470 HIS F 481 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH E 549 O HOH E 744 2.03
REMARK 500 OH TYR B 157 O HOH B 651 2.16
REMARK 500 OE2 GLU B 344 OH TYR B 468 2.18
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 ALA B 324 O HOH B 589 4575 2.18
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 427 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG F 353 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG F 427 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG F 427 NE - CZ - NH2 ANGL. DEV. = -3.5 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 TYR A 39 -134.57 -104.40
REMARK 500 TRP A 51 -60.30 74.29
REMARK 500 CYS A 172 -171.24 -171.98
REMARK 500 GLU A 209 60.27 34.38
REMARK 500 GLN A 220 145.88 -173.31
REMARK 500 CYS A 296 139.42 -172.74
REMARK 500 LEU A 339 -36.67 -132.70
REMARK 500 MET A 347 149.88 -173.30
REMARK 500 TRP A 380 -145.33 -71.99
REMARK 500 GLU A 387 68.97 -102.44
REMARK 500 SER A 449 -85.68 -124.70
REMARK 500 ASP A 480 -116.22 52.65
REMARK 500 TYR B 39 -134.82 -111.37
REMARK 500 TRP B 51 -59.89 68.76
REMARK 500 CYS B 172 -178.31 -176.16
REMARK 500 GLU B 209 60.04 33.88
REMARK 500 CYS B 296 137.45 -174.69
REMARK 500 TYR B 306 138.15 -171.52
REMARK 500 MET B 347 146.69 -170.91
REMARK 500 TRP B 380 -146.06 -73.87
REMARK 500 SER B 449 -74.06 -125.57
REMARK 500 ASP B 480 -122.87 52.57
REMARK 500 LEU B 496 61.86 30.26
REMARK 500 TYR C 39 -135.46 -113.31
REMARK 500 TRP C 51 -59.99 74.69
REMARK 500 ASP C 78 -157.87 -81.53
REMARK 500 ALA C 105 -169.64 -73.39
REMARK 500 ASN C 146 57.45 -117.12
REMARK 500 CYS C 172 -157.37 -170.55
REMARK 500 ASN C 174 54.93 -61.55
REMARK 500 GLU C 209 60.67 25.31
REMARK 500 GLN C 245 39.70 73.79
REMARK 500 SER C 286 128.91 -35.30
REMARK 500 LEU C 288 -19.01 -49.15
REMARK 500 TRP C 303 -0.09 68.54
REMARK 500 GLU C 335 122.32 174.11
REMARK 500 ILE C 338 94.26 -58.58
REMARK 500 MET C 347 144.90 -179.11
REMARK 500 TRP C 380 -146.42 -73.36
REMARK 500 TYR C 422 -62.59 -93.14
REMARK 500 MET C 430 151.11 -49.53
REMARK 500 SER C 449 -71.91 -137.16
REMARK 500 ASP C 480 -116.38 20.76
REMARK 500 ILE C 492 -19.50 -47.63
REMARK 500 LEU C 496 52.77 28.27
REMARK 500 ARG C 512 75.67 58.89
REMARK 500 TYR D 39 -128.13 -118.07
REMARK 500 TRP D 51 -53.14 65.26
REMARK 500 ARG D 75 76.40 -101.11
REMARK 500 ARG D 103 -48.03 -24.17
REMARK 500
REMARK 500 THIS ENTRY HAS 91 RAMACHANDRAN OUTLIERS.
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 THR E 346 MET E 347 -149.05
REMARK 500 THR F 346 MET F 347 -147.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-11098O RELATED DB: TARGETDB
DBREF 3CLW A 27 522 UNP Q5LF82 Q5LF82_BACFN 27 522
DBREF 3CLW B 27 522 UNP Q5LF82 Q5LF82_BACFN 27 522
DBREF 3CLW C 27 522 UNP Q5LF82 Q5LF82_BACFN 27 522
DBREF 3CLW D 27 522 UNP Q5LF82 Q5LF82_BACFN 27 522
DBREF 3CLW E 27 522 UNP Q5LF82 Q5LF82_BACFN 27 522
DBREF 3CLW F 27 522 UNP Q5LF82 Q5LF82_BACFN 27 522
SEQADV 3CLW MET A 24 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW SER A 25 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW LEU A 26 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLU A 523 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLY A 524 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS A 525 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS A 526 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS A 527 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS A 528 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS A 529 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS A 530 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW MET B 24 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW SER B 25 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW LEU B 26 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLU B 523 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLY B 524 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS B 525 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS B 526 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS B 527 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS B 528 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS B 529 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS B 530 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW MET C 24 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW SER C 25 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW LEU C 26 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLU C 523 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLY C 524 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS C 525 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS C 526 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS C 527 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS C 528 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS C 529 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS C 530 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW MET D 24 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW SER D 25 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW LEU D 26 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLU D 523 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLY D 524 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS D 525 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS D 526 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS D 527 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS D 528 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS D 529 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS D 530 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW MET E 24 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW SER E 25 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW LEU E 26 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLU E 523 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLY E 524 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS E 525 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS E 526 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS E 527 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS E 528 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS E 529 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS E 530 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW MET F 24 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW SER F 25 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW LEU F 26 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLU F 523 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW GLY F 524 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS F 525 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS F 526 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS F 527 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS F 528 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS F 529 UNP Q5LF82 EXPRESSION TAG
SEQADV 3CLW HIS F 530 UNP Q5LF82 EXPRESSION TAG
SEQRES 1 A 507 MET SER LEU ASN LYS LYS VAL PHE ILE ILE ASP LYS GLN
SEQRES 2 A 507 THR VAL TYR GLN GLU ILE ASP ASN PHE SER ALA SER ASP
SEQRES 3 A 507 ALA TRP ARG CYS ALA PHE ILE GLY LYS ASN TRP PRO GLN
SEQRES 4 A 507 GLU LYS LYS GLU LYS ILE ALA ASP LEU LEU PHE LYS ARG
SEQRES 5 A 507 GLU PHE ASP GLU LYS GLY ASN PRO ILE GLY MET ALA LEU
SEQRES 6 A 507 THR ASN TRP ARG VAL ASN ILE GLY ALA GLY SER TYR GLU
SEQRES 7 A 507 ASN ARG GLU ALA LYS GLU VAL ASP ASN SER TRP ASN ARG
SEQRES 8 A 507 THR GLU CYS PHE LEU SER PRO ASP GLY LYS TYR ASP PHE
SEQRES 9 A 507 THR LYS GLN ALA GLY GLN GLN TRP PHE MET LYS ALA ALA
SEQRES 10 A 507 ARG GLU ARG GLY MET ASN ASN PHE LEU PHE PHE THR ASN
SEQRES 11 A 507 SER ALA PRO TYR PHE MET THR ARG SER ALA SER THR VAL
SEQRES 12 A 507 SER THR ASP GLN ASP CYS ILE ASN LEU GLN ASN ASP LYS
SEQRES 13 A 507 PHE ASP ASP PHE ALA ARG PHE LEU VAL LYS SER ALA GLN
SEQRES 14 A 507 HIS PHE ARG GLU GLN GLY PHE HIS VAL ASN TYR ILE SER
SEQRES 15 A 507 PRO ASN ASN GLU PRO ASN GLY GLN TRP HIS ALA ASN SER
SEQRES 16 A 507 PHE GLN GLU GLY SER PHE ALA THR LYS ALA ASP LEU TYR
SEQRES 17 A 507 ARG MET VAL GLU GLU LEU ASP LYS ALA ILE SER GLU ALA
SEQRES 18 A 507 GLN ILE ASP THR LYS ILE LEU ILE PRO GLU VAL GLY ASP
SEQRES 19 A 507 MET LYS TYR LEU PHE GLU ILE ASP SER ILE ALA LYS THR
SEQRES 20 A 507 PRO ASP ASP ILE ILE HIS SER MET PHE TYR LYS ASP GLY
SEQRES 21 A 507 GLN TYR SER VAL LEU LYS PHE LYS ASN LEU PHE ASN CYS
SEQRES 22 A 507 VAL ALA ALA HIS ASP TYR TRP SER ALA TYR PRO ALA THR
SEQRES 23 A 507 LEU LEU VAL ASP ILE ARG ASN ARG ILE HIS LYS GLU LEU
SEQRES 24 A 507 SER ALA ASN GLY HIS ASN THR LYS PHE TRP ALA SER GLU
SEQRES 25 A 507 TYR CYS ILE LEU GLU LYS ASN GLU GLU ILE THR MET PRO
SEQRES 26 A 507 ALA SER PRO GLU ARG SER ILE ASN LEU GLY LEU TYR VAL
SEQRES 27 A 507 ALA ARG ILE ILE HIS ASN ASP LEU THR LEU ALA ASN ALA
SEQRES 28 A 507 SER ALA TRP GLN TRP TRP THR ALA VAL SER LEU GLY GLU
SEQRES 29 A 507 ASP VAL PRO ILE GLN LEU LEU PRO LEU GLU GLY SER ASN
SEQRES 30 A 507 GLY LEU SER LEU GLN TYR ASP GLY GLU ILE SER THR THR
SEQRES 31 A 507 LYS MET LEU TRP THR THR ALA ASN TYR SER PHE PHE VAL
SEQRES 32 A 507 ARG PRO GLY MET LYS ARG ILE ALA ILE LYS PRO THR TYR
SEQRES 33 A 507 LYS ILE SER ASP LEU GLU ALA ALA THR SER LEU MET ILE
SEQRES 34 A 507 SER SER TYR THR ASP GLY LYS GLU VAL VAL THR VAL ALA
SEQRES 35 A 507 ILE ASN TYR SER LYS GLU ASN GLN VAL ILE SER LEU ASN
SEQRES 36 A 507 CYS ASP HIS ALA GLN LYS GLY LYS VAL TYR LEU THR THR
SEQRES 37 A 507 ILE ASP LYS ASN LEU ARG TYR MET GLY GLU GLN PRO LEU
SEQRES 38 A 507 LYS LYS LEU GLN LEU PRO ALA ARG SER VAL ALA THR ILE
SEQRES 39 A 507 VAL VAL GLU ASP ASN GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 507 MET SER LEU ASN LYS LYS VAL PHE ILE ILE ASP LYS GLN
SEQRES 2 B 507 THR VAL TYR GLN GLU ILE ASP ASN PHE SER ALA SER ASP
SEQRES 3 B 507 ALA TRP ARG CYS ALA PHE ILE GLY LYS ASN TRP PRO GLN
SEQRES 4 B 507 GLU LYS LYS GLU LYS ILE ALA ASP LEU LEU PHE LYS ARG
SEQRES 5 B 507 GLU PHE ASP GLU LYS GLY ASN PRO ILE GLY MET ALA LEU
SEQRES 6 B 507 THR ASN TRP ARG VAL ASN ILE GLY ALA GLY SER TYR GLU
SEQRES 7 B 507 ASN ARG GLU ALA LYS GLU VAL ASP ASN SER TRP ASN ARG
SEQRES 8 B 507 THR GLU CYS PHE LEU SER PRO ASP GLY LYS TYR ASP PHE
SEQRES 9 B 507 THR LYS GLN ALA GLY GLN GLN TRP PHE MET LYS ALA ALA
SEQRES 10 B 507 ARG GLU ARG GLY MET ASN ASN PHE LEU PHE PHE THR ASN
SEQRES 11 B 507 SER ALA PRO TYR PHE MET THR ARG SER ALA SER THR VAL
SEQRES 12 B 507 SER THR ASP GLN ASP CYS ILE ASN LEU GLN ASN ASP LYS
SEQRES 13 B 507 PHE ASP ASP PHE ALA ARG PHE LEU VAL LYS SER ALA GLN
SEQRES 14 B 507 HIS PHE ARG GLU GLN GLY PHE HIS VAL ASN TYR ILE SER
SEQRES 15 B 507 PRO ASN ASN GLU PRO ASN GLY GLN TRP HIS ALA ASN SER
SEQRES 16 B 507 PHE GLN GLU GLY SER PHE ALA THR LYS ALA ASP LEU TYR
SEQRES 17 B 507 ARG MET VAL GLU GLU LEU ASP LYS ALA ILE SER GLU ALA
SEQRES 18 B 507 GLN ILE ASP THR LYS ILE LEU ILE PRO GLU VAL GLY ASP
SEQRES 19 B 507 MET LYS TYR LEU PHE GLU ILE ASP SER ILE ALA LYS THR
SEQRES 20 B 507 PRO ASP ASP ILE ILE HIS SER MET PHE TYR LYS ASP GLY
SEQRES 21 B 507 GLN TYR SER VAL LEU LYS PHE LYS ASN LEU PHE ASN CYS
SEQRES 22 B 507 VAL ALA ALA HIS ASP TYR TRP SER ALA TYR PRO ALA THR
SEQRES 23 B 507 LEU LEU VAL ASP ILE ARG ASN ARG ILE HIS LYS GLU LEU
SEQRES 24 B 507 SER ALA ASN GLY HIS ASN THR LYS PHE TRP ALA SER GLU
SEQRES 25 B 507 TYR CYS ILE LEU GLU LYS ASN GLU GLU ILE THR MET PRO
SEQRES 26 B 507 ALA SER PRO GLU ARG SER ILE ASN LEU GLY LEU TYR VAL
SEQRES 27 B 507 ALA ARG ILE ILE HIS ASN ASP LEU THR LEU ALA ASN ALA
SEQRES 28 B 507 SER ALA TRP GLN TRP TRP THR ALA VAL SER LEU GLY GLU
SEQRES 29 B 507 ASP VAL PRO ILE GLN LEU LEU PRO LEU GLU GLY SER ASN
SEQRES 30 B 507 GLY LEU SER LEU GLN TYR ASP GLY GLU ILE SER THR THR
SEQRES 31 B 507 LYS MET LEU TRP THR THR ALA ASN TYR SER PHE PHE VAL
SEQRES 32 B 507 ARG PRO GLY MET LYS ARG ILE ALA ILE LYS PRO THR TYR
SEQRES 33 B 507 LYS ILE SER ASP LEU GLU ALA ALA THR SER LEU MET ILE
SEQRES 34 B 507 SER SER TYR THR ASP GLY LYS GLU VAL VAL THR VAL ALA
SEQRES 35 B 507 ILE ASN TYR SER LYS GLU ASN GLN VAL ILE SER LEU ASN
SEQRES 36 B 507 CYS ASP HIS ALA GLN LYS GLY LYS VAL TYR LEU THR THR
SEQRES 37 B 507 ILE ASP LYS ASN LEU ARG TYR MET GLY GLU GLN PRO LEU
SEQRES 38 B 507 LYS LYS LEU GLN LEU PRO ALA ARG SER VAL ALA THR ILE
SEQRES 39 B 507 VAL VAL GLU ASP ASN GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 507 MET SER LEU ASN LYS LYS VAL PHE ILE ILE ASP LYS GLN
SEQRES 2 C 507 THR VAL TYR GLN GLU ILE ASP ASN PHE SER ALA SER ASP
SEQRES 3 C 507 ALA TRP ARG CYS ALA PHE ILE GLY LYS ASN TRP PRO GLN
SEQRES 4 C 507 GLU LYS LYS GLU LYS ILE ALA ASP LEU LEU PHE LYS ARG
SEQRES 5 C 507 GLU PHE ASP GLU LYS GLY ASN PRO ILE GLY MET ALA LEU
SEQRES 6 C 507 THR ASN TRP ARG VAL ASN ILE GLY ALA GLY SER TYR GLU
SEQRES 7 C 507 ASN ARG GLU ALA LYS GLU VAL ASP ASN SER TRP ASN ARG
SEQRES 8 C 507 THR GLU CYS PHE LEU SER PRO ASP GLY LYS TYR ASP PHE
SEQRES 9 C 507 THR LYS GLN ALA GLY GLN GLN TRP PHE MET LYS ALA ALA
SEQRES 10 C 507 ARG GLU ARG GLY MET ASN ASN PHE LEU PHE PHE THR ASN
SEQRES 11 C 507 SER ALA PRO TYR PHE MET THR ARG SER ALA SER THR VAL
SEQRES 12 C 507 SER THR ASP GLN ASP CYS ILE ASN LEU GLN ASN ASP LYS
SEQRES 13 C 507 PHE ASP ASP PHE ALA ARG PHE LEU VAL LYS SER ALA GLN
SEQRES 14 C 507 HIS PHE ARG GLU GLN GLY PHE HIS VAL ASN TYR ILE SER
SEQRES 15 C 507 PRO ASN ASN GLU PRO ASN GLY GLN TRP HIS ALA ASN SER
SEQRES 16 C 507 PHE GLN GLU GLY SER PHE ALA THR LYS ALA ASP LEU TYR
SEQRES 17 C 507 ARG MET VAL GLU GLU LEU ASP LYS ALA ILE SER GLU ALA
SEQRES 18 C 507 GLN ILE ASP THR LYS ILE LEU ILE PRO GLU VAL GLY ASP
SEQRES 19 C 507 MET LYS TYR LEU PHE GLU ILE ASP SER ILE ALA LYS THR
SEQRES 20 C 507 PRO ASP ASP ILE ILE HIS SER MET PHE TYR LYS ASP GLY
SEQRES 21 C 507 GLN TYR SER VAL LEU LYS PHE LYS ASN LEU PHE ASN CYS
SEQRES 22 C 507 VAL ALA ALA HIS ASP TYR TRP SER ALA TYR PRO ALA THR
SEQRES 23 C 507 LEU LEU VAL ASP ILE ARG ASN ARG ILE HIS LYS GLU LEU
SEQRES 24 C 507 SER ALA ASN GLY HIS ASN THR LYS PHE TRP ALA SER GLU
SEQRES 25 C 507 TYR CYS ILE LEU GLU LYS ASN GLU GLU ILE THR MET PRO
SEQRES 26 C 507 ALA SER PRO GLU ARG SER ILE ASN LEU GLY LEU TYR VAL
SEQRES 27 C 507 ALA ARG ILE ILE HIS ASN ASP LEU THR LEU ALA ASN ALA
SEQRES 28 C 507 SER ALA TRP GLN TRP TRP THR ALA VAL SER LEU GLY GLU
SEQRES 29 C 507 ASP VAL PRO ILE GLN LEU LEU PRO LEU GLU GLY SER ASN
SEQRES 30 C 507 GLY LEU SER LEU GLN TYR ASP GLY GLU ILE SER THR THR
SEQRES 31 C 507 LYS MET LEU TRP THR THR ALA ASN TYR SER PHE PHE VAL
SEQRES 32 C 507 ARG PRO GLY MET LYS ARG ILE ALA ILE LYS PRO THR TYR
SEQRES 33 C 507 LYS ILE SER ASP LEU GLU ALA ALA THR SER LEU MET ILE
SEQRES 34 C 507 SER SER TYR THR ASP GLY LYS GLU VAL VAL THR VAL ALA
SEQRES 35 C 507 ILE ASN TYR SER LYS GLU ASN GLN VAL ILE SER LEU ASN
SEQRES 36 C 507 CYS ASP HIS ALA GLN LYS GLY LYS VAL TYR LEU THR THR
SEQRES 37 C 507 ILE ASP LYS ASN LEU ARG TYR MET GLY GLU GLN PRO LEU
SEQRES 38 C 507 LYS LYS LEU GLN LEU PRO ALA ARG SER VAL ALA THR ILE
SEQRES 39 C 507 VAL VAL GLU ASP ASN GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 D 507 MET SER LEU ASN LYS LYS VAL PHE ILE ILE ASP LYS GLN
SEQRES 2 D 507 THR VAL TYR GLN GLU ILE ASP ASN PHE SER ALA SER ASP
SEQRES 3 D 507 ALA TRP ARG CYS ALA PHE ILE GLY LYS ASN TRP PRO GLN
SEQRES 4 D 507 GLU LYS LYS GLU LYS ILE ALA ASP LEU LEU PHE LYS ARG
SEQRES 5 D 507 GLU PHE ASP GLU LYS GLY ASN PRO ILE GLY MET ALA LEU
SEQRES 6 D 507 THR ASN TRP ARG VAL ASN ILE GLY ALA GLY SER TYR GLU
SEQRES 7 D 507 ASN ARG GLU ALA LYS GLU VAL ASP ASN SER TRP ASN ARG
SEQRES 8 D 507 THR GLU CYS PHE LEU SER PRO ASP GLY LYS TYR ASP PHE
SEQRES 9 D 507 THR LYS GLN ALA GLY GLN GLN TRP PHE MET LYS ALA ALA
SEQRES 10 D 507 ARG GLU ARG GLY MET ASN ASN PHE LEU PHE PHE THR ASN
SEQRES 11 D 507 SER ALA PRO TYR PHE MET THR ARG SER ALA SER THR VAL
SEQRES 12 D 507 SER THR ASP GLN ASP CYS ILE ASN LEU GLN ASN ASP LYS
SEQRES 13 D 507 PHE ASP ASP PHE ALA ARG PHE LEU VAL LYS SER ALA GLN
SEQRES 14 D 507 HIS PHE ARG GLU GLN GLY PHE HIS VAL ASN TYR ILE SER
SEQRES 15 D 507 PRO ASN ASN GLU PRO ASN GLY GLN TRP HIS ALA ASN SER
SEQRES 16 D 507 PHE GLN GLU GLY SER PHE ALA THR LYS ALA ASP LEU TYR
SEQRES 17 D 507 ARG MET VAL GLU GLU LEU ASP LYS ALA ILE SER GLU ALA
SEQRES 18 D 507 GLN ILE ASP THR LYS ILE LEU ILE PRO GLU VAL GLY ASP
SEQRES 19 D 507 MET LYS TYR LEU PHE GLU ILE ASP SER ILE ALA LYS THR
SEQRES 20 D 507 PRO ASP ASP ILE ILE HIS SER MET PHE TYR LYS ASP GLY
SEQRES 21 D 507 GLN TYR SER VAL LEU LYS PHE LYS ASN LEU PHE ASN CYS
SEQRES 22 D 507 VAL ALA ALA HIS ASP TYR TRP SER ALA TYR PRO ALA THR
SEQRES 23 D 507 LEU LEU VAL ASP ILE ARG ASN ARG ILE HIS LYS GLU LEU
SEQRES 24 D 507 SER ALA ASN GLY HIS ASN THR LYS PHE TRP ALA SER GLU
SEQRES 25 D 507 TYR CYS ILE LEU GLU LYS ASN GLU GLU ILE THR MET PRO
SEQRES 26 D 507 ALA SER PRO GLU ARG SER ILE ASN LEU GLY LEU TYR VAL
SEQRES 27 D 507 ALA ARG ILE ILE HIS ASN ASP LEU THR LEU ALA ASN ALA
SEQRES 28 D 507 SER ALA TRP GLN TRP TRP THR ALA VAL SER LEU GLY GLU
SEQRES 29 D 507 ASP VAL PRO ILE GLN LEU LEU PRO LEU GLU GLY SER ASN
SEQRES 30 D 507 GLY LEU SER LEU GLN TYR ASP GLY GLU ILE SER THR THR
SEQRES 31 D 507 LYS MET LEU TRP THR THR ALA ASN TYR SER PHE PHE VAL
SEQRES 32 D 507 ARG PRO GLY MET LYS ARG ILE ALA ILE LYS PRO THR TYR
SEQRES 33 D 507 LYS ILE SER ASP LEU GLU ALA ALA THR SER LEU MET ILE
SEQRES 34 D 507 SER SER TYR THR ASP GLY LYS GLU VAL VAL THR VAL ALA
SEQRES 35 D 507 ILE ASN TYR SER LYS GLU ASN GLN VAL ILE SER LEU ASN
SEQRES 36 D 507 CYS ASP HIS ALA GLN LYS GLY LYS VAL TYR LEU THR THR
SEQRES 37 D 507 ILE ASP LYS ASN LEU ARG TYR MET GLY GLU GLN PRO LEU
SEQRES 38 D 507 LYS LYS LEU GLN LEU PRO ALA ARG SER VAL ALA THR ILE
SEQRES 39 D 507 VAL VAL GLU ASP ASN GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 E 507 MET SER LEU ASN LYS LYS VAL PHE ILE ILE ASP LYS GLN
SEQRES 2 E 507 THR VAL TYR GLN GLU ILE ASP ASN PHE SER ALA SER ASP
SEQRES 3 E 507 ALA TRP ARG CYS ALA PHE ILE GLY LYS ASN TRP PRO GLN
SEQRES 4 E 507 GLU LYS LYS GLU LYS ILE ALA ASP LEU LEU PHE LYS ARG
SEQRES 5 E 507 GLU PHE ASP GLU LYS GLY ASN PRO ILE GLY MET ALA LEU
SEQRES 6 E 507 THR ASN TRP ARG VAL ASN ILE GLY ALA GLY SER TYR GLU
SEQRES 7 E 507 ASN ARG GLU ALA LYS GLU VAL ASP ASN SER TRP ASN ARG
SEQRES 8 E 507 THR GLU CYS PHE LEU SER PRO ASP GLY LYS TYR ASP PHE
SEQRES 9 E 507 THR LYS GLN ALA GLY GLN GLN TRP PHE MET LYS ALA ALA
SEQRES 10 E 507 ARG GLU ARG GLY MET ASN ASN PHE LEU PHE PHE THR ASN
SEQRES 11 E 507 SER ALA PRO TYR PHE MET THR ARG SER ALA SER THR VAL
SEQRES 12 E 507 SER THR ASP GLN ASP CYS ILE ASN LEU GLN ASN ASP LYS
SEQRES 13 E 507 PHE ASP ASP PHE ALA ARG PHE LEU VAL LYS SER ALA GLN
SEQRES 14 E 507 HIS PHE ARG GLU GLN GLY PHE HIS VAL ASN TYR ILE SER
SEQRES 15 E 507 PRO ASN ASN GLU PRO ASN GLY GLN TRP HIS ALA ASN SER
SEQRES 16 E 507 PHE GLN GLU GLY SER PHE ALA THR LYS ALA ASP LEU TYR
SEQRES 17 E 507 ARG MET VAL GLU GLU LEU ASP LYS ALA ILE SER GLU ALA
SEQRES 18 E 507 GLN ILE ASP THR LYS ILE LEU ILE PRO GLU VAL GLY ASP
SEQRES 19 E 507 MET LYS TYR LEU PHE GLU ILE ASP SER ILE ALA LYS THR
SEQRES 20 E 507 PRO ASP ASP ILE ILE HIS SER MET PHE TYR LYS ASP GLY
SEQRES 21 E 507 GLN TYR SER VAL LEU LYS PHE LYS ASN LEU PHE ASN CYS
SEQRES 22 E 507 VAL ALA ALA HIS ASP TYR TRP SER ALA TYR PRO ALA THR
SEQRES 23 E 507 LEU LEU VAL ASP ILE ARG ASN ARG ILE HIS LYS GLU LEU
SEQRES 24 E 507 SER ALA ASN GLY HIS ASN THR LYS PHE TRP ALA SER GLU
SEQRES 25 E 507 TYR CYS ILE LEU GLU LYS ASN GLU GLU ILE THR MET PRO
SEQRES 26 E 507 ALA SER PRO GLU ARG SER ILE ASN LEU GLY LEU TYR VAL
SEQRES 27 E 507 ALA ARG ILE ILE HIS ASN ASP LEU THR LEU ALA ASN ALA
SEQRES 28 E 507 SER ALA TRP GLN TRP TRP THR ALA VAL SER LEU GLY GLU
SEQRES 29 E 507 ASP VAL PRO ILE GLN LEU LEU PRO LEU GLU GLY SER ASN
SEQRES 30 E 507 GLY LEU SER LEU GLN TYR ASP GLY GLU ILE SER THR THR
SEQRES 31 E 507 LYS MET LEU TRP THR THR ALA ASN TYR SER PHE PHE VAL
SEQRES 32 E 507 ARG PRO GLY MET LYS ARG ILE ALA ILE LYS PRO THR TYR
SEQRES 33 E 507 LYS ILE SER ASP LEU GLU ALA ALA THR SER LEU MET ILE
SEQRES 34 E 507 SER SER TYR THR ASP GLY LYS GLU VAL VAL THR VAL ALA
SEQRES 35 E 507 ILE ASN TYR SER LYS GLU ASN GLN VAL ILE SER LEU ASN
SEQRES 36 E 507 CYS ASP HIS ALA GLN LYS GLY LYS VAL TYR LEU THR THR
SEQRES 37 E 507 ILE ASP LYS ASN LEU ARG TYR MET GLY GLU GLN PRO LEU
SEQRES 38 E 507 LYS LYS LEU GLN LEU PRO ALA ARG SER VAL ALA THR ILE
SEQRES 39 E 507 VAL VAL GLU ASP ASN GLU GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 F 507 MET SER LEU ASN LYS LYS VAL PHE ILE ILE ASP LYS GLN
SEQRES 2 F 507 THR VAL TYR GLN GLU ILE ASP ASN PHE SER ALA SER ASP
SEQRES 3 F 507 ALA TRP ARG CYS ALA PHE ILE GLY LYS ASN TRP PRO GLN
SEQRES 4 F 507 GLU LYS LYS GLU LYS ILE ALA ASP LEU LEU PHE LYS ARG
SEQRES 5 F 507 GLU PHE ASP GLU LYS GLY ASN PRO ILE GLY MET ALA LEU
SEQRES 6 F 507 THR ASN TRP ARG VAL ASN ILE GLY ALA GLY SER TYR GLU
SEQRES 7 F 507 ASN ARG GLU ALA LYS GLU VAL ASP ASN SER TRP ASN ARG
SEQRES 8 F 507 THR GLU CYS PHE LEU SER PRO ASP GLY LYS TYR ASP PHE
SEQRES 9 F 507 THR LYS GLN ALA GLY GLN GLN TRP PHE MET LYS ALA ALA
SEQRES 10 F 507 ARG GLU ARG GLY MET ASN ASN PHE LEU PHE PHE THR ASN
SEQRES 11 F 507 SER ALA PRO TYR PHE MET THR ARG SER ALA SER THR VAL
SEQRES 12 F 507 SER THR ASP GLN ASP CYS ILE ASN LEU GLN ASN ASP LYS
SEQRES 13 F 507 PHE ASP ASP PHE ALA ARG PHE LEU VAL LYS SER ALA GLN
SEQRES 14 F 507 HIS PHE ARG GLU GLN GLY PHE HIS VAL ASN TYR ILE SER
SEQRES 15 F 507 PRO ASN ASN GLU PRO ASN GLY GLN TRP HIS ALA ASN SER
SEQRES 16 F 507 PHE GLN GLU GLY SER PHE ALA THR LYS ALA ASP LEU TYR
SEQRES 17 F 507 ARG MET VAL GLU GLU LEU ASP LYS ALA ILE SER GLU ALA
SEQRES 18 F 507 GLN ILE ASP THR LYS ILE LEU ILE PRO GLU VAL GLY ASP
SEQRES 19 F 507 MET LYS TYR LEU PHE GLU ILE ASP SER ILE ALA LYS THR
SEQRES 20 F 507 PRO ASP ASP ILE ILE HIS SER MET PHE TYR LYS ASP GLY
SEQRES 21 F 507 GLN TYR SER VAL LEU LYS PHE LYS ASN LEU PHE ASN CYS
SEQRES 22 F 507 VAL ALA ALA HIS ASP TYR TRP SER ALA TYR PRO ALA THR
SEQRES 23 F 507 LEU LEU VAL ASP ILE ARG ASN ARG ILE HIS LYS GLU LEU
SEQRES 24 F 507 SER ALA ASN GLY HIS ASN THR LYS PHE TRP ALA SER GLU
SEQRES 25 F 507 TYR CYS ILE LEU GLU LYS ASN GLU GLU ILE THR MET PRO
SEQRES 26 F 507 ALA SER PRO GLU ARG SER ILE ASN LEU GLY LEU TYR VAL
SEQRES 27 F 507 ALA ARG ILE ILE HIS ASN ASP LEU THR LEU ALA ASN ALA
SEQRES 28 F 507 SER ALA TRP GLN TRP TRP THR ALA VAL SER LEU GLY GLU
SEQRES 29 F 507 ASP VAL PRO ILE GLN LEU LEU PRO LEU GLU GLY SER ASN
SEQRES 30 F 507 GLY LEU SER LEU GLN TYR ASP GLY GLU ILE SER THR THR
SEQRES 31 F 507 LYS MET LEU TRP THR THR ALA ASN TYR SER PHE PHE VAL
SEQRES 32 F 507 ARG PRO GLY MET LYS ARG ILE ALA ILE LYS PRO THR TYR
SEQRES 33 F 507 LYS ILE SER ASP LEU GLU ALA ALA THR SER LEU MET ILE
SEQRES 34 F 507 SER SER TYR THR ASP GLY LYS GLU VAL VAL THR VAL ALA
SEQRES 35 F 507 ILE ASN TYR SER LYS GLU ASN GLN VAL ILE SER LEU ASN
SEQRES 36 F 507 CYS ASP HIS ALA GLN LYS GLY LYS VAL TYR LEU THR THR
SEQRES 37 F 507 ILE ASP LYS ASN LEU ARG TYR MET GLY GLU GLN PRO LEU
SEQRES 38 F 507 LYS LYS LEU GLN LEU PRO ALA ARG SER VAL ALA THR ILE
SEQRES 39 F 507 VAL VAL GLU ASP ASN GLU GLY HIS HIS HIS HIS HIS HIS
FORMUL 7 HOH *944(H2 O)
HELIX 1 1 ARG A 52 TRP A 60 1 9
HELIX 2 2 PRO A 61 LYS A 74 1 14
HELIX 3 3 GLN A 130 ARG A 143 1 14
HELIX 4 4 PRO A 156 THR A 160 5 5
HELIX 5 5 LYS A 179 GLN A 197 1 19
HELIX 6 6 GLN A 213 ASN A 217 5 5
HELIX 7 7 THR A 226 GLN A 245 1 20
HELIX 8 8 ASP A 257 PHE A 262 5 6
HELIX 9 9 ASP A 273 TYR A 280 1 8
HELIX 10 10 PRO A 307 ALA A 324 1 18
HELIX 11 11 SER A 350 LEU A 371 1 22
HELIX 12 12 GLY A 401 TYR A 406 5 6
HELIX 13 13 THR A 413 PHE A 424 1 12
HELIX 14 14 SER A 442 ALA A 447 1 6
HELIX 15 15 ARG B 52 TRP B 60 1 9
HELIX 16 16 PRO B 61 LYS B 74 1 14
HELIX 17 17 GLN B 130 ARG B 143 1 14
HELIX 18 18 PRO B 156 THR B 160 5 5
HELIX 19 19 LYS B 179 GLU B 196 1 18
HELIX 20 20 GLN B 213 ASN B 217 5 5
HELIX 21 21 THR B 226 GLN B 245 1 20
HELIX 22 22 ASP B 257 PHE B 262 5 6
HELIX 23 23 ASP B 273 TYR B 280 1 8
HELIX 24 24 PRO B 307 ALA B 324 1 18
HELIX 25 25 SER B 350 LEU B 371 1 22
HELIX 26 26 GLY B 401 TYR B 406 5 6
HELIX 27 27 THR B 413 PHE B 424 1 12
HELIX 28 28 SER B 442 ALA B 447 1 6
HELIX 29 29 ARG C 52 TRP C 60 1 9
HELIX 30 30 PRO C 61 LYS C 74 1 14
HELIX 31 31 GLN C 130 ARG C 143 1 14
HELIX 32 32 LYS C 179 GLU C 196 1 18
HELIX 33 33 GLN C 213 ASN C 217 5 5
HELIX 34 34 THR C 226 GLN C 245 1 20
HELIX 35 35 ASP C 257 PHE C 262 5 6
HELIX 36 36 ASP C 273 TYR C 280 1 8
HELIX 37 37 PRO C 307 ALA C 324 1 18
HELIX 38 38 SER C 350 LEU C 371 1 22
HELIX 39 39 GLY C 401 TYR C 406 5 6
HELIX 40 40 THR C 413 PHE C 424 1 12
HELIX 41 41 SER C 442 ALA C 447 1 6
HELIX 42 42 ARG D 52 TRP D 60 1 9
HELIX 43 43 PRO D 61 LYS D 74 1 14
HELIX 44 44 GLN D 130 ARG D 143 1 14
HELIX 45 45 PRO D 156 THR D 160 5 5
HELIX 46 46 LYS D 179 GLN D 197 1 19
HELIX 47 47 GLN D 213 ASN D 217 5 5
HELIX 48 48 THR D 226 GLN D 245 1 20
HELIX 49 49 ASP D 257 PHE D 262 5 6
HELIX 50 50 ASP D 273 TYR D 280 1 8
HELIX 51 51 PRO D 307 ALA D 324 1 18
HELIX 52 52 SER D 350 LEU D 371 1 22
HELIX 53 53 GLY D 401 TYR D 406 5 6
HELIX 54 54 THR D 413 PHE D 424 1 12
HELIX 55 55 SER D 442 THR D 448 1 7
HELIX 56 56 ARG E 52 TRP E 60 1 9
HELIX 57 57 PRO E 61 LYS E 74 1 14
HELIX 58 58 GLN E 130 ARG E 143 1 14
HELIX 59 59 PRO E 156 THR E 160 5 5
HELIX 60 60 LYS E 179 GLU E 196 1 18
HELIX 61 61 THR E 226 GLN E 245 1 20
HELIX 62 62 ASP E 257 PHE E 262 5 6
HELIX 63 63 ASP E 273 PHE E 279 1 7
HELIX 64 64 PRO E 307 ALA E 324 1 18
HELIX 65 65 SER E 350 LEU E 371 1 22
HELIX 66 66 GLY E 401 TYR E 406 5 6
HELIX 67 67 THR E 413 PHE E 424 1 12
HELIX 68 68 SER E 442 ALA E 447 1 6
HELIX 69 69 ARG F 52 TRP F 60 1 9
HELIX 70 70 PRO F 61 LYS F 74 1 14
HELIX 71 71 GLN F 130 ARG F 143 1 14
HELIX 72 72 PRO F 156 THR F 160 5 5
HELIX 73 73 LYS F 179 GLN F 197 1 19
HELIX 74 74 GLN F 213 ASN F 217 5 5
HELIX 75 75 THR F 226 GLN F 245 1 20
HELIX 76 76 ASP F 257 PHE F 262 5 6
HELIX 77 77 ASP F 273 TYR F 280 1 8
HELIX 78 78 PRO F 307 ALA F 324 1 18
HELIX 79 79 SER F 350 LEU F 371 1 22
HELIX 80 80 GLY F 401 TYR F 406 5 6
HELIX 81 81 THR F 413 PHE F 424 1 12
HELIX 82 82 SER F 442 ALA F 447 1 6
SHEET 1 A 9 ARG A 497 PRO A 503 0
SHEET 2 A 9 LYS A 484 THR A 490 -1 N VAL A 487 O MET A 499
SHEET 3 A 9 SER A 513 VAL A 519 -1 O THR A 516 N TYR A 488
SHEET 4 A 9 VAL A 461 ASN A 467 -1 N VAL A 461 O VAL A 519
SHEET 5 A 9 LEU A 450 THR A 456 -1 N MET A 451 O ILE A 466
SHEET 6 A 9 LYS A 431 PRO A 437 -1 N LYS A 431 O THR A 456
SHEET 7 A 9 LYS A 29 GLU A 41 -1 N TYR A 39 O ARG A 432
SHEET 8 A 9 GLN A 473 ASN A 478 1 O SER A 476 N PHE A 31
SHEET 9 A 9 LEU A 507 LEU A 509 -1 O LEU A 509 N GLN A 473
SHEET 1 B 9 ASN A 44 SER A 48 0
SHEET 2 B 9 TRP A 91 ASN A 94 1 O ARG A 92 N ALA A 47
SHEET 3 B 9 PHE A 148 PHE A 151 1 O LEU A 149 N VAL A 93
SHEET 4 B 9 VAL A 201 SER A 205 1 O SER A 205 N PHE A 150
SHEET 5 B 9 LYS A 249 VAL A 255 1 O LYS A 249 N ASN A 202
SHEET 6 B 9 LEU A 293 ALA A 299 1 O PHE A 294 N ILE A 250
SHEET 7 B 9 LYS A 330 ALA A 333 1 O TRP A 332 N VAL A 297
SHEET 8 B 9 ALA A 376 THR A 381 1 O ALA A 376 N ALA A 333
SHEET 9 B 9 ASN A 44 SER A 48 1 N SER A 46 O TRP A 379
SHEET 1 C 3 VAL A 383 SER A 384 0
SHEET 2 C 3 ILE A 391 LEU A 394 1 O LEU A 393 N SER A 384
SHEET 3 C 3 GLU A 409 THR A 412 -1 O SER A 411 N GLN A 392
SHEET 1 D 9 LYS B 494 PRO B 503 0
SHEET 2 D 9 LYS B 484 THR B 491 -1 N VAL B 487 O MET B 499
SHEET 3 D 9 SER B 513 VAL B 519 -1 O THR B 516 N TYR B 488
SHEET 4 D 9 VAL B 461 ASN B 467 -1 N THR B 463 O ILE B 517
SHEET 5 D 9 LEU B 450 THR B 456 -1 N MET B 451 O ILE B 466
SHEET 6 D 9 LYS B 431 PRO B 437 -1 N LYS B 431 O THR B 456
SHEET 7 D 9 LYS B 29 GLU B 41 -1 N TYR B 39 O ARG B 432
SHEET 8 D 9 GLN B 473 ASN B 478 1 O ASN B 478 N ILE B 33
SHEET 9 D 9 LEU B 507 LEU B 509 -1 O LEU B 509 N GLN B 473
SHEET 1 E 9 ASN B 44 SER B 48 0
SHEET 2 E 9 TRP B 91 ASN B 94 1 O ARG B 92 N ALA B 47
SHEET 3 E 9 PHE B 148 PHE B 151 1 O LEU B 149 N VAL B 93
SHEET 4 E 9 VAL B 201 SER B 205 1 O SER B 205 N PHE B 150
SHEET 5 E 9 LYS B 249 VAL B 255 1 O LYS B 249 N ASN B 202
SHEET 6 E 9 LEU B 293 ALA B 299 1 O PHE B 294 N ILE B 250
SHEET 7 E 9 LYS B 330 ALA B 333 1 O TRP B 332 N VAL B 297
SHEET 8 E 9 ALA B 376 THR B 381 1 O ALA B 376 N ALA B 333
SHEET 9 E 9 ASN B 44 SER B 48 1 N SER B 46 O TRP B 379
SHEET 1 F 3 VAL B 383 SER B 384 0
SHEET 2 F 3 ILE B 391 LEU B 394 1 O LEU B 393 N SER B 384
SHEET 3 F 3 GLU B 409 THR B 412 -1 O SER B 411 N GLN B 392
SHEET 1 G 9 LYS C 494 PRO C 503 0
SHEET 2 G 9 LYS C 484 THR C 491 -1 N VAL C 487 O MET C 499
SHEET 3 G 9 SER C 513 VAL C 519 -1 O VAL C 518 N LYS C 486
SHEET 4 G 9 VAL C 461 ASN C 467 -1 N ALA C 465 O ALA C 515
SHEET 5 G 9 LEU C 450 THR C 456 -1 N TYR C 455 O VAL C 462
SHEET 6 G 9 LYS C 431 PRO C 437 -1 N LYS C 431 O THR C 456
SHEET 7 G 9 VAL C 30 GLU C 41 -1 N TYR C 39 O ARG C 432
SHEET 8 G 9 GLN C 473 ASN C 478 1 O ASN C 478 N ILE C 33
SHEET 9 G 9 LEU C 507 LEU C 509 -1 O LEU C 509 N GLN C 473
SHEET 1 H 9 ASN C 44 SER C 48 0
SHEET 2 H 9 TRP C 91 ASN C 94 1 O ARG C 92 N ALA C 47
SHEET 3 H 9 PHE C 148 PHE C 151 1 O LEU C 149 N VAL C 93
SHEET 4 H 9 VAL C 201 SER C 205 1 O SER C 205 N PHE C 150
SHEET 5 H 9 LYS C 249 VAL C 255 1 O LYS C 249 N ASN C 202
SHEET 6 H 9 LEU C 293 ALA C 299 1 O PHE C 294 N ILE C 250
SHEET 7 H 9 LYS C 330 ALA C 333 1 O LYS C 330 N ASN C 295
SHEET 8 H 9 ALA C 376 THR C 381 1 O GLN C 378 N ALA C 333
SHEET 9 H 9 ASN C 44 SER C 48 1 N SER C 46 O TRP C 379
SHEET 1 I 3 VAL C 383 SER C 384 0
SHEET 2 I 3 ILE C 391 LEU C 394 1 O LEU C 393 N SER C 384
SHEET 3 I 3 GLU C 409 THR C 412 -1 O GLU C 409 N LEU C 394
SHEET 1 J 9 LYS D 494 PRO D 503 0
SHEET 2 J 9 LYS D 484 THR D 491 -1 N GLY D 485 O GLN D 502
SHEET 3 J 9 SER D 513 VAL D 519 -1 O VAL D 514 N THR D 490
SHEET 4 J 9 VAL D 461 ASN D 467 -1 N ALA D 465 O ALA D 515
SHEET 5 J 9 LEU D 450 THR D 456 -1 N MET D 451 O ILE D 466
SHEET 6 J 9 LYS D 431 PRO D 437 -1 N LYS D 431 O THR D 456
SHEET 7 J 9 VAL D 30 GLU D 41 -1 N TYR D 39 O ARG D 432
SHEET 8 J 9 GLN D 473 ASN D 478 1 O ASN D 478 N PHE D 31
SHEET 9 J 9 LEU D 507 LEU D 509 -1 O LEU D 509 N GLN D 473
SHEET 1 K 9 ASN D 44 SER D 48 0
SHEET 2 K 9 TRP D 91 ASN D 94 1 O ARG D 92 N ALA D 47
SHEET 3 K 9 PHE D 148 PHE D 151 1 O LEU D 149 N VAL D 93
SHEET 4 K 9 VAL D 201 SER D 205 1 O SER D 205 N PHE D 150
SHEET 5 K 9 LYS D 249 VAL D 255 1 O LYS D 249 N ASN D 202
SHEET 6 K 9 LEU D 293 ALA D 299 1 O PHE D 294 N ILE D 250
SHEET 7 K 9 LYS D 330 ALA D 333 1 O TRP D 332 N VAL D 297
SHEET 8 K 9 ALA D 376 THR D 381 1 O ALA D 376 N ALA D 333
SHEET 9 K 9 ASN D 44 SER D 48 1 N SER D 46 O TRP D 379
SHEET 1 L 3 VAL D 383 SER D 384 0
SHEET 2 L 3 ILE D 391 LEU D 394 1 O LEU D 393 N SER D 384
SHEET 3 L 3 GLU D 409 THR D 412 -1 O SER D 411 N GLN D 392
SHEET 1 M 9 ARG E 497 PRO E 503 0
SHEET 2 M 9 LYS E 484 THR E 490 -1 N VAL E 487 O MET E 499
SHEET 3 M 9 SER E 513 VAL E 519 -1 O THR E 516 N TYR E 488
SHEET 4 M 9 VAL E 461 ASN E 467 -1 N ALA E 465 O ALA E 515
SHEET 5 M 9 LEU E 450 THR E 456 -1 N MET E 451 O ILE E 466
SHEET 6 M 9 LYS E 431 PRO E 437 -1 N ILE E 433 O SER E 454
SHEET 7 M 9 VAL E 30 GLU E 41 -1 N TYR E 39 O ARG E 432
SHEET 8 M 9 GLN E 473 ASN E 478 1 O ASN E 478 N PHE E 31
SHEET 9 M 9 LEU E 507 LEU E 509 -1 O LEU E 509 N GLN E 473
SHEET 1 N 9 ASN E 44 SER E 48 0
SHEET 2 N 9 TRP E 91 ASN E 94 1 O ARG E 92 N ALA E 47
SHEET 3 N 9 PHE E 148 PHE E 151 1 O LEU E 149 N VAL E 93
SHEET 4 N 9 VAL E 201 SER E 205 1 O SER E 205 N PHE E 150
SHEET 5 N 9 LYS E 249 VAL E 255 1 O LYS E 249 N ILE E 204
SHEET 6 N 9 LEU E 293 ALA E 299 1 O PHE E 294 N ILE E 250
SHEET 7 N 9 LYS E 330 ALA E 333 1 O TRP E 332 N VAL E 297
SHEET 8 N 9 ALA E 376 THR E 381 1 O ALA E 376 N ALA E 333
SHEET 9 N 9 ASN E 44 SER E 48 1 N SER E 46 O TRP E 379
SHEET 1 O 3 VAL E 383 SER E 384 0
SHEET 2 O 3 ILE E 391 LEU E 394 1 O LEU E 393 N SER E 384
SHEET 3 O 3 GLU E 409 THR E 412 -1 O GLU E 409 N LEU E 394
SHEET 1 P 9 LYS F 494 PRO F 503 0
SHEET 2 P 9 LYS F 484 THR F 491 -1 N VAL F 487 O MET F 499
SHEET 3 P 9 SER F 513 VAL F 519 -1 O VAL F 514 N THR F 490
SHEET 4 P 9 VAL F 461 ASN F 467 -1 N ALA F 465 O ALA F 515
SHEET 5 P 9 LEU F 450 THR F 456 -1 N TYR F 455 O VAL F 462
SHEET 6 P 9 LYS F 431 PRO F 437 -1 N LYS F 431 O THR F 456
SHEET 7 P 9 LYS F 29 GLU F 41 -1 N TYR F 39 O ARG F 432
SHEET 8 P 9 GLN F 473 CYS F 479 1 O ASN F 478 N ILE F 33
SHEET 9 P 9 LEU F 507 LEU F 509 -1 O LEU F 509 N GLN F 473
SHEET 1 Q 9 ASN F 44 SER F 48 0
SHEET 2 Q 9 TRP F 91 ASN F 94 1 O ARG F 92 N ALA F 47
SHEET 3 Q 9 PHE F 148 PHE F 151 1 O LEU F 149 N VAL F 93
SHEET 4 Q 9 VAL F 201 SER F 205 1 O SER F 205 N PHE F 150
SHEET 5 Q 9 LYS F 249 VAL F 255 1 O LYS F 249 N ILE F 204
SHEET 6 Q 9 LEU F 293 ALA F 299 1 O PHE F 294 N ILE F 250
SHEET 7 Q 9 LYS F 330 ALA F 333 1 O TRP F 332 N VAL F 297
SHEET 8 Q 9 ALA F 376 THR F 381 1 O ALA F 376 N ALA F 333
SHEET 9 Q 9 ASN F 44 SER F 48 1 N SER F 46 O TRP F 379
SHEET 1 R 3 VAL F 383 SER F 384 0
SHEET 2 R 3 ILE F 391 LEU F 394 1 O LEU F 393 N SER F 384
SHEET 3 R 3 GLU F 409 THR F 412 -1 O SER F 411 N GLN F 392
CISPEP 1 ILE A 252 PRO A 253 0 -7.97
CISPEP 2 TYR A 306 PRO A 307 0 -4.44
CISPEP 3 ILE B 252 PRO B 253 0 -8.64
CISPEP 4 TYR B 306 PRO B 307 0 -4.90
CISPEP 5 ILE C 252 PRO C 253 0 -3.93
CISPEP 6 TYR C 306 PRO C 307 0 -13.93
CISPEP 7 ILE D 252 PRO D 253 0 -12.48
CISPEP 8 TYR D 306 PRO D 307 0 -3.23
CISPEP 9 ILE E 252 PRO E 253 0 -9.83
CISPEP 10 TYR E 306 PRO E 307 0 2.03
CISPEP 11 ILE F 252 PRO F 253 0 -7.39
CISPEP 12 TYR F 306 PRO F 307 0 -2.94
CRYST1 87.530 116.258 393.350 90.00 90.00 90.00 P 21 21 21 24
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 0.011425 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
