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HEADER HYDROLASE 11-AUG-20 7JQZ
TITLE CRYSTAL STRUCTURE OF CFL2 WILD-TYPE FROM BURKHOLDERIA CENOCEPACIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA (STRAIN MC0-3);
SOURCE 3 ORGANISM_TAXID: 406425;
SOURCE 4 STRAIN: MC0-3;
SOURCE 5 GENE: BCENMC03_3580;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DECAMER, ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.TAHER,D.R.MADDEN
REVDAT 1 17-MAR-21 7JQZ 0
JRNL AUTH N.M.TAHER,K.L.HVORECNY,C.M.BURKE,M.S.A.GILMAN,G.E.HEUSSLER,
JRNL AUTH 2 J.ADOLF-BRYFOGLE,C.D.BAHL,G.A.O'TOOLE,D.R.MADDEN
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF TWO CIF-LIKE
JRNL TITL 2 EPOXIDE HYDROLASES FROM BURKHOLDERIA CENOCEPACIA
JRNL REF CURR RES STRUCT BIOL 2021
JRNL REFN ESSN 2665-928X
JRNL DOI 10.1016/J.CRSTBI.2021.02.002
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 170263
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 8500
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.910
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.33
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7JQZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1000248678.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.18076
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 170389
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 48.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.6000
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) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : 2.450
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: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 784 MM SODIUM THIOCYANATE, 12% PEG
REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 91.36700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 105.23550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 91.36700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 105.23550
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 101830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -147.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 1
REMARK 465 TYR A 2
REMARK 465 GLN A 3
REMARK 465 HIS A 4
REMARK 465 GLN A 5
REMARK 465 SER A 6
REMARK 465 THR A 7
REMARK 465 GLU A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 HIS A 12
REMARK 465 LEU A 13
REMARK 465 GLU A 14
REMARK 465 ALA A 15
REMARK 465 MET B 1
REMARK 465 TYR B 2
REMARK 465 GLN B 3
REMARK 465 HIS B 4
REMARK 465 GLN B 5
REMARK 465 SER B 6
REMARK 465 THR B 7
REMARK 465 GLU B 8
REMARK 465 ALA B 9
REMARK 465 ALA B 10
REMARK 465 SER B 11
REMARK 465 HIS B 12
REMARK 465 LEU B 13
REMARK 465 GLU B 14
REMARK 465 ALA B 15
REMARK 465 MET C 1
REMARK 465 TYR C 2
REMARK 465 GLN C 3
REMARK 465 HIS C 4
REMARK 465 GLN C 5
REMARK 465 SER C 6
REMARK 465 THR C 7
REMARK 465 GLU C 8
REMARK 465 ALA C 9
REMARK 465 ALA C 10
REMARK 465 SER C 11
REMARK 465 HIS C 12
REMARK 465 LEU C 13
REMARK 465 GLU C 14
REMARK 465 ALA C 15
REMARK 465 MET D 1
REMARK 465 TYR D 2
REMARK 465 GLN D 3
REMARK 465 HIS D 4
REMARK 465 GLN D 5
REMARK 465 SER D 6
REMARK 465 THR D 7
REMARK 465 GLU D 8
REMARK 465 ALA D 9
REMARK 465 ALA D 10
REMARK 465 SER D 11
REMARK 465 HIS D 12
REMARK 465 LEU D 13
REMARK 465 GLU D 14
REMARK 465 ALA D 15
REMARK 465 MET E 1
REMARK 465 TYR E 2
REMARK 465 GLN E 3
REMARK 465 HIS E 4
REMARK 465 GLN E 5
REMARK 465 SER E 6
REMARK 465 THR E 7
REMARK 465 GLU E 8
REMARK 465 ALA E 9
REMARK 465 ALA E 10
REMARK 465 SER E 11
REMARK 465 HIS E 12
REMARK 465 LEU E 13
REMARK 465 GLU E 14
REMARK 465 ALA E 15
REMARK 465 MET F 1
REMARK 465 TYR F 2
REMARK 465 GLN F 3
REMARK 465 HIS F 4
REMARK 465 GLN F 5
REMARK 465 SER F 6
REMARK 465 THR F 7
REMARK 465 GLU F 8
REMARK 465 ALA F 9
REMARK 465 ALA F 10
REMARK 465 SER F 11
REMARK 465 HIS F 12
REMARK 465 LEU F 13
REMARK 465 GLU F 14
REMARK 465 ALA F 15
REMARK 465 MET G 1
REMARK 465 TYR G 2
REMARK 465 GLN G 3
REMARK 465 HIS G 4
REMARK 465 GLN G 5
REMARK 465 SER G 6
REMARK 465 THR G 7
REMARK 465 GLU G 8
REMARK 465 ALA G 9
REMARK 465 ALA G 10
REMARK 465 SER G 11
REMARK 465 HIS G 12
REMARK 465 LEU G 13
REMARK 465 GLU G 14
REMARK 465 ALA G 15
REMARK 465 MET H 1
REMARK 465 TYR H 2
REMARK 465 GLN H 3
REMARK 465 HIS H 4
REMARK 465 GLN H 5
REMARK 465 SER H 6
REMARK 465 THR H 7
REMARK 465 GLU H 8
REMARK 465 ALA H 9
REMARK 465 ALA H 10
REMARK 465 SER H 11
REMARK 465 HIS H 12
REMARK 465 LEU H 13
REMARK 465 GLU H 14
REMARK 465 ALA H 15
REMARK 465 MET I 1
REMARK 465 TYR I 2
REMARK 465 GLN I 3
REMARK 465 HIS I 4
REMARK 465 GLN I 5
REMARK 465 SER I 6
REMARK 465 THR I 7
REMARK 465 GLU I 8
REMARK 465 ALA I 9
REMARK 465 ALA I 10
REMARK 465 SER I 11
REMARK 465 HIS I 12
REMARK 465 LEU I 13
REMARK 465 GLU I 14
REMARK 465 ALA I 15
REMARK 465 MET J 1
REMARK 465 TYR J 2
REMARK 465 GLN J 3
REMARK 465 HIS J 4
REMARK 465 GLN J 5
REMARK 465 SER J 6
REMARK 465 THR J 7
REMARK 465 GLU J 8
REMARK 465 ALA J 9
REMARK 465 ALA J 10
REMARK 465 SER J 11
REMARK 465 HIS J 12
REMARK 465 LEU J 13
REMARK 465 GLU J 14
REMARK 465 ALA J 15
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 60 58.52 -98.92
REMARK 500 GLU A 61 -152.62 -121.11
REMARK 500 ASP A 124 -132.68 59.16
REMARK 500 ASP A 148 65.34 39.44
REMARK 500 VAL A 154 -46.12 -136.35
REMARK 500 ASP A 180 -37.59 68.36
REMARK 500 ASP A 223 111.50 -37.85
REMARK 500 PRO B 60 56.87 -99.63
REMARK 500 GLU B 61 -152.10 -120.18
REMARK 500 SER B 62 -175.06 -170.93
REMARK 500 ASP B 124 -132.67 60.82
REMARK 500 ASP B 180 -36.87 69.49
REMARK 500 ASP B 223 109.04 -36.43
REMARK 500 PRO C 60 57.07 -100.67
REMARK 500 GLU C 61 -152.50 -118.60
REMARK 500 ASP C 124 -133.07 63.08
REMARK 500 ASP C 180 -39.78 67.86
REMARK 500 PRO D 60 56.24 -99.83
REMARK 500 GLU D 61 -151.73 -117.11
REMARK 500 ASP D 124 -133.50 61.73
REMARK 500 VAL D 154 -44.21 -130.08
REMARK 500 ASP D 180 -36.85 69.73
REMARK 500 PRO E 60 58.07 -100.64
REMARK 500 GLU E 61 -151.82 -119.52
REMARK 500 SER E 62 -176.83 -171.09
REMARK 500 ASP E 124 -132.85 60.76
REMARK 500 VAL E 154 -33.32 -133.05
REMARK 500 ASP E 180 -39.24 68.82
REMARK 500 ASP E 223 116.83 -35.65
REMARK 500 PRO F 60 56.29 -100.09
REMARK 500 GLU F 61 -151.06 -119.71
REMARK 500 SER F 62 -175.21 -170.28
REMARK 500 ASP F 124 -133.26 61.12
REMARK 500 VAL F 154 -39.14 -132.73
REMARK 500 ASP F 180 -36.37 68.66
REMARK 500 ASP F 223 111.20 -38.82
REMARK 500 PRO G 60 56.76 -99.90
REMARK 500 GLU G 61 -152.31 -118.82
REMARK 500 SER G 62 -175.14 -170.49
REMARK 500 ASP G 124 -132.59 61.91
REMARK 500 ASP G 180 -38.25 69.62
REMARK 500 ASP G 223 112.81 -32.15
REMARK 500 PRO H 60 57.08 -103.40
REMARK 500 GLU H 61 -150.41 -118.38
REMARK 500 ASP H 124 -134.66 61.72
REMARK 500 VAL H 154 -59.52 -126.59
REMARK 500 ASP H 180 -39.22 68.99
REMARK 500 ASP H 223 114.05 -36.40
REMARK 500 PHE H 291 59.97 -93.74
REMARK 500 PRO I 60 55.84 -101.30
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH I 487 DISTANCE = 6.04 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7JQX RELATED DB: PDB
REMARK 900 7JQX IS FOR THE SAME CITATION
REMARK 900 RELATED ID: 7JQY RELATED DB: PDB
REMARK 900 7JQY IS FOR THE SAME CITATION
DBREF 7JQZ A 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ B 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ C 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ D 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ E 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ F 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ G 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ H 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ I 1 309 UNP B1K378 B1K378_BURCC 1 309
DBREF 7JQZ J 1 309 UNP B1K378 B1K378_BURCC 1 309
SEQRES 1 A 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 A 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 A 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 A 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 A 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 A 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 A 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 A 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 A 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 A 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 A 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 A 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 A 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 A 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 A 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 A 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 A 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 A 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 A 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 A 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 A 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 A 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 A 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 A 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 B 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 B 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 B 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 B 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 B 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 B 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 B 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 B 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 B 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 B 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 B 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 B 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 B 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 B 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 B 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 B 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 B 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 B 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 B 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 B 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 B 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 B 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 B 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 B 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 C 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 C 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 C 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 C 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 C 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 C 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 C 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 C 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 C 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 C 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 C 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 C 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 C 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 C 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 C 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 C 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 C 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 C 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 C 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 C 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 C 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 C 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 C 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 C 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 D 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 D 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 D 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 D 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 D 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 D 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 D 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 D 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 D 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 D 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 D 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 D 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 D 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 D 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 D 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 D 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 D 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 D 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 D 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 D 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 D 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 D 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 D 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 D 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 E 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 E 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 E 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 E 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 E 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 E 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 E 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 E 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 E 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 E 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 E 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 E 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 E 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 E 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 E 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 E 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 E 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 E 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 E 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 E 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 E 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 E 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 E 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 E 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 F 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 F 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 F 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 F 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 F 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 F 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 F 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 F 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 F 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 F 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 F 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 F 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 F 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 F 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 F 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 F 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 F 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 F 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 F 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 F 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 F 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 F 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 F 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 F 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 G 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 G 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 G 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 G 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 G 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 G 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 G 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 G 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 G 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 G 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 G 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 G 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 G 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 G 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 G 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 G 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 G 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 G 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 G 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 G 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 G 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 G 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 G 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 G 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 H 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 H 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 H 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 H 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 H 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 H 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 H 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 H 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 H 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 H 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 H 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 H 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 H 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 H 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 H 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 H 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 H 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 H 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 H 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 H 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 H 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 H 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 H 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 H 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 I 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 I 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 I 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 I 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 I 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 I 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 I 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 I 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 I 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 I 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 I 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 I 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 I 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 I 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 I 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 I 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 I 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 I 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 I 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 I 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 I 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 I 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 I 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 I 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
SEQRES 1 J 309 MET TYR GLN HIS GLN SER THR GLU ALA ALA SER HIS LEU
SEQRES 2 J 309 GLU ALA THR PRO TYR PHE ARG GLU ASP PRO ARG LEU THR
SEQRES 3 J 309 GLY PHE ARG HIS ARG PHE ASP THR VAL ASP GLY VAL ARG
SEQRES 4 J 309 LEU HIS PHE VAL GLU GLY GLY ARG ALA ASP GLY GLU THR
SEQRES 5 J 309 ILE VAL LEU LEU ALA GLY PHE PRO GLU SER TRP TYR ALA
SEQRES 6 J 309 TRP ARG ARG VAL MET PRO LEU LEU ALA ASP GLU PHE ARG
SEQRES 7 J 309 ILE VAL ALA PRO ASP LEU PRO GLY GLN GLY ASP SER ASP
SEQRES 8 J 309 ARG PRO LEU VAL GLY TYR ASP THR GLN THR VAL ALA ALA
SEQRES 9 J 309 THR LEU ALA ARG LEU LEU GLU ARG GLN ASN ILE ALA ARG
SEQRES 10 J 309 PHE TYR LEU ALA ALA HIS ASP VAL GLY ALA TRP VAL ALA
SEQRES 11 J 309 TYR PRO PHE ALA ALA MET TYR PRO GLU SER VAL LYS ARG
SEQRES 12 J 309 LEU ALA LEU LEU ASP ALA GLY ILE PRO GLY VAL THR LEU
SEQRES 13 J 309 PRO ALA ALA LEU PRO ILE GLU PRO GLY ASN ALA TRP ARG
SEQRES 14 J 309 THR TRP HIS PHE ALA PHE HIS THR VAL ALA ASP LEU PRO
SEQRES 15 J 309 GLU THR LEU ILE ALA GLY LYS GLU ARG GLU TYR LEU ASP
SEQRES 16 J 309 TRP PHE LEU ARG ARG LYS ALA ALA ASN PRO GLU SER PHE
SEQRES 17 J 309 SER ASP ALA ASP VAL ASP GLU TYR LEU ARG VAL PHE THR
SEQRES 18 J 309 ARG ASP GLY GLY LEU ARG ALA GLY LEU ALA PHE TYR ARG
SEQRES 19 J 309 ALA VAL SER GLU SER SER ALA GLN ASN ARG LYS LEU GLN
SEQRES 20 J 309 ALA LEU GLY LYS LEU LYS MET PRO VAL LEU ALA VAL SER
SEQRES 21 J 309 ALA ASP GLN GLY SER ILE PRO ASP MET ALA GLY PRO LEU
SEQRES 22 J 309 GLU HIS VAL ALA GLU GLU VAL THR ALA ALA THR ILE ALA
SEQRES 23 J 309 TYR SER GLY HIS PHE ILE PRO GLU GLU GLN PRO GLN ALA
SEQRES 24 J 309 LEU ALA ARG GLU LEU ARG ASP PHE PHE ARG
FORMUL 11 HOH *1141(H2 O)
HELIX 1 AA1 SER A 62 ARG A 67 5 6
HELIX 2 AA2 VAL A 69 ALA A 74 1 6
HELIX 3 AA3 ASP A 98 GLN A 113 1 16
HELIX 4 AA4 ASP A 124 TYR A 137 1 14
HELIX 5 AA5 ASN A 166 THR A 170 5 5
HELIX 6 AA6 TRP A 171 VAL A 178 1 8
HELIX 7 AA7 ASP A 180 ALA A 187 1 8
HELIX 8 AA8 LYS A 189 ALA A 202 1 14
HELIX 9 AA9 ASN A 204 PHE A 208 5 5
HELIX 10 AB1 SER A 209 ARG A 222 1 14
HELIX 11 AB2 GLY A 224 ALA A 235 1 12
HELIX 12 AB3 ALA A 235 ALA A 248 1 14
HELIX 13 AB4 MET A 269 HIS A 275 1 7
HELIX 14 AB5 PHE A 291 GLN A 296 1 6
HELIX 15 AB6 GLN A 296 PHE A 308 1 13
HELIX 16 AB7 SER B 62 ARG B 67 5 6
HELIX 17 AB8 VAL B 69 ALA B 74 1 6
HELIX 18 AB9 ASP B 98 GLN B 113 1 16
HELIX 19 AC1 ASP B 124 TYR B 137 1 14
HELIX 20 AC2 ASN B 166 TRP B 171 1 6
HELIX 21 AC3 TRP B 171 VAL B 178 1 8
HELIX 22 AC4 ASP B 180 ALA B 187 1 8
HELIX 23 AC5 LYS B 189 ALA B 202 1 14
HELIX 24 AC6 ASN B 204 PHE B 208 5 5
HELIX 25 AC7 SER B 209 ARG B 222 1 14
HELIX 26 AC8 GLY B 224 ALA B 235 1 12
HELIX 27 AC9 ALA B 235 LEU B 249 1 15
HELIX 28 AD1 MET B 269 GLU B 274 1 6
HELIX 29 AD2 PHE B 291 GLN B 296 1 6
HELIX 30 AD3 GLN B 296 PHE B 308 1 13
HELIX 31 AD4 SER C 62 ARG C 67 5 6
HELIX 32 AD5 VAL C 69 ALA C 74 1 6
HELIX 33 AD6 ASP C 98 GLN C 113 1 16
HELIX 34 AD7 ASP C 124 TYR C 137 1 14
HELIX 35 AD8 ASN C 166 THR C 170 5 5
HELIX 36 AD9 TRP C 171 VAL C 178 1 8
HELIX 37 AE1 ASP C 180 ALA C 187 1 8
HELIX 38 AE2 LYS C 189 ALA C 202 1 14
HELIX 39 AE3 ASN C 204 PHE C 208 5 5
HELIX 40 AE4 SER C 209 THR C 221 1 13
HELIX 41 AE5 GLY C 224 ALA C 235 1 12
HELIX 42 AE6 ALA C 235 LEU C 249 1 15
HELIX 43 AE7 MET C 269 GLU C 274 1 6
HELIX 44 AE8 PHE C 291 GLN C 296 1 6
HELIX 45 AE9 GLN C 296 PHE C 308 1 13
HELIX 46 AF1 SER D 62 ARG D 67 5 6
HELIX 47 AF2 VAL D 69 ALA D 74 1 6
HELIX 48 AF3 ASP D 98 GLN D 113 1 16
HELIX 49 AF4 ASP D 124 TYR D 137 1 14
HELIX 50 AF5 ASN D 166 THR D 170 5 5
HELIX 51 AF6 TRP D 171 VAL D 178 1 8
HELIX 52 AF7 ASP D 180 ALA D 187 1 8
HELIX 53 AF8 LYS D 189 ALA D 202 1 14
HELIX 54 AF9 ASN D 204 PHE D 208 5 5
HELIX 55 AG1 SER D 209 ARG D 222 1 14
HELIX 56 AG2 GLY D 224 ALA D 235 1 12
HELIX 57 AG3 ALA D 235 LEU D 249 1 15
HELIX 58 AG4 MET D 269 GLU D 274 1 6
HELIX 59 AG5 PHE D 291 GLN D 296 1 6
HELIX 60 AG6 GLN D 296 PHE D 308 1 13
HELIX 61 AG7 SER E 62 ARG E 67 5 6
HELIX 62 AG8 VAL E 69 ASP E 75 1 7
HELIX 63 AG9 ASP E 98 GLN E 113 1 16
HELIX 64 AH1 ASP E 124 TYR E 137 1 14
HELIX 65 AH2 GLU E 163 TRP E 168 1 6
HELIX 66 AH3 TRP E 171 VAL E 178 1 8
HELIX 67 AH4 ASP E 180 ALA E 187 1 8
HELIX 68 AH5 LYS E 189 ALA E 202 1 14
HELIX 69 AH6 ASN E 204 PHE E 208 5 5
HELIX 70 AH7 SER E 209 ARG E 222 1 14
HELIX 71 AH8 GLY E 224 ALA E 235 1 12
HELIX 72 AH9 ALA E 235 ALA E 248 1 14
HELIX 73 AI1 MET E 269 GLU E 274 1 6
HELIX 74 AI2 PHE E 291 GLN E 296 1 6
HELIX 75 AI3 GLN E 296 PHE E 308 1 13
HELIX 76 AI4 SER F 62 ARG F 67 5 6
HELIX 77 AI5 VAL F 69 ALA F 74 1 6
HELIX 78 AI6 ASP F 98 GLN F 113 1 16
HELIX 79 AI7 ASP F 124 TYR F 137 1 14
HELIX 80 AI8 GLU F 163 TRP F 168 1 6
HELIX 81 AI9 TRP F 171 VAL F 178 1 8
HELIX 82 AJ1 ASP F 180 ALA F 187 1 8
HELIX 83 AJ2 LYS F 189 ALA F 202 1 14
HELIX 84 AJ3 ASN F 204 PHE F 208 5 5
HELIX 85 AJ4 SER F 209 ARG F 222 1 14
HELIX 86 AJ5 GLY F 224 ALA F 235 1 12
HELIX 87 AJ6 ALA F 235 ALA F 248 1 14
HELIX 88 AJ7 MET F 269 GLU F 274 1 6
HELIX 89 AJ8 PHE F 291 GLN F 296 1 6
HELIX 90 AJ9 GLN F 296 PHE F 308 1 13
HELIX 91 AK1 SER G 62 ARG G 67 5 6
HELIX 92 AK2 VAL G 69 ASP G 75 1 7
HELIX 93 AK3 ASP G 98 GLN G 113 1 16
HELIX 94 AK4 ASP G 124 TYR G 137 1 14
HELIX 95 AK5 ASN G 166 TRP G 171 1 6
HELIX 96 AK6 TRP G 171 VAL G 178 1 8
HELIX 97 AK7 ASP G 180 ALA G 187 1 8
HELIX 98 AK8 LYS G 189 ALA G 202 1 14
HELIX 99 AK9 ASN G 204 PHE G 208 5 5
HELIX 100 AL1 SER G 209 ARG G 222 1 14
HELIX 101 AL2 GLY G 224 ALA G 235 1 12
HELIX 102 AL3 ALA G 235 ALA G 248 1 14
HELIX 103 AL4 MET G 269 GLU G 274 1 6
HELIX 104 AL5 PHE G 291 GLN G 296 1 6
HELIX 105 AL6 GLN G 296 PHE G 308 1 13
HELIX 106 AL7 SER H 62 ARG H 67 5 6
HELIX 107 AL8 VAL H 69 ALA H 74 1 6
HELIX 108 AL9 ASP H 98 GLN H 113 1 16
HELIX 109 AM1 ASP H 124 TYR H 137 1 14
HELIX 110 AM2 ASN H 166 TRP H 171 1 6
HELIX 111 AM3 TRP H 171 VAL H 178 1 8
HELIX 112 AM4 ASP H 180 ALA H 187 1 8
HELIX 113 AM5 LYS H 189 LYS H 201 1 13
HELIX 114 AM6 ASN H 204 PHE H 208 5 5
HELIX 115 AM7 SER H 209 THR H 221 1 13
HELIX 116 AM8 GLY H 224 ALA H 235 1 12
HELIX 117 AM9 ALA H 235 ALA H 248 1 14
HELIX 118 AN1 MET H 269 GLU H 274 1 6
HELIX 119 AN2 PHE H 291 GLN H 296 1 6
HELIX 120 AN3 GLN H 296 PHE H 308 1 13
HELIX 121 AN4 SER I 62 ARG I 67 5 6
HELIX 122 AN5 VAL I 69 ALA I 74 1 6
HELIX 123 AN6 ASP I 98 GLN I 113 1 16
HELIX 124 AN7 ASP I 124 TYR I 137 1 14
HELIX 125 AN8 ASN I 166 THR I 170 5 5
HELIX 126 AN9 TRP I 171 VAL I 178 1 8
HELIX 127 AO1 ASP I 180 ALA I 187 1 8
HELIX 128 AO2 LYS I 189 ALA I 202 1 14
HELIX 129 AO3 ASN I 204 PHE I 208 5 5
HELIX 130 AO4 SER I 209 ARG I 222 1 14
HELIX 131 AO5 GLY I 224 ALA I 235 1 12
HELIX 132 AO6 ALA I 235 ALA I 248 1 14
HELIX 133 AO7 MET I 269 GLU I 274 1 6
HELIX 134 AO8 PHE I 291 GLN I 296 1 6
HELIX 135 AO9 GLN I 296 PHE I 308 1 13
HELIX 136 AP1 SER J 62 ARG J 67 5 6
HELIX 137 AP2 VAL J 69 ALA J 74 1 6
HELIX 138 AP3 ASP J 98 GLN J 113 1 16
HELIX 139 AP4 ASP J 124 TYR J 137 1 14
HELIX 140 AP5 ASN J 166 THR J 170 5 5
HELIX 141 AP6 TRP J 171 VAL J 178 1 8
HELIX 142 AP7 ASP J 180 ALA J 187 1 8
HELIX 143 AP8 LYS J 189 ALA J 202 1 14
HELIX 144 AP9 ASN J 204 PHE J 208 5 5
HELIX 145 AQ1 SER J 209 ARG J 222 1 14
HELIX 146 AQ2 GLY J 224 ALA J 235 1 12
HELIX 147 AQ3 ALA J 235 ALA J 248 1 14
HELIX 148 AQ4 MET J 269 GLU J 274 1 6
HELIX 149 AQ5 PHE J 291 GLN J 296 1 6
HELIX 150 AQ6 GLN J 296 PHE J 308 1 13
SHEET 1 AA1 9 ARG A 20 GLU A 21 0
SHEET 2 AA1 9 ARG A 29 VAL A 35 -1 O HIS A 30 N ARG A 20
SHEET 3 AA1 9 VAL A 38 GLY A 46 -1 O VAL A 38 N VAL A 35
SHEET 4 AA1 9 ARG A 78 PRO A 82 -1 O ALA A 81 N VAL A 43
SHEET 5 AA1 9 THR A 52 LEU A 56 1 N ILE A 53 O ARG A 78
SHEET 6 AA1 9 PHE A 118 HIS A 123 1 O TYR A 119 N THR A 52
SHEET 7 AA1 9 VAL A 141 LEU A 147 1 O ALA A 145 N ALA A 122
SHEET 8 AA1 9 VAL A 256 ALA A 261 1 O LEU A 257 N LEU A 144
SHEET 9 AA1 9 VAL A 280 ILE A 285 1 O ILE A 285 N SER A 260
SHEET 1 AA2 2 ALA A 159 PRO A 161 0
SHEET 2 AA2 2 ALA B 159 PRO B 161 -1 O LEU B 160 N LEU A 160
SHEET 1 AA3 9 ARG B 20 GLU B 21 0
SHEET 2 AA3 9 ARG B 29 VAL B 35 -1 O HIS B 30 N ARG B 20
SHEET 3 AA3 9 VAL B 38 GLY B 46 -1 O VAL B 38 N VAL B 35
SHEET 4 AA3 9 ARG B 78 PRO B 82 -1 O ILE B 79 N GLY B 45
SHEET 5 AA3 9 THR B 52 LEU B 56 1 N ILE B 53 O ARG B 78
SHEET 6 AA3 9 PHE B 118 HIS B 123 1 O TYR B 119 N THR B 52
SHEET 7 AA3 9 VAL B 141 LEU B 147 1 O ALA B 145 N LEU B 120
SHEET 8 AA3 9 VAL B 256 ALA B 261 1 O VAL B 259 N LEU B 146
SHEET 9 AA3 9 VAL B 280 ILE B 285 1 O THR B 281 N ALA B 258
SHEET 1 AA4 9 ARG C 20 GLU C 21 0
SHEET 2 AA4 9 ARG C 29 VAL C 35 -1 O HIS C 30 N ARG C 20
SHEET 3 AA4 9 VAL C 38 GLY C 46 -1 O LEU C 40 N ASP C 33
SHEET 4 AA4 9 ARG C 78 PRO C 82 -1 O ALA C 81 N VAL C 43
SHEET 5 AA4 9 THR C 52 LEU C 56 1 N ILE C 53 O ARG C 78
SHEET 6 AA4 9 PHE C 118 HIS C 123 1 O TYR C 119 N THR C 52
SHEET 7 AA4 9 VAL C 141 LEU C 147 1 O LYS C 142 N PHE C 118
SHEET 8 AA4 9 VAL C 256 ALA C 261 1 O LEU C 257 N LEU C 144
SHEET 9 AA4 9 VAL C 280 ILE C 285 1 O THR C 281 N ALA C 258
SHEET 1 AA5 2 ALA C 159 PRO C 161 0
SHEET 2 AA5 2 ALA D 159 PRO D 161 -1 O LEU D 160 N LEU C 160
SHEET 1 AA6 9 ARG D 20 GLU D 21 0
SHEET 2 AA6 9 ARG D 29 VAL D 35 -1 O HIS D 30 N ARG D 20
SHEET 3 AA6 9 VAL D 38 GLY D 46 -1 O GLU D 44 N ARG D 29
SHEET 4 AA6 9 ARG D 78 PRO D 82 -1 O ALA D 81 N VAL D 43
SHEET 5 AA6 9 THR D 52 LEU D 56 1 N ILE D 53 O ARG D 78
SHEET 6 AA6 9 PHE D 118 HIS D 123 1 O TYR D 119 N THR D 52
SHEET 7 AA6 9 VAL D 141 LEU D 147 1 O ALA D 145 N LEU D 120
SHEET 8 AA6 9 VAL D 256 ALA D 261 1 O LEU D 257 N LEU D 144
SHEET 9 AA6 9 VAL D 280 ILE D 285 1 O THR D 281 N ALA D 258
SHEET 1 AA7 9 ARG E 20 GLU E 21 0
SHEET 2 AA7 9 ARG E 29 VAL E 35 -1 O HIS E 30 N ARG E 20
SHEET 3 AA7 9 VAL E 38 GLY E 46 -1 O VAL E 38 N VAL E 35
SHEET 4 AA7 9 ARG E 78 PRO E 82 -1 O ALA E 81 N VAL E 43
SHEET 5 AA7 9 THR E 52 LEU E 56 1 N ILE E 53 O ARG E 78
SHEET 6 AA7 9 PHE E 118 HIS E 123 1 O TYR E 119 N VAL E 54
SHEET 7 AA7 9 VAL E 141 LEU E 147 1 O ALA E 145 N LEU E 120
SHEET 8 AA7 9 VAL E 256 ALA E 261 1 O LEU E 257 N LEU E 144
SHEET 9 AA7 9 VAL E 280 ILE E 285 1 O THR E 281 N ALA E 258
SHEET 1 AA8 2 ALA E 159 PRO E 161 0
SHEET 2 AA8 2 ALA F 159 PRO F 161 -1 O LEU F 160 N LEU E 160
SHEET 1 AA9 9 ARG F 20 GLU F 21 0
SHEET 2 AA9 9 ARG F 29 VAL F 35 -1 O HIS F 30 N ARG F 20
SHEET 3 AA9 9 VAL F 38 GLY F 46 -1 O LEU F 40 N ASP F 33
SHEET 4 AA9 9 ARG F 78 PRO F 82 -1 O ALA F 81 N VAL F 43
SHEET 5 AA9 9 THR F 52 LEU F 56 1 N ILE F 53 O ARG F 78
SHEET 6 AA9 9 PHE F 118 HIS F 123 1 O TYR F 119 N VAL F 54
SHEET 7 AA9 9 VAL F 141 LEU F 147 1 O LYS F 142 N PHE F 118
SHEET 8 AA9 9 VAL F 256 ALA F 261 1 O LEU F 257 N LEU F 144
SHEET 9 AA9 9 VAL F 280 ILE F 285 1 O THR F 281 N ALA F 258
SHEET 1 AB1 9 ARG G 20 GLU G 21 0
SHEET 2 AB1 9 PHE G 28 VAL G 35 -1 O HIS G 30 N ARG G 20
SHEET 3 AB1 9 VAL G 38 GLY G 46 -1 O LEU G 40 N ASP G 33
SHEET 4 AB1 9 PHE G 77 PRO G 82 -1 O ALA G 81 N VAL G 43
SHEET 5 AB1 9 GLU G 51 LEU G 56 1 N GLU G 51 O ARG G 78
SHEET 6 AB1 9 PHE G 118 HIS G 123 1 O TYR G 119 N VAL G 54
SHEET 7 AB1 9 VAL G 141 LEU G 147 1 O ALA G 145 N LEU G 120
SHEET 8 AB1 9 VAL G 256 ALA G 261 1 O LEU G 257 N LEU G 144
SHEET 9 AB1 9 VAL G 280 ILE G 285 1 O THR G 281 N VAL G 256
SHEET 1 AB2 2 ALA G 159 PRO G 161 0
SHEET 2 AB2 2 ALA H 159 PRO H 161 -1 O LEU H 160 N LEU G 160
SHEET 1 AB3 9 ARG H 20 GLU H 21 0
SHEET 2 AB3 9 ARG H 29 VAL H 35 -1 O HIS H 30 N ARG H 20
SHEET 3 AB3 9 VAL H 38 GLY H 46 -1 O LEU H 40 N ASP H 33
SHEET 4 AB3 9 ARG H 78 PRO H 82 -1 O ALA H 81 N VAL H 43
SHEET 5 AB3 9 THR H 52 LEU H 56 1 N ILE H 53 O ARG H 78
SHEET 6 AB3 9 PHE H 118 HIS H 123 1 O TYR H 119 N THR H 52
SHEET 7 AB3 9 VAL H 141 LEU H 147 1 O ALA H 145 N LEU H 120
SHEET 8 AB3 9 VAL H 256 ALA H 261 1 O LEU H 257 N LEU H 144
SHEET 9 AB3 9 VAL H 280 ILE H 285 1 O ALA H 283 N SER H 260
SHEET 1 AB4 9 ARG I 20 GLU I 21 0
SHEET 2 AB4 9 ARG I 29 VAL I 35 -1 O HIS I 30 N ARG I 20
SHEET 3 AB4 9 VAL I 38 GLY I 46 -1 O VAL I 38 N VAL I 35
SHEET 4 AB4 9 PHE I 77 PRO I 82 -1 O ALA I 81 N VAL I 43
SHEET 5 AB4 9 GLU I 51 LEU I 56 1 N ILE I 53 O ARG I 78
SHEET 6 AB4 9 PHE I 118 HIS I 123 1 O TYR I 119 N THR I 52
SHEET 7 AB4 9 VAL I 141 LEU I 147 1 O LYS I 142 N PHE I 118
SHEET 8 AB4 9 VAL I 256 ALA I 261 1 O LEU I 257 N LEU I 144
SHEET 9 AB4 9 VAL I 280 ILE I 285 1 O ALA I 283 N SER I 260
SHEET 1 AB5 2 ALA I 159 PRO I 161 0
SHEET 2 AB5 2 ALA J 159 PRO J 161 -1 O LEU J 160 N LEU I 160
SHEET 1 AB6 9 ARG J 20 GLU J 21 0
SHEET 2 AB6 9 ARG J 29 VAL J 35 -1 O HIS J 30 N ARG J 20
SHEET 3 AB6 9 VAL J 38 GLY J 46 -1 O VAL J 38 N VAL J 35
SHEET 4 AB6 9 ARG J 78 PRO J 82 -1 O ALA J 81 N VAL J 43
SHEET 5 AB6 9 THR J 52 LEU J 56 1 N ILE J 53 O ARG J 78
SHEET 6 AB6 9 PHE J 118 HIS J 123 1 O TYR J 119 N THR J 52
SHEET 7 AB6 9 VAL J 141 LEU J 147 1 O ALA J 145 N LEU J 120
SHEET 8 AB6 9 VAL J 256 ALA J 261 1 O LEU J 257 N LEU J 144
SHEET 9 AB6 9 VAL J 280 ILE J 285 1 O ALA J 283 N SER J 260
CISPEP 1 PHE A 59 PRO A 60 0 -4.81
CISPEP 2 PHE B 59 PRO B 60 0 -3.14
CISPEP 3 PHE C 59 PRO C 60 0 -3.14
CISPEP 4 PHE D 59 PRO D 60 0 -3.82
CISPEP 5 PHE E 59 PRO E 60 0 -3.27
CISPEP 6 PHE F 59 PRO F 60 0 -3.77
CISPEP 7 PHE G 59 PRO G 60 0 -3.73
CISPEP 8 PHE H 59 PRO H 60 0 -2.92
CISPEP 9 PHE I 59 PRO I 60 0 -3.37
CISPEP 10 PHE J 59 PRO J 60 0 -3.50
CRYST1 182.734 210.471 86.956 90.00 90.00 90.00 P 21 21 2 40
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 0.005472 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004751 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011500 0.00000
TER 2349 ARG A 309
TER 4687 ARG B 309
TER 7014 ARG C 309
TER 9341 ARG D 309
TER 11668 ARG E 309
TER 14006 ARG F 309
TER 16344 ARG G 309
TER 18682 ARG H 309
TER 21009 ARG I 309
TER 23347 ARG J 309
MASTER 436 0 0 150 100 0 0 624401 10 0 240
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