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HEADER HYDROLASE 16-JAN-09 3FVR
TITLE CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE FROM BACILLUS
TITLE 2 PUMILUS, MONOCLINIC CRYSTAL FORM I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, L, M, N;
COMPND 4 EC: 3.1.1.6;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS PUMILUS;
SOURCE 3 ORGANISM_TAXID: 1408;
SOURCE 4 STRAIN: PS 213;
SOURCE 5 GENE: AXE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PBPEB2
KEYWDS ALPHA/BETA HYDROLASE, CARBOHYDRATE ESTERASE, CE7, BACILLUS
KEYWDS 2 PUMILUS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.KRASTANOVA,A.CASSETTA,D.LAMBA
REVDAT 1 05-JAN-10 3FVR 0
JRNL AUTH I.KRASTANOVA,A.CASSETTA,M.MASTIHUBOVA,P.BIELY,
JRNL AUTH 2 D.LAMBA
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES OF BACILLUS
JRNL TITL 2 PUMILUS ACETYL XYLAN ESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.KRASTANOVA,C.GUARNACCIA,S.ZAHARIEV,G.DEGRASSI,
REMARK 1 AUTH 2 D.LAMBA
REMARK 1 TITL HETEROLOGOUS EXPRESSION, PURIFICATION,
REMARK 1 TITL 2 CRYSTALLIZATION, X-RAY ANALYSIS AND PHASING OF THE
REMARK 1 TITL 3 ACETYL XYLAN ESTERASE FROM BACILLUS PUMILUS
REMARK 1 REF BIOCHIM.BIOPHYS.ACTA V.1748 222 2005
REMARK 1 REFN ISSN 0006-3002
REMARK 1 REFERENCE 2
REMARK 1 AUTH G.DEGRASSI,M.KOJIC,G.LJUBIJANKIC,V.VENTURI
REMARK 1 TITL THE ACETYL XYLAN ESTERASE OF BACILLUS PUMILUS
REMARK 1 TITL 2 BELONGS TO A FAMILY OF ESTERASES WITH BROAD
REMARK 1 TITL 3 SUBSTRATE SPECIFICITY
REMARK 1 REF MICROBIOLOGY V. 146 1585 2000
REMARK 1 REFN ISSN 0026-2617
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.DEGRASSI,B.C.OKEKE,C.V.BRUSCHI,V.VENTURI
REMARK 1 TITL PURIFICATION AND CHARACTERIZATION OF AN ACETYL
REMARK 1 TITL 2 XYLAN ESTERASE FROM BACILLUS PUMILUS
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 64 789 1998
REMARK 1 REFN ISSN 0099-2240
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 839462.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 135607
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 SET) : 0.184
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13527
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 19951
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2254
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.006
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 30522
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 134
REMARK 3 SOLVENT ATOMS : 1792
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.88000
REMARK 3 B22 (A**2) : 0.79000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.72000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.24
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.33
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.560 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.730 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 32.29
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : GOL.PAR
REMARK 3 PARAMETER FILE 6 : PEG.PAR
REMARK 3 PARAMETER FILE 7 : PGE.PAR
REMARK 3 PARAMETER FILE 8 : PG4.PAR
REMARK 3 PARAMETER FILE 9 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : GOL.TOP
REMARK 3 TOPOLOGY FILE 6 : PEG.TOP
REMARK 3 TOPOLOGY FILE 7 : PGE.TOP
REMARK 3 TOPOLOGY FILE 8 : PG4.TOP
REMARK 3 TOPOLOGY FILE 9 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3FVR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB051102.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.200
REMARK 200 MONOCHROMATOR : SI (111)
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
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 135665
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 29.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 2.500
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.24400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1ODS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM CHLORIDE, 5% PEG 6000,
REMARK 280 0.1M MES, PH 6.0, MICROBATCH, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 83.84300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -170.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, B, D, C, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, M, I, N, H, L
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 SER B 319
REMARK 465 THR B 320
REMARK 465 SER D 319
REMARK 465 THR D 320
REMARK 465 SER E 319
REMARK 465 THR E 320
REMARK 465 MET F 1
REMARK 465 SER F 319
REMARK 465 THR F 320
REMARK 465 MET G 1
REMARK 465 SER G 319
REMARK 465 THR G 320
REMARK 465 MET H 1
REMARK 465 SER H 319
REMARK 465 THR H 320
REMARK 465 THR I 320
REMARK 465 MET L 1
REMARK 465 SER L 319
REMARK 465 THR L 320
REMARK 465 SER M 319
REMARK 465 THR M 320
REMARK 465 MET N 1
REMARK 465 SER N 319
REMARK 465 THR N 320
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 PHE A 4 -26.72 -155.48
REMARK 500 PRO A 50 69.29 -67.34
REMARK 500 PHE A 64 135.21 -39.48
REMARK 500 ARG A 118 118.30 -25.67
REMARK 500 GLN A 120 -90.82 -93.32
REMARK 500 SER A 123 147.68 73.12
REMARK 500 SER A 181 -111.10 55.97
REMARK 500 TYR A 204 71.01 24.74
REMARK 500 LEU A 316 -61.33 -120.58
REMARK 500 LEU A 318 42.52 -98.98
REMARK 500 GLN B 2 146.31 40.11
REMARK 500 PHE B 4 -25.89 -156.16
REMARK 500 PRO B 50 69.04 -67.40
REMARK 500 PHE B 64 134.43 -38.88
REMARK 500 ARG B 118 117.77 -26.59
REMARK 500 GLN B 120 -90.43 -93.11
REMARK 500 SER B 123 147.25 73.55
REMARK 500 SER B 181 -112.28 58.07
REMARK 500 TYR B 204 72.23 24.53
REMARK 500 LEU B 316 -60.17 -121.03
REMARK 500 GLN C 2 152.69 61.08
REMARK 500 PHE C 4 -28.44 -154.72
REMARK 500 PRO C 50 68.15 -67.39
REMARK 500 ARG C 118 118.50 -26.16
REMARK 500 GLN C 120 -90.19 -92.91
REMARK 500 SER C 123 148.04 74.10
REMARK 500 SER C 181 -112.27 58.83
REMARK 500 TYR C 204 71.17 25.98
REMARK 500 LEU C 223 -9.46 -59.56
REMARK 500 LEU C 316 -60.96 -120.55
REMARK 500 LEU C 318 51.35 -105.04
REMARK 500 GLN D 2 135.51 56.07
REMARK 500 PHE D 4 -25.67 -155.86
REMARK 500 PRO D 50 70.74 -66.69
REMARK 500 PHE D 64 134.58 -37.99
REMARK 500 ARG D 118 118.98 -26.39
REMARK 500 GLN D 120 -90.98 -91.59
REMARK 500 SER D 123 146.71 73.29
REMARK 500 SER D 181 -111.98 57.40
REMARK 500 TYR D 204 72.10 24.62
REMARK 500 LEU D 223 -8.20 -59.97
REMARK 500 LEU D 316 -60.42 -121.07
REMARK 500 GLN E 2 151.78 27.66
REMARK 500 PHE E 4 -26.92 -155.79
REMARK 500 PRO E 50 69.99 -67.35
REMARK 500 ARG E 118 119.36 -26.70
REMARK 500 GLN E 120 -89.63 -92.88
REMARK 500 SER E 123 146.39 75.25
REMARK 500 SER E 181 -112.48 58.18
REMARK 500 TYR E 204 71.77 25.05
REMARK 500
REMARK 500 THIS ENTRY HAS 117 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 321
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 322
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 321
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 322
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 321
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 322
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE C 323
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 324
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 325
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 D 321
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 322
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 323
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 321
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 322
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 321
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE F 322
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 323
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 324
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 G 321
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 322
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 323
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG H 321
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 H 322
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG H 323
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 324
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 325
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL I 321
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 322
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 323
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 321
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 322
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 323
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG M 321
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 322
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 323
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 321
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 322
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ODS RELATED DB: PDB
REMARK 900 CEPHALOSPORIN C DEACETYLASE FROM BACILLUS SUBTILIS
REMARK 900 RELATED ID: 1ODT RELATED DB: PDB
REMARK 900 CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH ACETATE
REMARK 900 RELATED ID: 1L7A RELATED DB: PDB
REMARK 900 STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF CEPHALOSPORIN C
REMARK 900 DEACETYLASE
REMARK 900 RELATED ID: 1VLQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM
REMARK 900 THERMOTOGA MARITIMA AT 2.10 A RESOLUTION
REMARK 900 RELATED ID: 3FCY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE 1 FROM
REMARK 900 THERMOANAEROBACTERIUM SP. JW/SL YS485
REMARK 900 RELATED ID: 3FVT RELATED DB: PDB
DBREF 3FVR A 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR B 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR C 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR D 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR E 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR F 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR G 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR H 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR I 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR L 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR M 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
DBREF 3FVR N 1 320 UNP Q9K5F2 Q9K5F2_BACPU 1 320
SEQRES 1 A 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 A 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 A 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 A 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 A 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 A 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 A 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 A 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 A 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 A 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 A 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 A 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 A 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 A 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 A 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 A 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 A 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 A 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 A 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 A 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 A 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 A 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 A 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 A 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 A 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 B 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 B 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 B 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 B 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 B 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 B 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 B 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 B 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 B 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 B 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 B 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 B 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 B 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 B 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 B 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 B 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 B 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 B 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 B 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 B 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 B 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 B 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 B 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 B 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 B 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 C 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 C 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 C 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 C 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 C 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 C 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 C 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 C 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 C 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 C 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 C 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 C 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 C 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 C 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 C 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 C 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 C 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 C 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 C 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 C 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 C 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 C 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 C 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 C 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 C 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 D 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 D 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 D 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 D 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 D 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 D 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 D 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 D 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 D 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 D 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 D 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 D 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 D 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 D 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 D 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 D 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 D 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 D 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 D 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 D 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 D 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 D 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 D 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 D 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 D 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 E 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 E 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 E 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 E 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 E 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 E 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 E 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 E 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 E 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 E 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 E 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 E 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 E 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 E 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 E 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 E 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 E 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 E 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 E 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 E 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 E 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 E 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 E 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 E 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 E 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 F 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 F 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 F 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 F 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 F 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 F 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 F 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 F 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 F 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 F 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 F 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 F 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 F 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 F 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 F 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 F 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 F 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 F 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 F 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 F 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 F 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 F 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 F 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 F 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 F 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 G 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 G 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 G 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 G 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 G 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 G 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 G 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 G 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 G 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 G 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 G 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 G 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 G 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 G 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 G 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 G 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 G 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 G 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 G 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 G 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 G 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 G 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 G 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 G 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 G 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 H 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 H 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 H 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 H 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 H 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 H 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 H 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 H 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 H 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 H 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 H 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 H 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 H 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 H 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 H 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 H 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 H 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 H 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 H 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 H 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 H 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 H 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 H 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 H 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 H 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 I 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 I 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 I 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 I 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 I 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 I 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 I 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 I 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 I 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 I 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 I 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 I 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 I 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 I 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 I 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 I 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 I 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 I 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 I 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 I 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 I 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 I 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 I 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 I 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 I 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 L 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 L 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 L 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 L 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 L 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 L 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 L 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 L 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 L 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 L 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 L 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 L 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 L 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 L 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 L 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 L 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 L 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 L 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 L 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 L 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 L 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 L 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 L 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 L 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 L 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 M 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 M 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 M 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 M 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 M 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 M 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 M 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 M 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 M 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 M 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 M 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 M 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 M 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 M 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 M 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 M 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 M 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 M 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 M 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 M 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 M 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 M 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 M 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 M 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 M 320 GLN LYS HIS LEU LEU LEU SER THR
SEQRES 1 N 320 MET GLN LEU PHE ASP LEU SER LEU GLU GLU LEU LYS LYS
SEQRES 2 N 320 TYR LYS PRO LYS LYS THR ALA ARG PRO ASP PHE SER ASP
SEQRES 3 N 320 PHE TRP LYS LYS SER LEU GLU GLU LEU ARG GLN VAL GLU
SEQRES 4 N 320 ALA GLU PRO THR LEU GLU SER TYR ASP TYR PRO VAL LYS
SEQRES 5 N 320 GLY VAL LYS VAL TYR ARG LEU THR TYR GLN SER PHE GLY
SEQRES 6 N 320 HIS SER LYS ILE GLU GLY PHE TYR ALA VAL PRO ASP GLN
SEQRES 7 N 320 THR GLY PRO HIS PRO ALA LEU VAL ARG PHE HIS GLY TYR
SEQRES 8 N 320 ASN ALA SER TYR ASP GLY GLY ILE HIS ASP ILE VAL ASN
SEQRES 9 N 320 TRP ALA LEU HIS GLY TYR ALA THR PHE GLY MET LEU VAL
SEQRES 10 N 320 ARG GLY GLN GLY GLY SER GLU ASP THR SER VAL THR PRO
SEQRES 11 N 320 GLY GLY HIS ALA LEU GLY TRP MET THR LYS GLY ILE LEU
SEQRES 12 N 320 SER LYS ASP THR TYR TYR TYR ARG GLY VAL TYR LEU ASP
SEQRES 13 N 320 ALA VAL ARG ALA LEU GLU VAL ILE GLN SER PHE PRO GLU
SEQRES 14 N 320 VAL ASP GLU HIS ARG ILE GLY VAL ILE GLY GLY SER GLN
SEQRES 15 N 320 GLY GLY ALA LEU ALA ILE ALA ALA ALA ALA LEU SER ASP
SEQRES 16 N 320 ILE PRO LYS VAL VAL VAL ALA ASP TYR PRO TYR LEU SER
SEQRES 17 N 320 ASN PHE GLU ARG ALA VAL ASP VAL ALA LEU GLU GLN PRO
SEQRES 18 N 320 TYR LEU GLU ILE ASN SER TYR PHE ARG ARG ASN SER ASP
SEQRES 19 N 320 PRO LYS VAL GLU GLU LYS ALA PHE GLU THR LEU SER TYR
SEQRES 20 N 320 PHE ASP LEU ILE ASN LEU ALA GLY TRP VAL LYS GLN PRO
SEQRES 21 N 320 THR LEU MET ALA ILE GLY LEU ILE ASP LYS ILE THR PRO
SEQRES 22 N 320 PRO SER THR VAL PHE ALA ALA TYR ASN HIS LEU GLU THR
SEQRES 23 N 320 ASP LYS ASP LEU LYS VAL TYR ARG TYR PHE GLY HIS GLU
SEQRES 24 N 320 PHE ILE PRO ALA PHE GLN THR GLU LYS LEU SER PHE LEU
SEQRES 25 N 320 GLN LYS HIS LEU LEU LEU SER THR
HET CL A 321 1
HET CL A 322 1
HET CL B 321 1
HET CL B 322 1
HET GOL C 321 6
HET GOL C 322 6
HET PGE C 323 10
HET CL C 324 1
HET CL C 325 1
HET PG4 D 321 13
HET CL D 322 1
HET CL D 323 1
HET CL E 321 1
HET CL E 322 1
HET GOL F 321 6
HET PGE F 322 10
HET CL F 323 1
HET CL F 324 1
HET PG4 G 321 13
HET CL G 322 1
HET CL G 323 1
HET PEG H 321 7
HET PG4 H 322 13
HET PEG H 323 7
HET CL H 324 1
HET CL H 325 1
HET GOL I 321 6
HET CL I 322 1
HET CL I 323 1
HET GOL L 321 6
HET CL L 322 1
HET CL L 323 1
HET PEG M 321 7
HET CL M 322 1
HET CL M 323 1
HET CL N 321 1
HET CL N 322 1
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 13 CL 24(CL 1-)
FORMUL 17 GOL 5(C3 H8 O3)
FORMUL 19 PGE 2(C6 H14 O4)
FORMUL 22 PG4 3(C8 H18 O5)
FORMUL 34 PEG 3(C4 H10 O3)
FORMUL 50 HOH *1792(H2 O)
HELIX 1 1 SER A 7 TYR A 14 1 8
HELIX 2 2 ASP A 23 GLN A 37 1 15
HELIX 3 3 PHE A 64 HIS A 66 5 3
HELIX 4 4 TYR A 95 GLY A 97 5 3
HELIX 5 5 GLY A 98 HIS A 108 1 11
HELIX 6 6 TYR A 148 SER A 166 1 19
HELIX 7 7 SER A 181 SER A 194 1 14
HELIX 8 8 ASN A 209 ALA A 217 1 9
HELIX 9 9 TYR A 222 ASN A 232 1 11
HELIX 10 10 ASP A 234 TYR A 247 1 14
HELIX 11 11 ASP A 249 ALA A 254 1 6
HELIX 12 12 GLY A 255 VAL A 257 5 3
HELIX 13 13 PRO A 273 ASN A 282 1 10
HELIX 14 14 ILE A 301 LEU A 316 1 16
HELIX 15 15 SER B 7 TYR B 14 1 8
HELIX 16 16 ASP B 23 GLN B 37 1 15
HELIX 17 17 PHE B 64 HIS B 66 5 3
HELIX 18 18 TYR B 95 GLY B 97 5 3
HELIX 19 19 GLY B 98 HIS B 108 1 11
HELIX 20 20 TYR B 148 SER B 166 1 19
HELIX 21 21 SER B 181 SER B 194 1 14
HELIX 22 22 ASN B 209 ALA B 217 1 9
HELIX 23 23 LEU B 223 ASN B 232 1 10
HELIX 24 24 ASP B 234 TYR B 247 1 14
HELIX 25 25 ASP B 249 ALA B 254 1 6
HELIX 26 26 GLY B 255 VAL B 257 5 3
HELIX 27 27 PRO B 273 ASN B 282 1 10
HELIX 28 28 ILE B 301 LEU B 316 1 16
HELIX 29 29 SER C 7 TYR C 14 1 8
HELIX 30 30 ASP C 23 GLN C 37 1 15
HELIX 31 31 PHE C 64 HIS C 66 5 3
HELIX 32 32 TYR C 95 GLY C 97 5 3
HELIX 33 33 GLY C 98 HIS C 108 1 11
HELIX 34 34 TYR C 148 PHE C 167 1 20
HELIX 35 35 SER C 181 SER C 194 1 14
HELIX 36 36 ASN C 209 ALA C 217 1 9
HELIX 37 37 TYR C 222 ASN C 232 1 11
HELIX 38 38 ASP C 234 TYR C 247 1 14
HELIX 39 39 ASP C 249 ALA C 254 1 6
HELIX 40 40 GLY C 255 VAL C 257 5 3
HELIX 41 41 PRO C 273 ASN C 282 1 10
HELIX 42 42 ILE C 301 LEU C 316 1 16
HELIX 43 43 SER D 7 TYR D 14 1 8
HELIX 44 44 ASP D 23 GLN D 37 1 15
HELIX 45 45 PHE D 64 HIS D 66 5 3
HELIX 46 46 TYR D 95 GLY D 97 5 3
HELIX 47 47 GLY D 98 HIS D 108 1 11
HELIX 48 48 TYR D 148 SER D 166 1 19
HELIX 49 49 SER D 181 SER D 194 1 14
HELIX 50 50 ASN D 209 ALA D 217 1 9
HELIX 51 51 LEU D 223 ASN D 232 1 10
HELIX 52 52 ASP D 234 TYR D 247 1 14
HELIX 53 53 ASP D 249 ALA D 254 1 6
HELIX 54 54 GLY D 255 VAL D 257 5 3
HELIX 55 55 PRO D 273 ASN D 282 1 10
HELIX 56 56 ILE D 301 LEU D 316 1 16
HELIX 57 57 SER E 7 TYR E 14 1 8
HELIX 58 58 ASP E 23 GLN E 37 1 15
HELIX 59 59 PHE E 64 HIS E 66 5 3
HELIX 60 60 TYR E 95 GLY E 97 5 3
HELIX 61 61 GLY E 98 HIS E 108 1 11
HELIX 62 62 TYR E 148 SER E 166 1 19
HELIX 63 63 SER E 181 SER E 194 1 14
HELIX 64 64 ASN E 209 ALA E 217 1 9
HELIX 65 65 TYR E 222 ASN E 232 1 11
HELIX 66 66 ASP E 234 TYR E 247 1 14
HELIX 67 67 ASP E 249 ALA E 254 1 6
HELIX 68 68 GLY E 255 VAL E 257 5 3
HELIX 69 69 PRO E 273 ASN E 282 1 10
HELIX 70 70 ILE E 301 LEU E 316 1 16
HELIX 71 71 SER F 7 TYR F 14 1 8
HELIX 72 72 ASP F 23 GLN F 37 1 15
HELIX 73 73 PHE F 64 HIS F 66 5 3
HELIX 74 74 TYR F 95 GLY F 97 5 3
HELIX 75 75 GLY F 98 HIS F 108 1 11
HELIX 76 76 TYR F 148 SER F 166 1 19
HELIX 77 77 SER F 181 SER F 194 1 14
HELIX 78 78 ASN F 209 ALA F 217 1 9
HELIX 79 79 LEU F 223 ASN F 232 1 10
HELIX 80 80 ASP F 234 TYR F 247 1 14
HELIX 81 81 ASP F 249 ALA F 254 1 6
HELIX 82 82 GLY F 255 VAL F 257 5 3
HELIX 83 83 PRO F 273 ASN F 282 1 10
HELIX 84 84 ILE F 301 LEU F 316 1 16
HELIX 85 85 SER G 7 LYS G 12 1 6
HELIX 86 86 ASP G 23 GLN G 37 1 15
HELIX 87 87 PHE G 64 HIS G 66 5 3
HELIX 88 88 TYR G 95 GLY G 97 5 3
HELIX 89 89 GLY G 98 HIS G 108 1 11
HELIX 90 90 TYR G 148 PHE G 167 1 20
HELIX 91 91 SER G 181 SER G 194 1 14
HELIX 92 92 ASN G 209 ALA G 217 1 9
HELIX 93 93 TYR G 222 ASN G 232 1 11
HELIX 94 94 ASP G 234 TYR G 247 1 14
HELIX 95 95 ASP G 249 ALA G 254 1 6
HELIX 96 96 GLY G 255 VAL G 257 5 3
HELIX 97 97 PRO G 273 ASN G 282 1 10
HELIX 98 98 ILE G 301 LEU G 316 1 16
HELIX 99 99 SER H 7 TYR H 14 1 8
HELIX 100 100 ASP H 23 GLN H 37 1 15
HELIX 101 101 PHE H 64 HIS H 66 5 3
HELIX 102 102 TYR H 95 GLY H 97 5 3
HELIX 103 103 GLY H 98 HIS H 108 1 11
HELIX 104 104 TYR H 148 SER H 166 1 19
HELIX 105 105 SER H 181 SER H 194 1 14
HELIX 106 106 ASN H 209 ALA H 217 1 9
HELIX 107 107 LEU H 223 ASN H 232 1 10
HELIX 108 108 ASP H 234 TYR H 247 1 14
HELIX 109 109 ASP H 249 ALA H 254 1 6
HELIX 110 110 GLY H 255 VAL H 257 5 3
HELIX 111 111 PRO H 273 ASN H 282 1 10
HELIX 112 112 ILE H 301 LEU H 316 1 16
HELIX 113 113 SER I 7 TYR I 14 1 8
HELIX 114 114 ASP I 23 GLN I 37 1 15
HELIX 115 115 PHE I 64 HIS I 66 5 3
HELIX 116 116 TYR I 95 GLY I 97 5 3
HELIX 117 117 GLY I 98 HIS I 108 1 11
HELIX 118 118 TYR I 148 SER I 166 1 19
HELIX 119 119 SER I 181 SER I 194 1 14
HELIX 120 120 ASN I 209 ALA I 217 1 9
HELIX 121 121 TYR I 222 ASN I 232 1 11
HELIX 122 122 ASP I 234 TYR I 247 1 14
HELIX 123 123 ASP I 249 ALA I 254 1 6
HELIX 124 124 GLY I 255 VAL I 257 5 3
HELIX 125 125 PRO I 273 ASN I 282 1 10
HELIX 126 126 ILE I 301 LEU I 316 1 16
HELIX 127 127 SER L 7 TYR L 14 1 8
HELIX 128 128 ASP L 23 GLN L 37 1 15
HELIX 129 129 PHE L 64 HIS L 66 5 3
HELIX 130 130 TYR L 95 GLY L 97 5 3
HELIX 131 131 GLY L 98 HIS L 108 1 11
HELIX 132 132 TYR L 148 SER L 166 1 19
HELIX 133 133 SER L 181 SER L 194 1 14
HELIX 134 134 ASN L 209 ALA L 217 1 9
HELIX 135 135 LEU L 223 ASN L 232 1 10
HELIX 136 136 ASP L 234 TYR L 247 1 14
HELIX 137 137 ASP L 249 ALA L 254 1 6
HELIX 138 138 GLY L 255 VAL L 257 5 3
HELIX 139 139 PRO L 273 ASN L 282 1 10
HELIX 140 140 ILE L 301 LEU L 316 1 16
HELIX 141 141 SER M 7 TYR M 14 1 8
HELIX 142 142 ASP M 23 GLN M 37 1 15
HELIX 143 143 PHE M 64 HIS M 66 5 3
HELIX 144 144 TYR M 95 GLY M 97 5 3
HELIX 145 145 GLY M 98 HIS M 108 1 11
HELIX 146 146 TYR M 148 PHE M 167 1 20
HELIX 147 147 SER M 181 SER M 194 1 14
HELIX 148 148 ASN M 209 ALA M 217 1 9
HELIX 149 149 LEU M 223 ASN M 232 1 10
HELIX 150 150 ASP M 234 TYR M 247 1 14
HELIX 151 151 ASP M 249 ALA M 254 1 6
HELIX 152 152 GLY M 255 VAL M 257 5 3
HELIX 153 153 PRO M 273 ASN M 282 1 10
HELIX 154 154 ILE M 301 LEU M 316 1 16
HELIX 155 155 SER N 7 TYR N 14 1 8
HELIX 156 156 ASP N 23 GLN N 37 1 15
HELIX 157 157 PHE N 64 HIS N 66 5 3
HELIX 158 158 TYR N 95 GLY N 97 5 3
HELIX 159 159 GLY N 98 HIS N 108 1 11
HELIX 160 160 TYR N 148 SER N 166 1 19
HELIX 161 161 SER N 181 SER N 194 1 14
HELIX 162 162 ASN N 209 ALA N 217 1 9
HELIX 163 163 LEU N 223 ASN N 232 1 10
HELIX 164 164 ASP N 234 TYR N 247 1 14
HELIX 165 165 ASP N 249 ALA N 254 1 6
HELIX 166 166 GLY N 255 VAL N 257 5 3
HELIX 167 167 PRO N 273 ASN N 282 1 10
HELIX 168 168 ILE N 301 LEU N 316 1 16
SHEET 1 A 9 THR A 43 TYR A 47 0
SHEET 2 A 9 VAL A 54 SER A 63 -1 O VAL A 56 N TYR A 47
SHEET 3 A 9 SER A 67 PRO A 76 -1 O GLY A 71 N LEU A 59
SHEET 4 A 9 ALA A 111 MET A 115 -1 O THR A 112 N ALA A 74
SHEET 5 A 9 HIS A 82 PHE A 88 1 N PRO A 83 O ALA A 111
SHEET 6 A 9 VAL A 170 GLY A 180 1 O GLY A 176 N ALA A 84
SHEET 7 A 9 VAL A 199 ASP A 203 1 O ASP A 203 N GLY A 179
SHEET 8 A 9 THR A 261 GLY A 266 1 O LEU A 262 N ALA A 202
SHEET 9 A 9 LYS A 288 TYR A 293 1 O LYS A 291 N MET A 263
SHEET 1 B 9 THR B 43 SER B 46 0
SHEET 2 B 9 VAL B 54 SER B 63 -1 O ARG B 58 N GLU B 45
SHEET 3 B 9 SER B 67 PRO B 76 -1 O GLY B 71 N LEU B 59
SHEET 4 B 9 ALA B 111 MET B 115 -1 O THR B 112 N ALA B 74
SHEET 5 B 9 HIS B 82 PHE B 88 1 N PRO B 83 O ALA B 111
SHEET 6 B 9 VAL B 170 GLY B 180 1 O GLY B 176 N ALA B 84
SHEET 7 B 9 VAL B 199 ASP B 203 1 O ASP B 203 N GLY B 179
SHEET 8 B 9 THR B 261 GLY B 266 1 O LEU B 262 N ALA B 202
SHEET 9 B 9 LYS B 288 TYR B 293 1 O LYS B 291 N MET B 263
SHEET 1 C 9 THR C 43 SER C 46 0
SHEET 2 C 9 VAL C 54 SER C 63 -1 O ARG C 58 N GLU C 45
SHEET 3 C 9 SER C 67 PRO C 76 -1 O TYR C 73 N TYR C 57
SHEET 4 C 9 ALA C 111 MET C 115 -1 O THR C 112 N ALA C 74
SHEET 5 C 9 HIS C 82 PHE C 88 1 N ARG C 87 O PHE C 113
SHEET 6 C 9 VAL C 170 GLY C 180 1 O GLY C 176 N ALA C 84
SHEET 7 C 9 VAL C 199 ASP C 203 1 O ASP C 203 N GLY C 179
SHEET 8 C 9 THR C 261 GLY C 266 1 O LEU C 262 N ALA C 202
SHEET 9 C 9 LYS C 288 TYR C 293 1 O LYS C 291 N MET C 263
SHEET 1 D 9 THR D 43 TYR D 47 0
SHEET 2 D 9 VAL D 54 SER D 63 -1 O VAL D 56 N TYR D 47
SHEET 3 D 9 SER D 67 PRO D 76 -1 O TYR D 73 N TYR D 57
SHEET 4 D 9 ALA D 111 MET D 115 -1 O THR D 112 N ALA D 74
SHEET 5 D 9 HIS D 82 PHE D 88 1 N ARG D 87 O PHE D 113
SHEET 6 D 9 VAL D 170 GLY D 180 1 O GLY D 176 N ALA D 84
SHEET 7 D 9 VAL D 199 ASP D 203 1 O ASP D 203 N GLY D 179
SHEET 8 D 9 THR D 261 GLY D 266 1 O LEU D 262 N ALA D 202
SHEET 9 D 9 LYS D 288 TYR D 293 1 O LYS D 291 N MET D 263
SHEET 1 E 9 THR E 43 SER E 46 0
SHEET 2 E 9 VAL E 54 SER E 63 -1 O ARG E 58 N GLU E 45
SHEET 3 E 9 SER E 67 PRO E 76 -1 O TYR E 73 N TYR E 57
SHEET 4 E 9 ALA E 111 MET E 115 -1 O THR E 112 N ALA E 74
SHEET 5 E 9 HIS E 82 PHE E 88 1 N LEU E 85 O ALA E 111
SHEET 6 E 9 VAL E 170 GLY E 180 1 O GLY E 176 N ALA E 84
SHEET 7 E 9 VAL E 199 ASP E 203 1 O ASP E 203 N GLY E 179
SHEET 8 E 9 THR E 261 GLY E 266 1 O LEU E 262 N ALA E 202
SHEET 9 E 9 LYS E 288 TYR E 293 1 O TYR E 293 N ILE E 265
SHEET 1 F 9 THR F 43 SER F 46 0
SHEET 2 F 9 VAL F 54 SER F 63 -1 O ARG F 58 N GLU F 45
SHEET 3 F 9 SER F 67 PRO F 76 -1 O GLY F 71 N LEU F 59
SHEET 4 F 9 ALA F 111 MET F 115 -1 O THR F 112 N ALA F 74
SHEET 5 F 9 HIS F 82 PHE F 88 1 N PRO F 83 O ALA F 111
SHEET 6 F 9 VAL F 170 GLY F 180 1 O GLY F 176 N ALA F 84
SHEET 7 F 9 VAL F 199 ASP F 203 1 O ASP F 203 N GLY F 179
SHEET 8 F 9 THR F 261 GLY F 266 1 O LEU F 262 N ALA F 202
SHEET 9 F 9 LYS F 288 TYR F 293 1 O LYS F 291 N MET F 263
SHEET 1 G 9 THR G 43 SER G 46 0
SHEET 2 G 9 VAL G 54 SER G 63 -1 O ARG G 58 N GLU G 45
SHEET 3 G 9 SER G 67 PRO G 76 -1 O TYR G 73 N TYR G 57
SHEET 4 G 9 ALA G 111 MET G 115 -1 O THR G 112 N ALA G 74
SHEET 5 G 9 HIS G 82 PHE G 88 1 N PRO G 83 O ALA G 111
SHEET 6 G 9 VAL G 170 GLY G 180 1 O ARG G 174 N ALA G 84
SHEET 7 G 9 VAL G 199 ASP G 203 1 O ASP G 203 N GLY G 179
SHEET 8 G 9 THR G 261 GLY G 266 1 O LEU G 262 N ALA G 202
SHEET 9 G 9 LYS G 288 TYR G 293 1 O LYS G 291 N MET G 263
SHEET 1 H 9 THR H 43 TYR H 47 0
SHEET 2 H 9 VAL H 54 SER H 63 -1 O VAL H 56 N TYR H 47
SHEET 3 H 9 SER H 67 PRO H 76 -1 O GLY H 71 N LEU H 59
SHEET 4 H 9 ALA H 111 MET H 115 -1 O THR H 112 N ALA H 74
SHEET 5 H 9 HIS H 82 PHE H 88 1 N LEU H 85 O ALA H 111
SHEET 6 H 9 VAL H 170 GLY H 180 1 O ARG H 174 N ALA H 84
SHEET 7 H 9 VAL H 199 ASP H 203 1 O ASP H 203 N GLY H 179
SHEET 8 H 9 THR H 261 GLY H 266 1 O LEU H 262 N ALA H 202
SHEET 9 H 9 LYS H 288 TYR H 293 1 O TYR H 293 N ILE H 265
SHEET 1 I 9 THR I 43 SER I 46 0
SHEET 2 I 9 VAL I 54 SER I 63 -1 O ARG I 58 N GLU I 45
SHEET 3 I 9 SER I 67 PRO I 76 -1 O TYR I 73 N TYR I 57
SHEET 4 I 9 ALA I 111 MET I 115 -1 O THR I 112 N ALA I 74
SHEET 5 I 9 HIS I 82 PHE I 88 1 N PRO I 83 O ALA I 111
SHEET 6 I 9 VAL I 170 GLY I 180 1 O GLY I 176 N ALA I 84
SHEET 7 I 9 VAL I 199 ASP I 203 1 O ASP I 203 N GLY I 179
SHEET 8 I 9 THR I 261 GLY I 266 1 O LEU I 262 N ALA I 202
SHEET 9 I 9 LYS I 288 TYR I 293 1 O TYR I 293 N ILE I 265
SHEET 1 J 9 THR L 43 TYR L 47 0
SHEET 2 J 9 VAL L 54 SER L 63 -1 O VAL L 56 N TYR L 47
SHEET 3 J 9 SER L 67 PRO L 76 -1 O TYR L 73 N TYR L 57
SHEET 4 J 9 ALA L 111 MET L 115 -1 O THR L 112 N ALA L 74
SHEET 5 J 9 HIS L 82 PHE L 88 1 N PRO L 83 O ALA L 111
SHEET 6 J 9 VAL L 170 GLY L 180 1 O GLY L 176 N ALA L 84
SHEET 7 J 9 VAL L 199 ASP L 203 1 O ASP L 203 N GLY L 179
SHEET 8 J 9 THR L 261 GLY L 266 1 O LEU L 262 N ALA L 202
SHEET 9 J 9 LYS L 288 TYR L 293 1 O TYR L 293 N ILE L 265
SHEET 1 K 9 THR M 43 TYR M 47 0
SHEET 2 K 9 VAL M 54 SER M 63 -1 O VAL M 56 N TYR M 47
SHEET 3 K 9 SER M 67 PRO M 76 -1 O GLY M 71 N LEU M 59
SHEET 4 K 9 ALA M 111 MET M 115 -1 O THR M 112 N ALA M 74
SHEET 5 K 9 HIS M 82 PHE M 88 1 N PRO M 83 O ALA M 111
SHEET 6 K 9 VAL M 170 GLY M 180 1 O GLY M 176 N ALA M 84
SHEET 7 K 9 VAL M 199 ASP M 203 1 O ASP M 203 N GLY M 179
SHEET 8 K 9 THR M 261 GLY M 266 1 O LEU M 262 N ALA M 202
SHEET 9 K 9 LYS M 288 TYR M 293 1 O LYS M 291 N MET M 263
SHEET 1 L 9 THR N 43 TYR N 47 0
SHEET 2 L 9 VAL N 54 SER N 63 -1 O VAL N 56 N TYR N 47
SHEET 3 L 9 SER N 67 PRO N 76 -1 O TYR N 73 N TYR N 57
SHEET 4 L 9 ALA N 111 MET N 115 -1 O THR N 112 N ALA N 74
SHEET 5 L 9 HIS N 82 PHE N 88 1 N PRO N 83 O ALA N 111
SHEET 6 L 9 VAL N 170 GLY N 180 1 O GLY N 176 N ALA N 84
SHEET 7 L 9 VAL N 199 ASP N 203 1 O ASP N 203 N GLY N 179
SHEET 8 L 9 THR N 261 GLY N 266 1 O LEU N 262 N ALA N 202
SHEET 9 L 9 LYS N 288 TYR N 293 1 O TYR N 293 N ILE N 265
CISPEP 1 GLY A 80 PRO A 81 0 -0.06
CISPEP 2 GLN A 220 PRO A 221 0 -0.04
CISPEP 3 GLY B 80 PRO B 81 0 0.05
CISPEP 4 GLN B 220 PRO B 221 0 0.14
CISPEP 5 GLY C 80 PRO C 81 0 0.22
CISPEP 6 GLN C 220 PRO C 221 0 0.10
CISPEP 7 GLY D 80 PRO D 81 0 -0.04
CISPEP 8 GLN D 220 PRO D 221 0 0.00
CISPEP 9 GLY E 80 PRO E 81 0 0.00
CISPEP 10 GLN E 220 PRO E 221 0 0.15
CISPEP 11 GLY F 80 PRO F 81 0 0.07
CISPEP 12 GLN F 220 PRO F 221 0 0.28
CISPEP 13 GLY G 80 PRO G 81 0 0.03
CISPEP 14 GLN G 220 PRO G 221 0 0.05
CISPEP 15 GLY H 80 PRO H 81 0 -0.06
CISPEP 16 GLN H 220 PRO H 221 0 0.10
CISPEP 17 GLY I 80 PRO I 81 0 -0.24
CISPEP 18 GLN I 220 PRO I 221 0 -0.01
CISPEP 19 GLY L 80 PRO L 81 0 -0.12
CISPEP 20 GLN L 220 PRO L 221 0 0.00
CISPEP 21 GLY M 80 PRO M 81 0 0.01
CISPEP 22 GLN M 220 PRO M 221 0 0.18
CISPEP 23 GLY N 80 PRO N 81 0 0.03
CISPEP 24 GLN N 220 PRO N 221 0 0.31
SITE 1 AC1 4 GLY A 141 ILE A 142 LEU A 143 HOH A 925
SITE 1 AC2 3 LYS A 270 HIS A 298 HOH A1591
SITE 1 AC3 4 PRO B 130 GLY B 141 LEU B 143 HOH B 742
SITE 1 AC4 2 LYS B 270 HIS B 298
SITE 1 AC5 6 THR C 129 HIS C 133 LYS C 140 HOH C 863
SITE 2 AC5 6 HOH C1282 TRP E 137
SITE 1 AC6 7 ASP C 101 TRP C 105 HIS C 108 GLN C 305
SITE 2 AC6 7 PGE C 323 ASN D 104 HOH D1787
SITE 1 AC7 8 ARG C 87 TRP C 105 ILE C 178 GLY C 179
SITE 2 AC7 8 ASP C 203 GLN C 305 LYS C 308 GOL C 322
SITE 1 AC8 5 PRO C 130 GLY C 141 ILE C 142 LEU C 143
SITE 2 AC8 5 HOH C1065
SITE 1 AC9 2 LYS C 270 HIS C 298
SITE 1 BC1 3 TYR C 95 GLU D 299 PHE D 300
SITE 1 BC2 4 GLY D 141 ILE D 142 LEU D 143 HOH D 973
SITE 1 BC3 2 LYS D 270 HIS D 298
SITE 1 BC4 5 GLY E 141 ILE E 142 LEU E 143 HOH E 338
SITE 2 BC4 5 HOH E1099
SITE 1 BC5 2 LYS E 270 HIS E 298
SITE 1 BC6 6 ASN B 104 ASP F 101 ASN F 104 TRP F 105
SITE 2 BC6 6 HIS F 108 GLN F 305
SITE 1 BC7 8 GLY F 90 ILE F 178 GLY F 179 GLY F 180
SITE 2 BC7 8 SER F 181 TYR F 204 LYS F 308 HOH F 908
SITE 1 BC8 6 PRO F 130 GLY F 141 ILE F 142 LEU F 143
SITE 2 BC8 6 HOH F 328 HOH F 336
SITE 1 BC9 2 LYS F 270 HIS F 298
SITE 1 CC1 11 ARG G 87 ASP G 101 TRP G 105 HIS G 108
SITE 2 CC1 11 ILE G 178 GLY G 179 GLN G 305 LEU G 309
SITE 3 CC1 11 TYR L 49 HIS L 100 ASN L 104
SITE 1 CC2 3 GLY G 141 ILE G 142 LEU G 143
SITE 1 CC3 2 LYS G 270 HIS G 298
SITE 1 CC4 4 GLU H 299 PHE H 300 HOH H1071 TYR N 95
SITE 1 CC5 11 GLY H 90 GLY H 180 SER H 181 ASP H 203
SITE 2 CC5 11 TYR H 204 HIS H 298 GLU H 299 PHE H 300
SITE 3 CC5 11 ILE H 301 LYS H 308 HOH H 327
SITE 1 CC6 2 ALA H 192 TRP H 256
SITE 1 CC7 3 GLY H 141 ILE H 142 LEU H 143
SITE 1 CC8 2 LYS H 270 HIS H 298
SITE 1 CC9 5 TYR I 91 ASN I 92 GLN I 220 HOH I1060
SITE 2 CC9 5 LEU N 135
SITE 1 DC1 3 GLY I 141 ILE I 142 LEU I 143
SITE 1 DC2 2 LYS I 270 HIS I 298
SITE 1 DC3 7 ASP G 101 ASN G 104 HOH G 332 ASP L 101
SITE 2 DC3 7 ASN L 104 PHE L 300 HOH L1792
SITE 1 DC4 3 GLY L 141 ILE L 142 LEU L 143
SITE 1 DC5 2 LYS L 270 HIS L 298
SITE 1 DC6 3 GLN M 220 PRO M 221 GLU M 224
SITE 1 DC7 3 GLY M 141 ILE M 142 LEU M 143
SITE 1 DC8 2 LYS M 270 HIS M 298
SITE 1 DC9 4 GLY N 141 ILE N 142 LEU N 143 HOH N1724
SITE 1 EC1 2 LYS N 270 HIS N 298
CRYST1 87.485 167.686 144.961 90.00 91.35 90.00 P 1 21 1 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 0.011431 0.000000 0.000269 0.00000
SCALE2 0.000000 0.005964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006900 0.00000
TER 2559 THR A 320
TER 5104 LEU B 318
TER 7663 THR C 320
TER 10208 LEU D 318
TER 12753 LEU E 318
TER 15290 LEU F 318
TER 17827 LEU G 318
TER 20364 LEU H 318
TER 22915 SER I 319
TER 25452 LEU L 318
TER 27997 LEU M 318
TER 30534 LEU N 318
MASTER 484 0 37 168 108 0 51 632448 12 110 300
END |