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HEADER HYDROLASE 29-JAN-18 5Z7J
TITLE CRYSTAL STRUCTURE OF A LACTONASE DOUBLE MUTANT IN COMPLEX WITH LIGAND
TITLE 2 L
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTONASE FOR PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: UNP RESIDUES 3-266;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHINOCLADIELLA MACKENZIEI CBS 650.93;
SOURCE 3 ORGANISM_TAXID: 1442369;
SOURCE 4 GENE: Z518_04590;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-46 EK/LIC
KEYWDS ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Y.ZHENG,W.D.LIU,C.C.CHEN,R.T.GUO
REVDAT 1 02-MAY-18 5Z7J 0
JRNL AUTH Y.Y.ZHENG,W.T.LIU,C.C.CHEN,X.Y.HU,W.D.LIU,T.P.KO,X.K.TANG,
JRNL AUTH 2 H.L.WEI,J.W.HUANG,R.T.GUO
JRNL TITL CRYSTAL STRUCTURE OF A MYCOESTROGEN-DETOXIFYING LACTONASE
JRNL TITL 2 FROM RHINOCLADIELLA MACKENZIEI: MOLECULAR INSIGHT INTO ZHD
JRNL TITL 3 SUBSTRATE SELECTIVITY
JRNL REF ACS CATALYSIS V. 8 4294 2018
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.8B00464
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 188061
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2002
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.7163 - 4.2585 0.99 18919 202 0.1389 0.1663
REMARK 3 2 4.2585 - 3.3828 0.99 18836 200 0.1425 0.1859
REMARK 3 3 3.3828 - 2.9560 0.98 18826 201 0.1659 0.1945
REMARK 3 4 2.9560 - 2.6861 0.98 18742 207 0.1757 0.2374
REMARK 3 5 2.6861 - 2.4938 0.98 18687 195 0.1811 0.2394
REMARK 3 6 2.4938 - 2.3469 0.97 18626 208 0.1846 0.2250
REMARK 3 7 2.3469 - 2.2294 0.97 18633 205 0.1927 0.2670
REMARK 3 8 2.2294 - 2.1324 0.97 18529 182 0.2114 0.2778
REMARK 3 9 2.1324 - 2.0504 0.97 18445 199 0.2269 0.2991
REMARK 3 10 2.0504 - 1.9797 0.93 17816 203 0.2442 0.2868
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.10
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 : 0.008 17049
REMARK 3 ANGLE : 0.953 23281
REMARK 3 CHIRALITY : 0.057 2538
REMARK 3 PLANARITY : 0.007 3032
REMARK 3 DIHEDRAL : 12.834 10120
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 5Z7J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1300006384.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL15A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 188099
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.66000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5IE4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.085M SODIUM
REMARK 280 CACODYLATE PH 6.5, 25-28%(W/V) POLYETHYLENE GLYCOL 8000 AND 15%
REMARK 280 (V/V) GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 3
REMARK 465 ALA B 3
REMARK 465 LYS E 266
REMARK 465 ALA F 3
REMARK 465 LYS G 266
REMARK 465 ALA H 3
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 SER A 65 -126.60 45.72
REMARK 500 ALA A 105 -118.61 52.76
REMARK 500 GLU A 129 73.43 49.69
REMARK 500 ASN A 163 95.92 -173.52
REMARK 500 TYR A 189 -65.49 -105.68
REMARK 500 ASN A 242 -107.00 -123.36
REMARK 500 SER B 65 -124.78 46.66
REMARK 500 ALA B 105 -118.65 53.70
REMARK 500 GLU B 129 71.35 49.26
REMARK 500 ASN B 163 91.56 -176.13
REMARK 500 ASN B 242 -109.32 -126.08
REMARK 500 SER C 65 -122.92 47.81
REMARK 500 ALA C 105 -118.33 53.42
REMARK 500 GLU C 129 70.71 52.66
REMARK 500 ASN C 163 92.57 -178.89
REMARK 500 ASN C 242 -103.98 -120.00
REMARK 500 SER D 65 -126.29 42.81
REMARK 500 ALA D 105 -119.46 53.98
REMARK 500 GLU D 129 71.22 53.37
REMARK 500 ASN D 163 85.70 -174.61
REMARK 500 ASN D 242 -108.16 -120.58
REMARK 500 SER E 65 -123.48 43.63
REMARK 500 ALA E 105 -122.10 53.96
REMARK 500 GLU E 133 -140.64 -125.15
REMARK 500 ASN E 134 121.99 -174.58
REMARK 500 ASN E 163 92.44 -179.92
REMARK 500 ASN E 242 -106.50 -119.88
REMARK 500 ASP F 34 -168.63 -78.67
REMARK 500 SER F 65 -122.27 45.15
REMARK 500 TYR F 75 27.09 -148.34
REMARK 500 ALA F 105 -118.50 53.86
REMARK 500 GLU F 129 71.88 53.27
REMARK 500 GLU F 133 108.70 -161.57
REMARK 500 ASN F 163 92.68 -178.02
REMARK 500 ASN F 242 -107.99 -123.08
REMARK 500 ASP G 34 -169.53 -78.69
REMARK 500 SER G 65 -123.12 45.75
REMARK 500 ALA G 105 -119.74 53.80
REMARK 500 GLU G 129 71.55 49.66
REMARK 500 ASN G 163 94.97 -171.23
REMARK 500 ASN G 242 -105.95 -123.43
REMARK 500 SER H 65 -122.74 44.48
REMARK 500 ALA H 105 -121.09 55.06
REMARK 500 GLU H 129 74.03 48.98
REMARK 500 GLU H 133 115.82 -168.52
REMARK 500 ASN H 163 95.29 -175.15
REMARK 500 TYR H 189 -66.14 -109.89
REMARK 500 ASN H 242 -110.07 -118.19
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 G 667 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH G 668 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH H 576 DISTANCE = 5.83 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 36J H 301
DBREF1 5Z7J A 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J A A0A0D2ILK1 3 266
DBREF1 5Z7J B 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J B A0A0D2ILK1 3 266
DBREF1 5Z7J C 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J C A0A0D2ILK1 3 266
DBREF1 5Z7J D 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J D A0A0D2ILK1 3 266
DBREF1 5Z7J E 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J E A0A0D2ILK1 3 266
DBREF1 5Z7J F 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J F A0A0D2ILK1 3 266
DBREF1 5Z7J G 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J G A0A0D2ILK1 3 266
DBREF1 5Z7J H 3 266 UNP A0A0D2ILK1_9EURO
DBREF2 5Z7J H A0A0D2ILK1 3 266
SEQADV 5Z7J ALA A 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA A 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z7J ALA B 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA B 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z7J ALA C 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA C 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z7J ALA D 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA D 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z7J ALA E 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA E 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z7J ALA F 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA F 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z7J ALA G 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA G 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQADV 5Z7J ALA H 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5Z7J ALA H 160 UNP A0A0D2ILK TYR 160 ENGINEERED MUTATION
SEQRES 1 A 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 A 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 A 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 A 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 A 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 A 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 A 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 A 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 A 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 A 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 A 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 A 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 A 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 A 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 A 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 A 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 A 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 A 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 A 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 A 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 A 264 LYS TYR LEU LYS
SEQRES 1 B 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 B 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 B 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 B 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 B 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 B 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 B 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 B 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 B 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 B 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 B 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 B 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 B 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 B 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 B 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 B 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 B 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 B 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 B 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 B 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 B 264 LYS TYR LEU LYS
SEQRES 1 C 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 C 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 C 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 C 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 C 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 C 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 C 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 C 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 C 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 C 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 C 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 C 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 C 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 C 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 C 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 C 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 C 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 C 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 C 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 C 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 C 264 LYS TYR LEU LYS
SEQRES 1 D 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 D 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 D 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 D 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 D 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 D 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 D 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 D 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 D 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 D 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 D 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 D 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 D 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 D 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 D 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 D 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 D 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 D 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 D 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 D 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 D 264 LYS TYR LEU LYS
SEQRES 1 E 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 E 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 E 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 E 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 E 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 E 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 E 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 E 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 E 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 E 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 E 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 E 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 E 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 E 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 E 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 E 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 E 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 E 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 E 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 E 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 E 264 LYS TYR LEU LYS
SEQRES 1 F 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 F 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 F 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 F 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 F 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 F 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 F 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 F 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 F 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 F 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 F 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 F 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 F 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 F 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 F 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 F 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 F 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 F 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 F 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 F 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 F 264 LYS TYR LEU LYS
SEQRES 1 G 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 G 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 G 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 G 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 G 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 G 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 G 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 G 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 G 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 G 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 G 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 G 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 G 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 G 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 G 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 G 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 G 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 G 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 G 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 G 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 G 264 LYS TYR LEU LYS
SEQRES 1 H 264 ALA THR ARG THR ARG GLY TYR VAL THR THR LYS ASP GLY
SEQRES 2 H 264 ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY PRO ASP
SEQRES 3 H 264 VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 4 H 264 PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN GLY PHE
SEQRES 5 H 264 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 6 H 264 SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE THR GLY
SEQRES 7 H 264 ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU ASP THR
SEQRES 8 H 264 LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS ALA SER
SEQRES 9 H 264 GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP TYR PRO
SEQRES 10 H 264 GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL PRO THR
SEQRES 11 H 264 GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU VAL ASP
SEQRES 12 H 264 PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN SER ARG
SEQRES 13 H 264 ALA ALA SER GLY ASN VAL GLU ALA TRP ASP ALA LEU GLY
SEQRES 14 H 264 PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR PRO ARG
SEQRES 15 H 264 TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 H 264 PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO ILE ASP
SEQRES 17 H 264 TRP THR VAL GLY ALA SER THR PRO THR LYS LEU PHE PHE
SEQRES 18 H 264 GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE ASN ILE
SEQRES 19 H 264 GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL SER HIS
SEQRES 20 H 264 PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR SER ARG
SEQRES 21 H 264 LYS TYR LEU LYS
HET 36J A 301 23
HET 36J B 301 23
HET PEG B 302 7
HET PEG B 303 7
HET 36J C 301 23
HET 36J D 301 23
HET 36J E 301 23
HET 36J F 301 23
HET 36J G 301 23
HET 36J H 301 23
HETNAM 36J (3S,7R,11E)-7,14,16-TRIHYDROXY-3-METHYL-3,4,5,6,7,8,9,
HETNAM 2 36J 10-OCTAHYDRO-1H-2-BENZOXACYCLOTETRADECIN-1-ONE
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 9 36J 8(C18 H24 O5)
FORMUL 11 PEG 2(C4 H10 O3)
FORMUL 19 HOH *1864(H2 O)
HELIX 1 AA1 GLU A 38 MET A 41 5 4
HELIX 2 AA2 PHE A 42 SER A 51 1 10
HELIX 3 AA3 MET A 64 SER A 68 5 5
HELIX 4 AA4 PRO A 71 GLN A 76 5 6
HELIX 5 AA5 THR A 79 LEU A 94 1 16
HELIX 6 AA6 ALA A 105 TYR A 118 1 14
HELIX 7 AA7 PRO A 135 LEU A 139 5 5
HELIX 8 AA8 HIS A 140 VAL A 144 5 5
HELIX 9 AA9 ASP A 145 ALA A 160 1 16
HELIX 10 AB1 ASN A 163 ALA A 169 1 7
HELIX 11 AB2 GLY A 171 TYR A 189 1 19
HELIX 12 AB3 ILE A 193 ALA A 197 5 5
HELIX 13 AB4 LYS A 200 LEU A 204 5 5
HELIX 14 AB5 PRO A 218 GLU A 232 1 15
HELIX 15 AB6 PHE A 244 HIS A 249 1 6
HELIX 16 AB7 HIS A 249 LYS A 263 1 15
HELIX 17 AB8 GLU B 38 MET B 41 5 4
HELIX 18 AB9 PHE B 42 SER B 51 1 10
HELIX 19 AC1 MET B 64 SER B 68 5 5
HELIX 20 AC2 PRO B 71 GLN B 76 5 6
HELIX 21 AC3 THR B 79 LEU B 94 1 16
HELIX 22 AC4 ALA B 105 TYR B 118 1 14
HELIX 23 AC5 PRO B 135 LEU B 139 5 5
HELIX 24 AC6 HIS B 140 VAL B 144 5 5
HELIX 25 AC7 ASP B 145 ALA B 160 1 16
HELIX 26 AC8 ASN B 163 ALA B 169 1 7
HELIX 27 AC9 GLY B 171 TYR B 189 1 19
HELIX 28 AD1 ILE B 193 ALA B 197 5 5
HELIX 29 AD2 LYS B 200 LEU B 204 5 5
HELIX 30 AD3 PHE B 222 GLU B 232 1 11
HELIX 31 AD4 PHE B 244 HIS B 249 1 6
HELIX 32 AD5 HIS B 249 LYS B 263 1 15
HELIX 33 AD6 GLU C 38 MET C 41 5 4
HELIX 34 AD7 PHE C 42 SER C 51 1 10
HELIX 35 AD8 MET C 64 SER C 68 5 5
HELIX 36 AD9 PRO C 71 GLN C 76 5 6
HELIX 37 AE1 THR C 79 LEU C 94 1 16
HELIX 38 AE2 ALA C 105 TYR C 118 1 14
HELIX 39 AE3 PRO C 135 LEU C 139 5 5
HELIX 40 AE4 ASP C 145 ALA C 160 1 16
HELIX 41 AE5 ASN C 163 ALA C 169 1 7
HELIX 42 AE6 GLY C 171 TYR C 189 1 19
HELIX 43 AE7 ILE C 193 ALA C 197 5 5
HELIX 44 AE8 LYS C 200 LEU C 204 5 5
HELIX 45 AE9 PRO C 218 LEU C 221 5 4
HELIX 46 AF1 PHE C 222 GLY C 233 1 12
HELIX 47 AF2 PHE C 244 HIS C 249 1 6
HELIX 48 AF3 HIS C 249 LYS C 263 1 15
HELIX 49 AF4 GLU D 38 MET D 41 5 4
HELIX 50 AF5 PHE D 42 SER D 51 1 10
HELIX 51 AF6 MET D 64 SER D 68 5 5
HELIX 52 AF7 PRO D 71 GLN D 76 5 6
HELIX 53 AF8 THR D 79 LEU D 94 1 16
HELIX 54 AF9 ALA D 105 TYR D 118 1 14
HELIX 55 AG1 PRO D 135 LEU D 139 5 5
HELIX 56 AG2 ASP D 145 ALA D 160 1 16
HELIX 57 AG3 ASN D 163 ALA D 169 1 7
HELIX 58 AG4 GLY D 171 TYR D 189 1 19
HELIX 59 AG5 ILE D 193 ALA D 197 5 5
HELIX 60 AG6 LYS D 200 LEU D 204 5 5
HELIX 61 AG7 PRO D 218 LEU D 221 5 4
HELIX 62 AG8 PHE D 222 GLY D 233 1 12
HELIX 63 AG9 PHE D 244 HIS D 249 1 6
HELIX 64 AH1 HIS D 249 LYS D 263 1 15
HELIX 65 AH2 GLU E 38 MET E 41 5 4
HELIX 66 AH3 PHE E 42 SER E 51 1 10
HELIX 67 AH4 MET E 64 SER E 68 5 5
HELIX 68 AH5 PRO E 71 GLN E 76 5 6
HELIX 69 AH6 THR E 79 LEU E 94 1 16
HELIX 70 AH7 ALA E 105 TYR E 118 1 14
HELIX 71 AH8 PRO E 135 LEU E 139 5 5
HELIX 72 AH9 ASP E 145 ALA E 160 1 16
HELIX 73 AI1 ASN E 163 ALA E 169 1 7
HELIX 74 AI2 GLY E 171 TYR E 189 1 19
HELIX 75 AI3 ILE E 193 ALA E 197 5 5
HELIX 76 AI4 LYS E 200 LEU E 204 5 5
HELIX 77 AI5 PHE E 222 GLY E 233 1 12
HELIX 78 AI6 PHE E 244 HIS E 249 1 6
HELIX 79 AI7 HIS E 249 LYS E 263 1 15
HELIX 80 AI8 GLU F 38 MET F 41 5 4
HELIX 81 AI9 PHE F 42 SER F 51 1 10
HELIX 82 AJ1 MET F 64 SER F 68 5 5
HELIX 83 AJ2 PRO F 71 GLN F 76 5 6
HELIX 84 AJ3 THR F 79 LEU F 94 1 16
HELIX 85 AJ4 ALA F 105 TYR F 118 1 14
HELIX 86 AJ5 PRO F 135 LEU F 139 5 5
HELIX 87 AJ6 ASP F 145 ALA F 160 1 16
HELIX 88 AJ7 ASN F 163 ALA F 169 1 7
HELIX 89 AJ8 GLY F 171 TYR F 189 1 19
HELIX 90 AJ9 ILE F 193 ALA F 197 5 5
HELIX 91 AK1 PHE F 222 GLY F 233 1 12
HELIX 92 AK2 PHE F 244 HIS F 249 1 6
HELIX 93 AK3 HIS F 249 LYS F 263 1 15
HELIX 94 AK4 GLU G 38 MET G 41 5 4
HELIX 95 AK5 PHE G 42 SER G 51 1 10
HELIX 96 AK6 MET G 64 SER G 68 5 5
HELIX 97 AK7 PRO G 71 GLN G 76 5 6
HELIX 98 AK8 THR G 79 LEU G 94 1 16
HELIX 99 AK9 ALA G 105 TYR G 118 1 14
HELIX 100 AL1 ASP G 145 ALA G 160 1 16
HELIX 101 AL2 ASN G 163 ALA G 169 1 7
HELIX 102 AL3 GLY G 171 TYR G 189 1 19
HELIX 103 AL4 ILE G 193 ALA G 197 5 5
HELIX 104 AL5 LYS G 200 LEU G 204 5 5
HELIX 105 AL6 PHE G 222 GLY G 233 1 12
HELIX 106 AL7 PHE G 244 HIS G 249 1 6
HELIX 107 AL8 HIS G 249 LYS G 263 1 15
HELIX 108 AL9 GLU H 38 MET H 41 5 4
HELIX 109 AM1 PHE H 42 SER H 51 1 10
HELIX 110 AM2 MET H 64 SER H 68 5 5
HELIX 111 AM3 PRO H 71 GLN H 76 5 6
HELIX 112 AM4 THR H 79 LEU H 94 1 16
HELIX 113 AM5 ALA H 105 TYR H 118 1 14
HELIX 114 AM6 ASP H 145 ALA H 160 1 16
HELIX 115 AM7 ASN H 163 ALA H 169 1 7
HELIX 116 AM8 GLY H 171 TYR H 189 1 19
HELIX 117 AM9 ILE H 193 ALA H 197 5 5
HELIX 118 AN1 LYS H 200 HIS H 205 1 6
HELIX 119 AN2 PHE H 222 GLY H 233 1 12
HELIX 120 AN3 PHE H 244 HIS H 249 1 6
HELIX 121 AN4 HIS H 249 LYS H 263 1 15
SHEET 1 AA1 6 THR A 6 THR A 11 0
SHEET 2 AA1 6 LYS A 17 GLU A 23 -1 O GLN A 22 N THR A 6
SHEET 3 AA1 6 ARG A 55 PHE A 59 -1 O VAL A 56 N GLU A 23
SHEET 4 AA1 6 ASP A 28 ILE A 32 1 N VAL A 29 O ARG A 55
SHEET 5 AA1 6 ALA A 99 CYS A 104 1 O TRP A 102 N VAL A 30
SHEET 6 AA1 6 VAL A 122 HIS A 128 1 O MET A 126 N VAL A 101
SHEET 1 AA2 2 ASP A 210 GLY A 214 0
SHEET 2 AA2 2 ASN A 235 LEU A 239 1 O ASN A 235 N TRP A 211
SHEET 1 AA3 6 THR B 6 THR B 11 0
SHEET 2 AA3 6 LYS B 17 GLU B 23 -1 O GLN B 22 N THR B 6
SHEET 3 AA3 6 ARG B 55 PHE B 59 -1 O VAL B 56 N GLU B 23
SHEET 4 AA3 6 ASP B 28 ILE B 32 1 N VAL B 29 O THR B 57
SHEET 5 AA3 6 ALA B 99 CYS B 104 1 O TRP B 102 N VAL B 30
SHEET 6 AA3 6 VAL B 122 HIS B 128 1 O MET B 126 N VAL B 101
SHEET 1 AA4 2 ASP B 210 GLY B 214 0
SHEET 2 AA4 2 ASN B 235 LEU B 239 1 O ASN B 235 N TRP B 211
SHEET 1 AA5 6 THR C 6 THR C 11 0
SHEET 2 AA5 6 LYS C 17 GLU C 23 -1 O GLN C 22 N THR C 6
SHEET 3 AA5 6 ARG C 55 PHE C 59 -1 O VAL C 56 N GLU C 23
SHEET 4 AA5 6 ASP C 28 ILE C 32 1 N VAL C 29 O THR C 57
SHEET 5 AA5 6 ALA C 99 CYS C 104 1 O TRP C 102 N ILE C 32
SHEET 6 AA5 6 VAL C 122 HIS C 128 1 O MET C 126 N VAL C 101
SHEET 1 AA6 2 ASP C 210 GLY C 214 0
SHEET 2 AA6 2 ASN C 235 LEU C 239 1 O ASN C 235 N TRP C 211
SHEET 1 AA7 6 ARG D 5 THR D 11 0
SHEET 2 AA7 6 LYS D 17 GLU D 23 -1 O GLN D 22 N THR D 6
SHEET 3 AA7 6 ARG D 55 PHE D 59 -1 O VAL D 56 N GLU D 23
SHEET 4 AA7 6 ASP D 28 ILE D 32 1 N VAL D 29 O THR D 57
SHEET 5 AA7 6 ALA D 99 CYS D 104 1 O SER D 100 N VAL D 30
SHEET 6 AA7 6 VAL D 122 HIS D 128 1 O MET D 126 N VAL D 101
SHEET 1 AA8 2 ASP D 210 GLY D 214 0
SHEET 2 AA8 2 ASN D 235 LEU D 239 1 O ASN D 235 N TRP D 211
SHEET 1 AA9 6 ARG E 5 THR E 11 0
SHEET 2 AA9 6 LYS E 17 GLU E 23 -1 O GLN E 22 N THR E 6
SHEET 3 AA9 6 ARG E 55 PHE E 59 -1 O VAL E 56 N GLU E 23
SHEET 4 AA9 6 ASP E 28 ILE E 32 1 N VAL E 29 O THR E 57
SHEET 5 AA9 6 ALA E 99 CYS E 104 1 O TRP E 102 N ILE E 32
SHEET 6 AA9 6 VAL E 122 HIS E 128 1 O MET E 126 N VAL E 101
SHEET 1 AB1 2 ASP E 210 GLY E 214 0
SHEET 2 AB1 2 ASN E 235 LEU E 239 1 O ASN E 235 N TRP E 211
SHEET 1 AB2 6 ARG F 5 THR F 11 0
SHEET 2 AB2 6 LYS F 17 GLU F 23 -1 O GLN F 22 N THR F 6
SHEET 3 AB2 6 ARG F 55 PHE F 59 -1 O VAL F 56 N GLU F 23
SHEET 4 AB2 6 ASP F 28 ILE F 32 1 N LEU F 31 O THR F 57
SHEET 5 AB2 6 ALA F 99 CYS F 104 1 O TRP F 102 N ILE F 32
SHEET 6 AB2 6 VAL F 122 HIS F 128 1 O MET F 126 N VAL F 101
SHEET 1 AB3 2 ASP F 210 GLY F 214 0
SHEET 2 AB3 2 ASN F 235 LEU F 239 1 O ASN F 235 N TRP F 211
SHEET 1 AB4 6 THR G 6 THR G 11 0
SHEET 2 AB4 6 LYS G 17 GLU G 23 -1 O GLN G 22 N THR G 6
SHEET 3 AB4 6 ARG G 55 PHE G 59 -1 O VAL G 56 N GLU G 23
SHEET 4 AB4 6 ASP G 28 ILE G 32 1 N VAL G 29 O THR G 57
SHEET 5 AB4 6 ALA G 99 CYS G 104 1 O SER G 100 N VAL G 30
SHEET 6 AB4 6 VAL G 122 HIS G 128 1 O MET G 126 N VAL G 101
SHEET 1 AB5 2 ASP G 210 GLY G 214 0
SHEET 2 AB5 2 ASN G 235 LEU G 239 1 O ASN G 235 N TRP G 211
SHEET 1 AB6 6 THR H 6 THR H 11 0
SHEET 2 AB6 6 LYS H 17 GLU H 23 -1 O GLN H 22 N THR H 6
SHEET 3 AB6 6 ARG H 55 PHE H 59 -1 O VAL H 56 N GLU H 23
SHEET 4 AB6 6 ASP H 28 ILE H 32 1 N LEU H 31 O THR H 57
SHEET 5 AB6 6 ALA H 99 CYS H 104 1 O SER H 100 N VAL H 30
SHEET 6 AB6 6 VAL H 122 HIS H 128 1 O MET H 126 N VAL H 101
SHEET 1 AB7 2 ASP H 210 GLY H 214 0
SHEET 2 AB7 2 ASN H 235 LEU H 239 1 O ASN H 235 N TRP H 211
SITE 1 AC1 14 GLY A 35 LEU A 36 ALA A 105 SER A 106
SITE 2 AC1 14 ASN A 156 SER A 157 TRP A 185 TYR A 189
SITE 3 AC1 14 PRO A 190 ILE A 193 PRO A 194 PHE A 222
SITE 4 AC1 14 HIS A 243 PHE A 244
SITE 1 AC2 15 GLY B 35 LEU B 36 ALA B 105 SER B 106
SITE 2 AC2 15 ASN B 134 ASN B 156 SER B 157 TRP B 185
SITE 3 AC2 15 TYR B 189 PRO B 190 ILE B 193 PRO B 194
SITE 4 AC2 15 PHE B 222 HIS B 243 HOH B 467
SITE 1 AC3 2 ASP B 77 THR B 79
SITE 1 AC4 8 ARG B 158 ASP B 168 HIS B 175 HOH B 413
SITE 2 AC4 8 HOH B 509 HOH B 561 HOH B 580 PRO G 172
SITE 1 AC5 13 GLY C 35 LEU C 36 ALA C 105 SER C 106
SITE 2 AC5 13 ASN C 134 ASN C 156 SER C 157 ALA C 160
SITE 3 AC5 13 TRP C 185 TYR C 189 PRO C 190 PRO C 194
SITE 4 AC5 13 HIS C 243
SITE 1 AC6 13 GLY D 35 LEU D 36 ALA D 105 SER D 106
SITE 2 AC6 13 ASN D 134 ASN D 156 TRP D 185 TYR D 189
SITE 3 AC6 13 PRO D 190 ILE D 193 PRO D 194 PHE D 222
SITE 4 AC6 13 HIS D 243
SITE 1 AC7 15 GLY E 35 LEU E 36 ALA E 105 SER E 106
SITE 2 AC7 15 ASN E 134 LEU E 138 ASN E 156 SER E 157
SITE 3 AC7 15 ALA E 160 TRP E 185 TYR E 189 PRO E 194
SITE 4 AC7 15 PHE E 222 HIS E 243 HOH E 466
SITE 1 AC8 13 GLY F 35 LEU F 36 ALA F 105 SER F 106
SITE 2 AC8 13 PRO F 131 ASN F 134 MET F 153 ASN F 156
SITE 3 AC8 13 TRP F 185 TYR F 189 PRO F 194 HIS F 243
SITE 4 AC8 13 HOH F 502
SITE 1 AC9 13 GLY G 35 LEU G 36 ALA G 105 SER G 106
SITE 2 AC9 13 ASN G 156 SER G 157 TRP G 185 TYR G 189
SITE 3 AC9 13 PRO G 190 ILE G 193 PRO G 194 HIS G 243
SITE 4 AC9 13 HOH G 412
SITE 1 AD1 14 GLY H 35 LEU H 36 ALA H 105 SER H 106
SITE 2 AD1 14 ASN H 134 ILE H 137 MET H 153 ASN H 156
SITE 3 AD1 14 SER H 157 TRP H 185 PRO H 190 PRO H 194
SITE 4 AD1 14 PHE H 222 HIS H 243
CRYST1 75.335 94.759 100.449 90.73 92.36 91.59 P 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013274 0.000368 0.000553 0.00000
SCALE2 0.000000 0.010557 0.000147 0.00000
SCALE3 0.000000 0.000000 0.009965 0.00000
TER 2049 LYS A 266
TER 4098 LYS B 266
TER 6152 LYS C 266
TER 8206 LYS D 266
TER 10250 LEU E 265
TER 12299 LYS F 266
TER 14343 LEU G 265
TER 16392 LYS H 266
MASTER 360 0 10 121 64 0 35 618446 8 198 168
END |