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HEADER HYDROLASE 30-APR-19 6RKY
TITLE STRUCTURE OF ESTER-HYDROLASE EH1AB1 FROM THE METAGENOME OF LAKE ARREO
TITLE 2 COMPLEXED WITH A DERIVATIVE OF BIPYRIDINE PHOSPHONATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EH1AB1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PET-46 EK/LIC
KEYWDS ESTER HYDROLASE, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.CEA-RAMA,J.SANZ-APARICIO
REVDAT 1 25-DEC-19 6RKY 0
JRNL AUTH S.ALONSO,G.SANTIAGO,I.CEA-RAMA,L.FERNANDEZ-LOPEZ,C.COSCOLIN,
JRNL AUTH 2 J.MODREGGER,A.RESSMANN,M.MARTINEZ-MARTINEZ,H.MARRERO,
JRNL AUTH 3 R.BARGIELA,M.PITA,J.L.GONZALEZ-ALFONSO,M.BRIAND,D.ROJO,
JRNL AUTH 4 C.BARBAS,F.J.PLOU,P.N.GOLYSHIN,P.SHAHGALDIAN,
JRNL AUTH 5 J.SANZ-APARICIO,V.GUALLAR,M.FERRER
JRNL TITL GENETICALLY ENGINEERED PROTEINS WITH TWO ACTIVE SITES FOR
JRNL TITL 2 ENHANCED BIOCATALYSIS AND SYNERGISTIC CHEMO- AND
JRNL TITL 3 BIOCATALYSIS
JRNL REF NAT CATAL 2019
JRNL REFN ESSN 2520-1158
JRNL DOI 10.1038/S41929-019-0394-4
REMARK 2
REMARK 2 RESOLUTION. 2.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 35315
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1823
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.79
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2649
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 119
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9628
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 51.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.00000
REMARK 3 B22 (A**2) : 1.60000
REMARK 3 B33 (A**2) : -1.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.413
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.382
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.657
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9922 ; 0.007 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 9028 ; 0.003 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13462 ; 1.476 ; 1.664
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20824 ; 1.251 ; 1.589
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1256 ; 6.533 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 544 ;28.698 ;20.515
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1432 ;14.826 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 92 ;18.196 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1260 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11440 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2268 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5036 ; 3.846 ; 4.902
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5035 ; 3.842 ; 4.901
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6288 ; 5.862 ; 7.355
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6289 ; 5.863 ; 7.355
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4886 ; 4.639 ; 5.498
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4887 ; 4.639 ; 5.499
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7175 ; 7.299 ; 8.034
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10513 ; 9.923 ;58.300
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10512 ; 9.919 ;58.303
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 315 B 1 315 10234 0.02 0.05
REMARK 3 2 A 1 315 C 1 315 10160 0.02 0.05
REMARK 3 3 A 1 315 D 1 315 10163 0.03 0.05
REMARK 3 4 B 1 315 C 1 315 10176 0.02 0.05
REMARK 3 5 B 1 315 D 1 315 10178 0.03 0.05
REMARK 3 6 C 1 315 D 1 315 10180 0.03 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6RKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1292102071.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97926
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL-CUT, CRYOCOOLED
REMARK 200 OPTICS : KB FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 1.11.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37139
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.790
REMARK 200 RESOLUTION RANGE LOW (A) : 49.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.27700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 2.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.57200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 11.6.04
REMARK 200 STARTING MODEL: 6I8F
REMARK 200
REMARK 200 REMARK: PRISM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.1M BIS-TRIS PROPANE PH
REMARK 280 7.5, 0.2 M NAF, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 45.38300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 100.96000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 45.38300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 100.96000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 3000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 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: 2660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 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 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 A 160A
REMARK 465 SER B 160A
REMARK 465 SER C 160A
REMARK 465 SER D 160A
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 ALA A 62 28.35 -154.81
REMARK 500 SER A 63 173.40 172.54
REMARK 500 VAL A 92 -50.46 -126.34
REMARK 500 ASN A 95 -177.06 -172.14
REMARK 500 PHE A 184 145.50 -171.35
REMARK 500 TYR A 189 58.93 34.29
REMARK 500 PHE A 209 -70.34 68.18
REMARK 500 ASP A 228 107.68 -58.16
REMARK 500 TYR A 255 46.41 -108.08
REMARK 500 PRO A 257 -37.01 -39.97
REMARK 500 LEU A 291 47.96 -98.09
REMARK 500 ALA B 62 25.64 -151.38
REMARK 500 SER B 63 173.31 171.56
REMARK 500 VAL B 92 -50.38 -126.58
REMARK 500 ASN B 95 -176.60 -171.90
REMARK 500 PHE B 184 145.30 -170.28
REMARK 500 TYR B 189 60.31 34.43
REMARK 500 PHE B 209 -70.19 69.52
REMARK 500 ASP B 228 108.18 -59.82
REMARK 500 TYR B 255 46.79 -108.05
REMARK 500 LEU B 291 48.38 -98.44
REMARK 500 ALA C 62 34.25 -156.46
REMARK 500 SER C 63 175.29 170.88
REMARK 500 VAL C 92 -50.76 -126.66
REMARK 500 ASN C 95 -176.60 -173.12
REMARK 500 TYR C 189 59.91 34.05
REMARK 500 PHE C 209 -70.47 69.78
REMARK 500 ASP C 228 107.90 -58.71
REMARK 500 TYR C 255 47.48 -108.68
REMARK 500 LEU C 291 48.11 -97.26
REMARK 500 ALA D 62 34.02 -155.53
REMARK 500 SER D 63 175.98 171.24
REMARK 500 VAL D 92 -51.01 -126.42
REMARK 500 ASN D 95 -176.57 -173.07
REMARK 500 TYR D 189 58.87 35.18
REMARK 500 PHE D 209 -70.67 68.11
REMARK 500 ASP D 228 108.34 -58.72
REMARK 500 TYR D 255 48.02 -108.50
REMARK 500 LEU D 291 48.11 -97.96
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 GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP B 160 and K7K B
REMARK 800 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide K7K B 161 and ALA B
REMARK 800 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP C 160 and K7K C
REMARK 800 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide K7K C 161 and ALA C
REMARK 800 162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ASP D 160 and K7K D
REMARK 800 161
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide K7K D 161 and ALA D
REMARK 800 162
DBREF 6RKY A 1 315 PDB 6RKY 6RKY 1 315
DBREF 6RKY B 1 315 PDB 6RKY 6RKY 1 315
DBREF 6RKY C 1 315 PDB 6RKY 6RKY 1 315
DBREF 6RKY D 1 315 PDB 6RKY 6RKY 1 315
SEQRES 1 A 316 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 A 316 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 A 316 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 A 316 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 A 316 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 A 316 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 A 316 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 A 316 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 A 316 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 A 316 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 A 316 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 A 316 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 A 316 VAL GLY GLY ASP SER K7K ALA GLY GLY ALA MET ALA ALA
SEQRES 14 A 316 VAL VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY
SEQRES 15 A 316 PRO ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER
SEQRES 16 A 316 SER ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY
SEQRES 17 A 316 TYR PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU
SEQRES 18 A 316 ALA TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG
SEQRES 19 A 316 LEU SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO
SEQRES 20 A 316 PRO ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG
SEQRES 21 A 316 ASP GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA
SEQRES 22 A 316 GLY ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE
SEQRES 23 A 316 HIS GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY
SEQRES 24 A 316 LEU LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA
SEQRES 25 A 316 HIS PHE GLY THR
SEQRES 1 B 316 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 B 316 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 B 316 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 B 316 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 B 316 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 B 316 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 B 316 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 B 316 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 B 316 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 B 316 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 B 316 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 B 316 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 B 316 VAL GLY GLY ASP SER K7K ALA GLY GLY ALA MET ALA ALA
SEQRES 14 B 316 VAL VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY
SEQRES 15 B 316 PRO ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER
SEQRES 16 B 316 SER ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY
SEQRES 17 B 316 TYR PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU
SEQRES 18 B 316 ALA TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG
SEQRES 19 B 316 LEU SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO
SEQRES 20 B 316 PRO ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG
SEQRES 21 B 316 ASP GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA
SEQRES 22 B 316 GLY ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE
SEQRES 23 B 316 HIS GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY
SEQRES 24 B 316 LEU LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA
SEQRES 25 B 316 HIS PHE GLY THR
SEQRES 1 C 316 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 C 316 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 C 316 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 C 316 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 C 316 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 C 316 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 C 316 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 C 316 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 C 316 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 C 316 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 C 316 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 C 316 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 C 316 VAL GLY GLY ASP SER K7K ALA GLY GLY ALA MET ALA ALA
SEQRES 14 C 316 VAL VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY
SEQRES 15 C 316 PRO ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER
SEQRES 16 C 316 SER ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY
SEQRES 17 C 316 TYR PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU
SEQRES 18 C 316 ALA TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG
SEQRES 19 C 316 LEU SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO
SEQRES 20 C 316 PRO ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG
SEQRES 21 C 316 ASP GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA
SEQRES 22 C 316 GLY ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE
SEQRES 23 C 316 HIS GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY
SEQRES 24 C 316 LEU LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA
SEQRES 25 C 316 HIS PHE GLY THR
SEQRES 1 D 316 MET LEU LEU PRO GLU THR ARG ASN LEU LEU ASP LEU MET
SEQRES 2 D 316 ASP ALA ALA THR ARG GLY GLY ARG PRO GLY LEU ASP THR
SEQRES 3 D 316 LEU PRO HIS ALA VAL GLY ARG LYS ALA VAL ASP LYS MET
SEQRES 4 D 316 SER GLU ASP GLY GLU ALA ASP PRO PRO GLU VAL ALA GLU
SEQRES 5 D 316 VAL ALA ASN GLY GLY PHE ALA GLY PRO ALA SER GLU ILE
SEQRES 6 D 316 ARG PHE ARG ARG TYR ARG PRO LEU GLY GLU ALA ALA GLY
SEQRES 7 D 316 LEU LEU PRO THR LEU ILE TYR TYR HIS GLY GLY GLY PHE
SEQRES 8 D 316 VAL ILE GLY ASN ILE GLU THR HIS ASP SER THR CYS ARG
SEQRES 9 D 316 ARG LEU ALA ASN LYS SER ARG CYS GLN VAL ILE SER ILE
SEQRES 10 D 316 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA PRO
SEQRES 11 D 316 ILE ASP ASP GLY ILE ALA ALA PHE ARG HIS ILE ARG ASP
SEQRES 12 D 316 ASN ALA GLU SER PHE GLY ALA ASP ALA ALA ARG LEU ALA
SEQRES 13 D 316 VAL GLY GLY ASP SER K7K ALA GLY GLY ALA MET ALA ALA
SEQRES 14 D 316 VAL VAL CYS GLN ALA CYS ARG ASP ALA GLY GLU THR GLY
SEQRES 15 D 316 PRO ALA PHE GLN MET LEU ILE TYR PRO ALA THR ASP SER
SEQRES 16 D 316 SER ARG GLU SER ALA SER ARG VAL ALA PHE ALA GLU GLY
SEQRES 17 D 316 TYR PHE LEU SER LYS ALA HIS MET ASP TRP PHE TRP GLU
SEQRES 18 D 316 ALA TYR VAL PRO GLU ASP THR ASP LEU THR ASP LEU ARG
SEQRES 19 D 316 LEU SER PRO LEU LEU ALA THR ASP PHE THR GLY LEU PRO
SEQRES 20 D 316 PRO ALA PHE VAL LEU THR ALA GLY TYR ASP PRO LEU ARG
SEQRES 21 D 316 ASP GLU GLY ARG ALA TYR ALA ASP ARG LEU ILE GLU ALA
SEQRES 22 D 316 GLY ILE LYS THR THR TYR VAL ASN TYR PRO GLY THR ILE
SEQRES 23 D 316 HIS GLY PHE PHE SER LEU THR ARG PHE LEU SER GLN GLY
SEQRES 24 D 316 LEU LYS ALA ASN ASP GLU ALA ALA ALA VAL MET GLY ALA
SEQRES 25 D 316 HIS PHE GLY THR
HET K7K A 161 28
HET K7K B 161 28
HET K7K C 161 28
HET K7K D 161 28
HET GOL A 401 6
HET GOL B 401 6
HET GOL C 401 6
HET GOL C 402 6
HET PEG C 403 7
HET PEG C 404 7
HET PEG C 405 7
HET GOL D 401 6
HET GOL D 402 6
HET PEG D 403 7
HETNAM K7K 2-AZANYL-3-[HEXYL-[2-(3-OXIDANYLPYRIDIN-2-YL)PYRIDIN-3-
HETNAM 2 K7K YL]OXY-PHOSPHORYL]OXY-PROPANAL
HETNAM GOL GLYCEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 K7K 4(C19 H26 N3 O5 P)
FORMUL 5 GOL 6(C3 H8 O3)
FORMUL 9 PEG 4(C4 H10 O3)
FORMUL 15 HOH *72(H2 O)
HELIX 1 AA1 LEU A 3 GLY A 20 1 18
HELIX 2 AA2 GLY A 23 LEU A 27 5 5
HELIX 3 AA3 PRO A 28 ASP A 42 1 15
HELIX 4 AA4 ASN A 95 THR A 98 5 4
HELIX 5 AA5 HIS A 99 ARG A 111 1 13
HELIX 6 AA6 PRO A 128 ASP A 143 1 16
HELIX 7 AA7 ASN A 144 PHE A 148 5 5
HELIX 8 AA8 K7K A 161 ALA A 177 1 17
HELIX 9 AA9 SER A 198 PHE A 204 1 7
HELIX 10 AB1 SER A 211 VAL A 223 1 13
HELIX 11 AB2 SER A 235 ALA A 239 5 5
HELIX 12 AB3 LEU A 258 ALA A 272 1 15
HELIX 13 AB4 SER A 296 GLY A 314 1 19
HELIX 14 AB5 LEU B 3 GLY B 20 1 18
HELIX 15 AB6 GLY B 23 LEU B 27 5 5
HELIX 16 AB7 PRO B 28 ASP B 42 1 15
HELIX 17 AB8 ASN B 95 THR B 98 5 4
HELIX 18 AB9 HIS B 99 ARG B 111 1 13
HELIX 19 AC1 PRO B 128 ASP B 143 1 16
HELIX 20 AC2 ASN B 144 PHE B 148 5 5
HELIX 21 AC3 K7K B 161 ALA B 177 1 17
HELIX 22 AC4 SER B 198 PHE B 204 1 7
HELIX 23 AC5 SER B 211 VAL B 223 1 13
HELIX 24 AC6 SER B 235 ALA B 239 5 5
HELIX 25 AC7 LEU B 258 ALA B 272 1 15
HELIX 26 AC8 SER B 296 GLY B 314 1 19
HELIX 27 AC9 LEU C 3 GLY C 20 1 18
HELIX 28 AD1 GLY C 23 LEU C 27 5 5
HELIX 29 AD2 PRO C 28 GLU C 44 1 17
HELIX 30 AD3 ASN C 95 THR C 98 5 4
HELIX 31 AD4 HIS C 99 ARG C 111 1 13
HELIX 32 AD5 PRO C 128 ASP C 143 1 16
HELIX 33 AD6 ASN C 144 PHE C 148 5 5
HELIX 34 AD7 K7K C 161 ALA C 177 1 17
HELIX 35 AD8 SER C 198 PHE C 204 1 7
HELIX 36 AD9 SER C 211 VAL C 223 1 13
HELIX 37 AE1 SER C 235 ALA C 239 5 5
HELIX 38 AE2 LEU C 258 ALA C 272 1 15
HELIX 39 AE3 SER C 296 GLY C 314 1 19
HELIX 40 AE4 LEU D 3 GLY D 20 1 18
HELIX 41 AE5 GLY D 23 LEU D 27 5 5
HELIX 42 AE6 PRO D 28 GLU D 44 1 17
HELIX 43 AE7 ASN D 95 THR D 98 5 4
HELIX 44 AE8 HIS D 99 ARG D 111 1 13
HELIX 45 AE9 PRO D 128 ASP D 143 1 16
HELIX 46 AF1 ASN D 144 PHE D 148 5 5
HELIX 47 AF2 K7K D 161 ALA D 177 1 17
HELIX 48 AF3 SER D 198 PHE D 204 1 7
HELIX 49 AF4 SER D 211 VAL D 223 1 13
HELIX 50 AF5 SER D 235 ALA D 239 5 5
HELIX 51 AF6 LEU D 258 ALA D 272 1 15
HELIX 52 AF7 SER D 296 GLY D 314 1 19
SHEET 1 AA116 GLU A 52 ALA A 59 0
SHEET 2 AA116 GLU A 64 ARG A 71 -1 O ARG A 71 N GLU A 52
SHEET 3 AA116 GLN A 113 ASP A 118 -1 O ASP A 118 N ARG A 66
SHEET 4 AA116 LEU A 80 TYR A 86 1 N PRO A 81 O GLN A 113
SHEET 5 AA116 ALA A 150 ASP A 160 1 O ALA A 156 N ILE A 84
SHEET 6 AA116 GLN A 185 ILE A 188 1 O ILE A 188 N GLY A 159
SHEET 7 AA116 ALA A 248 TYR A 255 1 O PHE A 249 N LEU A 187
SHEET 8 AA116 THR A 276 ILE A 285 1 O TYR A 281 N THR A 252
SHEET 9 AA116 THR C 276 ILE C 285 -1 O TYR C 278 N TYR A 278
SHEET 10 AA116 ALA C 248 TYR C 255 1 N THR C 252 O TYR C 281
SHEET 11 AA116 GLN C 185 ILE C 188 1 N LEU C 187 O PHE C 249
SHEET 12 AA116 ALA C 150 ASP C 160 1 N GLY C 159 O ILE C 188
SHEET 13 AA116 LEU C 80 TYR C 86 1 N ILE C 84 O ALA C 156
SHEET 14 AA116 GLN C 113 ASP C 118 1 O GLN C 113 N PRO C 81
SHEET 15 AA116 GLU C 64 ARG C 71 -1 N ARG C 66 O ASP C 118
SHEET 16 AA116 GLU C 52 ALA C 59 -1 N GLU C 52 O ARG C 71
SHEET 1 AA216 GLU B 52 ALA B 59 0
SHEET 2 AA216 GLU B 64 ARG B 71 -1 O ARG B 71 N GLU B 52
SHEET 3 AA216 GLN B 113 ASP B 118 -1 O ASP B 118 N ARG B 66
SHEET 4 AA216 LEU B 80 TYR B 86 1 N PRO B 81 O GLN B 113
SHEET 5 AA216 ALA B 150 ASP B 160 1 O ALA B 156 N ILE B 84
SHEET 6 AA216 GLN B 185 ILE B 188 1 O ILE B 188 N GLY B 159
SHEET 7 AA216 ALA B 248 TYR B 255 1 O PHE B 249 N LEU B 187
SHEET 8 AA216 THR B 276 ILE B 285 1 O TYR B 281 N THR B 252
SHEET 9 AA216 THR D 276 ILE D 285 -1 O TYR D 278 N TYR B 278
SHEET 10 AA216 ALA D 248 TYR D 255 1 N THR D 252 O TYR D 281
SHEET 11 AA216 GLN D 185 ILE D 188 1 N LEU D 187 O PHE D 249
SHEET 12 AA216 ALA D 150 ASP D 160 1 N GLY D 159 O ILE D 188
SHEET 13 AA216 LEU D 80 TYR D 86 1 N ILE D 84 O ALA D 156
SHEET 14 AA216 GLN D 113 ASP D 118 1 O GLN D 113 N PRO D 81
SHEET 15 AA216 GLU D 64 ARG D 71 -1 N ARG D 66 O ASP D 118
SHEET 16 AA216 GLU D 52 ALA D 59 -1 N GLU D 52 O ARG D 71
LINK C ASP A 160 N K7K A 161 1555 1555 1.33
LINK C K7K A 161 N ALA A 162 1555 1555 1.33
LINK C ASP B 160 N K7K B 161 1555 1555 1.34
LINK C K7K B 161 N ALA B 162 1555 1555 1.33
LINK C ASP C 160 N K7K C 161 1555 1555 1.34
LINK C K7K C 161 N ALA C 162 1555 1555 1.34
LINK C ASP D 160 N K7K D 161 1555 1555 1.33
LINK C K7K D 161 N ALA D 162 1555 1555 1.34
CISPEP 1 ALA A 122 PRO A 123 0 7.06
CISPEP 2 PHE A 127 PRO A 128 0 5.97
CISPEP 3 ALA B 122 PRO B 123 0 6.06
CISPEP 4 PHE B 127 PRO B 128 0 5.83
CISPEP 5 ALA C 122 PRO C 123 0 7.11
CISPEP 6 PHE C 127 PRO C 128 0 5.78
CISPEP 7 ALA D 122 PRO D 123 0 6.78
CISPEP 8 PHE D 127 PRO D 128 0 5.55
SITE 1 AC1 3 ARG A 259 ASP A 260 ARG A 263
SITE 1 AC2 5 GLU B 49 VAL B 50 ASN B 55 GLY B 56
SITE 2 AC2 5 ARG B 104
SITE 1 AC3 1 GLY C 207
SITE 1 AC4 1 GLY C 60
SITE 1 AC5 1 ASP C 176
SITE 1 AC6 2 PRO C 61 SER C 63
SITE 1 AC7 2 ARG C 139 GLU C 179
SITE 1 AC8 4 ARG B 111 LYS D 109 ARG D 111 HOH D 505
SITE 1 AC9 2 ALA D 153 ALA D 183
SITE 1 AD1 3 GLY D 178 THR D 180 HOH D 508
SITE 1 AD2 19 TYR B 85 TYR B 86 HIS B 87 GLY B 88
SITE 2 AD2 19 GLY B 89 GLY B 90 HIS B 99 GLY B 159
SITE 3 AD2 19 ALA B 162 GLY B 163 GLY B 164 ALA B 165
SITE 4 AD2 19 ILE B 188 TYR B 189 PRO B 190 ALA B 191
SITE 5 AD2 19 PHE B 209 PHE B 218 HIS B 286
SITE 1 AD3 16 GLY B 88 GLY B 89 GLY B 90 PHE B 91
SITE 2 AD3 16 ASP B 160 GLY B 163 GLY B 164 ALA B 165
SITE 3 AD3 16 MET B 166 ILE B 188 TYR B 189 PRO B 190
SITE 4 AD3 16 ALA B 191 PHE B 209 PHE B 218 HIS B 286
SITE 1 AD4 19 TYR C 85 TYR C 86 HIS C 87 GLY C 88
SITE 2 AD4 19 GLY C 89 GLY C 90 HIS C 99 GLY C 159
SITE 3 AD4 19 ALA C 162 GLY C 163 GLY C 164 ALA C 165
SITE 4 AD4 19 ILE C 188 TYR C 189 PRO C 190 ALA C 191
SITE 5 AD4 19 PHE C 209 PHE C 218 HIS C 286
SITE 1 AD5 16 GLY C 88 GLY C 89 GLY C 90 PHE C 91
SITE 2 AD5 16 ASP C 160 GLY C 163 GLY C 164 ALA C 165
SITE 3 AD5 16 MET C 166 ILE C 188 TYR C 189 PRO C 190
SITE 4 AD5 16 ALA C 191 PHE C 209 PHE C 218 HIS C 286
SITE 1 AD6 19 TYR D 85 TYR D 86 HIS D 87 GLY D 88
SITE 2 AD6 19 GLY D 89 GLY D 90 HIS D 99 GLY D 159
SITE 3 AD6 19 ALA D 162 GLY D 163 GLY D 164 ALA D 165
SITE 4 AD6 19 ILE D 188 TYR D 189 PRO D 190 ALA D 191
SITE 5 AD6 19 PHE D 209 PHE D 218 HIS D 286
SITE 1 AD7 16 GLY D 88 GLY D 89 GLY D 90 PHE D 91
SITE 2 AD7 16 ASP D 160 GLY D 163 GLY D 164 ALA D 165
SITE 3 AD7 16 MET D 166 ILE D 188 TYR D 189 PRO D 190
SITE 4 AD7 16 ALA D 191 PHE D 209 PHE D 218 HIS D 286
CRYST1 90.766 201.920 90.637 90.00 112.19 90.00 C 1 2 1 16
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 0.011017 0.000000 0.004494 0.00000
SCALE2 0.000000 0.004952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011916 0.00000
TER 2408 THR A 315
TER 4816 THR B 315
TER 7224 THR C 315
TER 9632 THR D 315
MASTER 397 0 14 52 32 0 38 6 9764 4 184 100
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