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HEADER HYDROLASE 21-JUL-16 5LK6
TITLE CRYSTAL STRUCTURE OF A LIPASE CARBOXYLESTERASE FROM SULFOLOBUS
TITLE 2 ISLANDICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD-3 DOMAIN PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS ISLANDICUS (STRAIN REY15A);
SOURCE 3 ORGANISM_TAXID: 930945;
SOURCE 4 STRAIN: REY15A;
SOURCE 5 CELL_LINE: E233S;
SOURCE 6 CELL: PROKARYOT;
SOURCE 7 GENE: SIRE_0290;
SOURCE 8 EXPRESSION_SYSTEM: SULFOLOBUS ISLANDICUS REY15A;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 930945;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: SIRE_0290;
SOURCE 11 EXPRESSION_SYSTEM_VARIANT: REY15A;
SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: E233S;
SOURCE 13 EXPRESSION_SYSTEM_CELL: PROKARYOT;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PSESD
KEYWDS ESTERASE, LIPASE, SULFOLOBUS, THERMOSTABLE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SCHWARZ-LINNET,K.TEILUM,J.G.OLSEN
REVDAT 1 02-AUG-17 5LK6 0
JRNL AUTH T.SCHWARZ-LINNET,D.STIEFLER-JENSEN,C.DE LICHETENBERG,
JRNL AUTH 2 J.G.OLSEN,T.T.T.N.NGUYEN,K.D.RAND,K.TEILUM
JRNL TITL ESTA FROM SUFOLOBUS ISLANDICUS IS STABILIZED BY
JRNL TITL 2 MONO-METHYLATION OF LYSINE RESIDUES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0155
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 75089
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3952
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5403
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2200
REMARK 3 BIN FREE R VALUE SET COUNT : 284
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9368
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 438
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.219
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.985
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9624 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9216 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13072 ; 2.059 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 21164 ; 1.113 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1204 ; 6.979 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 424 ;35.977 ;23.585
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1528 ;17.402 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 64 ;18.650 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1460 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10868 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2212 ; 0.002 ; 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): 4828 ; 2.234 ; 2.588
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4827 ; 2.235 ; 2.587
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6028 ; 3.422 ; 3.875
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6029 ; 3.422 ; 3.876
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4796 ; 3.518 ; 2.959
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4762 ; 3.482 ; 2.947
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 6996 ; 5.442 ; 4.252
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 10806 ; 7.084 ;30.530
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10763 ; 7.008 ;30.451
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5LK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000783.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-12
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 : MAX II
REMARK 200 BEAMLINE : I911-3
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 : WATER-COOLED DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR, SI(111)
REMARK 200 OPTICS : FIRST MIRROR: WATER-COOLED
REMARK 200 VERTICALLY COLLIMATING
REMARK 200 CYLINDRICAL MIRROR (R = 7300 M).
REMARK 200 SECOND MIRROR: TOROID MIRROR FOR
REMARK 200 HORIZONTAL AND VERTICAL FOCUSING
REMARK 200 (R = 3300 M, R = 27 MM).
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS SEPTEMBER 26, 2012
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79041
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 29.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.13600
REMARK 200 R SYM (I) : 0.13600
REMARK 200 FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 10.62
REMARK 200 R MERGE FOR SHELL (I) : 0.54300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: 3AIK
REMARK 200
REMARK 200 REMARK: LARGER THAN 0.2 MM
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HAMPTON REASERCH CRYSTAL SCREEN 2 (HR2
REMARK 280 -112) CONDITION #23. 1.6 M AMMONIUM SULFATE, 0.1 M MES
REMARK 280 MONOHYDRATE PH 6.5, 10% V/V 1,4-DIOXANE. RESERVOIR VOLUME 600
REMARK 280 UL. 2 UL OF ESTA 10 MG/ML IN 50 MM TRIS PH 8, MIXED WITH 2 UL OF
REMARK 280 RESERVOIR VOLUME FOR HANGING DROP AT ROOM TEMPERATURE., VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 92.89000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 83.20500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 83.20500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 139.33500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 83.20500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 83.20500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 46.44500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 83.20500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 83.20500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 139.33500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 83.20500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 83.20500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.44500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 92.89000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 610 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 304
REMARK 465 SER A 305
REMARK 465 ALA A 306
REMARK 465 ALA A 307
REMARK 465 ALA A 308
REMARK 465 HIS A 309
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 MET B 1
REMARK 465 LYS B 304
REMARK 465 SER B 305
REMARK 465 ALA B 306
REMARK 465 ALA B 307
REMARK 465 ALA B 308
REMARK 465 HIS B 309
REMARK 465 HIS B 310
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 MET C 1
REMARK 465 LYS C 304
REMARK 465 SER C 305
REMARK 465 ALA C 306
REMARK 465 ALA C 307
REMARK 465 ALA C 308
REMARK 465 HIS C 309
REMARK 465 HIS C 310
REMARK 465 HIS C 311
REMARK 465 HIS C 312
REMARK 465 HIS C 313
REMARK 465 HIS C 314
REMARK 465 MET D 1
REMARK 465 LYS D 304
REMARK 465 SER D 305
REMARK 465 ALA D 306
REMARK 465 ALA D 307
REMARK 465 ALA D 308
REMARK 465 HIS D 309
REMARK 465 HIS D 310
REMARK 465 HIS D 311
REMARK 465 HIS D 312
REMARK 465 HIS D 313
REMARK 465 HIS D 314
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N GLY C 20 O HOH C 501 1.74
REMARK 500 O ILE C 19 O HOH C 502 1.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 88 CG GLU A 88 CD 0.092
REMARK 500 SER A 151 N SER A 151 CA 0.141
REMARK 500 SER A 151 CA SER A 151 CB 0.165
REMARK 500 SER A 151 CB SER A 151 OG 0.148
REMARK 500 SER B 151 N SER B 151 CA 0.127
REMARK 500 SER B 151 CA SER B 151 CB 0.120
REMARK 500 SER B 151 CB SER B 151 OG 0.163
REMARK 500 GLU C 115 CG GLU C 115 CD 0.111
REMARK 500 GLU C 115 CD GLU C 115 OE2 0.071
REMARK 500 SER C 151 N SER C 151 CA 0.145
REMARK 500 SER C 151 CA SER C 151 CB 0.167
REMARK 500 SER C 151 CB SER C 151 OG 0.150
REMARK 500 SER C 231 CB SER C 231 OG -0.079
REMARK 500 GLU D 88 CB GLU D 88 CG 0.125
REMARK 500 GLU D 88 CG GLU D 88 CD 0.135
REMARK 500 SER D 151 N SER D 151 CA 0.129
REMARK 500 SER D 151 CA SER D 151 CB 0.146
REMARK 500 SER D 151 CB SER D 151 OG 0.137
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 SER A 151 N - CA - CB ANGL. DEV. = 10.2 DEGREES
REMARK 500 ASP A 194 CB - CG - OD1 ANGL. DEV. = -6.9 DEGREES
REMARK 500 ARG A 200 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 200 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 299 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 32 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP B 303 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP C 194 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP C 244 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 268 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG C 268 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 GLU D 88 CB - CA - C ANGL. DEV. = 13.5 DEGREES
REMARK 500 GLU D 88 OE1 - CD - OE2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 SER D 151 CA - CB - OG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASP D 194 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG D 200 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG D 200 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG D 268 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 43 -158.96 -131.70
REMARK 500 ALA A 67 147.10 -36.59
REMARK 500 ASP A 86 169.14 174.11
REMARK 500 PRO A 119 34.24 -98.70
REMARK 500 ASN A 135 41.48 -145.80
REMARK 500 SER A 151 -126.78 62.47
REMARK 500 TYR A 172 148.68 -173.27
REMARK 500 TYR A 177 58.29 30.20
REMARK 500 PHE A 197 -58.89 80.96
REMARK 500 SER A 223 78.96 -115.36
REMARK 500 TYR A 243 69.45 -104.28
REMARK 500 PHE B 15 92.51 -169.28
REMARK 500 VAL B 43 -164.86 -117.57
REMARK 500 ASN B 102 48.74 39.88
REMARK 500 SER B 151 -132.07 59.52
REMARK 500 TYR B 177 61.54 26.51
REMARK 500 VAL B 185 -22.30 -145.20
REMARK 500 PHE B 197 -65.60 77.43
REMARK 500 ILE C 19 -72.12 -41.17
REMARK 500 VAL C 43 -161.34 -122.88
REMARK 500 ALA C 56 159.64 178.79
REMARK 500 ASP C 86 172.33 177.50
REMARK 500 ASP C 109 71.26 -100.47
REMARK 500 SER C 151 -129.84 55.12
REMARK 500 TYR C 177 63.52 28.76
REMARK 500 PHE C 197 -60.54 82.43
REMARK 500 SER C 223 76.50 -117.27
REMARK 500 SER C 231 151.07 -47.34
REMARK 500 TYR C 243 67.36 -101.64
REMARK 500 SER D 13 40.70 -109.96
REMARK 500 VAL D 43 -159.16 -122.37
REMARK 500 ASP D 86 -179.52 177.14
REMARK 500 SER D 151 -124.99 55.76
REMARK 500 LYS D 167 -51.13 -131.82
REMARK 500 TYR D 177 63.31 30.34
REMARK 500 VAL D 185 -31.34 -146.61
REMARK 500 PHE D 197 -61.62 71.17
REMARK 500 TYR D 243 66.76 -101.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 20 LYS B 21 -138.64
REMARK 500 SER D 184 VAL D 185 -147.87
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 401
DBREF 5LK6 A 1 305 UNP F0NDQ1 F0NDQ1_SULIR 1 305
DBREF 5LK6 B 1 305 UNP F0NDQ1 F0NDQ1_SULIR 1 305
DBREF 5LK6 C 1 305 UNP F0NDQ1 F0NDQ1_SULIR 1 305
DBREF 5LK6 D 1 305 UNP F0NDQ1 F0NDQ1_SULIR 1 305
SEQADV 5LK6 ALA A 306 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA A 307 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA A 308 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS A 309 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS A 310 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS A 311 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS A 312 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS A 313 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS A 314 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA B 306 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA B 307 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA B 308 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS B 309 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS B 310 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS B 311 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS B 312 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS B 313 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS B 314 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA C 306 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA C 307 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA C 308 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS C 309 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS C 310 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS C 311 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS C 312 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS C 313 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS C 314 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA D 306 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA D 307 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 ALA D 308 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS D 309 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS D 310 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS D 311 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS D 312 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS D 313 UNP F0NDQ1 EXPRESSION TAG
SEQADV 5LK6 HIS D 314 UNP F0NDQ1 EXPRESSION TAG
SEQRES 1 A 314 MET PRO LEU ASP PRO ARG ILE LYS GLU LEU LEU GLU SER
SEQRES 2 A 314 GLY PHE ILE VAL PRO ILE GLY LYS ALA SER VAL ASP GLU
SEQRES 3 A 314 VAL ARG LYS ILE PHE ARG GLN LEU ALA SER ALA ALA PRO
SEQRES 4 A 314 LYS VAL GLU VAL GLY LYS VAL GLU ASP ILE LYS ILE PRO
SEQRES 5 A 314 GLY SER GLU ALA ASN ILE ASN ALA ARG VAL TYR LEU PRO
SEQRES 6 A 314 LYS ALA ASN GLY PRO TYR GLY VAL LEU ILE TYR LEU HIS
SEQRES 7 A 314 GLY GLY GLY PHE VAL ILE GLY ASP VAL GLU SER TYR ASP
SEQRES 8 A 314 PRO LEU CYS ARG ALA ILE THR ASN ALA CYS ASN CYS VAL
SEQRES 9 A 314 VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU TYR LYS
SEQRES 10 A 314 PHE PRO SER ALA VAL ILE ASP SER PHE ASP ALA THR ASN
SEQRES 11 A 314 TRP VAL TYR ASN ASN LEU ASP LYS PHE ASP GLY LYS MET
SEQRES 12 A 314 GLY VAL ALA ILE ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 13 A 314 ALA ALA VAL VAL ALA LEU LEU SER LYS GLY LYS LEU ASN
SEQRES 14 A 314 LEU LYS TYR GLN ILE LEU ILE TYR PRO ALA VAL GLY PHE
SEQRES 15 A 314 ASP SER VAL SER ARG SER MET ILE GLU TYR SER ASP GLY
SEQRES 16 A 314 PHE PHE LEU THR ARG GLU HIS ILE GLU TRP PHE GLY SER
SEQRES 17 A 314 GLN TYR LEU ARG SER PRO ALA ASP LEU LEU ASP PHE ARG
SEQRES 18 A 314 PHE SER PRO ILE LEU ALA GLN ASP LEU SER GLY LEU PRO
SEQRES 19 A 314 PRO ALA LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG
SEQRES 20 A 314 ASP GLN GLY GLU ALA TYR ALA ASN ARG LEU LEU GLN ALA
SEQRES 21 A 314 GLY VAL PRO VAL THR SER VAL ARG PHE ASN ASN VAL ILE
SEQRES 22 A 314 HIS GLY PHE LEU SER PHE PHE PRO LEU ILE GLU GLN GLY
SEQRES 23 A 314 ARG ASP ALA ILE SER LEU ILE GLY SER VAL LEU ARG ARG
SEQRES 24 A 314 THR PHE TYR ASP LYS SER ALA ALA ALA HIS HIS HIS HIS
SEQRES 25 A 314 HIS HIS
SEQRES 1 B 314 MET PRO LEU ASP PRO ARG ILE LYS GLU LEU LEU GLU SER
SEQRES 2 B 314 GLY PHE ILE VAL PRO ILE GLY LYS ALA SER VAL ASP GLU
SEQRES 3 B 314 VAL ARG LYS ILE PHE ARG GLN LEU ALA SER ALA ALA PRO
SEQRES 4 B 314 LYS VAL GLU VAL GLY LYS VAL GLU ASP ILE LYS ILE PRO
SEQRES 5 B 314 GLY SER GLU ALA ASN ILE ASN ALA ARG VAL TYR LEU PRO
SEQRES 6 B 314 LYS ALA ASN GLY PRO TYR GLY VAL LEU ILE TYR LEU HIS
SEQRES 7 B 314 GLY GLY GLY PHE VAL ILE GLY ASP VAL GLU SER TYR ASP
SEQRES 8 B 314 PRO LEU CYS ARG ALA ILE THR ASN ALA CYS ASN CYS VAL
SEQRES 9 B 314 VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU TYR LYS
SEQRES 10 B 314 PHE PRO SER ALA VAL ILE ASP SER PHE ASP ALA THR ASN
SEQRES 11 B 314 TRP VAL TYR ASN ASN LEU ASP LYS PHE ASP GLY LYS MET
SEQRES 12 B 314 GLY VAL ALA ILE ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 13 B 314 ALA ALA VAL VAL ALA LEU LEU SER LYS GLY LYS LEU ASN
SEQRES 14 B 314 LEU LYS TYR GLN ILE LEU ILE TYR PRO ALA VAL GLY PHE
SEQRES 15 B 314 ASP SER VAL SER ARG SER MET ILE GLU TYR SER ASP GLY
SEQRES 16 B 314 PHE PHE LEU THR ARG GLU HIS ILE GLU TRP PHE GLY SER
SEQRES 17 B 314 GLN TYR LEU ARG SER PRO ALA ASP LEU LEU ASP PHE ARG
SEQRES 18 B 314 PHE SER PRO ILE LEU ALA GLN ASP LEU SER GLY LEU PRO
SEQRES 19 B 314 PRO ALA LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG
SEQRES 20 B 314 ASP GLN GLY GLU ALA TYR ALA ASN ARG LEU LEU GLN ALA
SEQRES 21 B 314 GLY VAL PRO VAL THR SER VAL ARG PHE ASN ASN VAL ILE
SEQRES 22 B 314 HIS GLY PHE LEU SER PHE PHE PRO LEU ILE GLU GLN GLY
SEQRES 23 B 314 ARG ASP ALA ILE SER LEU ILE GLY SER VAL LEU ARG ARG
SEQRES 24 B 314 THR PHE TYR ASP LYS SER ALA ALA ALA HIS HIS HIS HIS
SEQRES 25 B 314 HIS HIS
SEQRES 1 C 314 MET PRO LEU ASP PRO ARG ILE LYS GLU LEU LEU GLU SER
SEQRES 2 C 314 GLY PHE ILE VAL PRO ILE GLY LYS ALA SER VAL ASP GLU
SEQRES 3 C 314 VAL ARG LYS ILE PHE ARG GLN LEU ALA SER ALA ALA PRO
SEQRES 4 C 314 LYS VAL GLU VAL GLY LYS VAL GLU ASP ILE LYS ILE PRO
SEQRES 5 C 314 GLY SER GLU ALA ASN ILE ASN ALA ARG VAL TYR LEU PRO
SEQRES 6 C 314 LYS ALA ASN GLY PRO TYR GLY VAL LEU ILE TYR LEU HIS
SEQRES 7 C 314 GLY GLY GLY PHE VAL ILE GLY ASP VAL GLU SER TYR ASP
SEQRES 8 C 314 PRO LEU CYS ARG ALA ILE THR ASN ALA CYS ASN CYS VAL
SEQRES 9 C 314 VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU TYR LYS
SEQRES 10 C 314 PHE PRO SER ALA VAL ILE ASP SER PHE ASP ALA THR ASN
SEQRES 11 C 314 TRP VAL TYR ASN ASN LEU ASP LYS PHE ASP GLY LYS MET
SEQRES 12 C 314 GLY VAL ALA ILE ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 13 C 314 ALA ALA VAL VAL ALA LEU LEU SER LYS GLY LYS LEU ASN
SEQRES 14 C 314 LEU LYS TYR GLN ILE LEU ILE TYR PRO ALA VAL GLY PHE
SEQRES 15 C 314 ASP SER VAL SER ARG SER MET ILE GLU TYR SER ASP GLY
SEQRES 16 C 314 PHE PHE LEU THR ARG GLU HIS ILE GLU TRP PHE GLY SER
SEQRES 17 C 314 GLN TYR LEU ARG SER PRO ALA ASP LEU LEU ASP PHE ARG
SEQRES 18 C 314 PHE SER PRO ILE LEU ALA GLN ASP LEU SER GLY LEU PRO
SEQRES 19 C 314 PRO ALA LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG
SEQRES 20 C 314 ASP GLN GLY GLU ALA TYR ALA ASN ARG LEU LEU GLN ALA
SEQRES 21 C 314 GLY VAL PRO VAL THR SER VAL ARG PHE ASN ASN VAL ILE
SEQRES 22 C 314 HIS GLY PHE LEU SER PHE PHE PRO LEU ILE GLU GLN GLY
SEQRES 23 C 314 ARG ASP ALA ILE SER LEU ILE GLY SER VAL LEU ARG ARG
SEQRES 24 C 314 THR PHE TYR ASP LYS SER ALA ALA ALA HIS HIS HIS HIS
SEQRES 25 C 314 HIS HIS
SEQRES 1 D 314 MET PRO LEU ASP PRO ARG ILE LYS GLU LEU LEU GLU SER
SEQRES 2 D 314 GLY PHE ILE VAL PRO ILE GLY LYS ALA SER VAL ASP GLU
SEQRES 3 D 314 VAL ARG LYS ILE PHE ARG GLN LEU ALA SER ALA ALA PRO
SEQRES 4 D 314 LYS VAL GLU VAL GLY LYS VAL GLU ASP ILE LYS ILE PRO
SEQRES 5 D 314 GLY SER GLU ALA ASN ILE ASN ALA ARG VAL TYR LEU PRO
SEQRES 6 D 314 LYS ALA ASN GLY PRO TYR GLY VAL LEU ILE TYR LEU HIS
SEQRES 7 D 314 GLY GLY GLY PHE VAL ILE GLY ASP VAL GLU SER TYR ASP
SEQRES 8 D 314 PRO LEU CYS ARG ALA ILE THR ASN ALA CYS ASN CYS VAL
SEQRES 9 D 314 VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU TYR LYS
SEQRES 10 D 314 PHE PRO SER ALA VAL ILE ASP SER PHE ASP ALA THR ASN
SEQRES 11 D 314 TRP VAL TYR ASN ASN LEU ASP LYS PHE ASP GLY LYS MET
SEQRES 12 D 314 GLY VAL ALA ILE ALA GLY ASP SER ALA GLY GLY ASN LEU
SEQRES 13 D 314 ALA ALA VAL VAL ALA LEU LEU SER LYS GLY LYS LEU ASN
SEQRES 14 D 314 LEU LYS TYR GLN ILE LEU ILE TYR PRO ALA VAL GLY PHE
SEQRES 15 D 314 ASP SER VAL SER ARG SER MET ILE GLU TYR SER ASP GLY
SEQRES 16 D 314 PHE PHE LEU THR ARG GLU HIS ILE GLU TRP PHE GLY SER
SEQRES 17 D 314 GLN TYR LEU ARG SER PRO ALA ASP LEU LEU ASP PHE ARG
SEQRES 18 D 314 PHE SER PRO ILE LEU ALA GLN ASP LEU SER GLY LEU PRO
SEQRES 19 D 314 PRO ALA LEU ILE ILE THR ALA GLU TYR ASP PRO LEU ARG
SEQRES 20 D 314 ASP GLN GLY GLU ALA TYR ALA ASN ARG LEU LEU GLN ALA
SEQRES 21 D 314 GLY VAL PRO VAL THR SER VAL ARG PHE ASN ASN VAL ILE
SEQRES 22 D 314 HIS GLY PHE LEU SER PHE PHE PRO LEU ILE GLU GLN GLY
SEQRES 23 D 314 ARG ASP ALA ILE SER LEU ILE GLY SER VAL LEU ARG ARG
SEQRES 24 D 314 THR PHE TYR ASP LYS SER ALA ALA ALA HIS HIS HIS HIS
SEQRES 25 D 314 HIS HIS
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 B 401 5
HET SO4 B 402 5
HET SO4 C 401 5
HET SO4 C 402 5
HET SO4 C 403 5
HET SO4 D 401 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 8(O4 S 2-)
FORMUL 13 HOH *438(H2 O)
HELIX 1 AA1 ASP A 4 SER A 13 1 10
HELIX 2 AA2 SER A 23 ALA A 37 1 15
HELIX 3 AA3 TYR A 90 ASN A 102 1 13
HELIX 4 AA4 PRO A 119 ASN A 134 1 16
HELIX 5 AA5 ASN A 135 PHE A 139 5 5
HELIX 6 AA6 SER A 151 SER A 164 1 14
HELIX 7 AA7 SER A 186 TYR A 192 1 7
HELIX 8 AA8 THR A 199 LEU A 211 1 13
HELIX 9 AA9 SER A 213 ASP A 219 5 7
HELIX 10 AB1 SER A 223 ALA A 227 5 5
HELIX 11 AB2 LEU A 246 ALA A 260 1 15
HELIX 12 AB3 GLY A 275 PHE A 280 5 6
HELIX 13 AB4 GLU A 284 ASP A 303 1 20
HELIX 14 AB5 ASP B 4 SER B 13 1 10
HELIX 15 AB6 SER B 23 SER B 36 1 14
HELIX 16 AB7 ASP B 86 ASN B 102 1 17
HELIX 17 AB8 PRO B 119 ASN B 135 1 17
HELIX 18 AB9 LEU B 136 ASP B 140 5 5
HELIX 19 AC1 ALA B 152 SER B 164 1 13
HELIX 20 AC2 SER B 186 TYR B 192 1 7
HELIX 21 AC3 THR B 199 LEU B 211 1 13
HELIX 22 AC4 SER B 213 ASP B 219 5 7
HELIX 23 AC5 SER B 223 ALA B 227 5 5
HELIX 24 AC6 LEU B 246 ALA B 260 1 15
HELIX 25 AC7 GLU B 284 TYR B 302 1 19
HELIX 26 AC8 ASP C 4 SER C 13 1 10
HELIX 27 AC9 PRO C 18 ALA C 22 5 5
HELIX 28 AD1 SER C 23 SER C 36 1 14
HELIX 29 AD2 ASP C 86 ASN C 102 1 17
HELIX 30 AD3 PRO C 119 ASN C 134 1 16
HELIX 31 AD4 ASN C 135 ASP C 140 5 6
HELIX 32 AD5 ALA C 152 SER C 164 1 13
HELIX 33 AD6 SER C 186 TYR C 192 1 7
HELIX 34 AD7 THR C 199 LEU C 211 1 13
HELIX 35 AD8 SER C 213 ASP C 219 5 7
HELIX 36 AD9 SER C 223 ALA C 227 5 5
HELIX 37 AE1 LEU C 246 ALA C 260 1 15
HELIX 38 AE2 GLY C 275 PHE C 280 5 6
HELIX 39 AE3 GLU C 284 TYR C 302 1 19
HELIX 40 AE4 ASP D 4 GLU D 12 1 9
HELIX 41 AE5 SER D 23 ALA D 37 1 15
HELIX 42 AE6 ASP D 86 ASN D 102 1 17
HELIX 43 AE7 PRO D 119 ASN D 135 1 17
HELIX 44 AE8 LEU D 136 ASP D 140 5 5
HELIX 45 AE9 ALA D 152 SER D 164 1 13
HELIX 46 AF1 SER D 186 TYR D 192 1 7
HELIX 47 AF2 THR D 199 LEU D 211 1 13
HELIX 48 AF3 SER D 213 ASP D 219 5 7
HELIX 49 AF4 SER D 223 ALA D 227 5 5
HELIX 50 AF5 LEU D 246 ALA D 260 1 15
HELIX 51 AF6 GLY D 275 PHE D 280 5 6
HELIX 52 AF7 ILE D 283 TYR D 302 1 20
SHEET 1 AA116 VAL A 46 PRO A 52 0
SHEET 2 AA116 ASN A 57 TYR A 63 -1 O VAL A 62 N GLU A 47
SHEET 3 AA116 VAL A 104 VAL A 108 -1 O VAL A 105 N TYR A 63
SHEET 4 AA116 GLY A 72 LEU A 77 1 N LEU A 74 O VAL A 104
SHEET 5 AA116 GLY A 144 ASP A 150 1 O GLY A 144 N VAL A 73
SHEET 6 AA116 GLN A 173 ILE A 176 1 O ILE A 176 N GLY A 149
SHEET 7 AA116 ALA A 236 TYR A 243 1 O ILE A 239 N LEU A 175
SHEET 8 AA116 VAL A 264 ILE A 273 1 O PHE A 269 N THR A 240
SHEET 9 AA116 VAL B 264 ILE B 273 -1 O ASN B 270 N SER A 266
SHEET 10 AA116 ALA B 236 TYR B 243 1 N THR B 240 O PHE B 269
SHEET 11 AA116 TYR B 172 PRO B 178 1 N LEU B 175 O LEU B 237
SHEET 12 AA116 VAL B 145 SER B 151 1 N GLY B 149 O ILE B 176
SHEET 13 AA116 VAL B 73 LEU B 77 1 N ILE B 75 O ALA B 146
SHEET 14 AA116 VAL B 104 ASP B 109 1 O VAL B 106 N TYR B 76
SHEET 15 AA116 ASN B 57 TYR B 63 -1 N TYR B 63 O VAL B 105
SHEET 16 AA116 VAL B 46 PRO B 52 -1 N ILE B 49 O ALA B 60
SHEET 1 AA216 VAL C 46 PRO C 52 0
SHEET 2 AA216 ASN C 57 TYR C 63 -1 O VAL C 62 N GLU C 47
SHEET 3 AA216 VAL C 104 ASP C 109 -1 O ASP C 109 N ASN C 59
SHEET 4 AA216 GLY C 72 LEU C 77 1 N LEU C 74 O VAL C 104
SHEET 5 AA216 GLY C 144 SER C 151 1 O ALA C 146 N ILE C 75
SHEET 6 AA216 TYR C 172 PRO C 178 1 O ILE C 176 N GLY C 149
SHEET 7 AA216 ALA C 236 TYR C 243 1 O ILE C 239 N TYR C 177
SHEET 8 AA216 VAL C 264 ILE C 273 1 O PHE C 269 N THR C 240
SHEET 9 AA216 VAL D 264 ILE D 273 -1 O ARG D 268 N ARG C 268
SHEET 10 AA216 ALA D 236 TYR D 243 1 N THR D 240 O PHE D 269
SHEET 11 AA216 TYR D 172 PRO D 178 1 N TYR D 177 O ILE D 239
SHEET 12 AA216 VAL D 145 SER D 151 1 N GLY D 149 O ILE D 176
SHEET 13 AA216 VAL D 73 LEU D 77 1 N ILE D 75 O ALA D 146
SHEET 14 AA216 VAL D 104 ASP D 109 1 O VAL D 104 N LEU D 74
SHEET 15 AA216 ASN D 57 TYR D 63 -1 N TYR D 63 O VAL D 105
SHEET 16 AA216 VAL D 46 PRO D 52 -1 N GLU D 47 O VAL D 62
SSBOND 1 CYS A 101 CYS A 103 1555 1555 2.12
SSBOND 2 CYS B 101 CYS B 103 1555 1555 2.09
SSBOND 3 CYS C 101 CYS C 103 1555 1555 2.11
SSBOND 4 CYS D 101 CYS D 103 1555 1555 2.11
CISPEP 1 GLY A 69 PRO A 70 0 -8.68
CISPEP 2 ALA A 113 PRO A 114 0 4.20
CISPEP 3 PHE A 118 PRO A 119 0 4.85
CISPEP 4 GLY B 69 PRO B 70 0 -0.30
CISPEP 5 ALA B 113 PRO B 114 0 -1.14
CISPEP 6 PHE B 118 PRO B 119 0 6.37
CISPEP 7 GLY C 69 PRO C 70 0 -9.40
CISPEP 8 ALA C 113 PRO C 114 0 2.23
CISPEP 9 PHE C 118 PRO C 119 0 7.99
CISPEP 10 GLY D 69 PRO D 70 0 -0.77
CISPEP 11 ALA D 113 PRO D 114 0 1.77
CISPEP 12 PHE D 118 PRO D 119 0 8.66
SITE 1 AC1 3 ARG A 212 ARG A 221 HOH A 533
SITE 1 AC2 3 ARG A 298 HOH A 518 ARG B 298
SITE 1 AC3 3 ARG B 212 ARG B 221 HOH B 506
SITE 1 AC4 3 ARG A 298 ARG B 298 HOH B 584
SITE 1 AC5 4 ARG C 298 HOH C 504 HOH C 559 ARG D 298
SITE 1 AC6 3 ARG C 212 ARG C 221 HOH C 579
SITE 1 AC7 3 ARG C 298 HOH C 576 ARG D 298
SITE 1 AC8 3 ARG D 212 ARG D 221 HOH D 575
CRYST1 166.410 166.410 185.780 90.00 90.00 90.00 P 43 21 2 32
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 0.006009 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005383 0.00000
TER 2343 ASP A 303
TER 4686 ASP B 303
TER 7029 ASP C 303
TER 9372 ASP D 303
MASTER 521 0 8 52 32 0 8 6 9846 4 48 100
END |