HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 15-JUL-09 3IB6
TITLE CRYSTAL STRUCTURE OF AN UNCHARACTERIZED PROTEIN FROM LISTERIA
TITLE 2 MONOCYTOGENES SEROTYPE 4B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 634178;
SOURCE 4 STRAIN: CLIP81459;
SOURCE 5 GENE: LM4B_00283;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26
KEYWDS STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.BONANNO,M.GILMORE,K.T.BAIN,J.DO,S.OZYURT,J.M.SAUDER,S.K.BURLEY,
AUTHOR 2 S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS
AUTHOR 3 (NYSGXRC)
REVDAT 6 21-FEB-24 3IB6 1 REMARK
REVDAT 5 10-FEB-21 3IB6 1 AUTHOR JRNL SEQADV
REVDAT 4 21-NOV-18 3IB6 1 AUTHOR
REVDAT 3 01-NOV-17 3IB6 1 REMARK
REVDAT 2 13-JUL-11 3IB6 1 VERSN
REVDAT 1 28-JUL-09 3IB6 0
JRNL AUTH J.B.BONANNO,M.GILMORE,K.T.BAIN,J.DO,S.OZYURT,J.M.SAUDER,
JRNL AUTH 2 S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF AN UNCHARACTERIZED PROTEIN FROM
JRNL TITL 2 LISTERIA MONOCYTOGENES SEROTYPE 4B
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 36729
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.282
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1849
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2558
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3460
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.4180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5595
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 119
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : -1.11000
REMARK 3 B33 (A**2) : 0.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.29000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.336
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.206
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.061
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5722 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3694 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7824 ; 1.529 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9135 ; 0.954 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 711 ; 6.516 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 246 ;39.881 ;25.650
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 944 ;16.587 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.050 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 935 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6281 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1043 ; 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): 3587 ; 0.745 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1410 ; 0.158 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5853 ; 1.370 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2135 ; 2.042 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1971 ; 3.262 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3IB6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054193.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97958
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36797
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 38.101
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : 0.11500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.46300
REMARK 200 R SYM FOR SHELL (I) : 0.46300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 3350, 100MM AMMONIUM CHLORIDE,
REMARK 280 PH 7.0, VAPOR DIFFUSION, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 62.98500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 0
REMARK 465 SER A 1
REMARK 465 GLU A 181
REMARK 465 GLY A 182
REMARK 465 HIS A 183
REMARK 465 HIS A 184
REMARK 465 HIS A 185
REMARK 465 HIS A 186
REMARK 465 HIS A 187
REMARK 465 HIS A 188
REMARK 465 MET B 0
REMARK 465 SER B 1
REMARK 465 GLU B 181
REMARK 465 GLY B 182
REMARK 465 HIS B 183
REMARK 465 HIS B 184
REMARK 465 HIS B 185
REMARK 465 HIS B 186
REMARK 465 HIS B 187
REMARK 465 HIS B 188
REMARK 465 MET C 0
REMARK 465 SER C 1
REMARK 465 SER C 180
REMARK 465 GLU C 181
REMARK 465 GLY C 182
REMARK 465 HIS C 183
REMARK 465 HIS C 184
REMARK 465 HIS C 185
REMARK 465 HIS C 186
REMARK 465 HIS C 187
REMARK 465 HIS C 188
REMARK 465 MET D 0
REMARK 465 SER D 1
REMARK 465 GLU D 181
REMARK 465 GLY D 182
REMARK 465 HIS D 183
REMARK 465 HIS D 184
REMARK 465 HIS D 185
REMARK 465 HIS D 186
REMARK 465 HIS D 187
REMARK 465 HIS D 188
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 20 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 21 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 36 CG CD CE NZ
REMARK 470 GLU A 171 CG CD OE1 OE2
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LYS A 178 CG CD CE NZ
REMARK 470 ARG B 20 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 90 CG CD OE1 NE2
REMARK 470 GLN B 110 CG CD OE1 NE2
REMARK 470 GLU B 144 CG CD OE1 OE2
REMARK 470 GLU B 171 CG CD OE1 OE2
REMARK 470 ARG C 20 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 88 CG CD OE1 OE2
REMARK 470 GLN C 90 CG CD OE1 NE2
REMARK 470 LYS C 99 CG CD CE NZ
REMARK 470 GLU C 171 CG CD OE1 OE2
REMARK 470 LYS C 178 CG CD CE NZ
REMARK 470 ARG D 20 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 93 CG CD CE NZ
REMARK 470 LYS D 99 CG CD CE NZ
REMARK 470 GLU D 171 CG CD OE1 OE2
REMARK 470 LYS D 177 CG CD CE NZ
REMARK 470 LYS D 178 CG CD CE NZ
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 MET A 9 -75.31 -98.29
REMARK 500 THR A 12 -76.55 -129.86
REMARK 500 ARG A 20 -55.43 65.96
REMARK 500 ASN A 37 8.32 81.88
REMARK 500 ASN A 142 108.31 -42.02
REMARK 500 MET B 9 -75.48 -99.46
REMARK 500 THR B 12 -64.53 -122.85
REMARK 500 ARG B 20 -55.49 73.61
REMARK 500 ALA B 59 -73.15 -88.74
REMARK 500 MET C 9 -86.16 -95.56
REMARK 500 THR C 12 -62.55 -123.84
REMARK 500 ARG C 20 -72.60 80.85
REMARK 500 ALA C 59 -78.66 -94.16
REMARK 500 SER C 87 -7.40 -145.01
REMARK 500 LEU C 89 41.44 -109.71
REMARK 500 MET D 9 -69.73 -100.45
REMARK 500 THR D 12 -66.43 -126.48
REMARK 500 PRO D 143 -5.39 -59.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-13913A RELATED DB: TARGETDB
DBREF 3IB6 A 3 180 UNP C1KYJ5 C1KYJ5_LISMC 3 180
DBREF 3IB6 B 3 180 UNP C1KYJ5 C1KYJ5_LISMC 3 180
DBREF 3IB6 C 3 180 UNP C1KYJ5 C1KYJ5_LISMC 3 180
DBREF 3IB6 D 3 180 UNP C1KYJ5 C1KYJ5_LISMC 3 180
SEQADV 3IB6 MET A 0 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 SER A 1 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 LEU A 2 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLU A 181 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLY A 182 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS A 183 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS A 184 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS A 185 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS A 186 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS A 187 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS A 188 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 MET B 0 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 SER B 1 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 LEU B 2 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLU B 181 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLY B 182 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS B 183 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS B 184 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS B 185 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS B 186 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS B 187 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS B 188 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 MET C 0 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 SER C 1 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 LEU C 2 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLU C 181 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLY C 182 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS C 183 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS C 184 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS C 185 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS C 186 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS C 187 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS C 188 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 MET D 0 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 SER D 1 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 LEU D 2 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLU D 181 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 GLY D 182 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS D 183 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS D 184 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS D 185 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS D 186 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS D 187 UNP C1KYJ5 EXPRESSION TAG
SEQADV 3IB6 HIS D 188 UNP C1KYJ5 EXPRESSION TAG
SEQRES 1 A 189 MET SER LEU THR HIS VAL ILE TRP ASP MET GLY GLU THR
SEQRES 2 A 189 LEU ASN THR VAL PRO ASN THR ARG TYR ASP HIS HIS PRO
SEQRES 3 A 189 LEU ASP THR TYR PRO GLU VAL VAL LEU ARG LYS ASN ALA
SEQRES 4 A 189 LYS GLU THR LEU GLU LYS VAL LYS GLN LEU GLY PHE LYS
SEQRES 5 A 189 GLN ALA ILE LEU SER ASN THR ALA THR SER ASP THR GLU
SEQRES 6 A 189 VAL ILE LYS ARG VAL LEU THR ASN PHE GLY ILE ILE ASP
SEQRES 7 A 189 TYR PHE ASP PHE ILE TYR ALA SER ASN SER GLU LEU GLN
SEQRES 8 A 189 PRO GLY LYS MET GLU LYS PRO ASP LYS THR ILE PHE ASP
SEQRES 9 A 189 PHE THR LEU ASN ALA LEU GLN ILE ASP LYS THR GLU ALA
SEQRES 10 A 189 VAL MET VAL GLY ASN THR PHE GLU SER ASP ILE ILE GLY
SEQRES 11 A 189 ALA ASN ARG ALA GLY ILE HIS ALA ILE TRP LEU GLN ASN
SEQRES 12 A 189 PRO GLU VAL CYS LEU GLN ASP GLU ARG LEU PRO LEU VAL
SEQRES 13 A 189 ALA PRO PRO PHE VAL ILE PRO VAL TRP ASP LEU ALA ASP
SEQRES 14 A 189 VAL PRO GLU ALA LEU LEU LEU LEU LYS LYS ILE SER GLU
SEQRES 15 A 189 GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 189 MET SER LEU THR HIS VAL ILE TRP ASP MET GLY GLU THR
SEQRES 2 B 189 LEU ASN THR VAL PRO ASN THR ARG TYR ASP HIS HIS PRO
SEQRES 3 B 189 LEU ASP THR TYR PRO GLU VAL VAL LEU ARG LYS ASN ALA
SEQRES 4 B 189 LYS GLU THR LEU GLU LYS VAL LYS GLN LEU GLY PHE LYS
SEQRES 5 B 189 GLN ALA ILE LEU SER ASN THR ALA THR SER ASP THR GLU
SEQRES 6 B 189 VAL ILE LYS ARG VAL LEU THR ASN PHE GLY ILE ILE ASP
SEQRES 7 B 189 TYR PHE ASP PHE ILE TYR ALA SER ASN SER GLU LEU GLN
SEQRES 8 B 189 PRO GLY LYS MET GLU LYS PRO ASP LYS THR ILE PHE ASP
SEQRES 9 B 189 PHE THR LEU ASN ALA LEU GLN ILE ASP LYS THR GLU ALA
SEQRES 10 B 189 VAL MET VAL GLY ASN THR PHE GLU SER ASP ILE ILE GLY
SEQRES 11 B 189 ALA ASN ARG ALA GLY ILE HIS ALA ILE TRP LEU GLN ASN
SEQRES 12 B 189 PRO GLU VAL CYS LEU GLN ASP GLU ARG LEU PRO LEU VAL
SEQRES 13 B 189 ALA PRO PRO PHE VAL ILE PRO VAL TRP ASP LEU ALA ASP
SEQRES 14 B 189 VAL PRO GLU ALA LEU LEU LEU LEU LYS LYS ILE SER GLU
SEQRES 15 B 189 GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 C 189 MET SER LEU THR HIS VAL ILE TRP ASP MET GLY GLU THR
SEQRES 2 C 189 LEU ASN THR VAL PRO ASN THR ARG TYR ASP HIS HIS PRO
SEQRES 3 C 189 LEU ASP THR TYR PRO GLU VAL VAL LEU ARG LYS ASN ALA
SEQRES 4 C 189 LYS GLU THR LEU GLU LYS VAL LYS GLN LEU GLY PHE LYS
SEQRES 5 C 189 GLN ALA ILE LEU SER ASN THR ALA THR SER ASP THR GLU
SEQRES 6 C 189 VAL ILE LYS ARG VAL LEU THR ASN PHE GLY ILE ILE ASP
SEQRES 7 C 189 TYR PHE ASP PHE ILE TYR ALA SER ASN SER GLU LEU GLN
SEQRES 8 C 189 PRO GLY LYS MET GLU LYS PRO ASP LYS THR ILE PHE ASP
SEQRES 9 C 189 PHE THR LEU ASN ALA LEU GLN ILE ASP LYS THR GLU ALA
SEQRES 10 C 189 VAL MET VAL GLY ASN THR PHE GLU SER ASP ILE ILE GLY
SEQRES 11 C 189 ALA ASN ARG ALA GLY ILE HIS ALA ILE TRP LEU GLN ASN
SEQRES 12 C 189 PRO GLU VAL CYS LEU GLN ASP GLU ARG LEU PRO LEU VAL
SEQRES 13 C 189 ALA PRO PRO PHE VAL ILE PRO VAL TRP ASP LEU ALA ASP
SEQRES 14 C 189 VAL PRO GLU ALA LEU LEU LEU LEU LYS LYS ILE SER GLU
SEQRES 15 C 189 GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 D 189 MET SER LEU THR HIS VAL ILE TRP ASP MET GLY GLU THR
SEQRES 2 D 189 LEU ASN THR VAL PRO ASN THR ARG TYR ASP HIS HIS PRO
SEQRES 3 D 189 LEU ASP THR TYR PRO GLU VAL VAL LEU ARG LYS ASN ALA
SEQRES 4 D 189 LYS GLU THR LEU GLU LYS VAL LYS GLN LEU GLY PHE LYS
SEQRES 5 D 189 GLN ALA ILE LEU SER ASN THR ALA THR SER ASP THR GLU
SEQRES 6 D 189 VAL ILE LYS ARG VAL LEU THR ASN PHE GLY ILE ILE ASP
SEQRES 7 D 189 TYR PHE ASP PHE ILE TYR ALA SER ASN SER GLU LEU GLN
SEQRES 8 D 189 PRO GLY LYS MET GLU LYS PRO ASP LYS THR ILE PHE ASP
SEQRES 9 D 189 PHE THR LEU ASN ALA LEU GLN ILE ASP LYS THR GLU ALA
SEQRES 10 D 189 VAL MET VAL GLY ASN THR PHE GLU SER ASP ILE ILE GLY
SEQRES 11 D 189 ALA ASN ARG ALA GLY ILE HIS ALA ILE TRP LEU GLN ASN
SEQRES 12 D 189 PRO GLU VAL CYS LEU GLN ASP GLU ARG LEU PRO LEU VAL
SEQRES 13 D 189 ALA PRO PRO PHE VAL ILE PRO VAL TRP ASP LEU ALA ASP
SEQRES 14 D 189 VAL PRO GLU ALA LEU LEU LEU LEU LYS LYS ILE SER GLU
SEQRES 15 D 189 GLY HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *119(H2 O)
HELIX 1 1 PRO A 25 TYR A 29 5 5
HELIX 2 2 ASN A 37 LEU A 48 1 12
HELIX 3 3 ASP A 62 PHE A 73 1 12
HELIX 4 4 ILE A 75 ASP A 77 5 3
HELIX 5 5 ASP A 98 GLN A 110 1 13
HELIX 6 6 ASP A 112 THR A 114 5 3
HELIX 7 7 ASP A 126 ALA A 133 1 8
HELIX 8 8 ASP A 165 ALA A 167 5 3
HELIX 9 9 ASP A 168 SER A 180 1 13
HELIX 10 10 PRO B 25 TYR B 29 5 5
HELIX 11 11 ASN B 37 LEU B 48 1 12
HELIX 12 12 ASP B 62 PHE B 73 1 12
HELIX 13 13 ILE B 75 ASP B 77 5 3
HELIX 14 14 ASP B 98 GLN B 110 1 13
HELIX 15 15 ASP B 112 THR B 114 5 3
HELIX 16 16 ASP B 126 ALA B 133 1 8
HELIX 17 17 ASP B 165 ALA B 167 5 3
HELIX 18 18 ASP B 168 SER B 180 1 13
HELIX 19 19 PRO C 25 TYR C 29 5 5
HELIX 20 20 ASN C 37 GLY C 49 1 13
HELIX 21 21 ASP C 62 PHE C 73 1 12
HELIX 22 22 ILE C 75 ASP C 77 5 3
HELIX 23 23 ASP C 98 GLN C 110 1 13
HELIX 24 24 ASP C 112 THR C 114 5 3
HELIX 25 25 ASP C 126 ALA C 133 1 8
HELIX 26 26 ASP C 165 ALA C 167 5 3
HELIX 27 27 ASP C 168 ILE C 179 1 12
HELIX 28 28 PRO D 25 TYR D 29 5 5
HELIX 29 29 ASN D 37 LEU D 48 1 12
HELIX 30 30 ASP D 62 PHE D 73 1 12
HELIX 31 31 ILE D 75 ASP D 77 5 3
HELIX 32 32 ASP D 98 GLN D 110 1 13
HELIX 33 33 ASP D 112 THR D 114 5 3
HELIX 34 34 SER D 125 ALA D 133 1 9
HELIX 35 35 ASP D 165 ALA D 167 5 3
HELIX 36 36 ASP D 168 SER D 180 1 13
SHEET 1 A 6 PHE A 79 ALA A 84 0
SHEET 2 A 6 LYS A 51 SER A 56 1 N GLN A 52 O ASP A 80
SHEET 3 A 6 HIS A 4 TRP A 7 1 N TRP A 7 O ALA A 53
SHEET 4 A 6 ALA A 116 GLY A 120 1 O VAL A 117 N ILE A 6
SHEET 5 A 6 HIS A 136 LEU A 140 1 O ILE A 138 N MET A 118
SHEET 6 A 6 VAL A 160 VAL A 163 1 O ILE A 161 N ALA A 137
SHEET 1 B 6 PHE B 79 ALA B 84 0
SHEET 2 B 6 LYS B 51 SER B 56 1 N GLN B 52 O ASP B 80
SHEET 3 B 6 HIS B 4 TRP B 7 1 N TRP B 7 O ALA B 53
SHEET 4 B 6 ALA B 116 GLY B 120 1 O VAL B 117 N ILE B 6
SHEET 5 B 6 HIS B 136 LEU B 140 1 O ILE B 138 N MET B 118
SHEET 6 B 6 VAL B 160 VAL B 163 1 O ILE B 161 N ALA B 137
SHEET 1 C 6 PHE C 79 ALA C 84 0
SHEET 2 C 6 LYS C 51 SER C 56 1 N GLN C 52 O ASP C 80
SHEET 3 C 6 HIS C 4 TRP C 7 1 N TRP C 7 O ALA C 53
SHEET 4 C 6 ALA C 116 GLY C 120 1 O VAL C 117 N ILE C 6
SHEET 5 C 6 HIS C 136 LEU C 140 1 O ILE C 138 N MET C 118
SHEET 6 C 6 VAL C 160 VAL C 163 1 O ILE C 161 N TRP C 139
SHEET 1 D 6 PHE D 79 ALA D 84 0
SHEET 2 D 6 LYS D 51 SER D 56 1 N SER D 56 O TYR D 83
SHEET 3 D 6 HIS D 4 TRP D 7 1 N TRP D 7 O LEU D 55
SHEET 4 D 6 ALA D 116 GLY D 120 1 O VAL D 117 N ILE D 6
SHEET 5 D 6 HIS D 136 LEU D 140 1 O ILE D 138 N MET D 118
SHEET 6 D 6 VAL D 160 VAL D 163 1 O ILE D 161 N ALA D 137
CISPEP 1 LYS A 96 PRO A 97 0 6.40
CISPEP 2 ALA A 156 PRO A 157 0 -8.52
CISPEP 3 PRO A 157 PRO A 158 0 0.96
CISPEP 4 LYS B 96 PRO B 97 0 4.76
CISPEP 5 ALA B 156 PRO B 157 0 -10.17
CISPEP 6 PRO B 157 PRO B 158 0 0.95
CISPEP 7 LYS C 96 PRO C 97 0 6.17
CISPEP 8 ALA C 156 PRO C 157 0 -9.40
CISPEP 9 PRO C 157 PRO C 158 0 0.08
CISPEP 10 LYS D 96 PRO D 97 0 4.34
CISPEP 11 ALA D 156 PRO D 157 0 -3.06
CISPEP 12 PRO D 157 PRO D 158 0 -5.14
CRYST1 41.122 125.970 73.385 90.00 103.58 90.00 P 1 21 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 0.024318 0.000000 0.005872 0.00000
SCALE2 0.000000 0.007938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014018 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
