HEADER PROTEIN BINDING/CYTOKINE 28-FEB-11 3QWR
TITLE CRYSTAL STRUCTURE OF IL-23 IN COMPLEX WITH AN ADNECTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-12 SUBUNIT BETA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IL-12B, CYTOTOXIC LYMPHOCYTE MATURATION FACTOR 40 KDA
COMPND 5 SUBUNIT, CLMF P40, IL-12 SUBUNIT P40, NK CELL STIMULATORY FACTOR
COMPND 6 CHAIN 2, NKSF2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERLEUKIN-23 SUBUNIT ALPHA;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: IL-23 SUBUNIT ALPHA, IL-23-A, INTERLEUKIN-23 SUBUNIT P19,
COMPND 12 IL-23P19;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: ADNECTIN;
COMPND 16 CHAIN: D;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IL12B, NKSF2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFBDUAL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: IL23A, SGRF, UNQ2498/PRO5798;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PFBDUAL;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 23 ORGANISM_COMMON: HUMAN;
SOURCE 24 ORGANISM_TAXID: 9606;
SOURCE 25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 26 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 27 EXPRESSION_SYSTEM_STRAIN: HMS174;
SOURCE 28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 29 EXPRESSION_SYSTEM_PLASMID: PET9 PCT734
KEYWDS FOUR-HELIX BUNDLE CYTOKINE, IG DOMAIN, GLYCOPROTEIN, IMMUNOGLOBULIN
KEYWDS 2 DOMAIN, SECRETED, ANTIVIRAL DEFENSE, IMMUNE RESPONSE, INFLAMMATORY
KEYWDS 3 RESPONSE, INNATE IMMUNITY, TISSUE REMODELING, ADNECTIN, ENGINEERED
KEYWDS 4 BINDING PROTEIN, ANTIBODY MIMIC, PROTEIN BINDING-CYTOKINE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.WEI,S.SHERIFF
REVDAT 5 13-SEP-23 3QWR 1 HETSYN
REVDAT 4 29-JUL-20 3QWR 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 08-NOV-17 3QWR 1 REMARK
REVDAT 2 29-FEB-12 3QWR 1 JRNL
REVDAT 1 01-FEB-12 3QWR 0
JRNL AUTH V.RAMAMURTHY,S.R.KRYSTEK,A.BUSH,A.WEI,S.L.EMANUEL,
JRNL AUTH 2 R.DAS GUPTA,A.JANJUA,L.CHENG,M.MURDOCK,B.ABRAMCZYK,D.COHEN,
JRNL AUTH 3 Z.LIN,P.MORIN,J.H.DAVIS,M.DABRITZ,D.C.MCLAUGHLIN,K.A.RUSSO,
JRNL AUTH 4 G.CHAO,M.C.WRIGHT,V.A.JENNY,L.J.ENGLE,E.FURFINE,S.SHERIFF
JRNL TITL STRUCTURES OF ADNECTIN/PROTEIN COMPLEXES REVEAL AN EXPANDED
JRNL TITL 2 BINDING FOOTPRINT.
JRNL REF STRUCTURE V. 20 259 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22325775
JRNL DOI 10.1016/J.STR.2011.11.016
REMARK 2
REMARK 2 RESOLUTION. 3.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.13.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 12815
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.234
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.830
REMARK 3 FREE R VALUE TEST SET COUNT : 1003
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.71
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3043
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2362
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2810
REMARK 3 BIN R VALUE (WORKING SET) : 0.2306
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.66
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 233
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3989
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.75
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 100.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -16.62610
REMARK 3 B22 (A**2) : -10.18290
REMARK 3 B33 (A**2) : 26.80900
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.740
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.470
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4151 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5684 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1321 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 81 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 604 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4151 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 575 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 4588 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.36
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.38
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.15
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: A 2 A 305
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8537 -41.3024 -43.0592
REMARK 3 T TENSOR
REMARK 3 T11: 0.4959 T22: -0.3345
REMARK 3 T33: -0.4029 T12: 0.0386
REMARK 3 T13: -0.0572 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 0.9628 L22: 1.1726
REMARK 3 L33: 2.5297 L12: 0.3670
REMARK 3 L13: -0.8365 L23: -0.1579
REMARK 3 S TENSOR
REMARK 3 S11: 0.0791 S12: -0.0548 S13: 0.0651
REMARK 3 S21: 0.0172 S22: 0.0261 S23: -0.0039
REMARK 3 S31: -0.2801 S32: 0.0804 S33: -0.1052
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: B 7 B 168
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6541 -41.1183 -13.1264
REMARK 3 T TENSOR
REMARK 3 T11: 0.4931 T22: -0.0535
REMARK 3 T33: -0.4193 T12: 0.0262
REMARK 3 T13: -0.0993 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 3.7273 L22: 2.2769
REMARK 3 L33: 1.9797 L12: -0.1696
REMARK 3 L13: 1.2084 L23: -0.6465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: -0.4029 S13: 0.2053
REMARK 3 S21: 0.1645 S22: -0.0429 S23: -0.3459
REMARK 3 S31: -0.0397 S32: 0.4431 S33: 0.0036
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: D 3 D 93
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0208 -34.6959 -28.6838
REMARK 3 T TENSOR
REMARK 3 T11: 0.4814 T22: -0.3258
REMARK 3 T33: -0.4189 T12: -0.0418
REMARK 3 T13: -0.0384 T23: 0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 2.5614 L22: 4.0379
REMARK 3 L33: 0.8634 L12: 0.2341
REMARK 3 L13: -2.1047 L23: -0.0726
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: 0.4725 S13: -0.0770
REMARK 3 S21: -0.1717 S22: 0.2310 S23: 0.7036
REMARK 3 S31: -0.0058 S32: -0.3611 S33: -0.1939
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QWR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-11.
REMARK 100 THE DEPOSITION ID IS D_1000064200.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 : 17-ID
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12835
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250
REMARK 200 RESOLUTION RANGE LOW (A) : 42.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, AMORE
REMARK 200 STARTING MODEL: IL-23 FROM UNPUBLISHED STRUCTURE AND ADNECTIN FROM
REMARK 200 PDB ENTRY 1FNF RESIDUES 1421-1437, 1444-1466, 1470-1491, 1502-
REMARK 200 1509
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 1 M TRI-SODIUM
REMARK 280 CITRATE, 0.2 M NACL, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 38.85000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.85000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.85000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.85000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.85000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.85000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 112.90000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.85000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.85000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 112.90000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, 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 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 ILE A 1
REMARK 465 VAL A 158
REMARK 465 GLY A 257
REMARK 465 LYS A 258
REMARK 465 SER A 259
REMARK 465 LYS A 260
REMARK 465 ARG A 261
REMARK 465 GLU A 262
REMARK 465 ASN A 281
REMARK 465 ALA A 282
REMARK 465 SER A 306
REMARK 465 ARG B 1
REMARK 465 ALA B 2
REMARK 465 VAL B 3
REMARK 465 PRO B 4
REMARK 465 GLY B 5
REMARK 465 GLY B 6
REMARK 465 GLU B 39
REMARK 465 GLU B 40
REMARK 465 GLY B 41
REMARK 465 ASP B 42
REMARK 465 GLU B 43
REMARK 465 GLU B 44
REMARK 465 THR B 45
REMARK 465 THR B 46
REMARK 465 ASN B 47
REMARK 465 ASP B 48
REMARK 465 VAL B 49
REMARK 465 HIS B 121
REMARK 465 HIS B 122
REMARK 465 TRP B 123
REMARK 465 GLU B 124
REMARK 465 THR B 125
REMARK 465 GLN B 126
REMARK 465 GLN B 127
REMARK 465 ILE B 128
REMARK 465 PRO B 129
REMARK 465 SER B 130
REMARK 465 SER B 169
REMARK 465 PRO B 170
REMARK 465 MET D -1
REMARK 465 GLY D 0
REMARK 465 VAL D 1
REMARK 465 SER D 2
REMARK 465 THR D 94
REMARK 465 GLU D 95
REMARK 465 ILE D 96
REMARK 465 ASP D 97
REMARK 465 LYS D 98
REMARK 465 PRO D 99
REMARK 465 SER D 100
REMARK 465 GLN D 101
REMARK 465 HIS D 102
REMARK 465 HIS D 103
REMARK 465 HIS D 104
REMARK 465 HIS D 105
REMARK 465 HIS D 106
REMARK 465 HIS D 107
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 LYS A 5 CE NZ
REMARK 470 LYS A 6 CG CD CE NZ
REMARK 470 TYR A 16 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 23 SD CE
REMARK 470 GLU A 32 CG CD OE1 OE2
REMARK 470 GLU A 33 CG CD OE1 OE2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 LYS A 58 CG CD CE NZ
REMARK 470 GLU A 59 CG CD OE1 OE2
REMARK 470 LYS A 70 CG CD CE NZ
REMARK 470 SER A 78 OG
REMARK 470 LYS A 84 NZ
REMARK 470 ILE A 89 CG1 CG2 CD1
REMARK 470 GLU A 100 CG CD OE1 OE2
REMARK 470 LYS A 102 CG CD CE NZ
REMARK 470 LYS A 104 CD CE NZ
REMARK 470 LYS A 135 CG CD CE NZ
REMARK 470 ARG A 157 NE CZ NH1 NH2
REMARK 470 ARG A 159 CZ NH1 NH2
REMARK 470 ASP A 161 CG OD1 OD2
REMARK 470 ASN A 162 CG OD1 ND2
REMARK 470 LYS A 163 CG CD CE NZ
REMARK 470 LEU A 224 CG CD1 CD2
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 SER A 227 OG
REMARK 470 LYS A 264 CG CD CE NZ
REMARK 470 LYS A 280 CG CD CE NZ
REMARK 470 LYS B 20 CG CD CE NZ
REMARK 470 ARG B 38 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 61 CG CD OE1 NE2
REMARK 470 LEU B 63 CG CD1 CD2
REMARK 470 ARG B 64 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 66 CG OD1 ND2
REMARK 470 SER B 67 OG
REMARK 470 GLN B 68 CG CD OE1 NE2
REMARK 470 GLN B 72 CG CD OE1 NE2
REMARK 470 GLU B 82 CG CD OE1 OE2
REMARK 470 ASP B 88 CG OD1 OD2
REMARK 470 GLU B 93 CG CD OE1 OE2
REMARK 470 LEU B 97 CG CD1 CD2
REMARK 470 ASP B 99 CG OD1 OD2
REMARK 470 LEU B 116 CG CD1 CD2
REMARK 470 GLN B 117 CG CD OE1 NE2
REMARK 470 GLU B 119 CG CD OE1 OE2
REMARK 470 LEU B 131 CG CD1 CD2
REMARK 470 SER B 132 OG
REMARK 470 SER B 134 OG
REMARK 470 GLN B 135 CG CD OE1 NE2
REMARK 470 GLN B 138 CG CD OE1 NE2
REMARK 470 ARG B 139 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 3 CG OD1 OD2
REMARK 470 ARG D 6 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 23 CG CD OE1 OE2
REMARK 470 ARG D 29 CZ NH1 NH2
REMARK 470 LYS D 80 CE NZ
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 HIS B 34 C - N - CA ANGL. DEV. = 19.9 DEGREES
REMARK 500 VAL D 45 N - CA - CB ANGL. DEV. = 16.3 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 LYS A 5 157.45 71.35
REMARK 500 GLU A 12 98.65 76.88
REMARK 500 ALA A 19 118.39 17.59
REMARK 500 GLU A 22 134.28 -15.22
REMARK 500 GLU A 32 159.12 154.05
REMARK 500 ASP A 34 -141.34 -116.12
REMARK 500 ASP A 41 -130.94 53.41
REMARK 500 THR A 92 52.75 -140.61
REMARK 500 LYS A 99 1.61 57.48
REMARK 500 GLU A 100 -78.38 -61.61
REMARK 500 ASN A 103 -173.04 -69.09
REMARK 500 LYS A 104 59.65 17.77
REMARK 500 ASP A 142 64.82 -118.84
REMARK 500 ASN A 162 65.84 -115.29
REMARK 500 LYS A 195 -110.08 61.41
REMARK 500 ASN A 218 51.72 39.12
REMARK 500 LYS A 225 -105.63 -60.52
REMARK 500 ASN A 226 48.13 -81.09
REMARK 500 TYR A 246 -62.88 -103.49
REMARK 500 ASP A 265 100.97 113.20
REMARK 500 ARG A 279 -158.20 -73.22
REMARK 500 TYR A 293 -99.07 -94.31
REMARK 500 SER A 294 -98.66 179.98
REMARK 500 SER A 295 -178.43 68.12
REMARK 500 PRO B 9 29.73 -78.82
REMARK 500 VAL B 32 -116.88 -86.55
REMARK 500 GLN B 117 81.14 -152.75
REMARK 500 SER B 134 -84.41 -127.23
REMARK 500 VAL D 4 -75.15 -63.92
REMARK 500 ASP D 7 -16.49 -152.42
REMARK 500 PRO D 15 3.15 -68.30
REMARK 500 THR D 16 10.15 -141.04
REMARK 500 VAL D 45 108.04 75.08
REMARK 500 THR D 76 -89.75 -100.63
REMARK 500 SER D 77 -142.22 -134.06
REMARK 500 SER D 78 10.02 -144.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QWQ RELATED DB: PDB
DBREF 3QWR A 1 306 UNP P29460 IL12B_HUMAN 23 328
DBREF 3QWR B 1 170 UNP Q9NPF7 IL23A_HUMAN 20 189
DBREF 3QWR D -1 107 PDB 3QWR 3QWR -1 107
SEQRES 1 A 306 ILE TRP GLU LEU LYS LYS ASP VAL TYR VAL VAL GLU LEU
SEQRES 2 A 306 ASP TRP TYR PRO ASP ALA PRO GLY GLU MET VAL VAL LEU
SEQRES 3 A 306 THR CYS ASP THR PRO GLU GLU ASP GLY ILE THR TRP THR
SEQRES 4 A 306 LEU ASP GLN SER SER GLU VAL LEU GLY SER GLY LYS THR
SEQRES 5 A 306 LEU THR ILE GLN VAL LYS GLU PHE GLY ASP ALA GLY GLN
SEQRES 6 A 306 TYR THR CYS HIS LYS GLY GLY GLU VAL LEU SER HIS SER
SEQRES 7 A 306 LEU LEU LEU LEU HIS LYS LYS GLU ASP GLY ILE TRP SER
SEQRES 8 A 306 THR ASP ILE LEU LYS ASP GLN LYS GLU PRO LYS ASN LYS
SEQRES 9 A 306 THR PHE LEU ARG CYS GLU ALA LYS ASN TYR SER GLY ARG
SEQRES 10 A 306 PHE THR CYS TRP TRP LEU THR THR ILE SER THR ASP LEU
SEQRES 11 A 306 THR PHE SER VAL LYS SER SER ARG GLY SER SER ASP PRO
SEQRES 12 A 306 GLN GLY VAL THR CYS GLY ALA ALA THR LEU SER ALA GLU
SEQRES 13 A 306 ARG VAL ARG GLY ASP ASN LYS GLU TYR GLU TYR SER VAL
SEQRES 14 A 306 GLU CYS GLN GLU ASP SER ALA CYS PRO ALA ALA GLU GLU
SEQRES 15 A 306 SER LEU PRO ILE GLU VAL MET VAL ASP ALA VAL HIS LYS
SEQRES 16 A 306 LEU LYS TYR GLU ASN TYR THR SER SER PHE PHE ILE ARG
SEQRES 17 A 306 ASP ILE ILE LYS PRO ASP PRO PRO LYS ASN LEU GLN LEU
SEQRES 18 A 306 LYS PRO LEU LYS ASN SER ARG GLN VAL GLU VAL SER TRP
SEQRES 19 A 306 GLU TYR PRO ASP THR TRP SER THR PRO HIS SER TYR PHE
SEQRES 20 A 306 SER LEU THR PHE CYS VAL GLN VAL GLN GLY LYS SER LYS
SEQRES 21 A 306 ARG GLU LYS LYS ASP ARG VAL PHE THR ASP LYS THR SER
SEQRES 22 A 306 ALA THR VAL ILE CYS ARG LYS ASN ALA SER ILE SER VAL
SEQRES 23 A 306 ARG ALA GLN ASP ARG TYR TYR SER SER SER TRP SER GLU
SEQRES 24 A 306 TRP ALA SER VAL PRO CYS SER
SEQRES 1 B 170 ARG ALA VAL PRO GLY GLY SER SER PRO ALA TRP THR GLN
SEQRES 2 B 170 CYS GLN GLN LEU SER GLN LYS LEU CYS THR LEU ALA TRP
SEQRES 3 B 170 SER ALA HIS PRO LEU VAL GLY HIS MET ASP LEU ARG GLU
SEQRES 4 B 170 GLU GLY ASP GLU GLU THR THR ASN ASP VAL PRO HIS ILE
SEQRES 5 B 170 GLN CYS GLY ASP GLY CYS ASP PRO GLN GLY LEU ARG ASP
SEQRES 6 B 170 ASN SER GLN PHE CYS LEU GLN ARG ILE HIS GLN GLY LEU
SEQRES 7 B 170 ILE PHE TYR GLU LYS LEU LEU GLY SER ASP ILE PHE THR
SEQRES 8 B 170 GLY GLU PRO SER LEU LEU PRO ASP SER PRO VAL GLY GLN
SEQRES 9 B 170 LEU HIS ALA SER LEU LEU GLY LEU SER GLN LEU LEU GLN
SEQRES 10 B 170 PRO GLU GLY HIS HIS TRP GLU THR GLN GLN ILE PRO SER
SEQRES 11 B 170 LEU SER PRO SER GLN PRO TRP GLN ARG LEU LEU LEU ARG
SEQRES 12 B 170 PHE LYS ILE LEU ARG SER LEU GLN ALA PHE VAL ALA VAL
SEQRES 13 B 170 ALA ALA ARG VAL PHE ALA HIS GLY ALA ALA THR LEU SER
SEQRES 14 B 170 PRO
SEQRES 1 D 109 MET GLY VAL SER ASP VAL PRO ARG ASP LEU GLU VAL VAL
SEQRES 2 D 109 ALA ALA THR PRO THR SER LEU LEU ILE SER TRP GLU HIS
SEQRES 3 D 109 ASP TYR PRO TYR ARG ARG TYR TYR ARG ILE THR TYR GLY
SEQRES 4 D 109 GLU THR GLY GLY ASN SER PRO VAL GLN GLU PHE THR VAL
SEQRES 5 D 109 PRO LYS ASP VAL ASP THR ALA THR ILE SER GLY LEU LYS
SEQRES 6 D 109 PRO GLY VAL ASP TYR THR ILE THR VAL TYR ALA VAL THR
SEQRES 7 D 109 SER SER TYR LYS TYR ASP MET GLN TYR SER PRO ILE SER
SEQRES 8 D 109 ILE ASN TYR ARG THR GLU ILE ASP LYS PRO SER GLN HIS
SEQRES 9 D 109 HIS HIS HIS HIS HIS
MODRES 3QWR ASN A 200 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN C6 H12 O6
FORMUL 5 HOH *(H2 O)
HELIX 1 1 PHE A 206 ILE A 211 1 6
HELIX 2 2 ALA B 10 ALA B 28 1 19
HELIX 3 3 GLN B 53 GLY B 57 5 5
HELIX 4 4 ASP B 59 ASN B 66 1 8
HELIX 5 5 ASN B 66 SER B 87 1 22
HELIX 6 6 PRO B 101 GLN B 117 1 17
HELIX 7 7 GLN B 135 LEU B 168 1 34
SHEET 1 A 4 VAL A 8 VAL A 10 0
SHEET 2 A 4 SER A 78 LEU A 81 1 O LEU A 79 N TYR A 9
SHEET 3 A 4 GLY A 64 LYS A 70 -1 N TYR A 66 O SER A 78
SHEET 4 A 4 ILE A 36 LEU A 40 -1 N THR A 37 O HIS A 69
SHEET 1 B 3 LEU A 13 TRP A 15 0
SHEET 2 B 3 LYS A 84 GLU A 86 1 O LYS A 85 N LEU A 13
SHEET 3 B 3 ILE A 89 TRP A 90 -1 O ILE A 89 N GLU A 86
SHEET 1 C 2 MET A 23 THR A 27 0
SHEET 2 C 2 THR A 52 GLN A 56 -1 O LEU A 53 N LEU A 26
SHEET 1 D 4 LEU A 95 LYS A 96 0
SHEET 2 D 4 ARG A 117 THR A 124 -1 O LEU A 123 N LYS A 96
SHEET 3 D 4 TYR A 165 GLU A 173 -1 O TYR A 165 N THR A 124
SHEET 4 D 4 THR A 152 GLU A 156 -1 N SER A 154 O GLU A 166
SHEET 1 E 7 ARG A 108 GLU A 110 0
SHEET 2 E 7 ARG A 117 THR A 124 -1 O TRP A 121 N ARG A 108
SHEET 3 E 7 TYR A 165 GLU A 173 -1 O TYR A 165 N THR A 124
SHEET 4 E 7 GLN A 144 CYS A 148 -1 N THR A 147 O GLN A 172
SHEET 5 E 7 LEU A 130 ARG A 138 -1 N ARG A 138 O GLN A 144
SHEET 6 E 7 ILE A 186 HIS A 194 -1 O MET A 189 N LYS A 135
SHEET 7 E 7 LYS A 197 PHE A 205 -1 O PHE A 205 N ILE A 186
SHEET 1 F 3 LYS A 217 PRO A 223 0
SHEET 2 F 3 VAL A 230 GLU A 235 -1 O GLU A 235 N LYS A 217
SHEET 3 F 3 SER A 273 VAL A 276 -1 O ALA A 274 N VAL A 232
SHEET 1 G 4 ARG A 266 THR A 269 0
SHEET 2 G 4 LEU A 249 VAL A 255 -1 N VAL A 253 O VAL A 267
SHEET 3 G 4 ILE A 284 ASP A 290 -1 O SER A 285 N GLN A 254
SHEET 4 G 4 ALA A 301 VAL A 303 -1 O VAL A 303 N ILE A 284
SHEET 1 H 3 LEU D 8 ALA D 13 0
SHEET 2 H 3 LEU D 18 TRP D 22 -1 O LEU D 19 N ALA D 12
SHEET 3 H 3 THR D 56 ILE D 59 -1 O ALA D 57 N ILE D 20
SHEET 1 I 4 GLN D 46 PRO D 51 0
SHEET 2 I 4 TYR D 31 GLU D 38 -1 N ILE D 34 O PHE D 48
SHEET 3 I 4 TYR D 68 VAL D 75 -1 O THR D 69 N GLY D 37
SHEET 4 I 4 ILE D 88 TYR D 92 -1 O TYR D 92 N TYR D 68
SSBOND 1 CYS A 28 CYS A 68 1555 1555 2.04
SSBOND 2 CYS A 109 CYS A 120 1555 1555 2.07
SSBOND 3 CYS A 148 CYS A 171 1555 1555 2.06
SSBOND 4 CYS A 177 CYS B 54 1555 1555 2.05
SSBOND 5 CYS A 278 CYS A 305 1555 1555 2.04
SSBOND 6 CYS B 58 CYS B 70 1555 1555 2.06
LINK ND2 ASN A 200 C1 NAG C 1 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.42
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.46
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.46
CISPEP 1 PRO A 31 GLU A 32 0 3.98
CISPEP 2 THR A 242 PRO A 243 0 -1.31
CISPEP 3 GLU B 93 PRO B 94 0 -7.41
CRYST1 77.700 91.700 225.800 90.00 90.00 90.00 I 21 21 21 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 0.012870 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010905 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004429 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
