HEADER IMMUNE SYSTEM 13-MAY-02 1LQS
TITLE CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO SOLUBLE
TITLE 2 HUMAN IL-10R1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-10 RECEPTOR ALPHA CHAIN;
COMPND 3 CHAIN: R, S;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 22-235;
COMPND 5 SYNONYM: IL-10R-A, IL-10R1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: INTERLEUKIN-10-LIKE PROTEIN;
COMPND 10 CHAIN: L, M;
COMPND 11 FRAGMENT: RESIDUES 20-176;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMTV5HIS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 5;
SOURCE 12 ORGANISM_COMMON: HUMAN CYTOMEGALOVIRUS;
SOURCE 13 ORGANISM_TAXID: 10359;
SOURCE 14 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7227;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PMTV5HIS
KEYWDS INTERLEUKIN 10, HELIX BUNDLE, RECEPTOR COMPLEX, MOLECULAR
KEYWDS 2 RECOGNITION, STRUCTURE MIMIC, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR B.C.JONES,N.J.LOGSDON,K.JOSEPHSON,J.COOK,P.A.BARRY,M.R.WALTER
REVDAT 3 13-JUL-11 1LQS 1 VERSN
REVDAT 2 24-FEB-09 1LQS 1 VERSN
REVDAT 1 17-JUL-02 1LQS 0
JRNL AUTH B.C.JONES,N.J.LOGSDON,K.JOSEPHSON,J.COOK,P.A.BARRY,
JRNL AUTH 2 M.R.WALTER
JRNL TITL CRYSTAL STRUCTURE OF HUMAN CYTOMEGALOVIRUS IL-10 BOUND TO
JRNL TITL 2 SOLUBLE HUMAN IL-10R1.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 9404 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 12093920
JRNL DOI 10.1073/PNAS.152147499
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 26049
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1322
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.80
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 0.67
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE : 0.4260
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 101
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 : 5623
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 48
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LQS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-02.
REMARK 100 THE RCSB ID CODE IS RCSB016194.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26049
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.19500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1J7V
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-6000, 0.1M MGCL2, 100MM ADA, 0.75%
REMARK 280 PEG-400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 57.14500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.34000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.14500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.34000
REMARK 290 SMTRY3 4 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 APPLY THE FOLLOWING TO CHAINS: R, S, L, M
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 HIS R 1
REMARK 465 TYR R 209
REMARK 465 PHE R 210
REMARK 465 THR R 211
REMARK 465 VAL R 212
REMARK 465 THR R 213
REMARK 465 ASN R 214
REMARK 465 HIS S 1
REMARK 465 GLN S 208
REMARK 465 TYR S 209
REMARK 465 PHE S 210
REMARK 465 THR S 211
REMARK 465 VAL S 212
REMARK 465 THR S 213
REMARK 465 ASN S 214
REMARK 465 SER L -6
REMARK 465 GLU L -5
REMARK 465 GLU L -4
REMARK 465 ALA L -3
REMARK 465 LYS L -2
REMARK 465 PRO L -1
REMARK 465 ALA L 0
REMARK 465 THR L 1
REMARK 465 THR L 2
REMARK 465 THR L 3
REMARK 465 THR L 4
REMARK 465 ILE L 5
REMARK 465 LYS L 6
REMARK 465 ASN L 7
REMARK 465 LYS L 158
REMARK 465 SER M -6
REMARK 465 GLU M -5
REMARK 465 GLU M -4
REMARK 465 ALA M -3
REMARK 465 LYS M -2
REMARK 465 PRO M -1
REMARK 465 ALA M 0
REMARK 465 THR M 1
REMARK 465 THR M 2
REMARK 465 THR M 3
REMARK 465 THR M 4
REMARK 465 ILE M 5
REMARK 465 LYS M 6
REMARK 465 ASN M 7
REMARK 465 LYS M 158
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 R 207 CG CD NE CZ NH1 NH2
REMARK 470 GLN R 208 CG CD OE1 NE2
REMARK 470 ARG S 207 CG CD NE CZ NH1 NH2
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 ASP L 43 N - CA - C ANGL. DEV. = -18.7 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 THR R 3 75.73 71.44
REMARK 500 PHE R 17 109.35 -47.23
REMARK 500 HIS R 19 75.35 -150.03
REMARK 500 GLU R 46 80.36 -59.24
REMARK 500 ASP R 68 31.57 -95.07
REMARK 500 HIS R 71 20.41 -142.21
REMARK 500 SER R 72 -167.62 -125.00
REMARK 500 ASN R 115 62.04 35.78
REMARK 500 ALA R 132 -68.05 -14.96
REMARK 500 ASP R 134 66.45 -107.40
REMARK 500 PHE R 140 70.94 -105.65
REMARK 500 PRO R 154 17.98 -69.12
REMARK 500 GLN R 156 -161.27 -178.82
REMARK 500 PHE R 157 38.32 -96.05
REMARK 500 LYS R 162 113.35 -168.04
REMARK 500 SER R 174 86.12 -52.47
REMARK 500 ALA R 189 -26.20 -38.17
REMARK 500 ARG R 207 -14.64 -43.07
REMARK 500 PHE S 17 107.90 -48.34
REMARK 500 HIS S 19 79.37 -150.68
REMARK 500 GLU S 46 82.55 -60.73
REMARK 500 ASP S 68 33.16 -95.40
REMARK 500 HIS S 71 25.26 -143.51
REMARK 500 SER S 72 -167.01 -128.99
REMARK 500 ASN S 115 62.09 35.84
REMARK 500 ALA S 132 -67.79 -18.85
REMARK 500 ASP S 134 68.27 -109.84
REMARK 500 PHE S 140 70.65 -106.42
REMARK 500 PRO S 154 16.03 -68.85
REMARK 500 GLN S 156 -158.85 -178.38
REMARK 500 PHE S 157 38.01 -98.80
REMARK 500 LYS S 162 113.92 -170.96
REMARK 500 THR S 173 57.59 -94.13
REMARK 500 SER S 174 86.58 -49.18
REMARK 500 ALA S 189 -36.02 -31.37
REMARK 500 LEU S 205 -88.34 -72.22
REMARK 500 THR S 206 -169.14 -109.04
REMARK 500 GLN L 11 13.95 -66.76
REMARK 500 ASP L 42 98.20 32.18
REMARK 500 TYR L 44 39.61 -93.42
REMARK 500 TRP L 47 -62.70 -98.45
REMARK 500 ASP L 49 -165.20 -71.33
REMARK 500 VAL L 52 -41.51 -22.94
REMARK 500 GLN M 11 -12.24 -48.53
REMARK 500 GLU M 41 172.55 -48.79
REMARK 500 VAL M 52 -30.96 -37.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAG L 201
REMARK 610 NAG M 202
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG L 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG M 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J7V RELATED DB: PDB
REMARK 900 HUMAN IL-10 / IL-10R1 COMPLEX
DBREF 1LQS R 1 214 UNP Q13651 I10R1_HUMAN 22 235
DBREF 1LQS S 1 214 UNP Q13651 I10R1_HUMAN 22 235
DBREF 1LQS L -6 150 UNP P17150 IL10H_HCMVA 27 175
DBREF 1LQS M -6 150 UNP P17150 IL10H_HCMVA 27 175
SEQADV 1LQS GLN R 29 UNP Q13651 ASN 50 ENGINEERED
SEQADV 1LQS GLN R 53 UNP Q13651 ASN 74 ENGINEERED
SEQADV 1LQS GLN R 89 UNP Q13651 ASN 110 ENGINEERED
SEQADV 1LQS GLN R 133 UNP Q13651 ASN 154 ENGINEERED
SEQADV 1LQS GLN R 156 UNP Q13651 ASN 177 ENGINEERED
SEQADV 1LQS GLN R 168 UNP Q13651 ASN 189 ENGINEERED
SEQADV 1LQS GLN S 29 UNP Q13651 ASN 50 ENGINEERED
SEQADV 1LQS GLN S 53 UNP Q13651 ASN 74 ENGINEERED
SEQADV 1LQS GLN S 89 UNP Q13651 ASN 110 ENGINEERED
SEQADV 1LQS GLN S 133 UNP Q13651 ASN 154 ENGINEERED
SEQADV 1LQS GLN S 156 UNP Q13651 ASN 177 ENGINEERED
SEQADV 1LQS GLN S 168 UNP Q13651 ASN 189 ENGINEERED
SEQRES 1 R 214 HIS GLY THR GLU LEU PRO SER PRO PRO SER VAL TRP PHE
SEQRES 2 R 214 GLU ALA GLU PHE PHE HIS HIS ILE LEU HIS TRP THR PRO
SEQRES 3 R 214 ILE PRO GLN GLN SER GLU SER THR CYS TYR GLU VAL ALA
SEQRES 4 R 214 LEU LEU ARG TYR GLY ILE GLU SER TRP ASN SER ILE SER
SEQRES 5 R 214 GLN CYS SER GLN THR LEU SER TYR ASP LEU THR ALA VAL
SEQRES 6 R 214 THR LEU ASP LEU TYR HIS SER ASN GLY TYR ARG ALA ARG
SEQRES 7 R 214 VAL ARG ALA VAL ASP GLY SER ARG HIS SER GLN TRP THR
SEQRES 8 R 214 VAL THR ASN THR ARG PHE SER VAL ASP GLU VAL THR LEU
SEQRES 9 R 214 THR VAL GLY SER VAL ASN LEU GLU ILE HIS ASN GLY PHE
SEQRES 10 R 214 ILE LEU GLY LYS ILE GLN LEU PRO ARG PRO LYS MET ALA
SEQRES 11 R 214 PRO ALA GLN ASP THR TYR GLU SER ILE PHE SER HIS PHE
SEQRES 12 R 214 ARG GLU TYR GLU ILE ALA ILE ARG LYS VAL PRO GLY GLN
SEQRES 13 R 214 PHE THR PHE THR HIS LYS LYS VAL LYS HIS GLU GLN PHE
SEQRES 14 R 214 SER LEU LEU THR SER GLY GLU VAL GLY GLU PHE CYS VAL
SEQRES 15 R 214 GLN VAL LYS PRO SER VAL ALA SER ARG SER ASN LYS GLY
SEQRES 16 R 214 MET TRP SER LYS GLU GLU CYS ILE SER LEU THR ARG GLN
SEQRES 17 R 214 TYR PHE THR VAL THR ASN
SEQRES 1 S 214 HIS GLY THR GLU LEU PRO SER PRO PRO SER VAL TRP PHE
SEQRES 2 S 214 GLU ALA GLU PHE PHE HIS HIS ILE LEU HIS TRP THR PRO
SEQRES 3 S 214 ILE PRO GLN GLN SER GLU SER THR CYS TYR GLU VAL ALA
SEQRES 4 S 214 LEU LEU ARG TYR GLY ILE GLU SER TRP ASN SER ILE SER
SEQRES 5 S 214 GLN CYS SER GLN THR LEU SER TYR ASP LEU THR ALA VAL
SEQRES 6 S 214 THR LEU ASP LEU TYR HIS SER ASN GLY TYR ARG ALA ARG
SEQRES 7 S 214 VAL ARG ALA VAL ASP GLY SER ARG HIS SER GLN TRP THR
SEQRES 8 S 214 VAL THR ASN THR ARG PHE SER VAL ASP GLU VAL THR LEU
SEQRES 9 S 214 THR VAL GLY SER VAL ASN LEU GLU ILE HIS ASN GLY PHE
SEQRES 10 S 214 ILE LEU GLY LYS ILE GLN LEU PRO ARG PRO LYS MET ALA
SEQRES 11 S 214 PRO ALA GLN ASP THR TYR GLU SER ILE PHE SER HIS PHE
SEQRES 12 S 214 ARG GLU TYR GLU ILE ALA ILE ARG LYS VAL PRO GLY GLN
SEQRES 13 S 214 PHE THR PHE THR HIS LYS LYS VAL LYS HIS GLU GLN PHE
SEQRES 14 S 214 SER LEU LEU THR SER GLY GLU VAL GLY GLU PHE CYS VAL
SEQRES 15 S 214 GLN VAL LYS PRO SER VAL ALA SER ARG SER ASN LYS GLY
SEQRES 16 S 214 MET TRP SER LYS GLU GLU CYS ILE SER LEU THR ARG GLN
SEQRES 17 S 214 TYR PHE THR VAL THR ASN
SEQRES 1 L 157 SER GLU GLU ALA LYS PRO ALA THR THR THR THR ILE LYS
SEQRES 2 L 157 ASN THR LYS PRO GLN CYS ARG PRO GLU ASP TYR ALA THR
SEQRES 3 L 157 ARG LEU GLN ASP LEU ARG VAL THR PHE HIS ARG VAL LYS
SEQRES 4 L 157 PRO THR LEU GLN ARG GLU ASP ASP TYR SER VAL TRP LEU
SEQRES 5 L 157 ASP GLY THR VAL VAL LYS GLY CYS TRP GLY CYS SER VAL
SEQRES 6 L 157 MET ASP TRP LEU LEU ARG ARG TYR LEU GLU ILE VAL PHE
SEQRES 7 L 157 PRO ALA GLY ASP HIS VAL TYR PRO GLY LEU LYS THR GLU
SEQRES 8 L 157 LEU HIS SER MET ARG SER THR LEU GLU SER ILE TYR LYS
SEQRES 9 L 157 ASP MET ARG GLN CYS PRO LEU LEU GLY CYS GLY ASP LYS
SEQRES 10 L 157 SER VAL ILE SER ARG LEU SER GLN GLU ALA GLU ARG LYS
SEQRES 11 L 157 SER ASP ASN GLY THR ARG LYS GLY LEU SER GLU LEU ASP
SEQRES 12 L 157 THR LEU PHE SER ARG LEU GLU GLU TYR LEU HIS SER ARG
SEQRES 13 L 157 LYS
SEQRES 1 M 157 SER GLU GLU ALA LYS PRO ALA THR THR THR THR ILE LYS
SEQRES 2 M 157 ASN THR LYS PRO GLN CYS ARG PRO GLU ASP TYR ALA THR
SEQRES 3 M 157 ARG LEU GLN ASP LEU ARG VAL THR PHE HIS ARG VAL LYS
SEQRES 4 M 157 PRO THR LEU GLN ARG GLU ASP ASP TYR SER VAL TRP LEU
SEQRES 5 M 157 ASP GLY THR VAL VAL LYS GLY CYS TRP GLY CYS SER VAL
SEQRES 6 M 157 MET ASP TRP LEU LEU ARG ARG TYR LEU GLU ILE VAL PHE
SEQRES 7 M 157 PRO ALA GLY ASP HIS VAL TYR PRO GLY LEU LYS THR GLU
SEQRES 8 M 157 LEU HIS SER MET ARG SER THR LEU GLU SER ILE TYR LYS
SEQRES 9 M 157 ASP MET ARG GLN CYS PRO LEU LEU GLY CYS GLY ASP LYS
SEQRES 10 M 157 SER VAL ILE SER ARG LEU SER GLN GLU ALA GLU ARG LYS
SEQRES 11 M 157 SER ASP ASN GLY THR ARG LYS GLY LEU SER GLU LEU ASP
SEQRES 12 M 157 THR LEU PHE SER ARG LEU GLU GLU TYR LEU HIS SER ARG
SEQRES 13 M 157 LYS
HET NAG L 201 14
HET NAG M 202 14
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 7 HOH *48(H2 O)
HELIX 1 1 THR R 63 THR R 66 5 4
HELIX 2 2 ASP R 68 SER R 72 5 5
HELIX 3 3 SER R 98 ASP R 100 5 3
HELIX 4 4 THR R 135 PHE R 140 1 6
HELIX 5 5 THR S 63 SER S 72 5 10
HELIX 6 6 SER S 98 ASP S 100 5 3
HELIX 7 7 THR S 135 PHE S 140 1 6
HELIX 8 8 LYS L 9 ASP L 18 5 8
HELIX 9 9 TYR L 19 GLN L 38 1 20
HELIX 10 10 TRP L 60 ILE L 75 1 16
HELIX 11 11 ILE L 75 TYR L 84 1 10
HELIX 12 12 LEU L 87 ARG L 106 1 20
HELIX 13 13 GLN L 107 GLY L 112 5 6
HELIX 14 14 GLY L 116 ALA L 128 1 13
HELIX 15 15 GLY L 135 GLU L 142 1 8
HELIX 16 16 GLU L 142 ARG L 157 1 16
HELIX 17 17 LYS M 9 ASP M 18 5 8
HELIX 18 18 TYR M 19 GLN M 38 1 20
HELIX 19 19 TRP M 60 ILE M 75 1 16
HELIX 20 20 ILE M 75 HIS M 82 1 8
HELIX 21 21 VAL M 83 VAL M 83 5 1
HELIX 22 22 TYR M 84 GLY M 86 5 3
HELIX 23 23 LEU M 87 GLN M 107 1 21
HELIX 24 24 CYS M 108 GLY M 112 5 5
HELIX 25 25 ASP M 117 ARG M 130 1 14
HELIX 26 26 GLY M 135 GLU M 142 1 8
HELIX 27 27 GLU M 142 ARG M 157 1 16
SHEET 1 A 4 SER R 59 ASP R 61 0
SHEET 2 A 4 HIS R 19 TRP R 24 -1 N LEU R 22 O TYR R 60
SHEET 3 A 4 VAL R 11 GLU R 16 -1 N TRP R 12 O HIS R 23
SHEET 4 A 4 VAL R 102 THR R 103 1 O THR R 103 N ALA R 15
SHEET 1 B 4 TRP R 48 SER R 55 0
SHEET 2 B 4 CYS R 35 ARG R 42 -1 N VAL R 38 O ILE R 51
SHEET 3 B 4 TYR R 75 ASP R 83 -1 O ARG R 76 N LEU R 41
SHEET 4 B 4 ARG R 86 HIS R 87 -1 O ARG R 86 N ASP R 83
SHEET 1 C 4 TRP R 48 SER R 55 0
SHEET 2 C 4 CYS R 35 ARG R 42 -1 N VAL R 38 O ILE R 51
SHEET 3 C 4 TYR R 75 ASP R 83 -1 O ARG R 76 N LEU R 41
SHEET 4 C 4 THR R 91 VAL R 92 -1 O THR R 91 N VAL R 79
SHEET 1 D 3 SER R 108 HIS R 114 0
SHEET 2 D 3 PHE R 117 GLN R 123 -1 O GLN R 123 N SER R 108
SHEET 3 D 3 GLN R 168 LEU R 172 -1 O PHE R 169 N GLY R 120
SHEET 1 E 4 THR R 160 VAL R 164 0
SHEET 2 E 4 ARG R 144 LYS R 152 -1 N TYR R 146 O VAL R 164
SHEET 3 E 4 GLU R 179 VAL R 188 -1 O SER R 187 N GLU R 145
SHEET 4 E 4 GLU R 201 SER R 204 -1 O GLU R 201 N VAL R 182
SHEET 1 F 4 SER S 59 ASP S 61 0
SHEET 2 F 4 HIS S 19 TRP S 24 -1 N LEU S 22 O TYR S 60
SHEET 3 F 4 VAL S 11 GLU S 16 -1 N TRP S 12 O HIS S 23
SHEET 4 F 4 VAL S 102 THR S 103 1 O THR S 103 N ALA S 15
SHEET 1 G 4 ASN S 49 SER S 55 0
SHEET 2 G 4 CYS S 35 ARG S 42 -1 N VAL S 38 O ILE S 51
SHEET 3 G 4 TYR S 75 ASP S 83 -1 O ARG S 80 N GLU S 37
SHEET 4 G 4 ARG S 86 HIS S 87 -1 O ARG S 86 N ASP S 83
SHEET 1 H 4 ASN S 49 SER S 55 0
SHEET 2 H 4 CYS S 35 ARG S 42 -1 N VAL S 38 O ILE S 51
SHEET 3 H 4 TYR S 75 ASP S 83 -1 O ARG S 80 N GLU S 37
SHEET 4 H 4 THR S 91 VAL S 92 -1 O THR S 91 N VAL S 79
SHEET 1 I 3 SER S 108 HIS S 114 0
SHEET 2 I 3 PHE S 117 GLN S 123 -1 O GLN S 123 N SER S 108
SHEET 3 I 3 GLN S 168 LEU S 172 -1 O PHE S 169 N GLY S 120
SHEET 1 J 4 THR S 160 VAL S 164 0
SHEET 2 J 4 ARG S 144 LYS S 152 -1 N TYR S 146 O VAL S 164
SHEET 3 J 4 GLU S 179 VAL S 188 -1 O SER S 187 N GLU S 145
SHEET 4 J 4 GLU S 201 SER S 204 -1 O GLU S 201 N VAL S 182
SSBOND 1 CYS R 35 CYS R 54 1555 1555 2.03
SSBOND 2 CYS R 181 CYS R 202 1555 1555 2.04
SSBOND 3 CYS S 35 CYS S 54 1555 1555 2.03
SSBOND 4 CYS S 181 CYS S 202 1555 1555 2.03
SSBOND 5 CYS L 12 CYS L 108 1555 1555 2.03
SSBOND 6 CYS L 59 CYS M 59 1555 1555 2.02
SSBOND 7 CYS L 62 CYS L 114 1555 1555 2.03
SSBOND 8 CYS M 12 CYS M 108 1555 1555 2.04
SSBOND 9 CYS M 62 CYS M 114 1555 1555 2.04
SITE 1 AC1 1 ASN L 134
SITE 1 AC2 2 GLU M 129 ASN M 134
CRYST1 114.290 104.680 91.890 90.00 106.49 90.00 C 1 2 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 0.008750 0.000000 0.002590 0.00000
SCALE2 0.000000 0.009553 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011349 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
