REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.WILLIAMS,N.RUEGG,A.BIRCH,C.WEBER,K.HOFSTADTER, REMARK 1 AUTH 2 J.A.ROBINSON,M.AGUET,G.GAROTTA,D.SCHLATTER,W.HUBER REMARK 1 TITL DISSECTION OF THE EXTRACELLULAR HUMAN INTERFERON REMARK 1 TITL 2 GAMMA RECEPTOR ALPHA-CHAIN INTO TWO REMARK 1 TITL 3 IMMUNOGLOBULIN-LIKE DOMAINS. PRODUCTION IN AN REMARK 1 TITL 4 ESCHERICHIA COLI THIOREDOXIN GENE FUSION REMARK 1 TITL 5 EXPRESSION SYSTEM AND RECOGNITION BY NEUTRALIZING REMARK 1 TITL 6 ANTIBODIES REMARK 1 REF BIOCHEMISTRY V. 34 1787 1995 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.BRIDGES,A.BIRCH,G.WILLIAMS,M.AGUET,D.SCHLATTER, REMARK 1 AUTH 2 W.HUBER,G.GAROTTA,J.A.ROBINSON REMARK 1 TITL VARIABLE REGION CDNA SEQUENCES AND REMARK 1 TITL 2 CHARACTERIZATION OF MURINE ANTI-HUMAN INTERFERON REMARK 1 TITL 3 GAMMA RECEPTOR MONOCLONAL ANTIBODIES THAT INHIBIT REMARK 1 TITL 4 RECEPTOR BINDING BY INTERFERON GAMMA REMARK 1 REF MOL.IMMUNOL. V. 32 1329 1995 REMARK 1 REFN ISSN 0161-5890 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 19997 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.246 REMARK 3 FREE R VALUE : 0.314 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 954 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 : 10 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1793 REMARK 3 BIN R VALUE (WORKING SET) : 0.3220 REMARK 3 BIN FREE R VALUE : 0.3990 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 99 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 : 3454 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 30 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 58.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.10 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) : 0.40 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) : 0.011 REMARK 3 BOND ANGLES (DEGREES) : 1.85 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) : 2.000 ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.000 ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : 4.500 ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : 20.000; 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 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ATOMS WITH B-FACTORS > 80 A**2 MUST REMARK 3 BE CONSIDERED DISORDERED. REMARK 4 REMARK 4 1JRH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : FEB-96 REMARK 200 TEMPERATURE (KELVIN) : 120 REMARK 200 PH : 5.5 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 : ENRAF-NONIUS FR591 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARXDS REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19997 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.05900 REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.82 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.28800 REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.1 REMARK 200 STARTING MODEL: PDB ENTRIES 1BBJ, 1BBC, AND 2HFL REMARK 200 REMARK 200 REMARK: FOR FV_HEAVY AND FV_LIGHT, 1BBJ AND 1BBC, RESPECTIVELY. REMARK 200 FOR FC, 2HFL. THESE ARE COMBINED AND OPTIMIZED. <I/SIGMA(I)& REMARK 200 GT FOR THE DATA SET : 29.7 <I/SIGMA(I)> FOR SHELL : 5.9 REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10%(W/V) PEG ME 5000, 0.5M NACL, REMARK 280 50MM BIS/TRIS, PH 5.5 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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 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 42.87000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.79000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.40000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.79000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.87000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.40000 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3870 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 22390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I 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 PRO L 120 REMARK 465 SER L 121 REMARK 465 SER L 122 REMARK 465 GLU L 123 REMARK 465 GLN L 124 REMARK 465 LEU L 125 REMARK 465 THR L 126 REMARK 465 SER L 127 REMARK 465 GLY L 128 REMARK 465 GLY L 129 REMARK 465 ALA L 130 REMARK 465 SER L 131 REMARK 465 VAL L 132 REMARK 465 VAL L 133 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 ILE L 150 REMARK 465 ASP L 151 REMARK 465 GLY L 152 REMARK 465 SER L 153 REMARK 465 GLU L 154 REMARK 465 ARG L 155 REMARK 465 GLN L 156 REMARK 465 ASN L 157 REMARK 465 THR L 178 REMARK 465 LEU L 179 REMARK 465 THR L 180 REMARK 465 LEU L 181 REMARK 465 THR L 182 REMARK 465 LYS L 183 REMARK 465 ASP L 184 REMARK 465 GLU L 185 REMARK 465 TYR L 186 REMARK 465 GLU L 187 REMARK 465 ARG L 188 REMARK 465 HIS L 189 REMARK 465 ASN L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 SER L 208 REMARK 465 PHE L 209 REMARK 465 ASN L 210 REMARK 465 ARG L 211 REMARK 465 ASN L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 PRO H 121 REMARK 465 SER H 122 REMARK 465 VAL H 123 REMARK 465 TYR H 124 REMARK 465 PRO H 125 REMARK 465 LEU H 126 REMARK 465 ALA H 127 REMARK 465 PRO H 128 REMARK 465 GLY H 129 REMARK 465 SER H 130 REMARK 465 ALA H 131 REMARK 465 ALA H 132 REMARK 465 GLN H 133 REMARK 465 THR H 134 REMARK 465 ASN H 135 REMARK 465 SER H 136 REMARK 465 MET H 137 REMARK 465 VAL H 138 REMARK 465 THR H 139 REMARK 465 LEU H 140 REMARK 465 GLY H 141 REMARK 465 LYS H 145 REMARK 465 GLY H 146 REMARK 465 SER H 164 REMARK 465 LEU H 165 REMARK 465 VAL H 196 REMARK 465 PRO H 197 REMARK 465 SER H 198 REMARK 465 SER H 199 REMARK 465 PRO H 200 REMARK 465 ARG H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 GLU H 204 REMARK 465 THR H 205 REMARK 465 VAL H 206 REMARK 465 THR H 207 REMARK 465 LYS H 222 REMARK 465 ILE H 223 REMARK 465 GLU I 1 REMARK 465 MET I 2 REMARK 465 GLY I 3 REMARK 465 THR I 4 REMARK 465 ALA I 5 REMARK 465 ASP I 6 REMARK 465 LEU I 7 REMARK 465 GLY I 8 REMARK 465 PRO I 9 REMARK 465 SER I 10 REMARK 465 ARG I 106 REMARK 465 ASP I 107 REMARK 465 GLY I 108 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 SER I 11 OG REMARK 480 VAL I 89 CG1 CG2 REMARK 480 GLN I 91 CG CD OE1 NE2 REMARK 480 LYS I 92 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 PRO L 8 -155.39 -104.35 REMARK 500 TYR L 30 53.24 34.68 REMARK 500 ASN L 31 16.84 58.82 REMARK 500 ALA L 51 -39.02 62.75 REMARK 500 GLU L 57 -22.05 85.87 REMARK 500 SER L 67 165.37 178.88 REMARK 500 THR L 94 -137.47 54.27 REMARK 500 PRO L 141 -172.03 -65.72 REMARK 500 ILE L 144 146.12 -172.08 REMARK 500 SER L 171 62.31 -50.56 REMARK 500 LYS L 199 9.45 -65.99 REMARK 500 SER L 201 -159.43 -156.97 REMARK 500 THR L 202 -34.79 -143.82 REMARK 500 SER H 15 -9.61 67.06 REMARK 500 GLN H 16 -164.92 -75.65 REMARK 500 LEU H 48 -70.68 -97.83 REMARK 500 SER H 82B 46.73 39.62 REMARK 500 ALA H 88 -172.68 -171.84 REMARK 500 PRO H 97 35.73 -65.59 REMARK 500 ALA H 114 -147.07 -137.84 REMARK 500 LYS H 115 143.23 -170.59 REMARK 500 THR H 116 75.77 -49.15 REMARK 500 PHE H 148 142.67 -174.09 REMARK 500 SER H 162 24.89 49.50 REMARK 500 GLN H 179 -127.92 -80.96 REMARK 500 HIS H 212 77.78 -169.16 REMARK 500 SER H 216 28.13 38.78 REMARK 500 LYS H 218 67.84 -159.02 REMARK 500 ASP H 220 28.43 -79.54 REMARK 500 SER I 22 92.21 -161.27 REMARK 500 ASN I 24 -165.28 70.90 REMARK 500 MET I 25 52.16 -98.83 REMARK 500 ASN I 53 73.95 -154.05 REMARK 500 ASN I 62 76.75 26.05 REMARK 500 HIS I 66 45.84 -91.68 REMARK 500 CYS I 68 117.68 -161.09 REMARK 500 ASP I 76 92.27 68.84 REMARK 500 ALA I 103 -75.83 -114.53 REMARK 500 REMARK 500 REMARK: NULL