HEADER IMMUNE SYSTEM 06-DEC-21 7W7Q TITLE CRYSTAL STRUCTURE OF 1F11S ANTIBODY(SCFV) COMPND MOL_ID: 1; COMPND 2 MOLECULE: 1F11S ANTIBODY; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, SCFV, IFNGAMMA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR B.-W.KIM,J.PARK,J.WOO,W.-K.LEE REVDAT 1 07-DEC-22 7W7Q 0 JRNL AUTH B.-W.KIM,J.WOO JRNL TITL CRYSTAL STRUCTURE OF 1F11S ANTIBODY(SCFV) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.68 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 3 NUMBER OF REFLECTIONS : 32150 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.277 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 1610 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 28.6800 - 4.3500 0.98 2869 152 0.1712 0.2029 REMARK 3 2 4.3500 - 3.4600 0.98 2811 148 0.1673 0.2228 REMARK 3 3 3.4600 - 3.0200 0.99 2840 150 0.2048 0.2754 REMARK 3 4 3.0200 - 2.7500 0.98 2778 147 0.2241 0.2631 REMARK 3 5 2.7500 - 2.5500 0.98 2827 149 0.2485 0.3645 REMARK 3 6 2.5500 - 2.4000 0.97 2751 144 0.2876 0.3536 REMARK 3 7 2.4000 - 2.2800 0.97 2737 143 0.3154 0.4477 REMARK 3 8 2.2800 - 2.1800 0.97 2741 147 0.3494 0.3504 REMARK 3 9 2.1800 - 2.1000 0.96 2737 144 0.3926 0.4372 REMARK 3 10 2.1000 - 2.0200 0.97 2717 144 0.4329 0.4833 REMARK 3 11 2.0200 - 1.9600 0.95 2732 142 0.4680 0.5025 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.200 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.99 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.19 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 111 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.0072 21.0812 38.4975 REMARK 3 T TENSOR REMARK 3 T11: 0.3390 T22: 0.4178 REMARK 3 T33: 0.4022 T12: -0.0145 REMARK 3 T13: 0.0118 T23: -0.0239 REMARK 3 L TENSOR REMARK 3 L11: 1.5062 L22: 5.8857 REMARK 3 L33: 4.0252 L12: 0.7012 REMARK 3 L13: -0.8487 L23: -1.9830 REMARK 3 S TENSOR REMARK 3 S11: 0.0736 S12: 0.0514 S13: 0.0633 REMARK 3 S21: -0.1926 S22: -0.0453 S23: -0.0757 REMARK 3 S31: -0.0763 S32: -0.0308 S33: -0.0038 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 112 THROUGH 145 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.3357 24.7041 26.1986 REMARK 3 T TENSOR REMARK 3 T11: 0.3715 T22: 0.6171 REMARK 3 T33: 0.5677 T12: -0.0107 REMARK 3 T13: -0.0720 T23: 0.0449 REMARK 3 L TENSOR REMARK 3 L11: 1.2088 L22: 3.6943 REMARK 3 L33: 2.8202 L12: -1.0273 REMARK 3 L13: -1.3461 L23: 0.5257 REMARK 3 S TENSOR REMARK 3 S11: 0.0896 S12: 0.0072 S13: 0.4288 REMARK 3 S21: 0.0860 S22: 0.0230 S23: -0.2471 REMARK 3 S31: 0.1422 S32: -0.0610 S33: -0.0745 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 146 THROUGH 226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.4670 9.5160 19.7759 REMARK 3 T TENSOR REMARK 3 T11: 0.4966 T22: 0.3874 REMARK 3 T33: 0.3808 T12: -0.0022 REMARK 3 T13: 0.0480 T23: -0.0192 REMARK 3 L TENSOR REMARK 3 L11: 3.6002 L22: 5.4403 REMARK 3 L33: 8.3976 L12: -0.5372 REMARK 3 L13: -1.1881 L23: 0.2885 REMARK 3 S TENSOR REMARK 3 S11: -0.1732 S12: 0.1701 S13: -0.3202 REMARK 3 S21: -0.3224 S22: -0.0801 S23: 0.0736 REMARK 3 S31: 0.6799 S32: -0.4170 S33: 0.2293 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 43 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.7460 22.9713 20.7676 REMARK 3 T TENSOR REMARK 3 T11: 0.4743 T22: 0.4614 REMARK 3 T33: 0.4178 T12: 0.0414 REMARK 3 T13: -0.0401 T23: 0.0205 REMARK 3 L TENSOR REMARK 3 L11: 3.3697 L22: 3.2230 REMARK 3 L33: 2.0908 L12: 0.1404 REMARK 3 L13: 0.0596 L23: -0.5739 REMARK 3 S TENSOR REMARK 3 S11: -0.0444 S12: 0.0294 S13: 0.0178 REMARK 3 S21: -0.0599 S22: -0.1158 S23: -0.0020 REMARK 3 S31: -0.1460 S32: -0.1690 S33: 0.1863 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 44 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.1316 17.6701 26.3357 REMARK 3 T TENSOR REMARK 3 T11: 0.3791 T22: 0.4300 REMARK 3 T33: 0.4336 T12: 0.0714 REMARK 3 T13: -0.0214 T23: 0.0096 REMARK 3 L TENSOR REMARK 3 L11: 2.2536 L22: 2.8792 REMARK 3 L33: 4.8770 L12: 1.9235 REMARK 3 L13: -0.8834 L23: -0.1111 REMARK 3 S TENSOR REMARK 3 S11: -0.0983 S12: -0.4696 S13: -0.1021 REMARK 3 S21: 0.2378 S22: -0.0047 S23: -0.1085 REMARK 3 S31: 0.2424 S32: 0.5071 S33: 0.1097 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 138 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.9971 20.0570 16.8210 REMARK 3 T TENSOR REMARK 3 T11: 0.6806 T22: 0.5550 REMARK 3 T33: 0.5428 T12: -0.0091 REMARK 3 T13: 0.0673 T23: 0.0574 REMARK 3 L TENSOR REMARK 3 L11: 0.5690 L22: 0.5805 REMARK 3 L33: 1.3528 L12: -0.3656 REMARK 3 L13: -0.0530 L23: 0.6491 REMARK 3 S TENSOR REMARK 3 S11: -0.0481 S12: -0.2307 S13: -0.1694 REMARK 3 S21: -0.0560 S22: -0.0537 S23: 0.0183 REMARK 3 S31: 0.1746 S32: 0.0026 S33: 0.0273 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 139 THROUGH 195 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.6234 11.4396 1.6803 REMARK 3 T TENSOR REMARK 3 T11: 0.9216 T22: 0.5738 REMARK 3 T33: 0.5050 T12: 0.0632 REMARK 3 T13: 0.0421 T23: -0.0438 REMARK 3 L TENSOR REMARK 3 L11: 1.9025 L22: 2.1384 REMARK 3 L33: 3.1094 L12: 0.0433 REMARK 3 L13: -0.8487 L23: -0.1612 REMARK 3 S TENSOR REMARK 3 S11: 0.0088 S12: 0.1881 S13: -0.1185 REMARK 3 S21: 0.1823 S22: -0.0259 S23: 0.1926 REMARK 3 S31: 0.2173 S32: -0.4157 S33: -0.0045 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 196 THROUGH 226 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.2063 12.1029 -2.0332 REMARK 3 T TENSOR REMARK 3 T11: 0.9510 T22: 0.6638 REMARK 3 T33: 0.4784 T12: 0.0495 REMARK 3 T13: 0.1629 T23: -0.0326 REMARK 3 L TENSOR REMARK 3 L11: 2.3047 L22: 1.6062 REMARK 3 L33: 4.0548 L12: -0.2031 REMARK 3 L13: 0.4608 L23: -0.4963 REMARK 3 S TENSOR REMARK 3 S11: 0.1743 S12: 0.1769 S13: -0.2000 REMARK 3 S21: -0.0764 S22: 0.0935 S23: 0.2083 REMARK 3 S31: 0.0068 S32: -0.6407 S33: -0.1001 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 1 REMARK 3 NCS GROUP : 1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESID 2 THROUGH 101 OR REMARK 3 (RESID 104 THROUGH 107 AND (NAME N OR REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB )) REMARK 3 OR RESID 108 THROUGH 112 OR (RESID 113 REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME REMARK 3 O OR NAME CB )) OR RESID 114 THROUGH 138 REMARK 3 OR (RESID 139 AND (NAME N OR NAME CA OR REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID REMARK 3 140 THROUGH 159 OR (RESID 160 THROUGH 161 REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME REMARK 3 O OR NAME CB )) OR RESID 162 THROUGH 187 REMARK 3 OR (RESID 188 THROUGH 189 AND (NAME N OR REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB )) REMARK 3 OR RESID 190 THROUGH 192 OR RESID 194 REMARK 3 THROUGH 235 OR (RESID 236 AND (NAME N OR REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB )) REMARK 3 OR RESID 237 THROUGH 243)) REMARK 3 SELECTION : (CHAIN B AND (RESID 2 THROUGH 10 OR REMARK 3 (RESID 11 AND (NAME N OR NAME CA OR NAME REMARK 3 C OR NAME O OR NAME CB )) OR RESID 12 OR REMARK 3 (RESID 13 AND (NAME N OR NAME CA OR NAME REMARK 3 C OR NAME O OR NAME CB )) OR RESID 14 REMARK 3 THROUGH 162 OR (RESID 163 AND (NAME N OR REMARK 3 NAME CA OR NAME C OR NAME O OR NAME CB )) REMARK 3 OR RESID 164 THROUGH 177 OR (RESID 178 REMARK 3 THROUGH 179 AND (NAME N OR NAME CA OR REMARK 3 NAME C OR NAME O OR NAME CB )) OR RESID REMARK 3 180 THROUGH 188 OR (RESID 189 AND (NAME N REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB REMARK 3 )) OR RESID 190 THROUGH 243)) REMARK 3 ATOM PAIRS NUMBER : 1322 REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 7W7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-21. REMARK 100 THE DEPOSITION ID IS D_1300026079. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-JUL-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PAL/PLS REMARK 200 BEAMLINE : 5C (4A) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32477 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960 REMARK 200 RESOLUTION RANGE LOW (A) : 28.680 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.8700 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 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: PHASER REMARK 200 STARTING MODEL: 5GS3 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3350, 100 MM NA/K TARTRATE, REMARK 280 EVAPORATION, TEMPERATURE 293K 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 39.55000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.17500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.55000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 34.17500 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: DIMERIC 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 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 GLU A 1 REMARK 465 GLY A 122 REMARK 465 GLY A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 SER A 126 REMARK 465 GLY A 127 REMARK 465 GLY A 128 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 SER A 131 REMARK 465 GLY A 132 REMARK 465 GLY A 133 REMARK 465 GLY A 134 REMARK 465 GLY A 135 REMARK 465 SER A 136 REMARK 465 SER A 137 REMARK 465 LEU B 102 REMARK 465 GLU B 103 REMARK 465 SER B 121 REMARK 465 GLY B 122 REMARK 465 GLY B 123 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 SER B 126 REMARK 465 GLY B 127 REMARK 465 GLY B 128 REMARK 465 GLY B 129 REMARK 465 GLY B 130 REMARK 465 SER B 131 REMARK 465 GLY B 132 REMARK 465 GLY B 133 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 SER B 136 REMARK 465 GLY B 193 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 LEU A 11 CG CD1 CD2 REMARK 470 GLN A 13 CG CD OE1 NE2 REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 GLU A 103 CG CD OE1 OE2 REMARK 470 GLU A 104 CG CD OE1 OE2 REMARK 470 GLN A 163 CG CD OE1 NE2 REMARK 470 LYS A 178 CG CD CE NZ REMARK 470 ARG A 189 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 243 CG CD CE NZ REMARK 470 GLU B 1 CG CD OE1 OE2 REMARK 470 LYS B 43 CG CD CE NZ REMARK 470 GLU B 104 CG CD OE1 OE2 REMARK 470 TYR B 106 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN B 113 CG CD OE1 NE2 REMARK 470 GLN B 139 CG CD OE1 NE2 REMARK 470 ARG B 160 CG CD NE CZ NH1 NH2 REMARK 470 SER B 188 OG REMARK 470 GLN B 236 CG CD OE1 NE2 REMARK 470 LYS B 243 CG CD CE NZ 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 O HOH A 339 O HOH A 344 2.02 REMARK 500 OE2 GLU A 89 O HOH A 301 2.08 REMARK 500 O ARG A 197 O HOH A 302 2.08 REMARK 500 O PRO A 41 O HOH A 303 2.14 REMARK 500 O HOH A 332 O HOH A 343 2.16 REMARK 500 O HOH B 324 O HOH B 327 2.18 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 CYS A 96 CB CYS A 96 SG -0.184 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 LYS B 65 CA - CB - CG ANGL. DEV. = 13.8 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 43 -141.13 -83.35 REMARK 500 GLU A 103 -127.11 58.52 REMARK 500 SER A 166 -133.03 53.62 REMARK 500 ALA A 187 -40.42 71.27 REMARK 500 SER B 166 -127.65 54.08 REMARK 500 ALA B 187 -38.30 72.21 REMARK 500 REMARK 500 REMARK: NULL DBREF 7W7Q A 1 243 PDB 7W7Q 7W7Q 1 243 DBREF 7W7Q B 1 243 PDB 7W7Q 7W7Q 1 243 SEQRES 1 A 243 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 243 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 243 PHE THR PHE SER ASP TYR GLU MET HIS TRP VAL ARG GLN SEQRES 4 A 243 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER SEQRES 5 A 243 SER ASP GLY SER ASP THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 A 243 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 243 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 243 ALA VAL TYR TYR CYS ALA LYS HIS GLN VAL LEU GLU GLU SEQRES 9 A 243 ALA TYR ALA PHE ASP LEU TRP GLY GLN GLY THR LEU VAL SEQRES 10 A 243 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 A 243 SER GLY GLY GLY GLY SER SER ILE GLN MET THR GLN SER SEQRES 12 A 243 PRO SER SER LEU SER ALA SER VAL GLY ASP ARG VAL THR SEQRES 13 A 243 ILE THR CYS ARG ALA SER GLN ASP ILE SER ASN TRP LEU SEQRES 14 A 243 ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU SEQRES 15 A 243 LEU ILE TYR ALA ALA SER ARG LEU GLN SER GLY VAL PRO SEQRES 16 A 243 SER ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 17 A 243 LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE ALA THR SEQRES 18 A 243 TYR TYR CYS GLN GLN SER TYR SER PHE PRO TRP THR PHE SEQRES 19 A 243 GLY GLN GLY THR LYS VAL GLU ILE LYS SEQRES 1 B 243 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 243 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 243 PHE THR PHE SER ASP TYR GLU MET HIS TRP VAL ARG GLN SEQRES 4 B 243 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER SEQRES 5 B 243 SER ASP GLY SER ASP THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 B 243 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 B 243 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 B 243 ALA VAL TYR TYR CYS ALA LYS HIS GLN VAL LEU GLU GLU SEQRES 9 B 243 ALA TYR ALA PHE ASP LEU TRP GLY GLN GLY THR LEU VAL SEQRES 10 B 243 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 B 243 SER GLY GLY GLY GLY SER SER ILE GLN MET THR GLN SER SEQRES 12 B 243 PRO SER SER LEU SER ALA SER VAL GLY ASP ARG VAL THR SEQRES 13 B 243 ILE THR CYS ARG ALA SER GLN ASP ILE SER ASN TRP LEU SEQRES 14 B 243 ASN TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS LEU SEQRES 15 B 243 LEU ILE TYR ALA ALA SER ARG LEU GLN SER GLY VAL PRO SEQRES 16 B 243 SER ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 17 B 243 LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE ALA THR SEQRES 18 B 243 TYR TYR CYS GLN GLN SER TYR SER PHE PRO TRP THR PHE SEQRES 19 B 243 GLY GLN GLY THR LYS VAL GLU ILE LYS FORMUL 3 HOH *74(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASP A 62 LYS A 65 5 4 HELIX 3 AA3 ARG A 87 THR A 91 5 5 HELIX 4 AA4 GLN A 215 PHE A 219 5 5 HELIX 5 AA5 THR B 28 TYR B 32 5 5 HELIX 6 AA6 ARG B 87 THR B 91 5 5 HELIX 7 AA7 GLN B 215 PHE B 219 5 5 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O ALA A 23 N VAL A 5 SHEET 3 AA1 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA1 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA2 6 GLY A 10 VAL A 12 0 SHEET 2 AA2 6 THR A 115 VAL A 119 1 O THR A 118 N VAL A 12 SHEET 3 AA2 6 ALA A 92 LEU A 102 -1 N TYR A 94 O THR A 115 SHEET 4 AA2 6 GLU A 33 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 THR A 58 TYR A 60 -1 O ASP A 59 N GLY A 50 SHEET 1 AA3 4 GLY A 10 VAL A 12 0 SHEET 2 AA3 4 THR A 115 VAL A 119 1 O THR A 118 N VAL A 12 SHEET 3 AA3 4 ALA A 92 LEU A 102 -1 N TYR A 94 O THR A 115 SHEET 4 AA3 4 ALA A 105 TRP A 111 -1 O ALA A 105 N LEU A 102 SHEET 1 AA4 4 MET A 140 SER A 143 0 SHEET 2 AA4 4 VAL A 155 ALA A 161 -1 O THR A 158 N SER A 143 SHEET 3 AA4 4 ASP A 206 ILE A 211 -1 O PHE A 207 N CYS A 159 SHEET 4 AA4 4 PHE A 198 SER A 203 -1 N SER A 199 O THR A 210 SHEET 1 AA5 6 SER A 146 ALA A 149 0 SHEET 2 AA5 6 THR A 238 ILE A 242 1 O GLU A 241 N LEU A 147 SHEET 3 AA5 6 THR A 221 GLN A 226 -1 N TYR A 222 O THR A 238 SHEET 4 AA5 6 LEU A 169 GLN A 174 -1 N TYR A 172 O TYR A 223 SHEET 5 AA5 6 PRO A 180 TYR A 185 -1 O LEU A 183 N TRP A 171 SHEET 6 AA5 6 ARG A 189 LEU A 190 -1 O ARG A 189 N TYR A 185 SHEET 1 AA6 4 SER A 146 ALA A 149 0 SHEET 2 AA6 4 THR A 238 ILE A 242 1 O GLU A 241 N LEU A 147 SHEET 3 AA6 4 THR A 221 GLN A 226 -1 N TYR A 222 O THR A 238 SHEET 4 AA6 4 THR A 233 PHE A 234 -1 O THR A 233 N GLN A 226 SHEET 1 AA7 4 GLN B 3 SER B 7 0 SHEET 2 AA7 4 LEU B 18 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 3 AA7 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA7 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLN B 82 SHEET 1 AA8 6 GLY B 10 VAL B 12 0 SHEET 2 AA8 6 THR B 115 VAL B 119 1 O THR B 118 N GLY B 10 SHEET 3 AA8 6 ALA B 92 GLN B 100 -1 N TYR B 94 O THR B 115 SHEET 4 AA8 6 MET B 34 ALA B 40 -1 N VAL B 37 O TYR B 95 SHEET 5 AA8 6 GLY B 44 ILE B 51 -1 O SER B 49 N TRP B 36 SHEET 6 AA8 6 THR B 58 TYR B 60 -1 O ASP B 59 N GLY B 50 SHEET 1 AA9 4 GLY B 10 VAL B 12 0 SHEET 2 AA9 4 THR B 115 VAL B 119 1 O THR B 118 N GLY B 10 SHEET 3 AA9 4 ALA B 92 GLN B 100 -1 N TYR B 94 O THR B 115 SHEET 4 AA9 4 ALA B 107 TRP B 111 -1 O ALA B 107 N GLN B 100 SHEET 1 AB1 4 MET B 140 SER B 143 0 SHEET 2 AB1 4 VAL B 155 ALA B 161 -1 O THR B 158 N SER B 143 SHEET 3 AB1 4 ASP B 206 ILE B 211 -1 O LEU B 209 N ILE B 157 SHEET 4 AB1 4 PHE B 198 SER B 203 -1 N SER B 199 O THR B 210 SHEET 1 AB2 6 SER B 146 ALA B 149 0 SHEET 2 AB2 6 THR B 238 ILE B 242 1 O GLU B 241 N LEU B 147 SHEET 3 AB2 6 THR B 221 GLN B 226 -1 N TYR B 222 O THR B 238 SHEET 4 AB2 6 LEU B 169 GLN B 174 -1 N ASN B 170 O GLN B 225 SHEET 5 AB2 6 LYS B 181 TYR B 185 -1 O LEU B 183 N TRP B 171 SHEET 6 AB2 6 ARG B 189 LEU B 190 -1 O ARG B 189 N TYR B 185 SHEET 1 AB3 4 SER B 146 ALA B 149 0 SHEET 2 AB3 4 THR B 238 ILE B 242 1 O GLU B 241 N LEU B 147 SHEET 3 AB3 4 THR B 221 GLN B 226 -1 N TYR B 222 O THR B 238 SHEET 4 AB3 4 THR B 233 PHE B 234 -1 O THR B 233 N GLN B 226 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.07 SSBOND 2 CYS A 159 CYS A 224 1555 1555 2.11 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.03 SSBOND 4 CYS B 159 CYS B 224 1555 1555 2.09 CISPEP 1 SER A 143 PRO A 144 0 -3.85 CISPEP 2 PHE A 230 PRO A 231 0 3.81 CISPEP 3 SER B 143 PRO B 144 0 -6.12 CISPEP 4 PHE B 230 PRO B 231 0 5.24 CRYST1 79.100 68.350 90.710 90.00 108.45 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 0.012642 0.000000 0.004218 0.00000 SCALE2 0.000000 0.014631 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011621 0.00000