HEADER VIRAL PROTEIN 27-JAN-25 9I59 TITLE RVFV GNH COMPLEXED WITH RVFV-379 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPMENT POLYPROTEIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: M POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN OF FAB; COMPND 8 CHAIN: H, X; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN OF FAB; COMPND 12 CHAIN: L, Y; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RIFT VALLEY FEVER VIRUS; SOURCE 3 ORGANISM_TAXID: 11588; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS RVFV GLYCOPROTEIN FAB COMPLEX, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.C.PAESEN,T.A.BOWDEN REVDAT 1 26-NOV-25 9I59 0 JRNL AUTH G.C.PAESEN,N.S.CHAPMAN,J.L.B.WESTOVER,C.M.MCMILLAN, JRNL AUTH 2 N.A.KUZMINA,L.MYERS,R.STASS,J.M.MONTGOMERY,A.BUKREYEV, JRNL AUTH 3 A.L.HARTMAN,B.B.GOWEN,J.E.CROWE,T.A.BOWDEN JRNL TITL STRUCTURAL BASIS FOR RECOGNITION OF RIFT VALLEY FEVER VIRUS JRNL TITL 2 DETERMINE NEUTRALIZATION POTENCY GN PROTEIN BY A HUMAN JRNL TITL 3 NEUTRALIZING MONOCLONAL ANTIBODY ENCODED BY A KAPPA LIGHT JRNL TITL 4 CHAIN JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.09 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.1_5286 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.47 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 103247 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.214 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090 REMARK 3 FREE R VALUE TEST SET COUNT : 5253 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 39.4700 - 6.4900 0.99 3469 170 0.2088 0.2352 REMARK 3 2 6.4800 - 5.1500 1.00 3348 188 0.1997 0.2335 REMARK 3 3 5.1500 - 4.5000 1.00 3295 205 0.1685 0.2138 REMARK 3 4 4.5000 - 4.0900 1.00 3284 185 0.1671 0.1841 REMARK 3 5 4.0900 - 3.8000 1.00 3290 193 0.1870 0.2273 REMARK 3 6 3.8000 - 3.5700 1.00 3248 194 0.1863 0.2225 REMARK 3 7 3.5700 - 3.3900 1.00 3305 166 0.1920 0.2289 REMARK 3 8 3.3900 - 3.2500 1.00 3283 171 0.1983 0.2247 REMARK 3 9 3.2500 - 3.1200 1.00 3268 172 0.1988 0.2666 REMARK 3 10 3.1200 - 3.0100 1.00 3240 200 0.2024 0.2301 REMARK 3 11 3.0100 - 2.9200 1.00 3249 176 0.2095 0.2756 REMARK 3 12 2.9200 - 2.8400 1.00 3251 175 0.2194 0.2711 REMARK 3 13 2.8400 - 2.7600 1.00 3266 195 0.2182 0.2839 REMARK 3 14 2.7600 - 2.6900 1.00 3264 164 0.2235 0.2696 REMARK 3 15 2.6900 - 2.6300 1.00 3212 184 0.2389 0.2915 REMARK 3 16 2.6300 - 2.5800 1.00 3269 179 0.2487 0.3157 REMARK 3 17 2.5800 - 2.5300 1.00 3250 182 0.2467 0.2928 REMARK 3 18 2.5300 - 2.4800 1.00 3246 174 0.2504 0.2925 REMARK 3 19 2.4800 - 2.4300 1.00 3246 182 0.2522 0.3025 REMARK 3 20 2.4300 - 2.3900 1.00 3287 135 0.2539 0.3362 REMARK 3 21 2.3900 - 2.3500 1.00 3235 153 0.2631 0.2971 REMARK 3 22 2.3500 - 2.3200 1.00 3270 162 0.2687 0.3005 REMARK 3 23 2.3200 - 2.2800 1.00 3285 147 0.2668 0.3307 REMARK 3 24 2.2800 - 2.2500 1.00 3249 164 0.2634 0.3277 REMARK 3 25 2.2500 - 2.2200 1.00 3239 168 0.2807 0.3097 REMARK 3 26 2.2200 - 2.1900 1.00 3217 186 0.2941 0.3289 REMARK 3 27 2.1900 - 2.1600 1.00 3208 204 0.2833 0.3227 REMARK 3 28 2.1600 - 2.1400 1.00 3270 153 0.2998 0.3272 REMARK 3 29 2.1400 - 2.1100 1.00 3240 171 0.3120 0.3485 REMARK 3 30 2.1100 - 2.0900 1.00 3211 155 0.3172 0.3323 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.287 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.003 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 36.45 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.58 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 : 0.004 11026 REMARK 3 ANGLE : 0.723 14918 REMARK 3 CHIRALITY : 0.048 1667 REMARK 3 PLANARITY : 0.006 1900 REMARK 3 DIHEDRAL : 16.425 4016 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 155 through 233 or REMARK 3 resid 239 through 288 or resid 292 REMARK 3 through 330 or resid 338 through 404 or REMARK 3 resid 410 through 415 or resid 420 REMARK 3 through 425 or resid 430 through 448 or REMARK 3 resid 452 through 465)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 155 through 376 or REMARK 3 resid 394 through 465)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 2 through 124 or REMARK 3 resid 134 through 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "X" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 1 through 127 or REMARK 3 resid 131 through 149 or resid 155 REMARK 3 through 180 or resid 195 through 202 or REMARK 3 resid 204 through 206)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "Y" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9I59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1292144921. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-OCT-23 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 : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.6199 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X CDTE 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103314 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090 REMARK 200 RESOLUTION RANGE LOW (A) : 39.470 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 13.90 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 5% PEG4000, 50 MM MES PH 6.0, 5 MM REMARK 280 MGSO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.65K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 78.94000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.94000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 59.04500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 93.68500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 59.04500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 93.68500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.94000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 59.04500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 93.68500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.94000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 59.04500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 93.68500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 APPLY THE FOLLOWING TO CHAINS: A, H, L 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, X, Y 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH L 491 LIES ON A SPECIAL POSITION. 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 ASP A 333 REMARK 465 GLY A 334 REMARK 465 GLN A 335 REMARK 465 HIS A 377 REMARK 465 LYS A 378 REMARK 465 GLY A 379 REMARK 465 GLN A 380 REMARK 465 TYR A 381 REMARK 465 LYS A 382 REMARK 465 GLY A 383 REMARK 465 THR A 384 REMARK 465 MET A 385 REMARK 465 ASP A 386 REMARK 465 SER A 387 REMARK 465 GLY A 388 REMARK 465 GLN A 389 REMARK 465 THR A 390 REMARK 465 LYS A 391 REMARK 465 ARG A 392 REMARK 465 GLU A 393 REMARK 465 ALA A 470 REMARK 465 LYS A 471 REMARK 465 PRO A 472 REMARK 465 ILE A 473 REMARK 465 GLN A 474 REMARK 465 ARG A 475 REMARK 465 VAL A 476 REMARK 465 GLU A 477 REMARK 465 PRO A 478 REMARK 465 CYS A 479 REMARK 465 THR A 480 REMARK 465 THR A 481 REMARK 465 CYS A 482 REMARK 465 ILE A 483 REMARK 465 THR A 484 REMARK 465 LYS A 485 REMARK 465 CYS A 486 REMARK 465 GLU A 487 REMARK 465 PRO A 488 REMARK 465 HIS A 489 REMARK 465 GLY A 490 REMARK 465 THR A 491 REMARK 465 LYS A 492 REMARK 465 HIS A 493 REMARK 465 HIS A 494 REMARK 465 HIS A 495 REMARK 465 HIS A 496 REMARK 465 HIS A 497 REMARK 465 HIS A 498 REMARK 465 GLU B 154 REMARK 465 ALA B 234 REMARK 465 HIS B 235 REMARK 465 GLY B 236 REMARK 465 ASN B 237 REMARK 465 PRO B 238 REMARK 465 GLY B 289 REMARK 465 ALA B 290 REMARK 465 SER B 291 REMARK 465 LYS B 331 REMARK 465 CYS B 332 REMARK 465 ASP B 333 REMARK 465 GLY B 334 REMARK 465 GLN B 335 REMARK 465 LEU B 336 REMARK 465 SER B 337 REMARK 465 ILE B 405 REMARK 465 GLY B 406 REMARK 465 GLY B 407 REMARK 465 HIS B 408 REMARK 465 GLY B 409 REMARK 465 ASP B 416 REMARK 465 ALA B 417 REMARK 465 ALA B 418 REMARK 465 PHE B 419 REMARK 465 THR B 426 REMARK 465 ALA B 427 REMARK 465 GLN B 428 REMARK 465 TYR B 429 REMARK 465 GLY B 449 REMARK 465 VAL B 450 REMARK 465 TRP B 451 REMARK 465 ARG B 466 REMARK 465 GLU B 467 REMARK 465 LEU B 468 REMARK 465 SER B 469 REMARK 465 ALA B 470 REMARK 465 LYS B 471 REMARK 465 PRO B 472 REMARK 465 ILE B 473 REMARK 465 GLN B 474 REMARK 465 ARG B 475 REMARK 465 VAL B 476 REMARK 465 GLU B 477 REMARK 465 PRO B 478 REMARK 465 CYS B 479 REMARK 465 THR B 480 REMARK 465 THR B 481 REMARK 465 CYS B 482 REMARK 465 ILE B 483 REMARK 465 THR B 484 REMARK 465 LYS B 485 REMARK 465 CYS B 486 REMARK 465 GLU B 487 REMARK 465 PRO B 488 REMARK 465 HIS B 489 REMARK 465 GLY B 490 REMARK 465 THR B 491 REMARK 465 LYS B 492 REMARK 465 HIS B 493 REMARK 465 HIS B 494 REMARK 465 HIS B 495 REMARK 465 HIS B 496 REMARK 465 HIS B 497 REMARK 465 HIS B 498 REMARK 465 GLN H 1 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLN X 1 REMARK 465 ALA X 125 REMARK 465 PRO X 126 REMARK 465 SER X 127 REMARK 465 SER X 128 REMARK 465 LYS X 129 REMARK 465 SER X 130 REMARK 465 THR X 131 REMARK 465 SER X 132 REMARK 465 GLY X 133 REMARK 465 PRO X 213 REMARK 465 LYS X 214 REMARK 465 SER X 215 REMARK 465 CYS X 216 REMARK 465 GLY Y 128 REMARK 465 THR Y 129 REMARK 465 ALA Y 130 REMARK 465 VAL Y 150 REMARK 465 ASP Y 151 REMARK 465 ASN Y 152 REMARK 465 ALA Y 153 REMARK 465 LEU Y 154 REMARK 465 LEU Y 181 REMARK 465 SER Y 182 REMARK 465 LYS Y 183 REMARK 465 ALA Y 184 REMARK 465 ASP Y 185 REMARK 465 TYR Y 186 REMARK 465 GLU Y 187 REMARK 465 LYS Y 188 REMARK 465 HIS Y 189 REMARK 465 LYS Y 190 REMARK 465 VAL Y 191 REMARK 465 TYR Y 192 REMARK 465 ALA Y 193 REMARK 465 CYS Y 194 REMARK 465 SER Y 203 REMARK 465 LYS Y 207 REMARK 465 SER Y 208 REMARK 465 PHE Y 209 REMARK 465 ASN Y 210 REMARK 465 ARG Y 211 REMARK 465 GLY Y 212 REMARK 465 GLU Y 213 REMARK 465 CYS Y 214 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 ASN A 167 63.36 -117.78 REMARK 500 SER A 440 -167.25 -107.24 REMARK 500 ASN B 167 61.75 -117.67 REMARK 500 LYS B 274 -1.31 75.20 REMARK 500 SER B 440 -167.08 -104.97 REMARK 500 SER H 15 -15.00 77.22 REMARK 500 ASP H 101 121.59 -171.76 REMARK 500 ASP H 144 68.28 63.37 REMARK 500 GLU L 30 -125.57 55.27 REMARK 500 ALA L 51 -41.73 73.36 REMARK 500 SER L 52 -5.38 -141.01 REMARK 500 ASN L 138 73.95 56.45 REMARK 500 LYS L 169 -63.31 -105.18 REMARK 500 SER X 15 -10.77 76.16 REMARK 500 ASP X 101 121.31 -171.64 REMARK 500 ASP X 144 71.19 62.94 REMARK 500 GLU Y 30 -124.83 55.33 REMARK 500 ALA Y 51 -41.99 72.96 REMARK 500 SER Y 52 -5.44 -140.27 REMARK 500 ASN Y 138 73.73 58.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 747 DISTANCE = 5.91 ANGSTROMS DBREF 9I59 A 154 490 UNP A2T080 A2T080_RVFV 154 490 DBREF 9I59 B 154 490 UNP A2T080 A2T080_RVFV 154 490 DBREF 9I59 H 1 216 PDB 9I59 9I59 1 216 DBREF 9I59 L 1 214 PDB 9I59 9I59 1 214 DBREF 9I59 X 1 216 PDB 9I59 9I59 1 216 DBREF 9I59 Y 1 214 PDB 9I59 9I59 1 214 SEQADV 9I59 THR A 491 UNP A2T080 EXPRESSION TAG SEQADV 9I59 LYS A 492 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS A 493 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS A 494 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS A 495 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS A 496 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS A 497 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS A 498 UNP A2T080 EXPRESSION TAG SEQADV 9I59 THR B 491 UNP A2T080 EXPRESSION TAG SEQADV 9I59 LYS B 492 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS B 493 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS B 494 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS B 495 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS B 496 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS B 497 UNP A2T080 EXPRESSION TAG SEQADV 9I59 HIS B 498 UNP A2T080 EXPRESSION TAG SEQRES 1 A 345 GLU ASP PRO HIS LEU ARG ASN ARG PRO GLY LYS GLY HIS SEQRES 2 A 345 ASN TYR ILE ASP GLY MET THR GLN GLU ASP ALA THR CYS SEQRES 3 A 345 LYS PRO VAL THR TYR ALA GLY ALA CYS SER SER PHE ASP SEQRES 4 A 345 VAL LEU LEU GLU LYS GLY LYS PHE PRO LEU PHE GLN SER SEQRES 5 A 345 TYR ALA HIS HIS ARG THR LEU LEU GLU ALA VAL HIS ASP SEQRES 6 A 345 THR ILE ILE ALA LYS ALA ASP PRO PRO SER CYS ASP LEU SEQRES 7 A 345 GLN SER ALA HIS GLY ASN PRO CYS MET LYS GLU LYS LEU SEQRES 8 A 345 VAL MET LYS THR HIS CYS PRO ASN ASP TYR GLN SER ALA SEQRES 9 A 345 HIS TYR LEU ASN ASN ASP GLY LYS MET ALA SER VAL LYS SEQRES 10 A 345 CYS PRO PRO LYS TYR GLU LEU THR GLU ASP CYS ASN PHE SEQRES 11 A 345 CYS ARG GLN MET THR GLY ALA SER LEU LYS LYS GLY SER SEQRES 12 A 345 TYR PRO LEU GLN ASP LEU PHE CYS GLN SER SER GLU ASP SEQRES 13 A 345 ASP GLY SER LYS LEU LYS THR LYS MET LYS GLY VAL CYS SEQRES 14 A 345 GLU VAL GLY VAL GLN ALA LEU LYS LYS CYS ASP GLY GLN SEQRES 15 A 345 LEU SER THR ALA HIS GLU VAL VAL PRO PHE ALA VAL PHE SEQRES 16 A 345 LYS ASN SER LYS LYS VAL TYR LEU ASP LYS LEU ASP LEU SEQRES 17 A 345 LYS THR GLU GLU ASN LEU LEU PRO ASP SER PHE VAL CYS SEQRES 18 A 345 PHE GLU HIS LYS GLY GLN TYR LYS GLY THR MET ASP SER SEQRES 19 A 345 GLY GLN THR LYS ARG GLU LEU LYS SER PHE ASP ILE SER SEQRES 20 A 345 GLN CYS PRO LYS ILE GLY GLY HIS GLY SER LYS LYS CYS SEQRES 21 A 345 THR GLY ASP ALA ALA PHE CYS SER ALA TYR GLU CYS THR SEQRES 22 A 345 ALA GLN TYR ALA ASN ALA TYR CYS SER HIS ALA ASN GLY SEQRES 23 A 345 SER GLY ILE VAL GLN ILE GLN VAL SER GLY VAL TRP LYS SEQRES 24 A 345 LYS PRO LEU CYS VAL GLY TYR GLU ARG VAL VAL VAL LYS SEQRES 25 A 345 ARG GLU LEU SER ALA LYS PRO ILE GLN ARG VAL GLU PRO SEQRES 26 A 345 CYS THR THR CYS ILE THR LYS CYS GLU PRO HIS GLY THR SEQRES 27 A 345 LYS HIS HIS HIS HIS HIS HIS SEQRES 1 B 345 GLU ASP PRO HIS LEU ARG ASN ARG PRO GLY LYS GLY HIS SEQRES 2 B 345 ASN TYR ILE ASP GLY MET THR GLN GLU ASP ALA THR CYS SEQRES 3 B 345 LYS PRO VAL THR TYR ALA GLY ALA CYS SER SER PHE ASP SEQRES 4 B 345 VAL LEU LEU GLU LYS GLY LYS PHE PRO LEU PHE GLN SER SEQRES 5 B 345 TYR ALA HIS HIS ARG THR LEU LEU GLU ALA VAL HIS ASP SEQRES 6 B 345 THR ILE ILE ALA LYS ALA ASP PRO PRO SER CYS ASP LEU SEQRES 7 B 345 GLN SER ALA HIS GLY ASN PRO CYS MET LYS GLU LYS LEU SEQRES 8 B 345 VAL MET LYS THR HIS CYS PRO ASN ASP TYR GLN SER ALA SEQRES 9 B 345 HIS TYR LEU ASN ASN ASP GLY LYS MET ALA SER VAL LYS SEQRES 10 B 345 CYS PRO PRO LYS TYR GLU LEU THR GLU ASP CYS ASN PHE SEQRES 11 B 345 CYS ARG GLN MET THR GLY ALA SER LEU LYS LYS GLY SER SEQRES 12 B 345 TYR PRO LEU GLN ASP LEU PHE CYS GLN SER SER GLU ASP SEQRES 13 B 345 ASP GLY SER LYS LEU LYS THR LYS MET LYS GLY VAL CYS SEQRES 14 B 345 GLU VAL GLY VAL GLN ALA LEU LYS LYS CYS ASP GLY GLN SEQRES 15 B 345 LEU SER THR ALA HIS GLU VAL VAL PRO PHE ALA VAL PHE SEQRES 16 B 345 LYS ASN SER LYS LYS VAL TYR LEU ASP LYS LEU ASP LEU SEQRES 17 B 345 LYS THR GLU GLU ASN LEU LEU PRO ASP SER PHE VAL CYS SEQRES 18 B 345 PHE GLU HIS LYS GLY GLN TYR LYS GLY THR MET ASP SER SEQRES 19 B 345 GLY GLN THR LYS ARG GLU LEU LYS SER PHE ASP ILE SER SEQRES 20 B 345 GLN CYS PRO LYS ILE GLY GLY HIS GLY SER LYS LYS CYS SEQRES 21 B 345 THR GLY ASP ALA ALA PHE CYS SER ALA TYR GLU CYS THR SEQRES 22 B 345 ALA GLN TYR ALA ASN ALA TYR CYS SER HIS ALA ASN GLY SEQRES 23 B 345 SER GLY ILE VAL GLN ILE GLN VAL SER GLY VAL TRP LYS SEQRES 24 B 345 LYS PRO LEU CYS VAL GLY TYR GLU ARG VAL VAL VAL LYS SEQRES 25 B 345 ARG GLU LEU SER ALA LYS PRO ILE GLN ARG VAL GLU PRO SEQRES 26 B 345 CYS THR THR CYS ILE THR LYS CYS GLU PRO HIS GLY THR SEQRES 27 B 345 LYS HIS HIS HIS HIS HIS HIS SEQRES 1 H 223 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 223 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 223 ASP SER ILE SER GLY GLY ASP TYR TYR TRP SER TRP ILE SEQRES 4 H 223 ARG ARG PRO ALA GLY GLU GLY LEU GLU TRP ILE GLY ARG SEQRES 5 H 223 VAL HIS THR THR GLY SER THR ASP TYR ASN PRO SER LEU SEQRES 6 H 223 ARG THR ARG VAL THR ILE SER ILE ASP THR SER LYS ASN SEQRES 7 H 223 HIS PHE PHE LEU LYS MET THR SER VAL THR ALA ALA ASP SEQRES 8 H 223 THR ALA VAL TYR TYR CYS ALA ARG GLU GLY ASP TYR SER SEQRES 9 H 223 ALA TRP PHE ASP PRO TRP GLY GLN GLY ALA LEU VAL THR SEQRES 10 H 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 H 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 H 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 H 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 H 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 H 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 H 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 H 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 H 223 SER CYS SEQRES 1 L 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 215 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 215 GLN HIS ILE GLU SER PHE LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ILE ALA SER SEQRES 5 L 215 THR LEU GLN GLY GLY VAL PRO SER ARG PHE SER GLY ARG SEQRES 6 L 215 GLY PHE GLY THR ASP PHE THR LEU THR ILE ASN SER LEU SEQRES 7 L 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 215 TYR THR ILE SER PRO ILE THR PHE GLY GLN GLY THR ARG SEQRES 9 L 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 X 223 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 X 223 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 X 223 ASP SER ILE SER GLY GLY ASP TYR TYR TRP SER TRP ILE SEQRES 4 X 223 ARG ARG PRO ALA GLY GLU GLY LEU GLU TRP ILE GLY ARG SEQRES 5 X 223 VAL HIS THR THR GLY SER THR ASP TYR ASN PRO SER LEU SEQRES 6 X 223 ARG THR ARG VAL THR ILE SER ILE ASP THR SER LYS ASN SEQRES 7 X 223 HIS PHE PHE LEU LYS MET THR SER VAL THR ALA ALA ASP SEQRES 8 X 223 THR ALA VAL TYR TYR CYS ALA ARG GLU GLY ASP TYR SER SEQRES 9 X 223 ALA TRP PHE ASP PRO TRP GLY GLN GLY ALA LEU VAL THR SEQRES 10 X 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 X 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 X 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 X 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 X 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 X 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 X 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 X 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 X 223 SER CYS SEQRES 1 Y 215 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 Y 215 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 Y 215 GLN HIS ILE GLU SER PHE LEU ASN TRP TYR GLN GLN LYS SEQRES 4 Y 215 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ILE ALA SER SEQRES 5 Y 215 THR LEU GLN GLY GLY VAL PRO SER ARG PHE SER GLY ARG SEQRES 6 Y 215 GLY PHE GLY THR ASP PHE THR LEU THR ILE ASN SER LEU SEQRES 7 Y 215 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 Y 215 TYR THR ILE SER PRO ILE THR PHE GLY GLN GLY THR ARG SEQRES 9 Y 215 LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 Y 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 Y 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 Y 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 Y 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 Y 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 Y 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 Y 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 Y 215 SER PHE ASN ARG GLY GLU CYS HET GOL A 501 6 HET GOL H 301 6 HET GOL H 302 6 HET GOL L 301 6 HET PEG L 302 7 HET GOL X 301 6 HET GOL Y 301 6 HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 GOL 6(C3 H8 O3) FORMUL 11 PEG C4 H10 O3 FORMUL 14 HOH *540(H2 O) HELIX 1 AA1 GLU A 175 LYS A 180 1 6 HELIX 2 AA2 PHE A 191 GLU A 196 5 6 HELIX 3 AA3 PHE A 200 TYR A 206 1 7 HELIX 4 AA4 THR A 211 ASP A 218 1 8 HELIX 5 AA5 GLN A 232 ALA A 234 5 3 HELIX 6 AA6 ASN A 237 VAL A 245 1 9 HELIX 7 AA7 LEU A 368 ASP A 370 5 3 HELIX 8 AA8 ASP A 398 CYS A 402 5 5 HELIX 9 AA9 ASP A 416 TYR A 423 1 8 HELIX 10 AB1 GLU B 175 LYS B 180 1 6 HELIX 11 AB2 PHE B 191 GLU B 196 5 6 HELIX 12 AB3 PHE B 200 TYR B 206 1 7 HELIX 13 AB4 THR B 211 ASP B 218 1 8 HELIX 14 AB5 MET B 240 VAL B 245 1 6 HELIX 15 AB6 LEU B 368 ASP B 370 5 3 HELIX 16 AB7 ASP B 386 GLU B 393 1 8 HELIX 17 AB8 ASP B 398 CYS B 402 5 5 HELIX 18 AB9 PRO H 61 ARG H 64 5 4 HELIX 19 AC1 THR H 83 ASP H 86 5 4 HELIX 20 AC2 SER H 156 ALA H 158 5 3 HELIX 21 AC3 SER H 187 GLY H 190 5 4 HELIX 22 AC4 LYS H 201 ASN H 204 5 4 HELIX 23 AC5 GLN L 79 PHE L 83 5 5 HELIX 24 AC6 SER L 121 SER L 127 1 7 HELIX 25 AC7 LYS L 183 LYS L 188 1 6 HELIX 26 AC8 PRO X 61 ARG X 64 5 4 HELIX 27 AC9 THR X 73 LYS X 75 5 3 HELIX 28 AD1 THR X 83 ASP X 86 5 4 HELIX 29 AD2 SER X 156 ALA X 158 5 3 HELIX 30 AD3 SER X 187 GLY X 190 5 4 HELIX 31 AD4 LYS X 201 ASN X 204 5 4 HELIX 32 AD5 GLN Y 79 PHE Y 83 5 5 HELIX 33 AD6 SER Y 121 SER Y 127 1 7 SHEET 1 AA1 4 CYS A 229 ASP A 230 0 SHEET 2 AA1 4 MET A 266 LYS A 270 1 O SER A 268 N CYS A 229 SHEET 3 AA1 4 SER A 256 LEU A 260 -1 N TYR A 259 O ALA A 267 SHEET 4 AA1 4 TYR A 297 PRO A 298 1 O TYR A 297 N SER A 256 SHEET 1 AA2 4 MET A 246 LYS A 247 0 SHEET 2 AA2 4 CYS A 456 ARG A 466 -1 O ARG A 461 N LYS A 247 SHEET 3 AA2 4 VAL A 321 VAL A 324 -1 N CYS A 322 O LYS A 465 SHEET 4 AA2 4 GLN A 327 ALA A 328 -1 O GLN A 327 N VAL A 324 SHEET 1 AA3 4 ASP A 301 CYS A 304 0 SHEET 2 AA3 4 CYS A 456 ARG A 466 -1 O VAL A 457 N PHE A 303 SHEET 3 AA3 4 SER A 337 VAL A 347 -1 N ALA A 339 O VAL A 464 SHEET 4 AA3 4 VAL A 354 TYR A 355 -1 O VAL A 354 N ALA A 346 SHEET 1 AA4 2 GLU A 276 LEU A 277 0 SHEET 2 AA4 2 CYS A 284 ARG A 285 -1 O ARG A 285 N GLU A 276 SHEET 1 AA5 3 LEU A 361 GLU A 364 0 SHEET 2 AA5 3 ILE A 442 VAL A 447 -1 O ILE A 442 N GLU A 364 SHEET 3 AA5 3 VAL A 450 LYS A 452 -1 O VAL A 450 N VAL A 447 SHEET 1 AA6 4 SER A 396 PHE A 397 0 SHEET 2 AA6 4 PHE A 372 PHE A 375 -1 N CYS A 374 O PHE A 397 SHEET 3 AA6 4 ALA A 432 HIS A 436 -1 O SER A 435 N VAL A 373 SHEET 4 AA6 4 CYS A 413 GLY A 415 1 N THR A 414 O CYS A 434 SHEET 1 AA7 4 CYS B 229 ASP B 230 0 SHEET 2 AA7 4 MET B 266 LYS B 270 1 O SER B 268 N CYS B 229 SHEET 3 AA7 4 SER B 256 LEU B 260 -1 N TYR B 259 O ALA B 267 SHEET 4 AA7 4 TYR B 297 PRO B 298 1 O TYR B 297 N SER B 256 SHEET 1 AA8 2 GLU B 276 LEU B 277 0 SHEET 2 AA8 2 CYS B 284 ARG B 285 -1 O ARG B 285 N GLU B 276 SHEET 1 AA9 4 ASP B 301 CYS B 304 0 SHEET 2 AA9 4 CYS B 456 VAL B 464 -1 O VAL B 457 N PHE B 303 SHEET 3 AA9 4 ALA B 339 VAL B 347 -1 N ALA B 339 O VAL B 464 SHEET 4 AA9 4 VAL B 354 TYR B 355 -1 O VAL B 354 N ALA B 346 SHEET 1 AB1 2 GLU B 323 VAL B 324 0 SHEET 2 AB1 2 GLN B 327 ALA B 328 -1 O GLN B 327 N VAL B 324 SHEET 1 AB2 2 LEU B 361 GLU B 364 0 SHEET 2 AB2 2 ILE B 442 ILE B 445 -1 O ILE B 442 N GLU B 364 SHEET 1 AB3 4 LEU B 394 SER B 396 0 SHEET 2 AB3 4 PHE B 372 HIS B 377 -1 N GLU B 376 O LYS B 395 SHEET 3 AB3 4 ALA B 432 HIS B 436 -1 O SER B 435 N VAL B 373 SHEET 4 AB3 4 CYS B 413 THR B 414 1 N THR B 414 O CYS B 434 SHEET 1 AB4 4 GLN H 3 SER H 7 0 SHEET 2 AB4 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AB4 4 HIS H 77 MET H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AB4 4 VAL H 67 ASP H 72 -1 N ASP H 72 O HIS H 77 SHEET 1 AB5 6 LEU H 11 VAL H 12 0 SHEET 2 AB5 6 ALA H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB5 6 ALA H 88 GLU H 95 -1 N TYR H 90 O ALA H 107 SHEET 4 AB5 6 TYR H 33 PRO H 40 -1 N ILE H 37 O TYR H 91 SHEET 5 AB5 6 GLU H 46 HIS H 52 -1 O ILE H 48 N TRP H 36 SHEET 6 AB5 6 THR H 57 TYR H 59 -1 O ASP H 58 N ARG H 50 SHEET 1 AB6 4 LEU H 11 VAL H 12 0 SHEET 2 AB6 4 ALA H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AB6 4 ALA H 88 GLU H 95 -1 N TYR H 90 O ALA H 107 SHEET 4 AB6 4 PHE H 100B TRP H 103 -1 O ASP H 101 N ARG H 94 SHEET 1 AB7 4 SER H 120 LEU H 124 0 SHEET 2 AB7 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AB7 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AB7 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB8 4 SER H 120 LEU H 124 0 SHEET 2 AB8 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AB8 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145 SHEET 4 AB8 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB9 3 THR H 151 TRP H 154 0 SHEET 2 AB9 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB9 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AC1 4 MET L 4 SER L 7 0 SHEET 2 AC1 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AC1 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AC1 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AC2 6 SER L 10 SER L 14 0 SHEET 2 AC2 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AC2 6 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC2 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AC2 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AC3 4 SER L 10 SER L 14 0 SHEET 2 AC3 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AC3 4 ALA L 84 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AC3 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AC4 4 SER L 114 PHE L 118 0 SHEET 2 AC4 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AC4 4 TYR L 173 SER L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 AC4 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AC5 4 ALA L 153 LEU L 154 0 SHEET 2 AC5 4 ALA L 144 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AC5 4 VAL L 191 HIS L 198 -1 O ALA L 193 N LYS L 149 SHEET 4 AC5 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AC6 4 GLN X 3 SER X 7 0 SHEET 2 AC6 4 LEU X 18 SER X 25 -1 O THR X 21 N SER X 7 SHEET 3 AC6 4 HIS X 77 MET X 82 -1 O PHE X 78 N CYS X 22 SHEET 4 AC6 4 VAL X 67 ASP X 72 -1 N SER X 70 O PHE X 79 SHEET 1 AC7 6 LEU X 11 VAL X 12 0 SHEET 2 AC7 6 ALA X 107 VAL X 111 1 O THR X 110 N VAL X 12 SHEET 3 AC7 6 ALA X 88 GLU X 95 -1 N TYR X 90 O ALA X 107 SHEET 4 AC7 6 TYR X 33 PRO X 40 -1 N ILE X 37 O TYR X 91 SHEET 5 AC7 6 GLU X 46 HIS X 52 -1 O GLU X 46 N ARG X 38 SHEET 6 AC7 6 THR X 57 TYR X 59 -1 O ASP X 58 N ARG X 50 SHEET 1 AC8 4 LEU X 11 VAL X 12 0 SHEET 2 AC8 4 ALA X 107 VAL X 111 1 O THR X 110 N VAL X 12 SHEET 3 AC8 4 ALA X 88 GLU X 95 -1 N TYR X 90 O ALA X 107 SHEET 4 AC8 4 PHE X 100B TRP X 103 -1 O ASP X 101 N ARG X 94 SHEET 1 AC9 4 SER X 120 LEU X 124 0 SHEET 2 AC9 4 THR X 135 TYR X 145 -1 O LEU X 141 N PHE X 122 SHEET 3 AC9 4 TYR X 176 PRO X 185 -1 O TYR X 176 N TYR X 145 SHEET 4 AC9 4 VAL X 163 THR X 165 -1 N HIS X 164 O VAL X 181 SHEET 1 AD1 4 SER X 120 LEU X 124 0 SHEET 2 AD1 4 THR X 135 TYR X 145 -1 O LEU X 141 N PHE X 122 SHEET 3 AD1 4 TYR X 176 PRO X 185 -1 O TYR X 176 N TYR X 145 SHEET 4 AD1 4 VAL X 169 LEU X 170 -1 N VAL X 169 O SER X 177 SHEET 1 AD2 3 THR X 151 TRP X 154 0 SHEET 2 AD2 3 ILE X 195 HIS X 200 -1 O ASN X 197 N SER X 153 SHEET 3 AD2 3 THR X 205 LYS X 210 -1 O VAL X 207 N VAL X 198 SHEET 1 AD3 4 MET Y 4 SER Y 7 0 SHEET 2 AD3 4 VAL Y 19 ALA Y 25 -1 O THR Y 22 N SER Y 7 SHEET 3 AD3 4 ASP Y 70 ILE Y 75 -1 O LEU Y 73 N ILE Y 21 SHEET 4 AD3 4 PHE Y 62 GLY Y 66 -1 N SER Y 63 O THR Y 74 SHEET 1 AD4 6 SER Y 10 SER Y 14 0 SHEET 2 AD4 6 THR Y 102 LYS Y 107 1 O GLU Y 105 N LEU Y 11 SHEET 3 AD4 6 ALA Y 84 GLN Y 90 -1 N ALA Y 84 O LEU Y 104 SHEET 4 AD4 6 LEU Y 33 GLN Y 38 -1 N ASN Y 34 O GLN Y 89 SHEET 5 AD4 6 LYS Y 45 TYR Y 49 -1 O LEU Y 47 N TRP Y 35 SHEET 6 AD4 6 THR Y 53 LEU Y 54 -1 O THR Y 53 N TYR Y 49 SHEET 1 AD5 4 SER Y 10 SER Y 14 0 SHEET 2 AD5 4 THR Y 102 LYS Y 107 1 O GLU Y 105 N LEU Y 11 SHEET 3 AD5 4 ALA Y 84 GLN Y 90 -1 N ALA Y 84 O LEU Y 104 SHEET 4 AD5 4 THR Y 97 PHE Y 98 -1 O THR Y 97 N GLN Y 90 SHEET 1 AD6 4 SER Y 114 PHE Y 118 0 SHEET 2 AD6 4 VAL Y 132 PHE Y 139 -1 O ASN Y 137 N SER Y 114 SHEET 3 AD6 4 TYR Y 173 LEU Y 179 -1 O TYR Y 173 N PHE Y 139 SHEET 4 AD6 4 SER Y 159 VAL Y 163 -1 N GLN Y 160 O THR Y 178 SHEET 1 AD7 2 LYS Y 145 VAL Y 146 0 SHEET 2 AD7 2 VAL Y 196 THR Y 197 -1 O THR Y 197 N LYS Y 145 SSBOND 1 CYS A 179 CYS A 188 1555 1555 2.05 SSBOND 2 CYS A 229 CYS A 239 1555 1555 2.04 SSBOND 3 CYS A 250 CYS A 281 1555 1555 2.04 SSBOND 4 CYS A 271 CYS A 284 1555 1555 2.05 SSBOND 5 CYS A 304 CYS A 456 1555 1555 2.04 SSBOND 6 CYS A 322 CYS A 332 1555 1555 2.03 SSBOND 7 CYS A 374 CYS A 434 1555 1555 2.04 SSBOND 8 CYS A 402 CYS A 413 1555 1555 2.03 SSBOND 9 CYS A 420 CYS A 425 1555 1555 2.03 SSBOND 10 CYS B 179 CYS B 188 1555 1555 2.04 SSBOND 11 CYS B 229 CYS B 239 1555 1555 2.04 SSBOND 12 CYS B 250 CYS B 281 1555 1555 2.03 SSBOND 13 CYS B 271 CYS B 284 1555 1555 2.04 SSBOND 14 CYS B 304 CYS B 456 1555 1555 2.04 SSBOND 15 CYS B 374 CYS B 434 1555 1555 2.04 SSBOND 16 CYS B 402 CYS B 413 1555 1555 2.03 SSBOND 17 CYS B 420 CYS B 425 1555 1555 2.03 SSBOND 18 CYS H 22 CYS H 92 1555 1555 2.05 SSBOND 19 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 20 CYS H 216 CYS L 214 1555 1555 2.03 SSBOND 21 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 22 CYS L 134 CYS L 194 1555 1555 2.04 SSBOND 23 CYS X 22 CYS X 92 1555 1555 2.05 SSBOND 24 CYS X 140 CYS X 196 1555 1555 2.03 SSBOND 25 CYS Y 23 CYS Y 88 1555 1555 2.05 CISPEP 1 LYS A 180 PRO A 181 0 4.84 CISPEP 2 ASP A 225 PRO A 226 0 3.10 CISPEP 3 LYS B 180 PRO B 181 0 4.75 CISPEP 4 ASP B 225 PRO B 226 0 3.26 CISPEP 5 ASP H 101 PRO H 102 0 -1.45 CISPEP 6 PHE H 146 PRO H 147 0 -7.79 CISPEP 7 GLU H 148 PRO H 149 0 1.94 CISPEP 8 SER L 7 PRO L 8 0 -5.64 CISPEP 9 SER L 95 PRO L 95A 0 -5.84 CISPEP 10 TYR L 140 PRO L 141 0 2.14 CISPEP 11 ASP X 101 PRO X 102 0 -0.77 CISPEP 12 PHE X 146 PRO X 147 0 -6.91 CISPEP 13 GLU X 148 PRO X 149 0 1.14 CISPEP 14 SER Y 7 PRO Y 8 0 -7.08 CISPEP 15 SER Y 95 PRO Y 95A 0 -5.39 CISPEP 16 TYR Y 140 PRO Y 141 0 2.59 CRYST1 118.090 187.370 157.880 90.00 90.00 90.00 C 2 2 21 16 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 0.008468 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005337 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006334 0.00000 MTRIX1 1 -0.923214 0.033100 0.382857 -20.66727 1 MTRIX2 1 -0.009678 -0.997970 0.062943 -57.44282 1 MTRIX3 1 0.384164 0.054405 0.921661 6.44175 1 MTRIX1 2 -0.893524 -0.006465 0.448969 -23.72587 1 MTRIX2 2 0.042088 -0.996700 0.069409 -57.94052 1 MTRIX3 2 0.447039 0.080915 0.890847 7.13929 1 MTRIX1 3 -0.901133 -0.018293 0.433157 -24.01406 1 MTRIX2 3 0.060607 -0.994614 0.084082 -58.08184 1 MTRIX3 3 0.429286 0.102021 0.897388 8.35642 1