HEADER VIRAL PROTEIN 05-NOV-24 9KEF TITLE CRYSTAL STRUCUTRE OF RABV-G IN COMPLEX WITH SOJB-FAB COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: RABV-G; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SOJB-FAB HCHAIN; COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: SOJB-FAB LCHIAN; COMPND 11 CHAIN: L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RABIES VIRUS CVS-11; SOURCE 3 ORGANISM_TAXID: 11294; SOURCE 4 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 274590; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 274590 KEYWDS RABIES VIRUS, GLYCOPROTEIN, NEUTRALIZING ANTIBODY, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.LU,F.YANG,S.LIN REVDAT 1 23-APR-25 9KEF 0 JRNL AUTH F.YANG,L.ZHAI,K.YIN,S.LIN,J.YANG,F.YE,Z.CHEN,S.SHU,Y.YU, JRNL AUTH 2 L.GUO,B.HE,W.WANG,H.YE,Y.CAO,J.GAO,G.LU JRNL TITL MOLECULAR BASIS OF TWO BROAD-SPECTRUM ANTIBODIES JRNL TITL 2 NEUTRALIZING RABIES VIRUS AND OTHER PHYLOGROUP-I JRNL TITL 3 LYSSAVIRUSES BY BLOCKING STRUCTURAL TRANSITION BETWEEN THE JRNL TITL 4 PLECKSTRIN-HOMOLOGY AND FUSION DOMAINS IN THE GLYCOPROTEIN. JRNL REF INT.J.BIOL.MACROMOL. V. 308 42570 2025 JRNL REFN ISSN 0141-8130 JRNL PMID 40154685 JRNL DOI 10.1016/J.IJBIOMAC.2025.142570 REMARK 2 REMARK 2 RESOLUTION. 3.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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) : 3.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.84 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 16747 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.220 REMARK 3 R VALUE (WORKING SET) : 0.217 REMARK 3 FREE R VALUE : 0.264 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190 REMARK 3 FREE R VALUE TEST SET COUNT : 870 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 37.8400 - 6.1700 0.99 2838 183 0.2022 0.2427 REMARK 3 2 6.1700 - 4.9000 1.00 2761 156 0.2054 0.2494 REMARK 3 3 4.9000 - 4.2800 0.97 2639 191 0.1694 0.2403 REMARK 3 4 4.2800 - 3.8900 0.94 2608 120 0.2249 0.2868 REMARK 3 5 3.8900 - 3.6100 0.92 2538 106 0.2743 0.3324 REMARK 3 6 3.6100 - 3.4000 0.91 2493 114 0.3241 0.3971 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) : 0.530 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.620 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 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 : 0.012 6257 REMARK 3 ANGLE : 1.393 8502 REMARK 3 CHIRALITY : 0.075 965 REMARK 3 PLANARITY : 0.011 1079 REMARK 3 DIHEDRAL : 7.848 840 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -19.9637 29.3177 -43.7434 REMARK 3 T TENSOR REMARK 3 T11: 0.6077 T22: 0.7181 REMARK 3 T33: 0.7343 T12: 0.0094 REMARK 3 T13: -0.0141 T23: 0.0506 REMARK 3 L TENSOR REMARK 3 L11: 0.5620 L22: 1.1479 REMARK 3 L33: 0.7548 L12: 0.3947 REMARK 3 L13: -0.2693 L23: -0.5348 REMARK 3 S TENSOR REMARK 3 S11: -0.0115 S12: -0.0146 S13: 0.0338 REMARK 3 S21: -0.0721 S22: -0.1433 S23: -0.3135 REMARK 3 S31: 0.0010 S32: 0.1796 S33: 0.1707 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9KEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300053369. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-JUL-19 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 : SSRF REMARK 200 BEAMLINE : BL19U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17375 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 5.100 REMARK 200 R MERGE (I) : 0.13700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.5400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.11100 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 (%): 61.08 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 27 MM SODIUM FLUORIDE, 27 MM SODIUM REMARK 280 BROMIDE, 27 MM SODIUM IODIDE,100 MM TRIS AND 100 MM BACINE (PH REMARK 280 8.5), 20% V/V GLYCEROL, 10% W/V PEG 4000, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 289K 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 95.62400 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 95.62400 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 42.09200 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.20850 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.09200 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.20850 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 95.62400 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.09200 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.20850 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 95.62400 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.09200 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.20850 REMARK 290 SMTRY3 8 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 14010 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 76260 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A 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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 -42.09200 REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 77.20850 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 95.62400 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -42.09200 REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 -77.20850 REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 -95.62400 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 LYS A 1 REMARK 465 THR A 68 REMARK 465 GLU A 69 REMARK 465 ALA A 70 REMARK 465 GLU A 71 REMARK 465 THR A 72 REMARK 465 TYR A 73 REMARK 465 THR A 74 REMARK 465 GLY A 75 REMARK 465 GLY A 76 REMARK 465 SER A 77 REMARK 465 GLY A 78 REMARK 465 GLY A 79 REMARK 465 THR A 80 REMARK 465 THR A 81 REMARK 465 PHE A 82 REMARK 465 LYS A 83 REMARK 465 ARG A 84 REMARK 465 SER A 115 REMARK 465 LEU A 116 REMARK 465 HIS A 117 REMARK 465 ASN A 118 REMARK 465 PRO A 119 REMARK 465 TYR A 120 REMARK 465 GLY A 121 REMARK 465 GLY A 122 REMARK 465 SER A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 ARG A 126 REMARK 465 THR A 127 REMARK 465 THR A 128 REMARK 465 LYS A 129 REMARK 465 LEU A 260 REMARK 465 HIS A 261 REMARK 465 ASP A 262 REMARK 465 PHE A 263 REMARK 465 ARG A 264 REMARK 465 SER A 265 REMARK 465 ASP A 266 REMARK 465 GLU A 267 REMARK 465 ILE A 268 REMARK 465 GLU A 269 REMARK 465 HIS A 270 REMARK 465 LEU A 271 REMARK 465 VAL A 272 REMARK 465 VAL A 273 REMARK 465 GLU A 274 REMARK 465 GLU A 275 REMARK 465 GLY A 366 REMARK 465 PRO A 367 REMARK 465 HIS A 419 REMARK 465 LEU A 420 REMARK 465 PRO A 421 REMARK 465 ASP A 422 REMARK 465 VAL A 423 REMARK 465 TYR A 424 REMARK 465 LYS A 425 REMARK 465 GLN A 426 REMARK 465 ILE A 427 REMARK 465 SER A 428 REMARK 465 GLY A 429 REMARK 465 VAL A 430 REMARK 465 ASP A 431 REMARK 465 LEU A 432 REMARK 465 GLY A 433 REMARK 465 LEU A 434 REMARK 465 PRO A 435 REMARK 465 ASN A 436 REMARK 465 TRP A 437 REMARK 465 GLY A 438 REMARK 465 LYS A 439 REMARK 465 HIS A 440 REMARK 465 HIS A 441 REMARK 465 HIS A 442 REMARK 465 HIS A 443 REMARK 465 HIS A 444 REMARK 465 HIS A 445 REMARK 465 SER H 136 REMARK 465 SER H 137 REMARK 465 LYS H 138 REMARK 465 SER H 139 REMARK 465 THR H 140 REMARK 465 SER H 141 REMARK 465 GLY H 142 REMARK 465 GLY H 171 REMARK 465 VAL H 172 REMARK 465 SER H 224 REMARK 465 CYS H 225 REMARK 465 ASP H 226 REMARK 465 LYS H 227 REMARK 465 THR H 228 REMARK 465 HIS H 229 REMARK 465 THR H 230 REMARK 465 GLY H 231 REMARK 465 GLY H 232 REMARK 465 SER H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 HIS H 239 REMARK 465 GLN L 109 REMARK 465 ALA L 145 REMARK 465 TYR L 174 REMARK 465 GLU L 214 REMARK 465 CYS L 215 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 ASP A 369 CG OD1 OD2 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 NE2 GLN L 167 O SER L 172 1.99 REMARK 500 NH2 ARG H 68 OD2 ASP H 91 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD1 ASN A 182 CD PRO L 205 3554 2.05 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 THR A 245 CB - CA - C ANGL. DEV. = -17.2 DEGREES REMARK 500 SER A 246 N - CA - CB ANGL. DEV. = -13.3 DEGREES REMARK 500 PRO A 309 CB - CA - C ANGL. DEV. = -14.0 DEGREES REMARK 500 LEU A 381 CB - CA - C ANGL. DEV. = -16.0 DEGREES REMARK 500 LEU A 381 CA - CB - CG ANGL. DEV. = 14.4 DEGREES REMARK 500 VAL A 392 CB - CA - C ANGL. DEV. = 12.5 DEGREES REMARK 500 GLU A 411 CB - CA - C ANGL. DEV. = 12.5 DEGREES REMARK 500 GLU A 411 N - CA - CB ANGL. DEV. = 20.7 DEGREES REMARK 500 GLU A 411 N - CA - C ANGL. DEV. = -38.5 DEGREES REMARK 500 PHE A 415 N - CA - C ANGL. DEV. = -19.1 DEGREES REMARK 500 PHE H 24 CB - CA - C ANGL. DEV. = -15.5 DEGREES REMARK 500 SER H 25 N - CA - CB ANGL. DEV. = -13.6 DEGREES REMARK 500 ARG H 40 CB - CA - C ANGL. DEV. = -12.8 DEGREES REMARK 500 ASP H 74 N - CA - C ANGL. DEV. = -17.8 DEGREES REMARK 500 ALA H 123 N - CA - CB ANGL. DEV. = 10.8 DEGREES REMARK 500 THR H 144 CB - CA - C ANGL. DEV. = 16.5 DEGREES REMARK 500 ALA H 145 N - CA - CB ANGL. DEV. = 10.4 DEGREES REMARK 500 GLU L 82 N - CA - C ANGL. DEV. = -17.7 DEGREES REMARK 500 ALA L 83 N - CA - CB ANGL. DEV. = 10.4 DEGREES REMARK 500 SER L 169 CB - CA - C ANGL. DEV. = 12.0 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 ASP A 18 -167.82 -109.95 REMARK 500 SER A 23 141.44 -172.16 REMARK 500 GLU A 45 148.14 -171.49 REMARK 500 ASP A 105 -66.68 -96.16 REMARK 500 LYS A 147 19.74 49.51 REMARK 500 SER A 151 146.46 -178.99 REMARK 500 TYR A 175 38.96 -85.75 REMARK 500 LEU A 235 -67.35 -90.84 REMARK 500 THR A 239 122.22 -37.87 REMARK 500 ILE A 364 -168.56 -126.42 REMARK 500 LEU A 399 1.32 -69.01 REMARK 500 ASP H 56 43.07 -94.57 REMARK 500 PHE H 155 -78.67 -109.27 REMARK 500 THR H 200 -51.35 -126.30 REMARK 500 ASN H 213 35.07 37.49 REMARK 500 ASN L 50 -84.56 98.58 REMARK 500 PRO L 54 171.77 -54.33 REMARK 500 ASN L 68 30.32 -88.98 REMARK 500 ALA L 112 -168.18 -107.26 REMARK 500 ASN L 139 8.04 80.90 REMARK 500 TYR L 141 103.05 -174.68 REMARK 500 PRO L 142 -173.07 -69.47 REMARK 500 GLU L 166 -159.38 -102.34 REMARK 500 SER L 172 8.21 99.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 GLU H 157 PRO H 158 33.95 REMARK 500 TYR L 141 PRO L 142 31.22 REMARK 500 REMARK 500 REMARK: NULL DBREF 9KEF A 1 445 PDB 9KEF 9KEF 1 445 DBREF 9KEF H 1 239 PDB 9KEF 9KEF 1 239 DBREF 9KEF L 1 215 PDB 9KEF 9KEF 1 215 SEQRES 1 A 439 LYS PHE PRO ILE TYR THR ILE PRO ASP GLU LEU GLY PRO SEQRES 2 A 439 TRP SER PRO ILE ASP ILE HIS HIS LEU SER CYS PRO ASN SEQRES 3 A 439 ASN LEU VAL VAL GLU ASP GLU GLY CYS THR ASN LEU SER SEQRES 4 A 439 GLU PHE SER TYR MET GLU LEU LYS VAL GLY TYR ILE SER SEQRES 5 A 439 ALA ILE LYS VAL ASN GLY PHE THR CYS THR GLY VAL VAL SEQRES 6 A 439 THR GLU ALA GLU THR TYR THR GLY GLY SER GLY GLY THR SEQRES 7 A 439 THR PHE LYS ARG LYS HIS PHE ARG PRO THR PRO ASP ALA SEQRES 8 A 439 CYS ARG ALA ALA TYR ASN TRP LYS MET ALA GLY ASP PRO SEQRES 9 A 439 ARG TYR GLU GLU SER LEU HIS ASN PRO TYR GLY GLY SER SEQRES 10 A 439 GLY GLY ARG THR THR LYS GLU SER LEU ILE ILE ILE SER SEQRES 11 A 439 PRO SER VAL THR ASP LEU ASP PRO TYR ASP LYS SER LEU SEQRES 12 A 439 HIS SER ARG VAL PHE PRO GLY GLY LYS CYS SER GLY ILE SEQRES 13 A 439 THR VAL SER SER THR TYR CYS SER THR ASN HIS ASP TYR SEQRES 14 A 439 THR ILE TRP MET PRO GLU ASN PRO ARG PRO ARG THR PRO SEQRES 15 A 439 CYS ASP ILE PHE THR ASN SER ARG GLY LYS ARG ALA SER SEQRES 16 A 439 ASN GLY ASN LYS THR CYS GLY PHE VAL ASP GLU ARG GLY SEQRES 17 A 439 LEU TYR LYS SER LEU LYS GLY ALA CYS ARG LEU LYS LEU SEQRES 18 A 439 CYS GLY VAL LEU GLY LEU ARG LEU MET ASP GLY THR TRP SEQRES 19 A 439 VAL ALA MET GLN THR SER ASP GLU THR LYS TRP CYS PRO SEQRES 20 A 439 PRO ASP GLN LEU VAL ASN LEU HIS ASP PHE ARG SER ASP SEQRES 21 A 439 GLU ILE GLU HIS LEU VAL VAL GLU GLU LEU VAL LYS LYS SEQRES 22 A 439 ARG GLU GLU CYS LEU ASP ALA LEU GLU SER ILE MET THR SEQRES 23 A 439 THR LYS SER VAL SER PHE ARG ARG LEU SER HIS LEU ARG SEQRES 24 A 439 LYS LEU VAL PRO GLY PHE GLY LYS ALA TYR THR ILE PHE SEQRES 25 A 439 ASN LYS THR LEU MET GLU ALA ASP ALA HIS TYR LYS SER SEQRES 26 A 439 VAL ARG THR TRP ASN GLU ILE ILE PRO SER LYS GLY CYS SEQRES 27 A 439 LEU LYS VAL GLY GLY ARG CYS HIS PRO HIS VAL ASN GLY SEQRES 28 A 439 VAL PHE PHE ASN GLY ILE ILE LEU GLY PRO ASP ASP HIS SEQRES 29 A 439 VAL LEU ILE PRO GLU MET GLN SER SER LEU LEU GLN GLN SEQRES 30 A 439 HIS MET GLU LEU LEU LYS SER SER VAL ILE PRO LEU MET SEQRES 31 A 439 HIS PRO LEU ALA ASP PRO SER THR VAL PHE LYS GLU GLY SEQRES 32 A 439 ASP GLU ALA GLU ASP PHE VAL GLU VAL HIS LEU PRO ASP SEQRES 33 A 439 VAL TYR LYS GLN ILE SER GLY VAL ASP LEU GLY LEU PRO SEQRES 34 A 439 ASN TRP GLY LYS HIS HIS HIS HIS HIS HIS SEQRES 1 H 239 GLN ILE THR LEU LYS GLU THR GLY PRO THR LEU VAL LYS SEQRES 2 H 239 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 H 239 PHE SER LEU SER THR SER GLY VAL GLY VAL GLY TRP ILE SEQRES 4 H 239 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP VAL THR LEU SEQRES 5 H 239 ILE TYR TRP ASP ASP ASP LYS ARG TYR SER PRO SER LEU SEQRES 6 H 239 GLU ASN ARG VAL THR ILE ARG LYS ASP THR SER LYS ASN SEQRES 7 H 239 GLN VAL ALA LEU THR MET THR ASN MET ASP PRO LEU ASP SEQRES 8 H 239 THR GLY THR TYR TYR CYS ALA HIS ARG GLN HIS ILE SER SEQRES 9 H 239 SER PHE PRO TRP PHE ASP SER TRP GLY GLN GLY THR LEU SEQRES 10 H 239 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 239 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 239 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 239 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 239 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 239 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 239 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 239 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 239 PRO LYS SER CYS ASP LYS THR HIS THR GLY GLY SER HIS SEQRES 19 H 239 HIS HIS HIS HIS HIS SEQRES 1 L 215 SER TYR VAL LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 L 215 PRO GLY LYS THR ALA ARG ILE ASN CYS GLY GLY ASN ASN SEQRES 3 L 215 ILE GLU TYR ARG SER VAL HIS TRP TYR GLN GLN LYS SER SEQRES 4 L 215 GLY GLN ALA PRO VAL ALA VAL ILE TYR ASP ASN SER ASP SEQRES 5 L 215 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER LYS SEQRES 6 L 215 SER GLY ASN THR ALA THR LEU THR ILE SER ARG VAL GLU SEQRES 7 L 215 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 L 215 ILE SER SER ASP VAL VAL PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 215 THR VAL LEU GLY GLN PRO LYS 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 HET NAG A 501 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 4 NAG C8 H15 N O6 HELIX 1 AA1 THR A 90 MET A 102 1 13 HELIX 2 AA2 PHE A 154 GLY A 156 5 3 HELIX 3 AA3 VAL A 277 LYS A 294 1 18 HELIX 4 AA4 SER A 297 SER A 302 1 6 HELIX 5 AA5 HIS A 303 ARG A 305 5 3 HELIX 6 AA6 THR A 334 ILE A 338 5 5 HELIX 7 AA7 ILE A 373 SER A 390 1 18 HELIX 8 AA8 PRO H 63 GLU H 66 5 4 HELIX 9 AA9 ASP H 88 THR H 92 5 5 HELIX 10 AB1 LYS H 210 ASN H 213 5 4 HELIX 11 AB2 SER L 183 LYS L 189 1 7 SHEET 1 AA1 3 TYR A 5 LEU A 11 0 SHEET 2 AA1 3 THR A 321 VAL A 332 -1 O LYS A 330 N ILE A 7 SHEET 3 AA1 3 SER A 15 PRO A 16 -1 N SER A 15 O GLU A 324 SHEET 1 AA2 3 TYR A 5 LEU A 11 0 SHEET 2 AA2 3 THR A 321 VAL A 332 -1 O LYS A 330 N ILE A 7 SHEET 3 AA2 3 GLY A 310 PHE A 318 -1 N GLY A 310 O TYR A 329 SHEET 1 AA3 7 TYR A 216 SER A 218 0 SHEET 2 AA3 7 GLY A 208 VAL A 210 -1 N PHE A 209 O LYS A 217 SHEET 3 AA3 7 PHE A 192 SER A 201 -1 N ALA A 200 O GLY A 208 SHEET 4 AA3 7 ASN A 37 LEU A 46 -1 N GLU A 45 O THR A 193 SHEET 5 AA3 7 TRP A 240 ALA A 242 -1 O ALA A 242 N MET A 44 SHEET 6 AA3 7 VAL A 230 ARG A 234 -1 N LEU A 233 O VAL A 241 SHEET 7 AA3 7 CYS A 223 LEU A 227 -1 N LEU A 225 O GLY A 232 SHEET 1 AA4 6 LYS A 158 CYS A 159 0 SHEET 2 AA4 6 LEU A 149 HIS A 150 -1 N LEU A 149 O CYS A 159 SHEET 3 AA4 6 SER A 131 LEU A 142 -1 N ASP A 141 O HIS A 150 SHEET 4 AA4 6 LYS A 55 VAL A 64 -1 N GLY A 58 O SER A 138 SHEET 5 AA4 6 THR A 176 PRO A 180 -1 O ILE A 177 N CYS A 61 SHEET 6 AA4 6 CYS A 169 SER A 170 -1 N CYS A 169 O TRP A 178 SHEET 1 AA5 2 LYS A 346 VAL A 347 0 SHEET 2 AA5 2 ARG A 350 CYS A 351 -1 O ARG A 350 N VAL A 347 SHEET 1 AA6 4 LEU H 4 LYS H 5 0 SHEET 2 AA6 4 LEU H 18 PHE H 24 -1 O THR H 23 N LYS H 5 SHEET 3 AA6 4 GLN H 79 MET H 84 -1 O MET H 84 N LEU H 18 SHEET 4 AA6 4 VAL H 69 ASP H 74 -1 N THR H 70 O THR H 83 SHEET 1 AA7 6 LEU H 11 VAL H 12 0 SHEET 2 AA7 6 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA7 6 GLY H 93 ARG H 100 -1 N TYR H 95 O THR H 116 SHEET 4 AA7 6 GLY H 35 GLN H 41 -1 N GLY H 35 O ARG H 100 SHEET 5 AA7 6 GLU H 48 TYR H 54 -1 O VAL H 50 N TRP H 38 SHEET 6 AA7 6 LYS H 59 TYR H 61 -1 O ARG H 60 N LEU H 52 SHEET 1 AA8 4 LEU H 11 VAL H 12 0 SHEET 2 AA8 4 THR H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AA8 4 GLY H 93 ARG H 100 -1 N TYR H 95 O THR H 116 SHEET 4 AA8 4 PHE H 109 TRP H 112 -1 O SER H 111 N HIS H 99 SHEET 1 AA9 3 SER H 129 LEU H 133 0 SHEET 2 AA9 3 THR H 144 TYR H 154 -1 O GLY H 148 N LEU H 133 SHEET 3 AA9 3 TYR H 185 PRO H 194 -1 O TYR H 185 N TYR H 154 SHEET 1 AB1 3 THR H 160 TRP H 163 0 SHEET 2 AB1 3 TYR H 203 HIS H 209 -1 O ASN H 206 N SER H 162 SHEET 3 AB1 3 THR H 214 VAL H 220 -1 O VAL H 216 N VAL H 207 SHEET 1 AB2 4 LEU L 4 THR L 5 0 SHEET 2 AB2 4 ALA L 18 GLY L 24 -1 O GLY L 23 N THR L 5 SHEET 3 AB2 4 THR L 69 ILE L 74 -1 O ALA L 70 N CYS L 22 SHEET 4 AB2 4 PHE L 61 SER L 66 -1 N SER L 64 O THR L 71 SHEET 1 AB3 2 SER L 11 VAL L 12 0 SHEET 2 AB3 2 THR L 105 VAL L 106 1 O THR L 105 N VAL L 12 SHEET 1 AB4 4 VAL L 44 ILE L 47 0 SHEET 2 AB4 4 VAL L 32 GLN L 37 -1 N GLN L 36 O VAL L 44 SHEET 3 AB4 4 ASP L 84 VAL L 89 -1 O TYR L 86 N TYR L 35 SHEET 4 AB4 4 VAL L 97 PHE L 98 -1 O VAL L 97 N VAL L 89 SHEET 1 AB5 4 VAL L 44 ILE L 47 0 SHEET 2 AB5 4 VAL L 32 GLN L 37 -1 N GLN L 36 O VAL L 44 SHEET 3 AB5 4 ASP L 84 VAL L 89 -1 O TYR L 86 N TYR L 35 SHEET 4 AB5 4 THR L 102 LYS L 103 -1 O THR L 102 N TYR L 85 SHEET 1 AB6 4 SER L 115 PHE L 119 0 SHEET 2 AB6 4 SER L 132 ASN L 138 -1 O VAL L 134 N PHE L 119 SHEET 3 AB6 4 LEU L 176 THR L 181 -1 O LEU L 180 N VAL L 133 SHEET 4 AB6 4 GLN L 161 VAL L 164 -1 N SER L 163 O SER L 177 SHEET 1 AB7 4 ALA L 154 LEU L 155 0 SHEET 2 AB7 4 VAL L 147 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB7 4 TYR L 193 VAL L 197 -1 O ALA L 194 N LYS L 150 SHEET 4 AB7 4 VAL L 206 THR L 207 -1 O VAL L 206 N VAL L 197 SSBOND 1 CYS A 24 CYS A 283 1555 1555 2.06 SSBOND 2 CYS A 35 CYS A 207 1555 1555 2.01 SSBOND 3 CYS A 61 CYS A 94 1555 1555 2.02 SSBOND 4 CYS A 159 CYS A 169 1555 1555 2.04 SSBOND 5 CYS A 189 CYS A 228 1555 1555 2.05 SSBOND 6 CYS A 223 CYS A 252 1555 1555 2.04 SSBOND 7 CYS A 344 CYS A 351 1555 1555 2.04 SSBOND 8 CYS H 22 CYS H 97 1555 1555 2.03 SSBOND 9 CYS H 149 CYS H 205 1555 1555 2.04 SSBOND 10 CYS L 22 CYS L 87 1555 1555 2.05 SSBOND 11 CYS L 135 CYS L 195 1555 1555 2.04 LINK ND2 ASN A 319 C1 NAG A 501 1555 1555 1.51 CISPEP 1 SER A 136 PRO A 137 0 -7.65 CRYST1 84.184 154.417 191.248 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.011879 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006476 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005229 0.00000