HEADER VIRAL PROTEIN 22-FEB-24 8W3R TITLE CRYSTAL STRUCTURE OF PREFUSION-STABILIZED RSV F PROTEIN UFCR2-ISS-P2- TITLE 2 NQ IN COMPLEX WITH A4 SINGLE-CHAIN FRAGMENT VARIABLE COMPND MOL_ID: 1; COMPND 2 MOLECULE: A4 SINGLE-CHAIN FRAGMENT VARIABLE; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: PREFUSION-STABILIZED RSV F PROTEIN UFCR2-ISS-P2-NQ; COMPND 7 CHAIN: F; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; 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_COMMON: HUMAN; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS RESPIRATORY SYNCYTIAL VIRUS, GLYCOPROTEIN, PREFUSION VACCINE, KEYWDS 2 STABILIZED, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.Z.LEE,R.L.STANFIELD,I.A.WILSON,J.ZHU REVDAT 1 15-JAN-25 8W3R 0 JRNL AUTH Y.Z.LEE,J.HAN,Y.N.ZHANG,G.WARD,K.BRAZ GOMES,S.AUCLAIR, JRNL AUTH 2 R.L.STANFIELD,L.HE,I.A.WILSON,J.ZHU JRNL TITL RATIONAL DESIGN OF UNCLEAVED PREFUSION-CLOSED TRIMER JRNL TITL 2 VACCINES FOR HUMAN RESPIRATORY SYNCYTIAL VIRUS AND JRNL TITL 3 METAPNEUMOVIRUS. JRNL REF NAT COMMUN V. 15 9939 2024 JRNL REFN ESSN 2041-1723 JRNL PMID 39550381 JRNL DOI 10.1038/S41467-024-54287-X REMARK 2 REMARK 2 RESOLUTION. 4.02 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.02 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.12 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8 REMARK 3 NUMBER OF REFLECTIONS : 9470 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.252 REMARK 3 R VALUE (WORKING SET) : 0.249 REMARK 3 FREE R VALUE : 0.303 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.480 REMARK 3 FREE R VALUE TEST SET COUNT : 424 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 50.1200 - 5.8000 0.99 3295 138 0.2341 0.2754 REMARK 3 2 5.8000 - 4.6100 0.99 3097 172 0.2577 0.3027 REMARK 3 3 4.1700 - 4.0200 0.85 2654 114 0.2689 0.3533 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) : 0.523 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.384 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 84.78 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 109.9 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 : 0.005 5312 REMARK 3 ANGLE : 1.094 7212 REMARK 3 CHIRALITY : 0.058 844 REMARK 3 PLANARITY : 0.008 915 REMARK 3 DIHEDRAL : 4.535 736 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 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8W3R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-24. REMARK 100 THE DEPOSITION ID IS D_1000280353. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-SEP-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 : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9477 REMARK 200 RESOLUTION RANGE HIGH (A) : 4.020 REMARK 200 RESOLUTION RANGE LOW (A) : 50.120 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 16.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.02 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.17 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.63 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 5.87, 10 %(W/V) PEG REMARK 280 6,000., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 50.12000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 28.93680 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 196.07267 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 50.12000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 28.93680 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 196.07267 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 50.12000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 28.93680 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 196.07267 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 50.12000 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 28.93680 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 196.07267 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 50.12000 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 28.93680 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 196.07267 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 50.12000 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 28.93680 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 196.07267 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 57.87359 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 392.14533 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 57.87359 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 392.14533 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 57.87359 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 392.14533 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 57.87359 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 392.14533 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 57.87359 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 392.14533 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 57.87359 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 392.14533 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, F 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 GLY A 114 REMARK 465 GLY A 115 REMARK 465 GLY A 116 REMARK 465 SER A 117 REMARK 465 GLY A 118 REMARK 465 GLY A 119 REMARK 465 GLY A 120 REMARK 465 GLY A 121 REMARK 465 SER A 122 REMARK 465 GLY A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 GLY A 126 REMARK 465 SER A 127 REMARK 465 THR A 234 REMARK 465 SER A 235 REMARK 465 GLY A 236 REMARK 465 PRO A 237 REMARK 465 GLY A 238 REMARK 465 GLY A 239 REMARK 465 PRO A 240 REMARK 465 GLU A 241 REMARK 465 PRO A 242 REMARK 465 LYS A 243 REMARK 465 SER A 244 REMARK 465 SER A 245 REMARK 465 ASP A 246 REMARK 465 LYS A 247 REMARK 465 GLY A 248 REMARK 465 SER A 249 REMARK 465 HIS A 250 REMARK 465 HIS A 251 REMARK 465 HIS A 252 REMARK 465 HIS A 253 REMARK 465 HIS A 254 REMARK 465 HIS A 255 REMARK 465 MET F -3 REMARK 465 GLY F -2 REMARK 465 ILE F -1 REMARK 465 LEU F 0 REMARK 465 PRO F 1 REMARK 465 SER F 2 REMARK 465 PRO F 3 REMARK 465 GLY F 4 REMARK 465 MET F 5 REMARK 465 PRO F 6 REMARK 465 ALA F 7 REMARK 465 LEU F 8 REMARK 465 LEU F 9 REMARK 465 SER F 10 REMARK 465 LEU F 11 REMARK 465 VAL F 12 REMARK 465 SER F 13 REMARK 465 LEU F 14 REMARK 465 LEU F 15 REMARK 465 SER F 16 REMARK 465 VAL F 17 REMARK 465 LEU F 18 REMARK 465 LEU F 19 REMARK 465 MET F 20 REMARK 465 GLY F 21 REMARK 465 CYS F 22 REMARK 465 VAL F 23 REMARK 465 ALA F 24 REMARK 465 GLU F 25 REMARK 465 ASP F 510 REMARK 465 GLU F 511 REMARK 465 LEU F 512 REMARK 465 LEU F 513 REMARK 465 ALA F 514 REMARK 465 SER F 515 REMARK 465 GLY F 516 REMARK 465 TYR F 517 REMARK 465 ILE F 518 REMARK 465 PRO F 519 REMARK 465 GLU F 520 REMARK 465 ALA F 521 REMARK 465 PRO F 522 REMARK 465 ARG F 523 REMARK 465 ASP F 524 REMARK 465 GLY F 525 REMARK 465 GLN F 526 REMARK 465 ALA F 527 REMARK 465 TYR F 528 REMARK 465 VAL F 529 REMARK 465 ARG F 530 REMARK 465 LYS F 531 REMARK 465 ASP F 532 REMARK 465 GLY F 533 REMARK 465 GLU F 534 REMARK 465 TRP F 535 REMARK 465 VAL F 536 REMARK 465 LEU F 537 REMARK 465 LEU F 538 REMARK 465 SER F 539 REMARK 465 THR F 540 REMARK 465 PHE F 541 REMARK 465 LEU F 542 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 CB CYS F 149 SG CYS F 458 3455 1.72 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 GLN A 39 114.85 -160.40 REMARK 500 LEU A 48 -72.47 -128.45 REMARK 500 HIS A 100 13.49 56.38 REMARK 500 PHE A 100G 53.27 -146.03 REMARK 500 ALA A 135 -51.85 -122.08 REMARK 500 SER A 153 -61.88 66.59 REMARK 500 VAL A 153C -55.67 67.84 REMARK 500 PRO A 166 108.23 -55.28 REMARK 500 ASP A 176 -104.92 58.15 REMARK 500 VAL A 177 -30.09 -133.36 REMARK 500 SER A 193 89.21 -151.13 REMARK 500 SER A 219 -17.92 73.38 REMARK 500 LYS F 65 74.97 -114.74 REMARK 500 LYS F 68 127.16 -36.10 REMARK 500 THR F 72 -50.27 -142.76 REMARK 500 THR F 100 50.10 -111.36 REMARK 500 LEU F 171 36.54 -92.41 REMARK 500 CYS F 290 -102.91 -95.04 REMARK 500 SER F 362 -126.45 49.42 REMARK 500 ASN F 371 66.85 -118.19 REMARK 500 PHE F 488 -132.94 63.24 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 THR F 408 -11.83 REMARK 500 REMARK 500 REMARK: NULL DBREF 8W3R A 1 255 PDB 8W3R 8W3R 1 255 DBREF 8W3R F -3 542 PDB 8W3R 8W3R -3 542 SEQRES 1 A 272 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 272 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 272 PHE THR PHE THR THR TYR ALA MET HIS TRP VAL ARG GLN SEQRES 4 A 272 SER PRO GLY LYS GLY LEU GLU TRP LEU ALA SER ILE SER SEQRES 5 A 272 TYR ASP GLY THR SER GLN TYR TYR ALA GLU SER VAL LYS SEQRES 6 A 272 GLY ARG PHE THR VAL SER ARG ASP ASN SER LYS LYS THR SEQRES 7 A 272 LEU LEU LEU GLN VAL ASN SER LEU ARG PRO GLU ASP THR SEQRES 8 A 272 ALA VAL TYR TYR CYS ALA GLY SER PRO SER GLY HIS TYR SEQRES 9 A 272 SER TRP LEU GLY TYR PHE TYR ALA MET ASP VAL TRP GLY SEQRES 10 A 272 GLN GLY THR VAL THR VAL SER SER GLY GLY GLY GLY SER SEQRES 11 A 272 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLN SER ALA SEQRES 12 A 272 LEU THR GLN PRO ALA SER VAL SER GLY SER PRO GLY GLN SEQRES 13 A 272 SER ILE THR ILE SER CYS THR GLY ALA SER SER ASP VAL SEQRES 14 A 272 GLY GLY TYR ASP TYR VAL SER TRP TYR GLN GLN HIS PRO SEQRES 15 A 272 GLY LYS ALA PRO LYS LEU LEU ILE TYR ASP VAL SER ASP SEQRES 16 A 272 ARG PRO SER GLY VAL SER ASN ARG PHE SER GLY SER LYS SEQRES 17 A 272 SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU GLN SEQRES 18 A 272 THR GLU ASP GLU ALA ASP TYR TYR CYS SER SER TYR THR SEQRES 19 A 272 SER LYS ASN THR LEU ILE PHE GLY GLY GLY THR LYS LEU SEQRES 20 A 272 THR VAL LEU THR SER GLY PRO GLY GLY PRO GLU PRO LYS SEQRES 21 A 272 SER SER ASP LYS GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 507 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 F 507 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 F 507 VAL ALA GLU GLN ASN ILE THR GLU GLU PHE TYR GLN SER SEQRES 4 F 507 THR CYS SER ALA VAL SER LYS GLY TYR LEU GLY ALA LEU SEQRES 5 F 507 ARG THR GLY TRP TYR THR SER VAL ILE THR ILE GLU LEU SEQRES 6 F 507 SER ASN ILE LYS GLU ASN LYS CYS ASN GLY THR ASP ALA SEQRES 7 F 507 LYS VAL LYS LEU ILE LYS GLN GLU LEU ASP LYS TYR LYS SEQRES 8 F 507 ASN ALA VAL THR ASP LEU GLN LEU LEU MET GLN SER THR SEQRES 9 F 507 PRO ALA THR GLY SER GLY SER ALA ILE CYS SER GLY VAL SEQRES 10 F 507 ALA VAL CYS LYS VAL LEU HIS LEU GLU GLY GLU VAL ASN SEQRES 11 F 507 LYS ILE LYS SER ALA LEU LEU SER THR ASN LYS ALA VAL SEQRES 12 F 507 VAL SER LEU SER ASN GLY PRO SER VAL LEU THR SER LYS SEQRES 13 F 507 VAL LEU ASP LEU LYS ASN TYR ILE ASP LYS GLN LEU LEU SEQRES 14 F 507 PRO ILE VAL ASN LYS GLN SER CYS SER ILE PRO ASN ILE SEQRES 15 F 507 GLU THR VAL ILE GLU PHE GLN GLN LYS ASN ASN ARG LEU SEQRES 16 F 507 LEU GLU ILE THR ARG GLU PHE SER VAL ASN ALA GLY VAL SEQRES 17 F 507 THR THR PRO VAL SER THR TYR MET LEU THR ASN SER GLU SEQRES 18 F 507 LEU LEU SER LEU ILE ASN ASP MET PRO ILE THR ASN ASP SEQRES 19 F 507 GLN LYS LYS LEU MET SER ASN ASN VAL GLN ILE VAL ARG SEQRES 20 F 507 GLN GLN SER TYR SER ILE MET CYS ILE ILE LYS GLU GLU SEQRES 21 F 507 VAL LEU ALA TYR VAL VAL GLN LEU PRO LEU TYR GLY VAL SEQRES 22 F 507 ILE ASP THR PRO CYS TRP LYS LEU HIS THR SER PRO LEU SEQRES 23 F 507 CYS THR THR ASN THR LYS GLU GLY SER ASN ILE CYS LEU SEQRES 24 F 507 THR ARG THR ASP ARG GLY TRP TYR CYS ASP ASN ALA GLY SEQRES 25 F 507 SER VAL SER PHE PHE PRO GLN ALA GLU THR CYS LYS VAL SEQRES 26 F 507 GLN SER ASN ARG VAL PHE CYS ASP THR MET ASN SER LEU SEQRES 27 F 507 THR LEU PRO SER GLU VAL ASN LEU CYS ASN VAL ASP ILE SEQRES 28 F 507 PHE ASN PRO LYS TYR ASP CYS LYS ILE MET THR SER LYS SEQRES 29 F 507 THR ASP VAL SER SER SER VAL ILE THR SER LEU GLY ALA SEQRES 30 F 507 ILE VAL SER CYS TYR GLY LYS THR LYS CYS THR ALA SER SEQRES 31 F 507 ASN LYS ASN ARG GLY ILE ILE LYS THR PHE SER ASN GLY SEQRES 32 F 507 CYS ASP TYR VAL SER ASN LYS GLY VAL ASP THR VAL SER SEQRES 33 F 507 VAL GLY ASN THR LEU TYR CYS VAL ASN LYS GLN GLU GLY SEQRES 34 F 507 GLN SER LEU TYR VAL LYS GLY GLU PRO ILE ILE ASN PHE SEQRES 35 F 507 TYR ASP PRO LEU VAL PHE PRO SER ASN GLN PHE ASP ALA SEQRES 36 F 507 SER ILE SER GLN VAL ASN GLU LYS ILE ASN GLN SER LEU SEQRES 37 F 507 ALA PHE ILE ARG LYS SER ASP GLU LEU LEU ALA SER GLY SEQRES 38 F 507 TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL SEQRES 39 F 507 ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU HET NAG F 601 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 3 NAG C8 H15 N O6 HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 GLU A 61 LYS A 64 5 4 HELIX 3 AA3 ARG A 84 THR A 88 5 5 HELIX 4 AA4 TRP A 100C TYR A 100H 5 6 HELIX 5 AA5 ASP F 73 SER F 99 1 27 HELIX 6 AA6 ILE F 148 HIS F 159 1 12 HELIX 7 AA7 GLY F 162 LEU F 171 1 10 HELIX 8 AA8 LEU F 195 LEU F 203 1 9 HELIX 9 AA9 LEU F 203 ASN F 208 1 6 HELIX 10 AB1 ASN F 216 ASN F 240 1 25 HELIX 11 AB2 THR F 253 ASP F 263 1 11 HELIX 12 AB3 THR F 267 ASN F 277 1 11 HELIX 13 AB4 ASN F 277 GLN F 284 1 8 HELIX 14 AB5 GLN F 354 GLU F 356 5 3 HELIX 15 AB6 MET F 370 SER F 372 5 3 HELIX 16 AB7 PRO F 376 ASN F 383 5 8 HELIX 17 AB8 PRO F 473 TYR F 478 5 6 HELIX 18 AB9 SER F 491 LYS F 508 1 18 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 SER A 17 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 THR A 77 ASN A 83A-1 O VAL A 82 N LEU A 18 SHEET 4 AA1 4 PHE A 67 ASP A 72 -1 N SER A 70 O LEU A 79 SHEET 1 AA2 6 GLY A 10 LEU A 11 0 SHEET 2 AA2 6 THR A 107 VAL A 110 1 O VAL A 110 N GLY A 10 SHEET 3 AA2 6 ALA A 89 SER A 96 -1 N TYR A 91 O THR A 107 SHEET 4 AA2 6 ALA A 33 GLN A 39 -1 N VAL A 37 O TYR A 92 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA2 6 GLN A 57 TYR A 59 -1 O TYR A 58 N SER A 50 SHEET 1 AA3 5 SER A 136 GLY A 139 0 SHEET 2 AA3 5 THR A 228 VAL A 232 1 O THR A 231 N GLY A 139 SHEET 3 AA3 5 ASP A 211 TYR A 217 -1 N TYR A 212 O THR A 228 SHEET 4 AA3 5 VAL A 159 GLN A 164 -1 N SER A 160 O SER A 215 SHEET 5 AA3 5 PRO A 170 ILE A 174 -1 O LYS A 171 N GLN A 163 SHEET 1 AA4 4 SER A 136 GLY A 139 0 SHEET 2 AA4 4 THR A 228 VAL A 232 1 O THR A 231 N GLY A 139 SHEET 3 AA4 4 ASP A 211 TYR A 217 -1 N TYR A 212 O THR A 228 SHEET 4 AA4 4 LEU A 222 PHE A 224 -1 O ILE A 223 N SER A 216 SHEET 1 AA5 3 SER A 144 THR A 150 0 SHEET 2 AA5 3 THR A 196 SER A 202 -1 O ALA A 197 N CYS A 149 SHEET 3 AA5 3 SER A 189 SER A 193 -1 N SER A 189 O THR A 200 SHEET 1 AA6 7 CYS F 358 GLN F 361 0 SHEET 2 AA6 7 ARG F 364 ASP F 368 -1 O PHE F 366 N LYS F 359 SHEET 3 AA6 7 SER F 38 ARG F 49 1 N ARG F 49 O CYS F 367 SHEET 4 AA6 7 VAL F 308 THR F 318 -1 O THR F 311 N GLY F 46 SHEET 5 AA6 7 GLY F 340 ASN F 345 -1 O TYR F 342 N TRP F 314 SHEET 6 AA6 7 SER F 348 PHE F 352 -1 O SER F 350 N CYS F 343 SHEET 7 AA6 7 LEU F 373 LEU F 375 -1 O LEU F 373 N PHE F 351 SHEET 1 AA7 5 CYS F 358 GLN F 361 0 SHEET 2 AA7 5 ARG F 364 ASP F 368 -1 O PHE F 366 N LYS F 359 SHEET 3 AA7 5 SER F 38 ARG F 49 1 N ARG F 49 O CYS F 367 SHEET 4 AA7 5 THR F 29 TYR F 33 -1 N TYR F 33 O SER F 38 SHEET 5 AA7 5 GLN F 465 VAL F 469 1 O VAL F 469 N PHE F 32 SHEET 1 AA8 6 LYS F 176 SER F 180 0 SHEET 2 AA8 6 SER F 186 ASP F 194 -1 O THR F 189 N ALA F 177 SHEET 3 AA8 6 GLY F 51 GLU F 60 1 N THR F 58 O SER F 190 SHEET 4 AA8 6 VAL F 296 LEU F 305 -1 O TYR F 299 N ILE F 57 SHEET 5 AA8 6 TYR F 286 ILE F 292 -1 N TYR F 286 O GLN F 302 SHEET 6 AA8 6 VAL F 243 THR F 244 -1 N THR F 244 O SER F 287 SHEET 1 AA9 4 LEU F 321 CYS F 322 0 SHEET 2 AA9 4 CYS F 333 ARG F 336 -1 O LEU F 334 N LEU F 321 SHEET 3 AA9 4 ILE F 395 SER F 398 -1 O SER F 398 N CYS F 333 SHEET 4 AA9 4 ASP F 489 ALA F 490 -1 O ALA F 490 N ILE F 395 SHEET 1 AB1 3 SER F 404 THR F 408 0 SHEET 2 AB1 3 GLY F 411 CYS F 416 -1 O SER F 415 N SER F 404 SHEET 3 AB1 3 GLY F 438 SER F 443 -1 O GLY F 438 N CYS F 416 SHEET 1 AB2 3 CYS F 422 THR F 423 0 SHEET 2 AB2 3 THR F 449 VAL F 452 -1 O SER F 451 N THR F 423 SHEET 3 AB2 3 THR F 455 CYS F 458 -1 O TYR F 457 N VAL F 450 SSBOND 1 CYS A 22 CYS A 93 1555 1555 2.04 SSBOND 2 CYS A 149 CYS A 214 1555 1555 2.04 SSBOND 3 CYS F 37 CYS F 439 1555 1555 2.04 SSBOND 4 CYS F 69 CYS F 212 1555 1555 2.03 SSBOND 5 CYS F 149 CYS F 458 1555 3455 2.04 SSBOND 6 CYS F 155 CYS F 290 1555 1555 2.04 SSBOND 7 CYS F 313 CYS F 343 1555 1555 2.04 SSBOND 8 CYS F 322 CYS F 333 1555 1555 2.04 SSBOND 9 CYS F 358 CYS F 367 1555 1555 2.03 SSBOND 10 CYS F 382 CYS F 393 1555 1555 2.01 SSBOND 11 CYS F 416 CYS F 422 1555 1555 2.03 LINK ND2 ASN F 500 C1 NAG F 601 1555 1555 1.45 CISPEP 1 THR F 245 PRO F 246 0 2.32 CRYST1 100.240 100.240 588.218 90.00 90.00 120.00 H 3 2 18 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 0.009976 0.005760 0.000000 0.00000 SCALE2 0.000000 0.011519 0.000000 0.00000 SCALE3 0.000000 0.000000 0.001700 0.00000