HEADER VIRAL PROTEIN 15-JUL-24 9CN2 TITLE HUMAN ASTROVIRUS 2 SPIKE BOUND TO NEUTRALIZING SCFV 4B6 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NEUTRALIZING SCFV 4B6; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN ASTROVIRUS 2; SOURCE 3 ORGANISM_TAXID: 12701; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 STRAIN: BALB/C; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 EXPRESSION_SYSTEM_CELL: CHO-S KEYWDS ANTIBODY, SPIKE, HOMODIMER, NEUTRALIZATION, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.LANNING,R.M.DUBOIS REVDAT 1 25-DEC-24 9CN2 0 JRNL AUTH S.LANNING,R.M.DUBOIS,C.F.ARIAS JRNL TITL STRUCTURAL TECHNIQUES REVEAL 3 NOVEL NEUTRALIZING ANTIBODY JRNL TITL 2 EPITOPES ON THE HUMAN ASTROVIRUS SPIKE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.67 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) : 2.67 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.85 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 20583 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.700 REMARK 3 FREE R VALUE TEST SET COUNT : 1997 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 6.4100 - 5.1100 1.00 1379 149 0.1839 0.2162 REMARK 3 2 5.1000 - 4.4600 1.00 1342 144 0.1486 0.2074 REMARK 3 3 4.4600 - 4.0600 1.00 1328 143 0.1701 0.2279 REMARK 3 4 4.0500 - 3.7600 1.00 1334 144 0.2189 0.2483 REMARK 3 5 3.7600 - 3.5400 1.00 1315 140 0.2360 0.2451 REMARK 3 6 3.5400 - 3.3600 1.00 1308 142 0.2332 0.3025 REMARK 3 7 3.3600 - 3.2200 1.00 1315 139 0.2631 0.2924 REMARK 3 8 3.2200 - 3.0900 1.00 1298 139 0.3082 0.3865 REMARK 3 9 3.0900 - 2.9900 1.00 1289 139 0.3063 0.4146 REMARK 3 10 2.9900 - 2.8900 1.00 1319 142 0.2908 0.3423 REMARK 3 11 2.8900 - 2.8100 1.00 1287 138 0.2867 0.3136 REMARK 3 12 2.8100 - 2.7400 1.00 1299 140 0.2736 0.3586 REMARK 3 13 2.7400 - 2.6700 1.00 1294 139 0.3036 0.3318 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) : 0.340 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.950 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 : 0.009 NULL REMARK 3 ANGLE : 1.069 NULL REMARK 3 CHIRALITY : 0.059 539 REMARK 3 PLANARITY : 0.008 617 REMARK 3 DIHEDRAL : 6.662 479 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): -21.3371 20.8602 -10.2538 REMARK 3 T TENSOR REMARK 3 T11: 0.6335 T22: 0.3645 REMARK 3 T33: 0.3822 T12: 0.0377 REMARK 3 T13: 0.0239 T23: -0.0993 REMARK 3 L TENSOR REMARK 3 L11: 2.1328 L22: 0.3083 REMARK 3 L33: 1.4755 L12: -0.3468 REMARK 3 L13: 1.0708 L23: -0.8495 REMARK 3 S TENSOR REMARK 3 S11: -0.0474 S12: -0.2887 S13: 0.0174 REMARK 3 S21: 0.1856 S22: 0.0427 S23: -0.0184 REMARK 3 S31: -0.2248 S32: -0.1450 S33: -0.0043 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 9CN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1000284150. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-JUN-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20653 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.670 REMARK 200 RESOLUTION RANGE LOW (A) : 160.640 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 74.50 REMARK 200 R MERGE (I) : 0.19100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 23.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.72 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 3.29100 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: 4 SIDED DIAMOND SHAPE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.36 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.5, AND 0.74 M REMARK 280 SODIUM CITRATE PH 5.5, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 295.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 5555 Z,X,Y REMARK 290 6555 Z+1/2,-X+1/2,-Y REMARK 290 7555 -Z+1/2,-X,Y+1/2 REMARK 290 8555 -Z,X+1/2,-Y+1/2 REMARK 290 9555 Y,Z,X REMARK 290 10555 -Y,Z+1/2,-X+1/2 REMARK 290 11555 Y+1/2,-Z+1/2,-X REMARK 290 12555 -Y+1/2,-Z,X+1/2 REMARK 290 13555 Y+1/4,X+3/4,-Z+3/4 REMARK 290 14555 -Y+1/4,-X+1/4,-Z+1/4 REMARK 290 15555 Y+3/4,-X+3/4,Z+1/4 REMARK 290 16555 -Y+3/4,X+1/4,Z+3/4 REMARK 290 17555 X+1/4,Z+3/4,-Y+3/4 REMARK 290 18555 -X+3/4,Z+1/4,Y+3/4 REMARK 290 19555 -X+1/4,-Z+1/4,-Y+1/4 REMARK 290 20555 X+3/4,-Z+3/4,Y+1/4 REMARK 290 21555 Z+1/4,Y+3/4,-X+3/4 REMARK 290 22555 Z+3/4,-Y+3/4,X+1/4 REMARK 290 23555 -Z+3/4,Y+1/4,X+3/4 REMARK 290 24555 -Z+1/4,-Y+1/4,-X+1/4 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 80.17400 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.17400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 80.17400 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.17400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 80.17400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 80.17400 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 80.17400 REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 80.17400 REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 80.17400 REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 80.17400 REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 80.17400 REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 80.17400 REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 80.17400 REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 80.17400 REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 80.17400 REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 80.17400 REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 80.17400 REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 80.17400 REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 40.08700 REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 120.26100 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 120.26100 REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 40.08700 REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 40.08700 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 40.08700 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 120.26100 REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 120.26100 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 40.08700 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 120.26100 REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 40.08700 REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 120.26100 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 40.08700 REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 120.26100 REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 120.26100 REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 120.26100 REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 40.08700 REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 120.26100 REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 40.08700 REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 40.08700 REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 40.08700 REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 120.26100 REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 120.26100 REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 40.08700 REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 40.08700 REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 120.26100 REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 120.26100 REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 120.26100 REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 120.26100 REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 40.08700 REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 120.26100 REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 40.08700 REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 120.26100 REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 40.08700 REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 40.08700 REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 40.08700 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: TETRAMERIC 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -40.08700 REMARK 350 BIOMT2 2 0.000000 0.000000 1.000000 40.08700 REMARK 350 BIOMT3 2 0.000000 1.000000 0.000000 -40.08700 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 MET A 427 REMARK 465 GLY A 428 REMARK 465 ALA A 648 REMARK 465 GLU A 649 REMARK 465 LEU A 650 REMARK 465 ALA A 651 REMARK 465 LEU A 652 REMARK 465 VAL A 653 REMARK 465 PRO A 654 REMARK 465 ARG A 655 REMARK 465 SER B 117 REMARK 465 GLY B 118 REMARK 465 GLY B 119 REMARK 465 SER B 120 REMARK 465 GLY B 121 REMARK 465 GLY B 122 REMARK 465 GLY B 123 REMARK 465 GLY B 124 REMARK 465 SER B 125 REMARK 465 GLY B 126 REMARK 465 GLY B 127 REMARK 465 GLY B 128 REMARK 465 GLY B 129 REMARK 465 SER B 130 REMARK 465 GLY B 131 REMARK 465 GLY B 132 REMARK 465 GLY B 133 REMARK 465 ARG B 243 REMARK 465 ALA B 244 REMARK 465 SER B 245 REMARK 465 LEU B 246 REMARK 465 VAL B 247 REMARK 465 PRO B 248 REMARK 465 ARG B 249 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 462 69.46 -118.17 REMARK 500 GLN A 481 -71.92 -116.20 REMARK 500 ASN A 513 -115.19 52.78 REMARK 500 ASN A 601 -149.23 57.82 REMARK 500 ASP A 623 -131.12 47.32 REMARK 500 ILE A 630 -67.98 -107.02 REMARK 500 ASP A 636 -3.98 77.18 REMARK 500 ALA A 646 -160.75 -128.66 REMARK 500 LEU B 48 -66.25 -93.92 REMARK 500 SER B 68 110.23 -170.82 REMARK 500 ASP B 102 60.77 60.17 REMARK 500 THR B 186 -51.12 70.66 REMARK 500 SER B 202 140.86 -172.78 REMARK 500 REMARK 500 REMARK: NULL DBREF 9CN2 A 427 655 PDB 9CN2 9CN2 427 655 DBREF 9CN2 B 1 249 PDB 9CN2 9CN2 1 249 SEQRES 1 A 229 MET GLY GLY GLU LEU ARG VAL LEU LEU THR VAL GLY SER SEQRES 2 A 229 ILE MET SER PRO ASN SER ALA ASP ARG GLN VAL TRP LEU SEQRES 3 A 229 ASN LYS THR LEU THR ALA PRO GLY THR ASN PRO ASN ASP SEQRES 4 A 229 ASN LEU VAL LYS ILE ALA HIS ASP LEU GLY HIS TYR LEU SEQRES 5 A 229 ILE MET GLN GLY PHE MET HIS ILE LYS THR VAL GLU TRP SEQRES 6 A 229 TYR THR PRO ASP PHE GLN PRO SER ARG ASP PRO THR PRO SEQRES 7 A 229 ILE ALA GLY MET SER VAL MET VAL ASN ILE THR LYS LYS SEQRES 8 A 229 ALA ASP VAL TYR PHE MET LYS GLN PHE LYS ASN SER HIS SEQRES 9 A 229 THR ASN ASN ARG HIS GLN ILE THR SER ILE PHE LEU ILE SEQRES 10 A 229 LYS PRO LEU ALA ASP PHE LYS VAL GLN CYS TYR MET SER SEQRES 11 A 229 TYR PHE LYS ARG GLU SER HIS ASP ASN ASN ASP GLY VAL SEQRES 12 A 229 ALA ASN LEU THR VAL ARG SER MET THR SER PRO LYS THR SEQRES 13 A 229 ILE ARG PHE GLN ALA GLY GLU TRP TYR LEU LEU THR SER SEQRES 14 A 229 THR THR LEU LYS GLU ASN ASN LEU PRO GLU GLY TRP VAL SEQRES 15 A 229 TRP ASP ARG VAL GLU LEU LYS SER ASP THR PRO TYR TYR SEQRES 16 A 229 ALA ASP GLN ALA LEU THR TYR PHE ILE THR PRO PRO PRO SEQRES 17 A 229 VAL ASP SER GLN ILE LEU PHE GLU GLY ASN THR ALA ALA SEQRES 18 A 229 ALA GLU LEU ALA LEU VAL PRO ARG SEQRES 1 B 249 GLN VAL GLN LEU LYS GLU SER GLY PRO GLY LEU VAL ALA SEQRES 2 B 249 PRO SER GLN SER LEU SER ILE THR CYS THR VAL SER GLY SEQRES 3 B 249 PHE SER LEU THR SER TYR GLY VAL HIS TRP VAL ARG GLN SEQRES 4 B 249 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 B 249 ALA ASP GLY SER THR ASN TYR ASN SER ALA LEU MET SER SEQRES 6 B 249 ARG LEU SER ILE SER LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 B 249 PHE LEU LYS MET ASN SER LEU GLN THR ASP ASP THR ALA SEQRES 8 B 249 MET TYR TYR CYS ALA ARG TRP THR TYR GLY ASP TYR PHE SEQRES 9 B 249 ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER SEQRES 10 B 249 GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 11 B 249 GLY GLY GLY GLY SER ASP ILE GLN MET THR GLN THR THR SEQRES 12 B 249 SER SER LEU SER ALA SER LEU GLY ASP ARG VAL THR ILE SEQRES 13 B 249 SER CYS SER ALA SER GLN GLY ILE SER ASN TYR LEU ASN SEQRES 14 B 249 TRP TYR GLN GLN LYS PRO ASP GLY THR VAL LYS LEU LEU SEQRES 15 B 249 ILE TYR TYR THR SER SER LEU HIS SER GLY VAL PRO SER SEQRES 16 B 249 ARG PHE SER GLY SER GLY SER GLY THR ASP TYR SER LEU SEQRES 17 B 249 THR ILE SER ASN LEU GLU PRO GLU ASP ILE ALA THR TYR SEQRES 18 B 249 TYR CYS GLN GLN TYR SER LYS LEU PRO TYR THR PHE GLY SEQRES 19 B 249 GLY GLY THR LYS LEU GLU ILE LYS ARG ALA SER LEU VAL SEQRES 20 B 249 PRO ARG FORMUL 3 HOH *3(H2 O) HELIX 1 AA1 ASN A 462 LEU A 467 5 6 HELIX 2 AA2 ALA A 625 PHE A 629 5 5 HELIX 3 AA3 LEU B 63 SER B 65 5 3 HELIX 4 AA4 GLN B 86 THR B 90 5 5 HELIX 5 AA5 GLU B 214 ILE B 218 5 5 SHEET 1 AA110 TYR A 477 ILE A 479 0 SHEET 2 AA110 LYS A 469 HIS A 472 -1 N ILE A 470 O LEU A 478 SHEET 3 AA110 MET A 508 VAL A 512 -1 O MET A 511 N LYS A 469 SHEET 4 AA110 THR A 515 HIS A 530 -1 O LYS A 517 N VAL A 510 SHEET 5 AA110 GLN A 638 ASN A 644 -1 O ASN A 644 N MET A 523 SHEET 6 AA110 GLU A 430 VAL A 437 -1 N LEU A 435 O ILE A 639 SHEET 7 AA110 GLY A 482 TYR A 492 -1 O THR A 488 N THR A 436 SHEET 8 AA110 TRP A 590 GLU A 600 -1 O LEU A 592 N MET A 484 SHEET 9 AA110 ARG A 534 PRO A 545 -1 N ILE A 543 O TYR A 591 SHEET 10 AA110 THR A 515 HIS A 530 -1 N PHE A 526 O THR A 538 SHEET 1 AA2 3 TRP A 451 ASN A 453 0 SHEET 2 AA2 3 PHE A 549 ARG A 560 -1 O SER A 556 N LEU A 452 SHEET 3 AA2 3 LEU A 572 VAL A 574 -1 O THR A 573 N LYS A 559 SHEET 1 AA3 3 TRP A 451 ASN A 453 0 SHEET 2 AA3 3 PHE A 549 ARG A 560 -1 O SER A 556 N LEU A 452 SHEET 3 AA3 3 SER A 579 PHE A 585 -1 O PHE A 585 N PHE A 549 SHEET 1 AA4 4 GLN B 3 SER B 7 0 SHEET 2 AA4 4 LEU B 18 SER B 25 -1 O THR B 21 N SER B 7 SHEET 3 AA4 4 GLN B 77 MET B 82 -1 O VAL B 78 N CYS B 22 SHEET 4 AA4 4 LEU B 67 ASP B 72 -1 N SER B 70 O PHE B 79 SHEET 1 AA5 6 LEU B 11 VAL B 12 0 SHEET 2 AA5 6 THR B 111 VAL B 115 1 O THR B 114 N VAL B 12 SHEET 3 AA5 6 ALA B 91 TRP B 98 -1 N TYR B 93 O THR B 111 SHEET 4 AA5 6 GLY B 33 GLN B 39 -1 N VAL B 37 O TYR B 94 SHEET 5 AA5 6 GLU B 46 ILE B 51 -1 O LEU B 48 N TRP B 36 SHEET 6 AA5 6 THR B 57 TYR B 59 -1 O ASN B 58 N VAL B 50 SHEET 1 AA6 4 LEU B 11 VAL B 12 0 SHEET 2 AA6 4 THR B 111 VAL B 115 1 O THR B 114 N VAL B 12 SHEET 3 AA6 4 ALA B 91 TRP B 98 -1 N TYR B 93 O THR B 111 SHEET 4 AA6 4 PHE B 104 TRP B 107 -1 O TYR B 106 N ARG B 97 SHEET 1 AA7 4 MET B 139 THR B 140 0 SHEET 2 AA7 4 VAL B 154 ALA B 160 -1 O SER B 159 N THR B 140 SHEET 3 AA7 4 ASP B 205 ILE B 210 -1 O LEU B 208 N ILE B 156 SHEET 4 AA7 4 PHE B 197 SER B 202 -1 N SER B 200 O SER B 207 SHEET 1 AA8 6 SER B 145 SER B 147 0 SHEET 2 AA8 6 THR B 237 GLU B 240 1 O LYS B 238 N LEU B 146 SHEET 3 AA8 6 THR B 220 GLN B 225 -1 N TYR B 221 O THR B 237 SHEET 4 AA8 6 LEU B 168 GLN B 173 -1 N GLN B 173 O THR B 220 SHEET 5 AA8 6 VAL B 179 TYR B 184 -1 O ILE B 183 N TRP B 170 SHEET 6 AA8 6 SER B 188 LEU B 189 -1 O SER B 188 N TYR B 184 SHEET 1 AA9 4 SER B 145 SER B 147 0 SHEET 2 AA9 4 THR B 237 GLU B 240 1 O LYS B 238 N LEU B 146 SHEET 3 AA9 4 THR B 220 GLN B 225 -1 N TYR B 221 O THR B 237 SHEET 4 AA9 4 THR B 232 PHE B 233 -1 O THR B 232 N GLN B 225 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.06 SSBOND 2 CYS B 158 CYS B 223 1555 1555 2.06 CISPEP 1 SER A 442 PRO A 443 0 11.77 CISPEP 2 LEU B 229 PRO B 230 0 14.33 CRYST1 160.348 160.348 160.348 90.00 90.00 90.00 P 43 3 2 24 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 0.006236 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006236 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006236 0.00000