HEADER IMMUNE SYSTEM 11-MAR-25 9NQ3 TITLE CRYSTAL STRUCTURE OF SARS-COV-2 S2 DIRECTED FAB 1871 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 1871 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 1871 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SARS-COV-2, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR K.MUTHURAMAN,D.IVANOCHKO,J.P.JULIEN REVDAT 1 12-NOV-25 9NQ3 0 JRNL AUTH K.MUTHURAMAN,M.J.JACKMAN,J.P.JULIEN JRNL TITL CRYO-EM STRUCTURE OF BROAD BETACORONAVIRUS BINDING ANTIBODY JRNL TITL 2 1871 IN COMPLEX WITH OC43 S2 SUBUNIT JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.20 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.390 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 39679 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) : 0.216 REMARK 3 FREE R VALUE : 0.251 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 70.2000 - 6.0200 1.00 2880 154 0.1920 0.2019 REMARK 3 2 6.0200 - 4.7800 1.00 2761 145 0.1603 0.1973 REMARK 3 3 4.7800 - 4.1800 1.00 2717 145 0.1487 0.1837 REMARK 3 4 4.1800 - 3.8000 1.00 2696 143 0.1818 0.2090 REMARK 3 5 3.8000 - 3.5200 1.00 2678 141 0.2008 0.2256 REMARK 3 6 3.5200 - 3.3200 1.00 2696 143 0.2194 0.2558 REMARK 3 7 3.3200 - 3.1500 1.00 2684 142 0.2507 0.3051 REMARK 3 8 3.1500 - 3.0100 1.00 2671 141 0.2721 0.3618 REMARK 3 9 3.0100 - 2.9000 1.00 2648 140 0.2770 0.2896 REMARK 3 10 2.9000 - 2.8000 1.00 2664 141 0.2823 0.3474 REMARK 3 11 2.8000 - 2.7100 1.00 2660 142 0.2769 0.3337 REMARK 3 12 2.7100 - 2.6300 1.00 2661 141 0.2849 0.3242 REMARK 3 13 2.6300 - 2.5600 1.00 2617 139 0.2821 0.3020 REMARK 3 14 2.5600 - 2.5000 1.00 2648 141 0.2891 0.3276 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) : 0.341 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.214 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.74 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 6778 REMARK 3 ANGLE : 0.858 9236 REMARK 3 CHIRALITY : 0.053 1042 REMARK 3 PLANARITY : 0.007 1186 REMARK 3 DIHEDRAL : 14.354 2390 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 226) REMARK 3 ORIGIN FOR THE GROUP (A): 13.4799 57.4848 -7.0886 REMARK 3 T TENSOR REMARK 3 T11: 0.2842 T22: 0.6862 REMARK 3 T33: 0.3800 T12: 0.1822 REMARK 3 T13: 0.0692 T23: 0.1079 REMARK 3 L TENSOR REMARK 3 L11: -0.8281 L22: 0.5706 REMARK 3 L33: 3.3399 L12: 0.3428 REMARK 3 L13: 0.0726 L23: -0.9178 REMARK 3 S TENSOR REMARK 3 S11: 0.1142 S12: 0.1567 S13: 0.0816 REMARK 3 S21: 0.1085 S22: 0.2442 S23: 0.2408 REMARK 3 S31: -0.4716 S32: -1.2842 S33: -0.2585 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 215) REMARK 3 ORIGIN FOR THE GROUP (A): 30.3731 53.1913 -8.6211 REMARK 3 T TENSOR REMARK 3 T11: 0.1854 T22: 0.2217 REMARK 3 T33: 0.2179 T12: 0.0416 REMARK 3 T13: -0.0123 T23: -0.0090 REMARK 3 L TENSOR REMARK 3 L11: 0.6863 L22: 0.5471 REMARK 3 L33: 3.0269 L12: 0.2336 REMARK 3 L13: -0.7101 L23: -0.5903 REMARK 3 S TENSOR REMARK 3 S11: 0.0692 S12: 0.0949 S13: -0.0018 REMARK 3 S21: -0.0958 S22: -0.0373 S23: 0.0471 REMARK 3 S31: 0.0369 S32: -0.2550 S33: -0.0444 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 226) REMARK 3 ORIGIN FOR THE GROUP (A): 27.8730 108.2239 -4.1914 REMARK 3 T TENSOR REMARK 3 T11: 0.2266 T22: 0.3809 REMARK 3 T33: 0.4304 T12: -0.0194 REMARK 3 T13: 0.0265 T23: -0.0609 REMARK 3 L TENSOR REMARK 3 L11: 0.0667 L22: 0.7643 REMARK 3 L33: 3.9257 L12: -0.1815 REMARK 3 L13: -0.2109 L23: 0.6484 REMARK 3 S TENSOR REMARK 3 S11: 0.0472 S12: -0.0993 S13: -0.1291 REMARK 3 S21: -0.0829 S22: 0.0950 S23: -0.2569 REMARK 3 S31: -0.0783 S32: 0.7069 S33: -0.1585 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 215) REMARK 3 ORIGIN FOR THE GROUP (A): 10.8818 104.2194 -2.8381 REMARK 3 T TENSOR REMARK 3 T11: 0.2197 T22: 0.2009 REMARK 3 T33: 0.2767 T12: 0.0058 REMARK 3 T13: -0.0204 T23: 0.0236 REMARK 3 L TENSOR REMARK 3 L11: 0.8295 L22: 1.7422 REMARK 3 L33: 2.6622 L12: -0.2684 REMARK 3 L13: -0.6113 L23: 1.1608 REMARK 3 S TENSOR REMARK 3 S11: 0.0912 S12: -0.0459 S13: -0.0492 REMARK 3 S21: 0.0532 S22: -0.0715 S23: -0.0784 REMARK 3 S31: 0.1213 S32: 0.2494 S33: -0.0183 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 12 or REMARK 3 (resid 13 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 14 REMARK 3 through 42 or (resid 43 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 44 through 226)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and ((resid 1 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 2 or (resid 3 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 4 through 140 or (resid 141 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 142 through 226)) 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 "B" and (resid 1 through 189 or REMARK 3 (resid 190 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 191 REMARK 3 through 214 or (resid 215 and (name N or REMARK 3 name CA or name C or name O or name CB ))) REMARK 3 ) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 1 through 144 or REMARK 3 (resid 145 through 146 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 147 through 215)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9NQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000292778. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-DEC-23 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CLSI REMARK 200 BEAMLINE : 08ID-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033167 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XPREP REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47883 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 70.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 7.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.1400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56 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 (%): 58.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, PH 4.6 AND 3.5 M REMARK 280 SODIUM FORMATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,-Y,-Z+1/2 REMARK 290 4555 -X+1/2,-Y,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 41.09600 REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.49100 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 41.09600 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 67.49100 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER H 227 REMARK 465 SER A 227 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 LYS H 13 CG CD CE NZ REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 LYS H 213 CG CD CE NZ REMARK 470 LYS H 218 CG CD CE NZ REMARK 470 LYS H 226 CG CD CE NZ REMARK 470 ASP L 124 CG OD1 OD2 REMARK 470 LYS L 171 CG CD CE NZ REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 LYS L 192 CG CD CE NZ REMARK 470 GLU L 215 CG CD OE1 OE2 REMARK 470 GLU A 1 CG CD OE1 OE2 REMARK 470 GLN A 3 CG CD OE1 NE2 REMARK 470 LYS A 141 CG CD CE NZ REMARK 470 LYS A 213 CG CD CE NZ REMARK 470 LYS A 218 CG CD CE NZ REMARK 470 LYS A 226 CG CD CE NZ REMARK 470 ASP B 124 CG OD1 OD2 REMARK 470 GLU B 145 CG CD OE1 OE2 REMARK 470 LYS B 171 CG CD CE NZ REMARK 470 LYS B 192 CG CD CE NZ 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 OG SER H 7 OG SER H 7 2555 2.05 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 H 99 -125.16 -121.17 REMARK 500 SER H 144 -78.54 -119.70 REMARK 500 ASP H 156 69.92 63.38 REMARK 500 ASN H 216 64.12 -114.89 REMARK 500 ARG L 30 -122.30 57.95 REMARK 500 ALA L 51 -33.69 66.72 REMARK 500 TYR L 91 44.43 -148.97 REMARK 500 ASP L 92 -77.40 -74.33 REMARK 500 ASP A 99 -124.26 -122.86 REMARK 500 ASP A 156 69.50 63.42 REMARK 500 ARG B 30 -122.91 58.16 REMARK 500 ALA B 51 -34.29 66.66 REMARK 500 TYR B 91 45.85 -149.56 REMARK 500 ASP B 92 -78.27 -73.02 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 PRO L 95 PRO L 96 -142.32 REMARK 500 REMARK 500 REMARK: NULL DBREF 9NQ3 H 1 227 PDB 9NQ3 9NQ3 1 227 DBREF 9NQ3 L 1 215 PDB 9NQ3 9NQ3 1 215 DBREF 9NQ3 A 1 227 PDB 9NQ3 9NQ3 1 227 DBREF 9NQ3 B 1 215 PDB 9NQ3 9NQ3 1 215 SEQRES 1 H 227 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 227 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 H 227 PHE SER PHE SER ILE TYR SER MET ASN TRP VAL ARG GLN SEQRES 4 H 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE SER SEQRES 5 H 227 SER SER SER SER TYR LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 H 227 GLY ARG PHE SER VAL SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 227 LEU TYR LEU GLN LEU ASN GLY LEU ARG ALA GLU ASP THR SEQRES 8 H 227 ALA VAL TYR TYR CYS ALA ARG ASP GLY TYR CYS PRO LYS SEQRES 9 H 227 GLY VAL CYS THR TYR TYR GLY MET ASP VAL TRP GLY GLN SEQRES 10 H 227 GLY THR THR VAL THR VAL SER ALA ALA SER THR LYS GLY SEQRES 11 H 227 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 H 227 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 H 227 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 H 227 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 H 227 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 H 227 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 H 227 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 H 227 LYS VAL GLU PRO LYS SER SEQRES 1 L 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 L 215 SER PRO GLY GLU ARG VAL THR LEU SER CYS ARG ALA SER SEQRES 3 L 215 GLN SER VAL ARG SER ARG LEU ALA TRP PHE GLN GLN LYS SEQRES 4 L 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 215 ILE ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 215 GLY SER GLY THR GLU PHE THR LEU ILE ILE SER SER LEU SEQRES 7 L 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 L 215 ASP ASN TRP PRO PRO ALA TYR THR PHE GLY GLN GLY THR SEQRES 9 L 215 LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 L 215 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 L 215 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 L 215 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 L 215 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 L 215 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 L 215 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 L 215 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 L 215 LYS SER PHE ASN ARG GLY GLU SEQRES 1 A 227 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 A 227 PRO GLY GLY SER LEU ARG LEU SER CYS VAL ALA SER GLY SEQRES 3 A 227 PHE SER PHE SER ILE TYR SER MET ASN TRP VAL ARG GLN SEQRES 4 A 227 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE SER SEQRES 5 A 227 SER SER SER SER TYR LYS TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 227 GLY ARG PHE SER VAL SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 A 227 LEU TYR LEU GLN LEU ASN GLY LEU ARG ALA GLU ASP THR SEQRES 8 A 227 ALA VAL TYR TYR CYS ALA ARG ASP GLY TYR CYS PRO LYS SEQRES 9 A 227 GLY VAL CYS THR TYR TYR GLY MET ASP VAL TRP GLY GLN SEQRES 10 A 227 GLY THR THR VAL THR VAL SER ALA ALA SER THR LYS GLY SEQRES 11 A 227 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 A 227 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 A 227 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 A 227 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 A 227 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 A 227 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 A 227 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 A 227 LYS VAL GLU PRO LYS SER SEQRES 1 B 215 GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL SEQRES 2 B 215 SER PRO GLY GLU ARG VAL THR LEU SER CYS ARG ALA SER SEQRES 3 B 215 GLN SER VAL ARG SER ARG LEU ALA TRP PHE GLN GLN LYS SEQRES 4 B 215 PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 B 215 ILE ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 215 GLY SER GLY THR GLU PHE THR LEU ILE ILE SER SER LEU SEQRES 7 B 215 GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR SEQRES 8 B 215 ASP ASN TRP PRO PRO ALA TYR THR PHE GLY GLN GLY THR SEQRES 9 B 215 LYS LEU GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL SEQRES 10 B 215 PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY SEQRES 11 B 215 THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO SEQRES 12 B 215 ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU SEQRES 13 B 215 GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SEQRES 14 B 215 SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR SEQRES 15 B 215 LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA SEQRES 16 B 215 CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR SEQRES 17 B 215 LYS SER PHE ASN ARG GLY GLU FORMUL 5 HOH *22(H2 O) HELIX 1 AA1 SER H 28 SER H 30 5 3 HELIX 2 AA2 ARG H 87 THR H 91 5 5 HELIX 3 AA3 PRO H 103 VAL H 106 5 4 HELIX 4 AA4 SER H 139 THR H 143 5 5 HELIX 5 AA5 SER H 168 ALA H 170 5 3 HELIX 6 AA6 SER H 199 LEU H 201 5 3 HELIX 7 AA7 GLN L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 123 LYS L 128 1 6 HELIX 9 AA9 LYS L 185 LYS L 190 1 6 HELIX 10 AB1 SER A 28 TYR A 32 5 5 HELIX 11 AB2 ARG A 87 THR A 91 5 5 HELIX 12 AB3 SER A 139 LYS A 141 5 3 HELIX 13 AB4 SER A 168 ALA A 170 5 3 HELIX 14 AB5 SER A 199 LEU A 201 5 3 HELIX 15 AB6 GLN B 79 PHE B 83 5 5 HELIX 16 AB7 SER B 123 GLY B 130 1 8 HELIX 17 AB8 LYS B 185 LYS B 190 1 6 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 SER H 78 LEU H 83 -1 O LEU H 83 N LEU H 18 SHEET 4 AA1 4 PHE H 68 ASP H 73 -1 N SER H 71 O TYR H 80 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 119 VAL H 123 1 O THR H 122 N VAL H 12 SHEET 3 AA2 6 ALA H 92 TYR H 101 -1 N TYR H 94 O THR H 119 SHEET 4 AA2 6 TYR H 32 GLN H 39 -1 N VAL H 37 O TYR H 95 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 6 AA2 6 LYS H 58 TYR H 60 -1 O TYR H 59 N TYR H 50 SHEET 1 AA3 4 SER H 132 LEU H 136 0 SHEET 2 AA3 4 THR H 147 TYR H 157 -1 O LYS H 155 N SER H 132 SHEET 3 AA3 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AA3 4 VAL H 175 THR H 177 -1 N HIS H 176 O VAL H 193 SHEET 1 AA4 4 SER H 132 LEU H 136 0 SHEET 2 AA4 4 THR H 147 TYR H 157 -1 O LYS H 155 N SER H 132 SHEET 3 AA4 4 TYR H 188 PRO H 197 -1 O TYR H 188 N TYR H 157 SHEET 4 AA4 4 VAL H 181 LEU H 182 -1 N VAL H 181 O SER H 189 SHEET 1 AA5 3 THR H 163 TRP H 166 0 SHEET 2 AA5 3 TYR H 206 HIS H 212 -1 O ASN H 209 N SER H 165 SHEET 3 AA5 3 THR H 217 VAL H 223 -1 O VAL H 223 N TYR H 206 SHEET 1 AA6 4 MET L 4 THR L 5 0 SHEET 2 AA6 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA6 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA6 4 PHE L 62 SER L 67 -1 N SER L 63 O ILE L 74 SHEET 1 AA7 6 THR L 10 VAL L 13 0 SHEET 2 AA7 6 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 11 SHEET 3 AA7 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 104 SHEET 4 AA7 6 LEU L 33 GLN L 38 -1 N GLN L 38 O VAL L 85 SHEET 5 AA7 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA7 6 ILE L 53 ARG L 54 -1 O ILE L 53 N TYR L 49 SHEET 1 AA8 4 THR L 10 VAL L 13 0 SHEET 2 AA8 4 THR L 104 ILE L 108 1 O GLU L 107 N LEU L 11 SHEET 3 AA8 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 104 SHEET 4 AA8 4 THR L 99 PHE L 100 -1 O THR L 99 N GLN L 90 SHEET 1 AA9 4 SER L 116 PHE L 120 0 SHEET 2 AA9 4 THR L 131 PHE L 141 -1 O LEU L 137 N PHE L 118 SHEET 3 AA9 4 TYR L 175 SER L 184 -1 O LEU L 177 N LEU L 138 SHEET 4 AA9 4 SER L 161 VAL L 165 -1 N GLN L 162 O THR L 180 SHEET 1 AB1 3 ALA L 146 VAL L 152 0 SHEET 2 AB1 3 VAL L 193 HIS L 200 -1 O ALA L 195 N LYS L 151 SHEET 3 AB1 3 VAL L 207 ASN L 212 -1 O VAL L 207 N VAL L 198 SHEET 1 AB2 4 GLN A 3 SER A 7 0 SHEET 2 AB2 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AB2 4 SER A 78 LEU A 83 -1 O LEU A 83 N LEU A 18 SHEET 4 AB2 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AB3 6 LEU A 11 VAL A 12 0 SHEET 2 AB3 6 THR A 119 VAL A 123 1 O THR A 122 N VAL A 12 SHEET 3 AB3 6 ALA A 92 ARG A 98 -1 N TYR A 94 O THR A 119 SHEET 4 AB3 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AB3 6 LEU A 45 ILE A 51 -1 O VAL A 48 N TRP A 36 SHEET 6 AB3 6 LYS A 58 TYR A 60 -1 O TYR A 59 N TYR A 50 SHEET 1 AB4 4 SER A 132 LEU A 136 0 SHEET 2 AB4 4 THR A 147 TYR A 157 -1 O LYS A 155 N SER A 132 SHEET 3 AB4 4 TYR A 188 PRO A 197 -1 O TYR A 188 N TYR A 157 SHEET 4 AB4 4 VAL A 175 THR A 177 -1 N HIS A 176 O VAL A 193 SHEET 1 AB5 4 THR A 143 SER A 144 0 SHEET 2 AB5 4 THR A 147 TYR A 157 -1 O THR A 147 N SER A 144 SHEET 3 AB5 4 TYR A 188 PRO A 197 -1 O TYR A 188 N TYR A 157 SHEET 4 AB5 4 VAL A 181 LEU A 182 -1 N VAL A 181 O SER A 189 SHEET 1 AB6 3 THR A 163 TRP A 166 0 SHEET 2 AB6 3 TYR A 206 HIS A 212 -1 O ASN A 209 N SER A 165 SHEET 3 AB6 3 THR A 217 VAL A 223 -1 O THR A 217 N HIS A 212 SHEET 1 AB7 4 MET B 4 THR B 5 0 SHEET 2 AB7 4 VAL B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB7 4 GLU B 70 ILE B 75 -1 O LEU B 73 N LEU B 21 SHEET 4 AB7 4 PHE B 62 SER B 67 -1 N SER B 63 O ILE B 74 SHEET 1 AB8 6 THR B 10 VAL B 13 0 SHEET 2 AB8 6 THR B 104 ILE B 108 1 O GLU B 107 N LEU B 11 SHEET 3 AB8 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 104 SHEET 4 AB8 6 LEU B 33 GLN B 38 -1 N GLN B 38 O VAL B 85 SHEET 5 AB8 6 ARG B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AB8 6 ILE B 53 ARG B 54 -1 O ILE B 53 N TYR B 49 SHEET 1 AB9 4 THR B 10 VAL B 13 0 SHEET 2 AB9 4 THR B 104 ILE B 108 1 O GLU B 107 N LEU B 11 SHEET 3 AB9 4 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 104 SHEET 4 AB9 4 THR B 99 PHE B 100 -1 O THR B 99 N GLN B 90 SHEET 1 AC1 4 SER B 116 PHE B 120 0 SHEET 2 AC1 4 THR B 131 PHE B 141 -1 O LEU B 137 N PHE B 118 SHEET 3 AC1 4 TYR B 175 SER B 184 -1 O TYR B 175 N PHE B 141 SHEET 4 AC1 4 SER B 161 VAL B 165 -1 N SER B 164 O SER B 178 SHEET 1 AC2 3 ALA B 146 VAL B 152 0 SHEET 2 AC2 3 VAL B 193 HIS B 200 -1 O GLU B 197 N GLN B 149 SHEET 3 AC2 3 VAL B 207 ASN B 212 -1 O VAL B 207 N VAL B 198 SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.04 SSBOND 2 CYS H 102 CYS H 107 1555 1555 2.04 SSBOND 3 CYS H 152 CYS H 208 1555 1555 2.04 SSBOND 4 CYS L 23 CYS L 88 1555 1555 2.07 SSBOND 5 CYS L 136 CYS L 196 1555 1555 2.04 SSBOND 6 CYS A 22 CYS A 96 1555 1555 2.04 SSBOND 7 CYS A 102 CYS A 107 1555 1555 2.03 SSBOND 8 CYS A 152 CYS A 208 1555 1555 2.04 SSBOND 9 CYS B 23 CYS B 88 1555 1555 2.06 SSBOND 10 CYS B 136 CYS B 196 1555 1555 2.05 CISPEP 1 PHE H 158 PRO H 159 0 -6.17 CISPEP 2 GLU H 160 PRO H 161 0 -4.17 CISPEP 3 SER L 7 PRO L 8 0 1.83 CISPEP 4 TYR L 142 PRO L 143 0 1.64 CISPEP 5 PHE A 158 PRO A 159 0 -6.35 CISPEP 6 GLU A 160 PRO A 161 0 -3.15 CISPEP 7 SER B 7 PRO B 8 0 2.46 CISPEP 8 TYR B 142 PRO B 143 0 1.82 CRYST1 82.192 101.333 134.982 90.00 90.00 90.00 P 21 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 0.012167 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009868 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007408 0.00000 MTRIX1 1 -0.999588 0.011439 -0.026313 39.99714 1 MTRIX2 1 0.011475 0.999933 -0.001234 -50.94467 1 MTRIX3 1 0.026297 -0.001536 -0.999653 -11.79823 1 MTRIX1 2 -0.999406 0.016905 -0.030040 39.39040 1 MTRIX2 2 0.017120 0.999830 -0.006915 -51.08753 1 MTRIX3 2 0.029918 -0.007425 -0.999525 -11.11964 1