HEADER IMMUNE SYSTEM 11-APR-21 7MFV TITLE CRYSTAL STRUCTURE OF SYNTHETIC NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: SYNTHETIC NANOBODY #16 (SB16); COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 3 ORGANISM_TAXID: 32630; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1211845; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET21B KEYWDS SARS-COV-2, SPIKE PROTEIN, RBD, ANTIBODY, NANOBODY, SYBODY, VIRAL KEYWDS 2 PROTEIN, EPITOPE, NEUTRALIZATION, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.JIANG,J.AHMAD,K.NATARAJAN,L.F.BOYD,D.H.MARGULIES REVDAT 1 02-JUN-21 7MFV 0 SPRSDE 02-JUN-21 7MFV 7KGL JRNL AUTH J.AHMAD,J.JIANG,L.F.BOYD,K.NATARAJAN,D.H.MARGULIES JRNL TITL SYNTHETIC NANOBODY-SARS-COV-2 RECEPTOR-BINDING DOMAIN JRNL TITL 2 STRUCTURES IDENTIFY DISTINCT EPITOPES. JRNL REF BIORXIV 2021 JRNL REFN JRNL PMID 33532775 JRNL DOI 10.1101/2021.01.27.428466 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18.2_3874 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) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.87 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 3 NUMBER OF REFLECTIONS : 11787 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.228 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000 REMARK 3 FREE R VALUE TEST SET COUNT : 707 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 39.8700 - 3.2500 0.99 2493 160 0.1942 0.2136 REMARK 3 2 3.2500 - 2.5800 0.98 2288 145 0.2517 0.2780 REMARK 3 3 2.5800 - 2.2500 0.96 2209 141 0.2598 0.3129 REMARK 3 4 2.2500 - 2.0500 0.92 2112 135 0.2700 0.3403 REMARK 3 5 2.0500 - 1.9000 0.87 1978 126 0.3148 0.3453 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) : 0.283 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.387 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 31.80 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.03 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 : 0.014 934 REMARK 3 ANGLE : 1.174 1269 REMARK 3 CHIRALITY : 0.080 134 REMARK 3 PLANARITY : 0.008 160 REMARK 3 DIHEDRAL : 21.342 324 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 33 ) REMARK 3 ORIGIN FOR THE GROUP (A): 12.2866 19.7997 13.7317 REMARK 3 T TENSOR REMARK 3 T11: 0.2778 T22: 0.6006 REMARK 3 T33: 0.3164 T12: 0.0885 REMARK 3 T13: -0.0128 T23: 0.1048 REMARK 3 L TENSOR REMARK 3 L11: 3.9740 L22: 3.6786 REMARK 3 L33: 3.3226 L12: 0.6217 REMARK 3 L13: 0.1360 L23: 0.5295 REMARK 3 S TENSOR REMARK 3 S11: -0.2822 S12: -1.0659 S13: -0.0719 REMARK 3 S21: 0.3161 S22: 0.3154 S23: 0.4299 REMARK 3 S31: 0.2007 S32: -0.2326 S33: -0.0634 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 45 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.2495 9.3886 14.0376 REMARK 3 T TENSOR REMARK 3 T11: 0.3745 T22: 0.6180 REMARK 3 T33: 0.4895 T12: -0.0115 REMARK 3 T13: -0.0045 T23: 0.2829 REMARK 3 L TENSOR REMARK 3 L11: 5.3774 L22: 4.1545 REMARK 3 L33: 6.6123 L12: -1.1185 REMARK 3 L13: -0.3947 L23: -3.3130 REMARK 3 S TENSOR REMARK 3 S11: -0.0714 S12: -1.2515 S13: -1.2836 REMARK 3 S21: 0.5170 S22: 0.2676 S23: 0.3137 REMARK 3 S31: 0.6604 S32: -0.4616 S33: -0.1633 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 58 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.3263 24.1187 15.0441 REMARK 3 T TENSOR REMARK 3 T11: 0.2292 T22: 0.4483 REMARK 3 T33: 0.2408 T12: 0.0209 REMARK 3 T13: 0.0149 T23: 0.0015 REMARK 3 L TENSOR REMARK 3 L11: 3.5791 L22: 9.6766 REMARK 3 L33: 2.6015 L12: 2.3880 REMARK 3 L13: 0.3282 L23: -2.2438 REMARK 3 S TENSOR REMARK 3 S11: 0.0058 S12: -0.5564 S13: 0.2403 REMARK 3 S21: 0.3975 S22: 0.0997 S23: -0.3119 REMARK 3 S31: -0.3281 S32: 0.0025 S33: -0.1040 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 74 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.4408 20.8927 7.0815 REMARK 3 T TENSOR REMARK 3 T11: 0.2649 T22: 0.2680 REMARK 3 T33: 0.1658 T12: -0.0254 REMARK 3 T13: 0.0103 T23: 0.0251 REMARK 3 L TENSOR REMARK 3 L11: 7.5782 L22: 4.7798 REMARK 3 L33: 6.7966 L12: -2.6856 REMARK 3 L13: 0.8590 L23: 2.2327 REMARK 3 S TENSOR REMARK 3 S11: -0.1276 S12: -0.3644 S13: 0.1261 REMARK 3 S21: -0.1802 S22: 0.1341 S23: -0.0117 REMARK 3 S31: -0.3206 S32: 0.0535 S33: 0.0387 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 75 THROUGH 92 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.0115 18.8806 6.4295 REMARK 3 T TENSOR REMARK 3 T11: 0.2104 T22: 0.2425 REMARK 3 T33: 0.2344 T12: -0.0538 REMARK 3 T13: -0.0520 T23: 0.0390 REMARK 3 L TENSOR REMARK 3 L11: 8.3486 L22: 9.1440 REMARK 3 L33: 9.4263 L12: -3.4419 REMARK 3 L13: -2.3469 L23: 5.0012 REMARK 3 S TENSOR REMARK 3 S11: -0.0677 S12: -0.7028 S13: -0.1321 REMARK 3 S21: -0.7770 S22: 0.4985 S23: 0.2287 REMARK 3 S31: -0.4763 S32: 0.2823 S33: -0.3990 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 93 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.1172 12.5185 15.6419 REMARK 3 T TENSOR REMARK 3 T11: 0.4609 T22: 0.6119 REMARK 3 T33: 0.3764 T12: 0.1287 REMARK 3 T13: 0.0499 T23: 0.3595 REMARK 3 L TENSOR REMARK 3 L11: 2.7946 L22: 1.4227 REMARK 3 L33: 5.5135 L12: 0.1684 REMARK 3 L13: 1.7538 L23: 1.5256 REMARK 3 S TENSOR REMARK 3 S11: -0.1294 S12: -1.4913 S13: -1.4378 REMARK 3 S21: 0.7624 S22: 0.6215 S23: 0.4024 REMARK 3 S31: 1.2272 S32: -0.1846 S33: -0.2834 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 7MFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-21. REMARK 100 THE DEPOSITION ID IS D_1000256147. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-FEB-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.1 - 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 22-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12360 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5 REMARK 200 DATA REDUNDANCY : 12.40 REMARK 200 R MERGE (I) : 0.07390 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.1900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97 REMARK 200 COMPLETENESS FOR SHELL (%) : 85.0 REMARK 200 DATA REDUNDANCY IN SHELL : 12.60 REMARK 200 R MERGE FOR SHELL (I) : 1.80000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.690 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: 7KGL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.1M MES PH 6.0, 0.2M REMARK 280 LISO4, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 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 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/2 REMARK 290 6555 X-Y,X,Z+1/2 REMARK 290 7555 Y,X,-Z REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z REMARK 290 10555 -Y,-X,-Z+1/2 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-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 -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 -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 53.58500 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.58500 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 53.58500 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 53.58500 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 53.58500 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 53.58500 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: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ARG B 60 CG CD NE CZ NH1 NH2 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 GLN B 1 NE2 REMARK 480 MET B 34 CG REMARK 480 GLU B 44 CB CG CD REMARK 480 LYS B 57 CG CD CE NZ REMARK 480 TRP B 58 CZ2 CH2 REMARK 480 GLU B 90 OE2 REMARK 480 GLN B 108 CG CD OE1 NE2 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 TRP B 58 115.70 -165.65 REMARK 500 VAL B 101 74.35 -119.65 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7KGJ RELATED DB: PDB REMARK 900 RELATED ID: 7KGK RELATED DB: PDB REMARK 900 RELATED ID: 7KGL RELATED DB: PDB REMARK 900 RELATED ID: 7KLW RELATED DB: PDB DBREF 7MFV B 1 116 PDB 7MFV 7MFV 1 116 SEQRES 1 B 116 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 116 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 B 116 PHE PRO VAL ALA TYR LYS THR MET TRP TRP TYR ARG GLN SEQRES 4 B 116 ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ALA ILE GLU SEQRES 5 B 116 SER TYR GLY ILE LYS TRP THR ARG TYR ALA ASP SER VAL SEQRES 6 B 116 LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SEQRES 7 B 116 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 B 116 THR ALA VAL TYR TYR CYS ILE VAL TRP VAL GLY ALA GLN SEQRES 9 B 116 TYR HIS GLY GLN GLY THR GLN VAL THR VAL SER ALA HET EDO B 201 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 2 EDO C2 H6 O2 FORMUL 3 HOH *65(H2 O) HELIX 1 AA1 PRO B 28 LYS B 32 5 5 HELIX 2 AA2 LYS B 88 THR B 92 5 5 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 LEU B 18 SER B 25 -1 O SER B 21 N SER B 7 SHEET 3 AA1 4 THR B 79 MET B 84 -1 O MET B 84 N LEU B 18 SHEET 4 AA1 4 PHE B 69 ASP B 74 -1 N SER B 72 O TYR B 81 SHEET 1 AA2 6 GLY B 10 GLN B 13 0 SHEET 2 AA2 6 THR B 110 SER B 115 1 O THR B 113 N GLY B 10 SHEET 3 AA2 6 ALA B 93 TRP B 100 -1 N TYR B 95 O THR B 110 SHEET 4 AA2 6 MET B 34 GLN B 39 -1 N TYR B 37 O TYR B 96 SHEET 5 AA2 6 GLU B 46 ILE B 51 -1 O GLU B 46 N ARG B 38 SHEET 6 AA2 6 THR B 59 TYR B 61 -1 O ARG B 60 N ALA B 50 SHEET 1 AA3 4 GLY B 10 GLN B 13 0 SHEET 2 AA3 4 THR B 110 SER B 115 1 O THR B 113 N GLY B 10 SHEET 3 AA3 4 ALA B 93 TRP B 100 -1 N TYR B 95 O THR B 110 SHEET 4 AA3 4 GLN B 104 HIS B 106 -1 O TYR B 105 N VAL B 99 SSBOND 1 CYS B 22 CYS B 97 1555 1555 2.04 CRYST1 68.920 68.920 107.170 90.00 90.00 120.00 P 63 2 2 12 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 0.014510 0.008377 0.000000 0.00000 SCALE2 0.000000 0.016754 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009331 0.00000