HEADER IMMUNE SYSTEM 23-DEC-24 9HV1 TITLE CRYSTAL STRUCTURE OF TRI-SPECIFIC FMDV MAB-17 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_TAXID: 9913; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 9 ORGANISM_TAXID: 9913; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: HEK293 KEYWDS FOOT-AND-MOUTH DISEASE VIRUS, CATTLE ANTIBODY, CROSS-REACTIVE, LINEAR KEYWDS 2 EPITOPE, ANTIBODY STRUCTURE, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.REN,H.M.E.DUYVESTEYN,D.I.STUART REVDAT 1 14-JAN-26 9HV1 0 JRNL AUTH M.BONNET-DI PLACIDO,D.I.STUART JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF BROADLY JRNL TITL 2 NEUTRALIZING ANTI FOOT-AND-MOUTH DISEASE VIRUS BOVINE JRNL TITL 3 ANTIBODIES FROM A SERIAL VACCINATION STUDY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.96 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.96 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.55 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.1 REMARK 3 NUMBER OF REFLECTIONS : 51896 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.236 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300 REMARK 3 FREE R VALUE TEST SET COUNT : 2748 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 44.5500 - 5.3200 1.00 2933 172 0.1461 0.1630 REMARK 3 2 5.3200 - 4.2200 1.00 2907 133 0.1371 0.1545 REMARK 3 3 4.2200 - 3.6900 1.00 2862 159 0.1744 0.2167 REMARK 3 4 3.6900 - 3.3500 1.00 2833 175 0.2141 0.2436 REMARK 3 5 3.3500 - 3.1100 1.00 2875 165 0.2271 0.2647 REMARK 3 6 3.1100 - 2.9300 1.00 2822 165 0.2470 0.2698 REMARK 3 7 2.9300 - 2.7800 1.00 2849 153 0.2550 0.2661 REMARK 3 8 2.7800 - 2.6600 0.99 2817 165 0.2904 0.3012 REMARK 3 9 2.6600 - 2.5600 0.99 2834 146 0.3065 0.3096 REMARK 3 10 2.5600 - 2.4700 1.00 2806 192 0.3085 0.3160 REMARK 3 11 2.4700 - 2.3900 0.99 2838 143 0.3229 0.3408 REMARK 3 12 2.3900 - 2.3300 0.99 2820 159 0.3379 0.3621 REMARK 3 13 2.3200 - 2.2600 1.00 2827 168 0.3486 0.3312 REMARK 3 14 2.2600 - 2.2100 1.00 2827 164 0.3974 0.3962 REMARK 3 15 2.2100 - 2.1600 0.99 2802 149 0.3965 0.3916 REMARK 3 16 2.1600 - 2.1100 0.99 2856 163 0.4180 0.4430 REMARK 3 17 2.1100 - 2.0700 0.66 1847 100 0.4573 0.4851 REMARK 3 18 2.0700 - 2.0300 0.49 1418 58 0.5021 0.5468 REMARK 3 19 2.0300 - 2.0000 0.10 285 13 0.8945 0.8941 REMARK 3 20 1.9900 - 1.9600 0.03 90 6 1.2896 2.0097 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) : 0.384 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.796 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 52.72 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.23 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 3336 REMARK 3 ANGLE : 0.798 4545 REMARK 3 CHIRALITY : 0.049 532 REMARK 3 PLANARITY : 0.006 574 REMARK 3 DIHEDRAL : 12.137 1178 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 8 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.8719 -21.3741 -15.3499 REMARK 3 T TENSOR REMARK 3 T11: 1.0036 T22: 0.4230 REMARK 3 T33: 0.4036 T12: 0.1595 REMARK 3 T13: -0.0186 T23: -0.0378 REMARK 3 L TENSOR REMARK 3 L11: 3.8816 L22: 3.7886 REMARK 3 L33: 2.7212 L12: -2.3076 REMARK 3 L13: -1.5374 L23: -0.7800 REMARK 3 S TENSOR REMARK 3 S11: -0.2181 S12: 0.5214 S13: 0.6004 REMARK 3 S21: -0.6613 S22: -0.1597 S23: 0.3166 REMARK 3 S31: -0.5780 S32: 0.2903 S33: 0.1945 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 110 ) REMARK 3 ORIGIN FOR THE GROUP (A): -44.9713 -31.1419 -9.0802 REMARK 3 T TENSOR REMARK 3 T11: 0.9926 T22: 0.5531 REMARK 3 T33: 0.5072 T12: 0.3065 REMARK 3 T13: 0.1050 T23: -0.0101 REMARK 3 L TENSOR REMARK 3 L11: 3.2520 L22: 4.1721 REMARK 3 L33: 3.6588 L12: -1.6976 REMARK 3 L13: -0.0128 L23: 0.6238 REMARK 3 S TENSOR REMARK 3 S11: -0.2369 S12: -0.1203 S13: -0.3242 REMARK 3 S21: -0.4356 S22: 0.0669 S23: 0.0148 REMARK 3 S31: 0.2258 S32: 0.5449 S33: 0.1514 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 111 THROUGH 188 ) REMARK 3 ORIGIN FOR THE GROUP (A): -62.4912 -3.2744 -7.3400 REMARK 3 T TENSOR REMARK 3 T11: 1.0187 T22: 0.3344 REMARK 3 T33: 0.4121 T12: -0.0572 REMARK 3 T13: 0.0411 T23: -0.0245 REMARK 3 L TENSOR REMARK 3 L11: 1.9372 L22: 1.6889 REMARK 3 L33: 3.2084 L12: -0.5460 REMARK 3 L13: 0.6898 L23: -1.4905 REMARK 3 S TENSOR REMARK 3 S11: 0.1923 S12: -0.1691 S13: 0.0673 REMARK 3 S21: -0.1427 S22: 0.0431 S23: 0.1701 REMARK 3 S31: -0.1384 S32: -0.0092 S33: -0.2544 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 189 THROUGH 225 ) REMARK 3 ORIGIN FOR THE GROUP (A): -64.6483 9.1600 -8.1852 REMARK 3 T TENSOR REMARK 3 T11: 1.4560 T22: 0.3766 REMARK 3 T33: 0.5482 T12: -0.0300 REMARK 3 T13: 0.0934 T23: 0.0014 REMARK 3 L TENSOR REMARK 3 L11: 5.9278 L22: 2.9317 REMARK 3 L33: 1.6896 L12: 1.5292 REMARK 3 L13: 2.0152 L23: -1.0752 REMARK 3 S TENSOR REMARK 3 S11: 0.3720 S12: -0.3828 S13: 0.9791 REMARK 3 S21: -0.1227 S22: -0.0218 S23: -0.0304 REMARK 3 S31: -1.4691 S32: -0.7835 S33: -0.2754 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 74 ) REMARK 3 ORIGIN FOR THE GROUP (A): -45.0308 -25.3474 12.3339 REMARK 3 T TENSOR REMARK 3 T11: 0.9031 T22: 0.8671 REMARK 3 T33: 0.4953 T12: 0.4542 REMARK 3 T13: -0.0147 T23: -0.0178 REMARK 3 L TENSOR REMARK 3 L11: 3.9366 L22: 3.8621 REMARK 3 L33: 5.5816 L12: 0.1208 REMARK 3 L13: -1.1227 L23: 1.0905 REMARK 3 S TENSOR REMARK 3 S11: -0.5253 S12: -0.7998 S13: -0.0994 REMARK 3 S21: 0.7613 S22: 0.4019 S23: 0.0057 REMARK 3 S31: -0.0224 S32: 0.5578 S33: 0.1269 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 75 THROUGH 101 ) REMARK 3 ORIGIN FOR THE GROUP (A): -48.1576 -25.2706 7.3643 REMARK 3 T TENSOR REMARK 3 T11: 0.9105 T22: 0.7417 REMARK 3 T33: 0.5433 T12: 0.3823 REMARK 3 T13: 0.0672 T23: -0.0275 REMARK 3 L TENSOR REMARK 3 L11: 3.1111 L22: 7.7352 REMARK 3 L33: 6.7699 L12: -0.7496 REMARK 3 L13: 0.2001 L23: 2.8772 REMARK 3 S TENSOR REMARK 3 S11: -0.5433 S12: -0.5936 S13: 0.0025 REMARK 3 S21: 0.2201 S22: 0.2347 S23: 0.1685 REMARK 3 S31: 0.0626 S32: 0.2403 S33: 0.3100 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 102 THROUGH 129 ) REMARK 3 ORIGIN FOR THE GROUP (A): -66.8434 -2.2230 3.8937 REMARK 3 T TENSOR REMARK 3 T11: 0.8994 T22: 0.3752 REMARK 3 T33: 0.3859 T12: 0.0607 REMARK 3 T13: 0.0438 T23: -0.0256 REMARK 3 L TENSOR REMARK 3 L11: 3.7513 L22: 3.3182 REMARK 3 L33: 0.9407 L12: -0.1988 REMARK 3 L13: -1.2905 L23: 1.1209 REMARK 3 S TENSOR REMARK 3 S11: -0.1653 S12: 0.4788 S13: 0.5362 REMARK 3 S21: 0.1606 S22: 0.2171 S23: -0.1008 REMARK 3 S31: -0.0668 S32: 0.3710 S33: -0.0906 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 130 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): -72.2181 -5.6814 4.0596 REMARK 3 T TENSOR REMARK 3 T11: 0.9876 T22: 0.3031 REMARK 3 T33: 0.4444 T12: -0.0569 REMARK 3 T13: -0.0041 T23: 0.0327 REMARK 3 L TENSOR REMARK 3 L11: 3.9784 L22: 1.4687 REMARK 3 L33: 6.8542 L12: -0.0314 REMARK 3 L13: -0.3521 L23: 0.1472 REMARK 3 S TENSOR REMARK 3 S11: 0.0989 S12: 0.1445 S13: -0.0971 REMARK 3 S21: 0.0632 S22: 0.1587 S23: 0.0609 REMARK 3 S31: 0.4308 S32: -0.6193 S33: -0.2886 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 9HV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1292144283. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-FEB-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 : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : XIA2 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60338 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.960 REMARK 200 RESOLUTION RANGE LOW (A) : 68.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 21.10 REMARK 200 R MERGE (I) : 0.13800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.96 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE PH 8.5, 15 % POLYETHYLENE REMARK 280 GLYCOL (PEG) 1,500, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 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 26.55767 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 53.11533 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 39.83650 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 66.39417 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 13.27883 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL 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 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 CYS H 226 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 142 CG CD CE NZ 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 LEU H 189 CA - CB - CG ANGL. DEV. = 14.1 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 SER H 15 -23.15 71.32 REMARK 500 SER H 84 70.57 48.18 REMARK 500 SER H 137 71.41 -109.65 REMARK 500 CYS H 139 -68.33 -105.31 REMARK 500 ASP H 141 -97.46 50.42 REMARK 500 LYS H 142 -119.70 68.24 REMARK 500 SER H 155 65.50 60.31 REMARK 500 THR H 202 44.57 -89.52 REMARK 500 ASP L 50 -45.97 66.91 REMARK 500 SER L 51 -0.46 -140.09 REMARK 500 SER L 89 -158.61 -147.85 REMARK 500 ASP L 139 40.87 71.17 REMARK 500 SER L 171 -9.30 74.16 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HV1 H 1 226 PDB 9HV1 9HV1 1 226 DBREF 9HV1 L 1 212 PDB 9HV1 9HV1 1 212 SEQRES 1 H 226 GLN VAL GLN LEU ARG GLU SER GLY PRO SER SER LEU LYS SEQRES 2 H 226 PRO SER GLN THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 226 PHE SER LEU SER THR TYR ALA VAL GLY TRP VAL ARG GLN SEQRES 4 H 226 ALA PRO GLY LYS ALA LEU GLU TRP VAL GLY ASP ILE THR SEQRES 5 H 226 SER SER GLY ASP THR PHE TYR ASN PRO ALA LEU LYS SER SEQRES 6 H 226 ARG PHE SER ILE THR LYS ASP ASN SER LYS ASN GLN VAL SEQRES 7 H 226 SER LEU SER VAL GLY SER VAL THR PRO GLU ASP THR ALA SEQRES 8 H 226 THR PHE TYR CYS THR ARG LEU THR CYS GLY ASP ASP CYS SEQRES 9 H 226 SER THR ALA TRP HIS ASN PHE ASP ALA TRP GLY GLN GLY SEQRES 10 H 226 LEU LEU VAL THR VAL SER SER ALA SER THR THR ALA PRO SEQRES 11 H 226 LYS VAL TYR PRO LEU SER SER CYS CYS GLY ASP LYS SER SEQRES 12 H 226 SER SER THR VAL THR LEU GLY CYS LEU VAL SER SER TYR SEQRES 13 H 226 MET PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY ALA SEQRES 14 H 226 LEU LYS SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 226 SER SER GLY LEU TYR SER LEU SER SER MET VAL THR VAL SEQRES 16 H 226 PRO GLY SER THR SER GLY THR GLN THR PHE THR CYS ASN SEQRES 17 H 226 VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS ALA SEQRES 18 H 226 VAL ASP PRO ARG CYS SEQRES 1 L 212 SER TYR GLU LEU THR GLN PRO THR SER VAL SER VAL ALA SEQRES 2 L 212 LEU GLY GLN THR ALA LYS ILE THR CYS SER GLY ASP LEU SEQRES 3 L 212 LEU ASP VAL GLN TYR THR GLN TRP TYR GLN GLN LYS PRO SEQRES 4 L 212 GLY GLN GLY PRO VAL ARG VAL ILE TYR LYS ASP SER GLU SEQRES 5 L 212 ARG PRO SER GLY ILE SER ASP ARG PHE SER GLY SER SER SEQRES 6 L 212 SER GLY LYS THR ALA THR LEU ILE ILE SER GLY ALA GLN SEQRES 7 L 212 THR GLU ASP GLU ALA ASP TYR TYR CYS GLN SER THR ASP SEQRES 8 L 212 SER SER GLN TYR GLY ILE PHE GLY ARG GLY THR THR LEU SEQRES 9 L 212 THR VAL LEU GLY GLN PRO LYS SER PRO PRO SER VAL THR SEQRES 10 L 212 LEU PHE PRO PRO SER THR GLU GLU LEU ASN GLY ASN LYS SEQRES 11 L 212 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 L 212 SER VAL THR VAL VAL TRP LYS ALA ASP GLY SER THR ILE SEQRES 13 L 212 THR ARG ASN VAL GLU THR THR ARG ALA SER LYS GLN SER SEQRES 14 L 212 ASN SER LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 L 212 SER SER ASP TRP LYS SER LYS GLY SER TYR SER CYS GLU SEQRES 16 L 212 VAL THR HIS GLU GLY SER THR VAL THR LYS THR VAL LYS SEQRES 17 L 212 PRO SER GLU CYS HET GOL H 301 6 HET GOL H 302 6 HET GOL L 301 6 HET GOL L 302 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL 4(C3 H8 O3) FORMUL 7 HOH *74(H2 O) HELIX 1 AA1 PRO H 61 LYS H 64 5 4 HELIX 2 AA2 ASN H 73 LYS H 75 5 3 HELIX 3 AA3 THR H 86 THR H 90 5 5 HELIX 4 AA4 SER H 167 ALA H 169 5 3 HELIX 5 AA5 PRO H 212 SER H 215 5 4 HELIX 6 AA6 GLN L 78 GLU L 82 5 5 HELIX 7 AA7 SER L 122 ASN L 127 1 6 HELIX 8 AA8 SER L 183 LYS L 187 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O ALA H 23 N ARG H 5 SHEET 3 AA1 4 GLN H 77 VAL H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N THR H 70 O SER H 79 SHEET 1 AA2 6 SER H 11 LEU H 12 0 SHEET 2 AA2 6 LEU H 118 VAL H 122 1 O THR H 121 N LEU H 12 SHEET 3 AA2 6 ALA H 91 CYS H 100 -1 N PHE H 93 O LEU H 118 SHEET 4 AA2 6 VAL H 34 GLN H 39 -1 N GLY H 35 O THR H 96 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O PHE H 58 N ASP H 50 SHEET 1 AA3 4 SER H 11 LEU H 12 0 SHEET 2 AA3 4 LEU H 118 VAL H 122 1 O THR H 121 N LEU H 12 SHEET 3 AA3 4 ALA H 91 CYS H 100 -1 N PHE H 93 O LEU H 118 SHEET 4 AA3 4 ALA H 107 TRP H 114 -1 O ALA H 113 N ARG H 97 SHEET 1 AA4 4 LYS H 131 LEU H 135 0 SHEET 2 AA4 4 THR H 146 TYR H 156 -1 O LEU H 152 N TYR H 133 SHEET 3 AA4 4 TYR H 187 PRO H 196 -1 O LEU H 189 N VAL H 153 SHEET 4 AA4 4 GLY H 173 THR H 176 -1 N HIS H 175 O MET H 192 SHEET 1 AA5 4 LYS H 131 LEU H 135 0 SHEET 2 AA5 4 THR H 146 TYR H 156 -1 O LEU H 152 N TYR H 133 SHEET 3 AA5 4 TYR H 187 PRO H 196 -1 O LEU H 189 N VAL H 153 SHEET 4 AA5 4 VAL H 180 LEU H 181 -1 N VAL H 180 O SER H 188 SHEET 1 AA6 3 THR H 162 TRP H 165 0 SHEET 2 AA6 3 PHE H 205 HIS H 211 -1 O ASN H 208 N THR H 164 SHEET 3 AA6 3 THR H 216 VAL H 222 -1 O VAL H 218 N VAL H 209 SHEET 1 AA7 5 SER L 9 ALA L 13 0 SHEET 2 AA7 5 THR L 102 LEU L 107 1 O THR L 105 N VAL L 10 SHEET 3 AA7 5 ASP L 84 THR L 90 -1 N TYR L 85 O THR L 102 SHEET 4 AA7 5 GLN L 33 GLN L 37 -1 N GLN L 37 O ASP L 84 SHEET 5 AA7 5 VAL L 44 ILE L 47 -1 O VAL L 44 N GLN L 36 SHEET 1 AA8 4 SER L 9 ALA L 13 0 SHEET 2 AA8 4 THR L 102 LEU L 107 1 O THR L 105 N VAL L 10 SHEET 3 AA8 4 ASP L 84 THR L 90 -1 N TYR L 85 O THR L 102 SHEET 4 AA8 4 GLY L 96 PHE L 98 -1 O ILE L 97 N SER L 89 SHEET 1 AA9 3 ALA L 18 SER L 23 0 SHEET 2 AA9 3 THR L 69 ILE L 74 -1 O LEU L 72 N ILE L 20 SHEET 3 AA9 3 PHE L 61 SER L 66 -1 N SER L 62 O ILE L 73 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 LYS L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AB1 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 131 SHEET 4 AB1 4 VAL L 160 THR L 162 -1 N GLU L 161 O TYR L 178 SHEET 1 AB2 4 SER L 115 PHE L 119 0 SHEET 2 AB2 4 LYS L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AB2 4 TYR L 173 THR L 182 -1 O LEU L 181 N ALA L 131 SHEET 4 AB2 4 SER L 166 LYS L 167 -1 N SER L 166 O ALA L 174 SHEET 1 AB3 4 SER L 154 ILE L 156 0 SHEET 2 AB3 4 THR L 146 ALA L 151 -1 N ALA L 151 O SER L 154 SHEET 3 AB3 4 TYR L 192 HIS L 198 -1 O GLU L 195 N VAL L 148 SHEET 4 AB3 4 SER L 201 VAL L 207 -1 O SER L 201 N HIS L 198 SSBOND 1 CYS H 22 CYS H 95 1555 1555 2.04 SSBOND 2 CYS H 100 CYS H 104 1555 1555 2.04 SSBOND 3 CYS H 139 CYS L 212 1555 1555 2.05 SSBOND 4 CYS H 151 CYS H 207 1555 1555 2.04 SSBOND 5 CYS L 22 CYS L 87 1555 1555 2.05 SSBOND 6 CYS L 135 CYS L 194 1555 1555 2.02 CISPEP 1 MET H 157 PRO H 158 0 -6.94 CISPEP 2 GLU H 159 PRO H 160 0 4.01 CISPEP 3 TYR L 141 PRO L 142 0 -2.94 CRYST1 136.092 136.092 79.673 90.00 90.00 120.00 P 61 6 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 0.007348 0.004242 0.000000 0.00000 SCALE2 0.000000 0.008485 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012551 0.00000