HEADER IMMUNE SYSTEM 24-DEC-24 9HV8 TITLE CRYSTAL STRUCTURE OF TRI-SPECIFIC FMDV MAB-49 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 9HV8 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. 1.72 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) : 1.72 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.29 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 90.5 REMARK 3 NUMBER OF REFLECTIONS : 55353 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.211 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640 REMARK 3 FREE R VALUE TEST SET COUNT : 2570 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 42.2900 - 4.5100 1.00 3443 189 0.1555 0.1672 REMARK 3 2 4.5000 - 3.5800 1.00 3331 143 0.1468 0.1740 REMARK 3 3 3.5800 - 3.1200 1.00 3287 142 0.1641 0.1998 REMARK 3 4 3.1200 - 2.8400 1.00 3282 150 0.1805 0.2028 REMARK 3 5 2.8400 - 2.6400 1.00 3247 162 0.2027 0.2388 REMARK 3 6 2.6400 - 2.4800 1.00 3198 172 0.2004 0.2347 REMARK 3 7 2.4800 - 2.3600 1.00 3239 172 0.1962 0.2781 REMARK 3 8 2.3600 - 2.2500 1.00 3203 145 0.2106 0.2384 REMARK 3 9 2.2500 - 2.1700 1.00 3198 167 0.2148 0.2611 REMARK 3 10 2.1700 - 2.0900 1.00 3179 161 0.2158 0.2419 REMARK 3 11 2.0900 - 2.0300 0.99 3219 143 0.2187 0.2080 REMARK 3 12 2.0300 - 1.9700 0.99 3198 159 0.2155 0.2551 REMARK 3 13 1.9700 - 1.9200 0.97 3117 150 0.2275 0.2598 REMARK 3 14 1.9200 - 1.8700 0.92 2927 139 0.2556 0.2881 REMARK 3 15 1.8700 - 1.8300 0.78 2483 129 0.3126 0.3255 REMARK 3 16 1.8300 - 1.7900 0.66 2122 102 0.3639 0.4291 REMARK 3 17 1.7900 - 1.7500 0.58 1852 81 0.4177 0.4222 REMARK 3 18 1.7500 - 1.7200 0.40 1258 64 0.5307 0.4746 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) : 0.239 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.392 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 33.73 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.57 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 : 0.006 3377 REMARK 3 ANGLE : 0.791 4597 REMARK 3 CHIRALITY : 0.055 536 REMARK 3 PLANARITY : 0.005 580 REMARK 3 DIHEDRAL : 12.396 1198 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 7 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 90 ) REMARK 3 ORIGIN FOR THE GROUP (A): 1.9179 -11.0189 22.4278 REMARK 3 T TENSOR REMARK 3 T11: 0.2700 T22: 0.2766 REMARK 3 T33: 0.2407 T12: 0.0544 REMARK 3 T13: 0.0921 T23: 0.0726 REMARK 3 L TENSOR REMARK 3 L11: 3.5027 L22: 4.6912 REMARK 3 L33: 3.1072 L12: -0.4814 REMARK 3 L13: -0.5725 L23: -1.3684 REMARK 3 S TENSOR REMARK 3 S11: -0.0012 S12: 0.1505 S13: -0.0339 REMARK 3 S21: -0.0436 S22: 0.0354 S23: 0.2055 REMARK 3 S31: -0.1418 S32: -0.2797 S33: -0.0324 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 91 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 13.2422 -18.8719 22.4540 REMARK 3 T TENSOR REMARK 3 T11: 0.3726 T22: 0.3405 REMARK 3 T33: 0.4484 T12: 0.0138 REMARK 3 T13: 0.0902 T23: 0.1067 REMARK 3 L TENSOR REMARK 3 L11: 6.6528 L22: 7.8611 REMARK 3 L33: 5.9784 L12: -2.3005 REMARK 3 L13: 0.8198 L23: -1.3215 REMARK 3 S TENSOR REMARK 3 S11: 0.1307 S12: -0.1142 S13: -0.7311 REMARK 3 S21: 0.3961 S22: -0.2806 S23: -0.5511 REMARK 3 S31: 0.7349 S32: 0.2984 S33: 0.1206 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 118 THROUGH 191 ) REMARK 3 ORIGIN FOR THE GROUP (A): 4.7277 13.4573 1.0577 REMARK 3 T TENSOR REMARK 3 T11: 0.2080 T22: 0.2958 REMARK 3 T33: 0.2619 T12: -0.0031 REMARK 3 T13: 0.0344 T23: -0.0226 REMARK 3 L TENSOR REMARK 3 L11: 0.9293 L22: 3.4193 REMARK 3 L33: 2.3789 L12: -1.4928 REMARK 3 L13: 0.4876 L23: -2.3656 REMARK 3 S TENSOR REMARK 3 S11: -0.0482 S12: -0.0129 S13: -0.0372 REMARK 3 S21: 0.3288 S22: 0.1998 S23: 0.2392 REMARK 3 S31: -0.1845 S32: 0.0580 S33: -0.1777 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 192 THROUGH 231 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.5370 20.8530 -7.4842 REMARK 3 T TENSOR REMARK 3 T11: 0.3123 T22: 0.3138 REMARK 3 T33: 0.2223 T12: -0.0273 REMARK 3 T13: -0.0027 T23: -0.0230 REMARK 3 L TENSOR REMARK 3 L11: 7.2850 L22: 4.6931 REMARK 3 L33: 4.9147 L12: -0.0851 REMARK 3 L13: -1.2328 L23: -1.5485 REMARK 3 S TENSOR REMARK 3 S11: -0.0499 S12: 0.7582 S13: 0.2815 REMARK 3 S21: -0.2433 S22: 0.1323 S23: 0.1077 REMARK 3 S31: -0.4923 S32: 0.1459 S33: -0.0550 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 74 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.3605 -9.6293 17.7808 REMARK 3 T TENSOR REMARK 3 T11: 0.1869 T22: 0.2551 REMARK 3 T33: 0.2552 T12: 0.0439 REMARK 3 T13: 0.0147 T23: 0.0795 REMARK 3 L TENSOR REMARK 3 L11: 3.4112 L22: 4.8623 REMARK 3 L33: 5.1765 L12: 0.9408 REMARK 3 L13: -1.2334 L23: -1.6272 REMARK 3 S TENSOR REMARK 3 S11: 0.0000 S12: -0.1929 S13: -0.1305 REMARK 3 S21: 0.1735 S22: -0.2028 S23: -0.4961 REMARK 3 S31: 0.0812 S32: 0.3844 S33: 0.1763 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 75 THROUGH 114 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.1474 -4.6480 12.7757 REMARK 3 T TENSOR REMARK 3 T11: 0.2264 T22: 0.2410 REMARK 3 T33: 0.2126 T12: 0.0346 REMARK 3 T13: 0.0035 T23: 0.0360 REMARK 3 L TENSOR REMARK 3 L11: 2.0875 L22: 4.3562 REMARK 3 L33: 4.3452 L12: 1.1179 REMARK 3 L13: -0.8900 L23: -4.0386 REMARK 3 S TENSOR REMARK 3 S11: 0.0492 S12: -0.1349 S13: -0.1063 REMARK 3 S21: 0.2639 S22: -0.0645 S23: -0.1223 REMARK 3 S31: -0.0986 S32: 0.0183 S33: 0.0409 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 115 THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 15.1261 18.9392 7.6001 REMARK 3 T TENSOR REMARK 3 T11: 0.2163 T22: 0.1941 REMARK 3 T33: 0.1399 T12: 0.0069 REMARK 3 T13: 0.0165 T23: 0.0181 REMARK 3 L TENSOR REMARK 3 L11: 4.6645 L22: 4.4294 REMARK 3 L33: 2.4019 L12: -2.8543 REMARK 3 L13: -0.1842 L23: -0.3464 REMARK 3 S TENSOR REMARK 3 S11: -0.2366 S12: -0.2318 S13: 0.1393 REMARK 3 S21: 0.4534 S22: 0.1266 S23: 0.0343 REMARK 3 S31: -0.2504 S32: -0.0074 S33: 0.0835 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 9HV8 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_1292144285. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-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 : 56341 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720 REMARK 200 RESOLUTION RANGE LOW (A) : 62.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.1 REMARK 200 DATA REDUNDANCY : 12.70 REMARK 200 R MERGE (I) : 0.06600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75 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 (%): 58.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 9.1 M IMIDAZOLE PH 7.0, 20 % W/V PEG REMARK 280 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 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 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 36.00450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.18900 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.27600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.18900 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.00450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.27600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: 4800 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20000 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 GLY H 232 REMARK 465 LYS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 HIS H 237 REMARK 465 HIS H 238 REMARK 465 HIS H 239 REMARK 465 SER L 1 REMARK 465 SER L 213 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH H 447 O HOH L 562 2.17 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 -12.91 80.74 REMARK 500 SER H 160 64.31 66.14 REMARK 500 THR H 204 -77.92 -55.31 REMARK 500 THR H 207 0.48 -68.81 REMARK 500 ASP L 50 -46.52 77.79 REMARK 500 SER L 89 -146.80 -140.03 REMARK 500 SER L 171 -5.85 81.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9HV1 RELATED DB: PDB REMARK 900 RELATED ID: 9HV2 RELATED DB: PDB DBREF 9HV8 H 1 239 PDB 9HV8 9HV8 1 239 DBREF 9HV8 L 1 213 PDB 9HV8 9HV8 1 213 SEQRES 1 H 239 GLN VAL GLN LEU ARG GLU SER GLY PRO SER LEU VAL LYS SEQRES 2 H 239 PRO SER GLN THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 239 PHE SER LEU THR ASN TYR ALA VAL GLY TRP VAL ARG GLN SEQRES 4 H 239 ALA PRO GLY LYS ALA ILE GLN SER LEU SER ILE ILE SER SEQRES 5 H 239 THR THR GLY ASP THR TYR TYR ASN PRO ALA LEU LYS SER SEQRES 6 H 239 ARG LEU SER ILE THR LYS ASP ASN SER LYS SER GLN VAL SEQRES 7 H 239 SER LEU SER VAL SER SER VAL ALA PRO GLU ASP THR ALA SEQRES 8 H 239 THR TYR TYR CYS VAL LYS PHE CYS GLY ASN ALA ASP SER SEQRES 9 H 239 ALA GLY HIS GLY TRP GLY CYS ASP TYR GLY ASP ASN GLU SEQRES 10 H 239 ASN TRP GLY GLN GLY LEU LEU VAL THR VAL SER SER ALA SEQRES 11 H 239 SER THR THR ALA PRO LYS VAL TYR PRO LEU SER SER CYS SEQRES 12 H 239 CYS GLY ASP LYS SER SER SER THR VAL THR LEU GLY CYS SEQRES 13 H 239 LEU VAL SER SER TYR MET PRO GLU PRO VAL THR VAL THR SEQRES 14 H 239 TRP ASN SER GLY ALA LEU LYS SER GLY VAL HIS THR PHE SEQRES 15 H 239 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 239 SER MET VAL THR VAL PRO GLY SER THR SER GLY THR GLN SEQRES 17 H 239 THR PHE THR CYS ASN VAL ALA HIS PRO ALA SER SER THR SEQRES 18 H 239 LYS VAL ASP LYS ALA VAL ASP PRO ARG CYS GLY LYS HIS SEQRES 19 H 239 HIS HIS HIS HIS HIS SEQRES 1 L 213 SER TYR GLU LEU THR GLN PRO THR SER VAL SER VAL ALA SEQRES 2 L 213 LEU GLY GLN THR ALA LYS ILE THR CYS SER GLY ASP LEU SEQRES 3 L 213 LEU ASP GLU GLN TYR THR GLN TRP TYR GLN GLN LYS PRO SEQRES 4 L 213 GLY GLN GLY PRO VAL ARG VAL ILE TYR LYS ASP SER GLU SEQRES 5 L 213 ARG PRO SER GLY ILE SER ASP ARG PHE SER GLY SER SER SEQRES 6 L 213 SER GLY LYS THR ALA THR LEU THR ILE SER GLY ALA GLN SEQRES 7 L 213 THR GLU ASP GLU ALA ASP TYR TYR CYS GLN SER PHE TYR SEQRES 8 L 213 SER SER THR ASP PRO VAL PHE GLY SER GLY THR THR LEU SEQRES 9 L 213 THR VAL LEU GLY GLN PRO LYS SER PRO PRO SER VAL THR SEQRES 10 L 213 LEU PHE PRO PRO SER THR GLU GLU LEU ASN GLY ASN LYS SEQRES 11 L 213 ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY SEQRES 12 L 213 SER VAL THR VAL VAL TRP LYS ALA ASP GLY SER THR ILE SEQRES 13 L 213 THR ARG ASN VAL GLU THR THR ARG ALA SER LYS GLN SER SEQRES 14 L 213 ASN SER LYS TYR ALA ALA SER SER TYR LEU SER LEU THR SEQRES 15 L 213 SER SER ASP TRP LYS SER LYS GLY SER TYR SER CYS GLU SEQRES 16 L 213 VAL THR HIS GLU GLY SER THR VAL THR LYS THR VAL LYS SEQRES 17 L 213 PRO SER GLU CYS SER HET GOL H 301 6 HET GOL H 302 6 HET GOL H 303 6 HET GOL H 304 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 6(C3 H8 O3) FORMUL 9 HOH *367(H2 O) HELIX 1 AA1 LEU H 63 SER H 65 5 3 HELIX 2 AA2 ALA H 86 THR H 90 5 5 HELIX 3 AA3 SER H 172 ALA H 174 5 3 HELIX 4 AA4 PRO H 201 THR H 204 5 4 HELIX 5 AA5 PRO H 217 SER H 220 5 4 HELIX 6 AA6 GLN L 78 GLU L 82 5 5 HELIX 7 AA7 SER L 122 GLY L 128 1 7 HELIX 8 AA8 SER L 183 SER L 188 1 6 HELIX 9 AA9 LYS L 208 CYS L 212 5 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AA1 4 GLN H 77 VAL H 82 -1 O VAL H 82 N LEU H 18 SHEET 4 AA1 4 LEU H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 LEU H 123 VAL H 127 1 O THR H 126 N VAL H 12 SHEET 3 AA2 6 ALA H 91 LYS H 97 -1 N ALA H 91 O VAL H 125 SHEET 4 AA2 6 VAL H 34 GLN H 39 -1 N VAL H 37 O TYR H 94 SHEET 5 AA2 6 GLN H 46 ILE H 51 -1 O GLN H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O TYR H 58 N ILE H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 LEU H 123 VAL H 127 1 O THR H 126 N VAL H 12 SHEET 3 AA3 4 ALA H 91 LYS H 97 -1 N ALA H 91 O VAL H 125 SHEET 4 AA3 4 ASN H 118 TRP H 119 -1 O ASN H 118 N LYS H 97 SHEET 1 AA4 4 LYS H 136 SER H 141 0 SHEET 2 AA4 4 VAL H 152 TYR H 161 -1 O SER H 159 N LYS H 136 SHEET 3 AA4 4 TYR H 192 VAL H 200 -1 O TYR H 192 N TYR H 161 SHEET 4 AA4 4 VAL H 179 THR H 181 -1 N HIS H 180 O MET H 197 SHEET 1 AA5 4 LYS H 136 SER H 141 0 SHEET 2 AA5 4 VAL H 152 TYR H 161 -1 O SER H 159 N LYS H 136 SHEET 3 AA5 4 TYR H 192 VAL H 200 -1 O TYR H 192 N TYR H 161 SHEET 4 AA5 4 VAL H 185 LEU H 186 -1 N VAL H 185 O SER H 193 SHEET 1 AA6 3 THR H 167 TRP H 170 0 SHEET 2 AA6 3 THR H 211 HIS H 216 -1 O ASN H 213 N THR H 169 SHEET 3 AA6 3 THR H 221 ALA H 226 -1 O VAL H 223 N VAL H 214 SHEET 1 AA7 5 SER L 9 VAL L 12 0 SHEET 2 AA7 5 THR L 102 VAL L 106 1 O THR L 103 N VAL L 10 SHEET 3 AA7 5 ALA L 83 PHE L 90 -1 N ALA L 83 O LEU L 104 SHEET 4 AA7 5 GLN L 33 GLN L 37 -1 N GLN L 33 O GLN L 88 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 VAL L 12 0 SHEET 2 AA8 4 THR L 102 VAL L 106 1 O THR L 103 N VAL L 10 SHEET 3 AA8 4 ALA L 83 PHE L 90 -1 N ALA L 83 O LEU L 104 SHEET 4 AA8 4 PRO L 96 PHE L 98 -1 O VAL 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 THR 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 SER L 138 N SER L 115 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 SER L 138 N SER L 115 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 TRP L 149 O ILE L 156 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 2.03 SSBOND 2 CYS H 99 CYS H 111 1555 1555 2.01 SSBOND 3 CYS H 143 CYS H 231 1555 1555 2.03 SSBOND 4 CYS H 144 CYS L 212 1555 1555 2.03 SSBOND 5 CYS H 156 CYS H 212 1555 1555 2.03 SSBOND 6 CYS L 22 CYS L 87 1555 1555 2.06 SSBOND 7 CYS L 135 CYS L 194 1555 1555 2.04 CISPEP 1 MET H 162 PRO H 163 0 -6.64 CISPEP 2 GLU H 164 PRO H 165 0 0.38 CISPEP 3 TYR L 141 PRO L 142 0 -1.47 CRYST1 72.009 78.552 100.378 90.00 90.00 90.00 P 21 21 21 4 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 0.013887 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012730 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009962 0.00000