HEADER TOXIN 09-OCT-22 8H3X TITLE BACTEROIDE FRAGILIS TOXIN IN COMPLEX WITH NANOBODY 282 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRAGILYSIN; COMPND 3 CHAIN: C; COMPND 4 SYNONYM: ENTEROTOXIN; COMPND 5 EC: 3.4.24.74; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NANOBODY 282; COMPND 9 CHAIN: A; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES FRAGILIS; SOURCE 3 ORGANISM_TAXID: 817; SOURCE 4 GENE: BTFP; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS BACTEROIDE FRAGILIS TOXIN, NANOBODY, TOXIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.WEN,Y.GUO REVDAT 1 08-FEB-23 8H3X 0 JRNL AUTH Y.GUO,Z.OUYANG,W.HE,J.ZHANG,Q.QIN,M.JIAO,S.MUYLDERMANS, JRNL AUTH 2 F.FANG ZHENG,Y.WEN JRNL TITL SCREENING AND EPITOPE CHARACTERIZATION OF DIAGNOSTIC JRNL TITL 2 NANOBODY AGAINST TOTAL AND ACTIVATED BACTEROIDE FRAGILIS JRNL TITL 3 TOXIN. JRNL REF FRONT IMMUNOL V. 14 2023 JRNL REFN ESSN 1664-3224 JRNL DOI 10.3389/FIMMU.2023.1065274 REMARK 2 REMARK 2 RESOLUTION. 1.66 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19 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) : 1.66 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.17 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 117825 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 : 0.216 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.260 REMARK 3 FREE R VALUE TEST SET COUNT : 3839 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 35.1700 - 4.9600 1.00 4240 148 0.1599 0.1468 REMARK 3 2 4.9600 - 3.9400 1.00 4227 139 0.1321 0.1595 REMARK 3 3 3.9400 - 3.4400 1.00 4259 142 0.1404 0.2002 REMARK 3 4 3.4400 - 3.1300 1.00 4249 145 0.1634 0.1775 REMARK 3 5 3.1300 - 2.9000 1.00 4251 147 0.1754 0.2073 REMARK 3 6 2.9000 - 2.7300 1.00 4265 142 0.1818 0.1936 REMARK 3 7 2.7300 - 2.6000 1.00 4241 144 0.1845 0.2520 REMARK 3 8 2.6000 - 2.4800 1.00 4264 140 0.1870 0.2335 REMARK 3 9 2.4800 - 2.3900 1.00 4237 144 0.1884 0.2602 REMARK 3 10 2.3900 - 2.3100 1.00 4226 138 0.1895 0.2348 REMARK 3 11 2.3100 - 2.2300 0.99 4230 142 0.1974 0.2674 REMARK 3 12 2.2300 - 2.1700 1.00 4249 144 0.1864 0.2196 REMARK 3 13 2.1700 - 2.1100 1.00 4269 143 0.1810 0.2106 REMARK 3 14 2.1100 - 2.0600 1.00 4227 145 0.1805 0.2404 REMARK 3 15 2.0600 - 2.0100 1.00 4305 144 0.2118 0.2393 REMARK 3 16 2.0100 - 1.9700 1.00 4241 144 0.2273 0.2849 REMARK 3 17 1.9700 - 1.9300 1.00 4275 141 0.2256 0.2808 REMARK 3 18 1.9300 - 1.9000 0.98 4143 140 0.3092 0.3621 REMARK 3 19 1.9000 - 1.8600 1.00 4206 143 0.2216 0.2669 REMARK 3 20 1.8600 - 1.8300 1.00 4317 141 0.2370 0.2665 REMARK 3 21 1.8300 - 1.8000 1.00 4204 144 0.2503 0.2718 REMARK 3 22 1.8000 - 1.7700 1.00 4221 143 0.2864 0.3160 REMARK 3 23 1.7700 - 1.7500 1.00 4226 141 0.3160 0.3412 REMARK 3 24 1.7500 - 1.7200 1.00 4278 145 0.3650 0.3472 REMARK 3 25 1.7200 - 1.7000 0.99 4209 140 0.4042 0.4159 REMARK 3 26 1.7000 - 1.6800 0.96 4111 140 0.4593 0.4824 REMARK 3 27 1.6800 - 1.6600 0.91 3816 130 0.5624 0.4890 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) : 0.285 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.419 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.55 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 : 0.007 3882 REMARK 3 ANGLE : 1.041 5268 REMARK 3 CHIRALITY : 0.062 574 REMARK 3 PLANARITY : 0.009 687 REMARK 3 DIHEDRAL : 6.126 536 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): 6.4848 6.7883 14.2374 REMARK 3 T TENSOR REMARK 3 T11: 0.1906 T22: 0.1975 REMARK 3 T33: 0.1878 T12: 0.0211 REMARK 3 T13: -0.0071 T23: 0.0185 REMARK 3 L TENSOR REMARK 3 L11: 0.7853 L22: 0.8583 REMARK 3 L33: 0.5263 L12: 0.4112 REMARK 3 L13: -0.0205 L23: -0.0773 REMARK 3 S TENSOR REMARK 3 S11: 0.0491 S12: -0.0126 S13: 0.0112 REMARK 3 S21: 0.0254 S22: -0.0428 S23: -0.0328 REMARK 3 S31: -0.0250 S32: 0.0359 S33: -0.0122 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 8H3X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 12-OCT-22. REMARK 100 THE DEPOSITION ID IS D_1300032756. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-NOV-20 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 : SSRF REMARK 200 BEAMLINE : BL18U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117825 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660 REMARK 200 RESOLUTION RANGE LOW (A) : 35.170 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 12.30 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.8300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72 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: MOLREP REMARK 200 STARTING MODEL: 3P24 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM THIOCYANATE, 20 % W/V REMARK 280 PEG 3350, 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 27.83150 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.06600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.10600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.06600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.83150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.10600 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 APPLY THE FOLLOWING TO CHAINS: C, A 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 MET C 1 REMARK 465 LYS C 2 REMARK 465 ASN C 3 REMARK 465 VAL C 4 REMARK 465 LYS C 5 REMARK 465 LEU C 6 REMARK 465 LEU C 7 REMARK 465 LEU C 8 REMARK 465 MET C 9 REMARK 465 LEU C 10 REMARK 465 GLY C 11 REMARK 465 THR C 12 REMARK 465 ALA C 13 REMARK 465 ALA C 14 REMARK 465 LEU C 15 REMARK 465 LEU C 16 REMARK 465 ALA C 17 REMARK 465 ALA C 18 REMARK 465 CYS C 19 REMARK 465 SER C 20 REMARK 465 ASN C 21 REMARK 465 GLU C 22 REMARK 465 ALA C 23 REMARK 465 ASP C 24 REMARK 465 SER C 25 REMARK 465 LEU C 26 REMARK 465 THR C 27 REMARK 465 THR C 28 REMARK 465 SER C 29 REMARK 465 ILE C 30 REMARK 465 ASP C 31 REMARK 465 ALA C 32 REMARK 465 PRO C 33 REMARK 465 THR C 163 REMARK 465 ARG C 164 REMARK 465 SER C 165 REMARK 465 ALA C 166 REMARK 465 ILE C 205 REMARK 465 THR C 206 REMARK 465 GLU C 207 REMARK 465 HIS A 125 REMARK 465 HIS A 126 REMARK 465 HIS A 127 REMARK 465 HIS A 128 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 C 144 CG CD CE NZ REMARK 470 LYS C 145 CG CD CE NZ REMARK 470 ARG C 147 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 188 CG CD OE1 OE2 REMARK 470 GLN C 200 CG CD OE1 NE2 REMARK 470 ARG C 211 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 292 CG CD CE NZ REMARK 470 HIS A 124 CG ND1 CD2 CE1 NE2 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 C 604 O HOH C 853 2.16 REMARK 500 O ASP C 66 O HOH C 501 2.17 REMARK 500 OE2 GLU C 216 O HOH C 502 2.18 REMARK 500 O ASN C 311 O HOH C 503 2.19 REMARK 500 O HOH A 336 O HOH A 339 2.19 REMARK 500 REMARK 500 REMARK: NULL 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 O HOH C 762 O HOH C 868 4455 2.18 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 C 42 18.70 -146.32 REMARK 500 SER C 100 67.97 31.87 REMARK 500 SER C 161 -88.78 -44.08 REMARK 500 ALA A 92 168.43 178.86 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH C 898 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH C 899 DISTANCE = 6.13 ANGSTROMS REMARK 525 HOH C 900 DISTANCE = 6.76 ANGSTROMS REMARK 525 HOH A 362 DISTANCE = 6.21 ANGSTROMS REMARK 525 HOH A 363 DISTANCE = 6.64 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN C 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 194 OD1 REMARK 620 2 ASP C 194 OD2 59.1 REMARK 620 3 HIS C 348 NE2 158.6 100.8 REMARK 620 4 HIS C 352 NE2 96.5 102.5 94.9 REMARK 620 5 HIS C 358 NE2 96.4 150.3 100.3 96.3 REMARK 620 N 1 2 3 4 DBREF 8H3X C 1 397 UNP P54355 ENTM_BACFG 9 405 DBREF 8H3X A 1 128 PDB 8H3X 8H3X 1 128 SEQRES 1 C 397 MET LYS ASN VAL LYS LEU LEU LEU MET LEU GLY THR ALA SEQRES 2 C 397 ALA LEU LEU ALA ALA CYS SER ASN GLU ALA ASP SER LEU SEQRES 3 C 397 THR THR SER ILE ASP ALA PRO VAL THR ALA SER ILE ASP SEQRES 4 C 397 LEU GLN SER VAL SER TYR THR ASP LEU ALA THR GLN LEU SEQRES 5 C 397 ASN ASP VAL SER ASP PHE GLY LYS MET ILE ILE LEU LYS SEQRES 6 C 397 ASP ASN GLY PHE ASN ARG GLN VAL HIS VAL SER MET ASP SEQRES 7 C 397 LYS ARG THR LYS ILE GLN LEU ASP ASN GLU ASN VAL ARG SEQRES 8 C 397 LEU PHE ASN GLY ARG ASP LYS ASP SER THR SER PHE ILE SEQRES 9 C 397 LEU GLY ASP GLU PHE ALA VAL LEU ARG PHE TYR ARG ASN SEQRES 10 C 397 GLY GLU SER ILE SER TYR ILE ALA TYR LYS GLU ALA GLN SEQRES 11 C 397 MET MET ASN GLU ILE ALA GLU PHE TYR ALA ALA PRO PHE SEQRES 12 C 397 LYS LYS THR ARG ALA ILE ASN GLU LYS GLU ALA PHE GLU SEQRES 13 C 397 CYS ILE TYR ASP SER ARG THR ARG SER ALA GLY LYS ASP SEQRES 14 C 397 ILE VAL SER VAL LYS ILE ASN ILE ASP LYS ALA LYS LYS SEQRES 15 C 397 ILE LEU ASN LEU PRO GLU CYS ASP TYR ILE ASN ASP TYR SEQRES 16 C 397 ILE LYS THR PRO GLN VAL PRO HIS GLY ILE THR GLU SER SEQRES 17 C 397 GLN THR ARG ALA VAL PRO SER GLU PRO LYS THR VAL TYR SEQRES 18 C 397 VAL ILE CYS LEU ARG GLU ASN GLY SER THR ILE TYR PRO SEQRES 19 C 397 ASN GLU VAL SER ALA GLN MET GLN ASP ALA ALA ASN SER SEQRES 20 C 397 VAL TYR ALA VAL HIS GLY LEU LYS ARG TYR VAL ASN PHE SEQRES 21 C 397 HIS PHE VAL LEU TYR THR THR GLU TYR SER CYS PRO SER SEQRES 22 C 397 GLY ASP ALA LYS GLU GLY LEU GLU GLY PHE THR ALA SER SEQRES 23 C 397 LEU LYS SER ASN PRO LYS ALA GLU GLY TYR ASP ASP GLN SEQRES 24 C 397 ILE TYR PHE LEU ILE ARG TRP GLY THR TRP ASP ASN LYS SEQRES 25 C 397 ILE LEU GLY MET SER TRP PHE ASN SER TYR ASN VAL ASN SEQRES 26 C 397 THR ALA SER ASP PHE GLU ALA SER GLY MET SER THR THR SEQRES 27 C 397 GLN LEU MET TYR PRO GLY VAL MET ALA HIS GLU LEU GLY SEQRES 28 C 397 HIS ILE LEU GLY ALA GLU HIS THR ASP ASN SER LYS ASP SEQRES 29 C 397 LEU MET TYR ALA THR PHE THR GLY TYR LEU SER HIS LEU SEQRES 30 C 397 SER GLU LYS ASN MET ASP ILE ILE ALA LYS ASN LEU GLY SEQRES 31 C 397 TRP GLU ALA ALA ASP GLY ASP SEQRES 1 A 128 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 128 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 128 PHE THR PHE SER ARG TYR THR MET THR TRP VAL ARG GLN SEQRES 4 A 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASN ILE ASN SEQRES 5 A 128 SER ASP GLY GLY ARG THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 A 128 GLY ARG PHE THR ILE SER ARG ASP ASN THR LYS ASN THR SEQRES 7 A 128 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 A 128 ALA VAL TYR TYR CYS ALA ILE PRO LYS ARG THR TYR VAL SEQRES 9 A 128 PRO PRO SER GLN PHE ASP ASP ARG GLY GLN GLY THR GLN SEQRES 10 A 128 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS HET ZN C 401 1 HETNAM ZN ZINC ION FORMUL 3 ZN ZN 2+ FORMUL 4 HOH *563(H2 O) HELIX 1 AA1 SER C 44 ASP C 54 1 11 HELIX 2 AA2 GLU C 128 ALA C 141 1 14 HELIX 3 AA3 PRO C 142 LYS C 144 5 3 HELIX 4 AA4 ASN C 150 ALA C 154 1 5 HELIX 5 AA5 ILE C 177 ASN C 185 1 9 HELIX 6 AA6 TYR C 233 ALA C 250 1 18 HELIX 7 AA7 GLY C 253 ARG C 256 5 4 HELIX 8 AA8 ASP C 275 SER C 289 1 15 HELIX 9 AA9 ASN C 290 GLU C 294 5 5 HELIX 10 AB1 TRP C 309 ILE C 313 5 5 HELIX 11 AB2 GLY C 344 LEU C 354 1 11 HELIX 12 AB3 SER C 378 LEU C 389 1 12 HELIX 13 AB4 GLU C 392 GLY C 396 5 5 HELIX 14 AB5 THR A 28 TYR A 32 5 5 HELIX 15 AB6 LYS A 87 THR A 91 5 5 SHEET 1 AA1 9 ALA C 36 ASP C 39 0 SHEET 2 AA1 9 LYS C 60 ASP C 66 1 O LYS C 65 N ILE C 38 SHEET 3 AA1 9 PHE C 69 MET C 77 -1 O ARG C 71 N LEU C 64 SHEET 4 AA1 9 ASN C 89 ASN C 94 -1 O ASN C 94 N SER C 76 SHEET 5 AA1 9 SER C 102 GLY C 106 -1 O LEU C 105 N ARG C 91 SHEET 6 AA1 9 PHE C 109 ARG C 116 -1 O PHE C 109 N GLY C 106 SHEET 7 AA1 9 GLU C 119 TYR C 126 -1 O ILE C 121 N PHE C 114 SHEET 8 AA1 9 ILE C 170 ASN C 176 -1 O ILE C 175 N SER C 122 SHEET 9 AA1 9 PHE C 155 TYR C 159 -1 N ILE C 158 O SER C 172 SHEET 1 AA211 ALA C 36 ASP C 39 0 SHEET 2 AA211 LYS C 60 ASP C 66 1 O LYS C 65 N ILE C 38 SHEET 3 AA211 PHE C 69 MET C 77 -1 O ARG C 71 N LEU C 64 SHEET 4 AA211 ASN C 89 ASN C 94 -1 O ASN C 94 N SER C 76 SHEET 5 AA211 LYS C 82 GLN C 84 -1 N ILE C 83 O VAL C 90 SHEET 6 AA211 VAL C 258 THR C 266 1 O PHE C 262 N LYS C 82 SHEET 7 AA211 LYS C 218 ARG C 226 1 N CYS C 224 O VAL C 263 SHEET 8 AA211 ILE C 300 ARG C 305 1 O ILE C 300 N ILE C 223 SHEET 9 AA211 SER C 333 THR C 337 1 O SER C 336 N LEU C 303 SHEET 10 AA211 GLY C 315 TRP C 318 -1 N MET C 316 O MET C 335 SHEET 11 AA211 TYR C 195 ILE C 196 1 N ILE C 196 O SER C 317 SHEET 1 AA3 4 GLN A 3 SER A 7 0 SHEET 2 AA3 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA3 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA3 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA4 6 GLY A 10 VAL A 12 0 SHEET 2 AA4 6 THR A 116 VAL A 120 1 O THR A 119 N GLY A 10 SHEET 3 AA4 6 ALA A 92 PRO A 99 -1 N TYR A 94 O THR A 116 SHEET 4 AA4 6 MET A 34 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA4 6 GLU A 46 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA4 6 THR A 58 TYR A 60 -1 O TYR A 59 N ASN A 50 SHEET 1 AA5 4 GLY A 10 VAL A 12 0 SHEET 2 AA5 4 THR A 116 VAL A 120 1 O THR A 119 N GLY A 10 SHEET 3 AA5 4 ALA A 92 PRO A 99 -1 N TYR A 94 O THR A 116 SHEET 4 AA5 4 PHE A 109 ARG A 112 -1 O ASP A 110 N ILE A 98 SSBOND 1 CYS A 22 CYS A 96 1555 1555 2.04 LINK OD1 ASP C 194 ZN ZN C 401 1555 1555 2.21 LINK OD2 ASP C 194 ZN ZN C 401 1555 1555 2.23 LINK NE2 HIS C 348 ZN ZN C 401 1555 1555 2.23 LINK NE2 HIS C 352 ZN ZN C 401 1555 1555 2.21 LINK NE2 HIS C 358 ZN ZN C 401 1555 1555 2.15 CISPEP 1 VAL A 104 PRO A 105 0 -3.37 CRYST1 55.663 78.212 118.132 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 0.017965 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012786 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008465 0.00000