HEADER TOXIN/IMMUNE SYSTEM 16-JUN-22 8DCM TITLE CRYSTAL STRUCTURE OF CLOSTRIDIOIDES DIFFICILE BINARY TOXIN PROCDTB TITLE 2 LACKING D4 IN COMPLEX WITH BINTOXB/22 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: BINTOXB/22 FAB HEAVY CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: BINTOXB/22 FAB LIGHT CHAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ADP-RIBOSYLATING BINARY TOXIN BINDING SUBUNIT CDTB; COMPND 11 CHAIN: C; COMPND 12 FRAGMENT: LACKING D4; COMPND 13 SYNONYM: ADP-RIBOSYLTRANSFERASE BINDING COMPONENT,CDTB, PROCDTB; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: CLOSTRIDIOIDES DIFFICILE; SOURCE 13 ORGANISM_TAXID: 1496; SOURCE 14 GENE: CDTB, E5F34_11700; SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS VIRULENCE, ANTIBODIES, NEUTRALIZATION, BACTERIA, TOXIN, TOXIN-IMMUNE KEYWDS 2 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR J.A.GOLDSMITH,J.S.MCLELLAN JRNL AUTH J.A.GOLDSMITH,V.DEWAR,P.HERMAND,N.BLAIS,J.S.MCLELLAN JRNL TITL STRUCTURAL BASIS FOR BINDING OF NEUTRALIZING ANTIBODIES TO JRNL TITL 2 CLOSTRIDIOIDES DIFFICILE BINARY TOXIN. JRNL REF J.BACTERIOL. 45622 2023 JRNL REFN ESSN 1098-5530 JRNL PMID 36951574 JRNL DOI 10.1128/JB.00456-22 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2 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) : 59.24 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 45722 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.199 REMARK 3 R VALUE (WORKING SET) : 0.198 REMARK 3 FREE R VALUE : 0.227 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820 REMARK 3 FREE R VALUE TEST SET COUNT : 2204 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 59.2400 - 6.3000 0.96 3005 143 0.1762 0.1720 REMARK 3 2 6.3000 - 5.0000 0.94 2769 153 0.1835 0.2116 REMARK 3 3 5.0000 - 4.3700 1.00 2928 143 0.1507 0.1975 REMARK 3 4 4.3700 - 3.9700 1.00 2917 148 0.1643 0.1777 REMARK 3 5 3.9700 - 3.6800 0.97 2795 162 0.1769 0.2091 REMARK 3 6 3.6800 - 3.4700 0.94 2725 120 0.1830 0.2290 REMARK 3 7 3.4700 - 3.2900 0.99 2863 148 0.2137 0.2189 REMARK 3 8 3.2900 - 3.1500 0.99 2854 159 0.2150 0.2502 REMARK 3 9 3.1500 - 3.0300 0.98 2835 117 0.2171 0.2782 REMARK 3 10 3.0300 - 2.9200 0.99 2822 140 0.2376 0.2424 REMARK 3 11 2.9200 - 2.8300 0.96 2756 143 0.2393 0.2678 REMARK 3 12 2.8300 - 2.7500 0.84 2438 111 0.2422 0.3175 REMARK 3 13 2.7500 - 2.6800 0.90 2556 145 0.2442 0.2956 REMARK 3 14 2.6800 - 2.6100 0.87 2486 129 0.2394 0.2519 REMARK 3 15 2.6100 - 2.5500 0.84 2372 129 0.2535 0.3041 REMARK 3 16 2.5500 - 2.5000 0.83 2397 114 0.2620 0.3037 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) : 0.238 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.037 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 28.11 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.50 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 : 0.003 8997 REMARK 3 ANGLE : 0.643 12215 REMARK 3 CHIRALITY : 0.044 1364 REMARK 3 PLANARITY : 0.004 1580 REMARK 3 DIHEDRAL : 15.436 3311 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 8DCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000266377. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-FEB-21 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 19-ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45722 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 96.460 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.5000 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) : 2.58 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: 6UWT REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG8000, 0.09 M SODIUM NITRATE, REMARK 280 0.09 M SODIUM PHOSPHATE DIBASIC, 0.09 M AMMONIUM SULFATE, 0.1 M REMARK 280 IMIDAZOLE PH 6.5, 0.1 M MES PH 6.5, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 295K 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 35.11450 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.05950 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.24000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.05950 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.11450 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.24000 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 A 216 REMARK 465 LYS A 217 REMARK 465 GLY A 218 REMARK 465 LEU A 219 REMARK 465 GLU A 220 REMARK 465 VAL A 221 REMARK 465 LEU A 222 REMARK 465 PHE A 223 REMARK 465 GLN A 224 REMARK 465 MET C 42 REMARK 465 GLU C 43 REMARK 465 ILE C 44 REMARK 465 VAL C 45 REMARK 465 ASN C 46 REMARK 465 GLU C 47 REMARK 465 ASP C 48 REMARK 465 ILE C 49 REMARK 465 LEU C 50 REMARK 465 PRO C 51 REMARK 465 HIS C 747 REMARK 465 HIS C 748 REMARK 465 HIS C 749 REMARK 465 HIS C 750 REMARK 465 HIS C 751 REMARK 465 HIS C 752 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 SER C 493 OG 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 A 346 O HOH A 353 2.14 REMARK 500 OD1 ASP C 111 N LYS C 143 2.18 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 OG SER A 115 OE1 GLN A 131 4445 1.98 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 ALA A 129 70.17 56.20 REMARK 500 ALA A 130 100.92 -166.61 REMARK 500 GLN A 131 98.26 -160.05 REMARK 500 SER B 7 -71.97 -60.78 REMARK 500 SER B 30 -116.86 49.15 REMARK 500 ALA B 51 -51.47 67.27 REMARK 500 GLN B 198 -161.93 -112.32 REMARK 500 LYS C 110 129.68 -170.60 REMARK 500 THR C 129 19.32 53.49 REMARK 500 ASP C 155 101.13 -164.57 REMARK 500 ASP C 197 69.25 -150.33 REMARK 500 ASN C 225 14.76 84.34 REMARK 500 SER C 316 45.32 -95.09 REMARK 500 LEU C 379 -33.34 -130.01 REMARK 500 LYS C 423 79.20 -114.74 REMARK 500 ASN C 431 -54.35 64.06 REMARK 500 SER C 492 -108.70 60.61 REMARK 500 ASN C 567 -114.71 53.48 REMARK 500 ASP C 623 -115.93 -126.66 REMARK 500 ASN C 626 90.95 -163.85 REMARK 500 ALA C 690 -118.45 -128.21 REMARK 500 THR C 714 -123.53 -117.61 REMARK 500 SER C 728 59.73 -147.49 REMARK 500 REMARK 500 REMARK: NULL 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 NA C 804 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 78 O REMARK 620 2 SER C 166 O 146.9 REMARK 620 3 SER C 166 OG 75.4 74.9 REMARK 620 4 PRO C 167 O 83.5 76.1 77.6 REMARK 620 5 ASN C 168 OD1 81.7 121.9 153.1 86.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 802 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 220 OD1 REMARK 620 2 ASP C 222 OD1 77.0 REMARK 620 3 ASP C 224 OD1 78.0 73.8 REMARK 620 4 ILE C 226 O 77.8 152.3 89.8 REMARK 620 5 GLU C 231 OE2 171.0 105.3 94.2 97.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 801 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 222 OD2 REMARK 620 2 ASP C 224 OD2 90.6 REMARK 620 3 GLU C 231 OE1 127.7 96.5 REMARK 620 4 GLU C 231 OE2 83.0 73.4 50.7 REMARK 620 5 ASN C 260 O 79.8 164.8 80.6 93.7 REMARK 620 6 GLU C 263 O 75.6 110.1 145.0 158.3 79.0 REMARK 620 7 ASP C 273 OD2 152.1 88.5 80.1 123.2 105.5 78.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA C 803 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASN C 621 O REMARK 620 2 ASP C 623 OD2 67.9 REMARK 620 3 GLN C 644 O 145.4 77.6 REMARK 620 4 SER C 646 O 92.0 95.8 88.3 REMARK 620 5 ASP C 734 OD1 78.4 146.2 136.1 88.1 REMARK 620 6 ASP C 734 OD2 131.9 159.7 82.7 88.7 53.5 REMARK 620 N 1 2 3 4 5 DBREF 8DCM A 1 224 PDB 8DCM 8DCM 1 224 DBREF 8DCM B 1 214 PDB 8DCM 8DCM 1 214 DBREF 8DCM C 43 746 UNP A8DS70 A8DS70_CLODI 43 746 SEQADV 8DCM MET C 42 UNP A8DS70 INITIATING METHIONINE SEQADV 8DCM HIS C 747 UNP A8DS70 EXPRESSION TAG SEQADV 8DCM HIS C 748 UNP A8DS70 EXPRESSION TAG SEQADV 8DCM HIS C 749 UNP A8DS70 EXPRESSION TAG SEQADV 8DCM HIS C 750 UNP A8DS70 EXPRESSION TAG SEQADV 8DCM HIS C 751 UNP A8DS70 EXPRESSION TAG SEQADV 8DCM HIS C 752 UNP A8DS70 EXPRESSION TAG SEQRES 1 A 229 GLN ILE GLN LEU VAL GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 A 229 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA SER GLY SEQRES 3 A 229 TYR THR PHE THR ASN TYR GLY MET ASN TRP VAL LYS GLN SEQRES 4 A 229 ALA PRO GLY LYS ASP LEU LYS TRP MET GLY TRP MET SER SEQRES 5 A 229 THR TYR THR GLY GLU PRO THR TYR ALA ASP ASP PHE LYS SEQRES 6 A 229 GLY ARG PHE ALA PHE SER LEU GLU THR SER ALA SER THR SEQRES 7 A 229 ALA TYR LEU GLN ILE ASN ASN LEU LYS ASN GLU ASP MET SEQRES 8 A 229 ALA THR TYR PHE CYS ALA ARG ARG GLY ASN TYR LEU SER SEQRES 9 A 229 PHE ASP TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SEQRES 10 A 229 SER ALA SER THR THR PRO PRO SER VAL TYR PRO LEU ALA SEQRES 11 A 229 PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR LEU SEQRES 12 A 229 GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR SEQRES 13 A 229 VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL HIS SEQRES 14 A 229 THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SEQRES 15 A 229 SER SER SER VAL THR VAL PRO SER SER THR TRP PRO SER SEQRES 16 A 229 GLU THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER SEQRES 17 A 229 THR LYS VAL ASP LYS LYS ILE VAL PRO ARG ASP CYS GLY SEQRES 18 A 229 LYS GLY LEU GLU VAL LEU PHE GLN SEQRES 1 B 212 ASP ILE VAL MET THR GLN SER HIS LYS PHE MET SER THR SEQRES 2 B 212 SER VAL GLY ASP ARG VAL SER ILE THR CYS LYS ALA SER SEQRES 3 B 212 GLN ASP VAL SER THR ALA VAL GLY TRP TYR GLN GLN LYS SEQRES 4 B 212 PRO GLY GLN SER PRO LYS LEU LEU ILE TYR SER ALA SER SEQRES 5 B 212 TYR ARG TYR THR GLY VAL PRO ASP ARG PHE THR GLY SER SEQRES 6 B 212 GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER VAL SEQRES 7 B 212 GLN ALA GLU ASP LEU ALA VAL TYR TYR CYS GLN GLN HIS SEQRES 8 B 212 TYR SER PRO PRO PHE THR PHE GLY SER GLY THR GLU LEU SEQRES 9 B 212 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 B 212 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 B 212 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 B 212 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 B 212 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 B 212 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 B 212 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 B 212 ALA THR GLN GLY THR THR SER ILE VAL LYS SER PHE ASN SEQRES 17 B 212 ARG ASN GLU CYS SEQRES 1 C 711 MET GLU ILE VAL ASN GLU ASP ILE LEU PRO ASN ASN GLY SEQRES 2 C 711 LEU MET GLY TYR TYR PHE THR ASP GLU HIS PHE LYS ASP SEQRES 3 C 711 LEU LYS LEU MET ALA PRO ILE LYS ASP GLY ASN LEU LYS SEQRES 4 C 711 PHE GLU GLU LYS LYS VAL ASP LYS LEU LEU ASP LYS ASP SEQRES 5 C 711 LYS SER ASP VAL LYS SER ILE ARG TRP THR GLY ARG ILE SEQRES 6 C 711 ILE PRO SER LYS ASP GLY GLU TYR THR LEU SER THR ASP SEQRES 7 C 711 ARG ASP ASP VAL LEU MET GLN VAL ASN THR GLU SER THR SEQRES 8 C 711 ILE SER ASN THR LEU LYS VAL ASN MET LYS LYS GLY LYS SEQRES 9 C 711 GLU TYR LYS VAL ARG ILE GLU LEU GLN ASP LYS ASN LEU SEQRES 10 C 711 GLY SER ILE ASP ASN LEU SER SER PRO ASN LEU TYR TRP SEQRES 11 C 711 GLU LEU ASP GLY MET LYS LYS ILE ILE PRO GLU GLU ASN SEQRES 12 C 711 LEU PHE LEU ARG ASP TYR SER ASN ILE GLU LYS ASP ASP SEQRES 13 C 711 PRO PHE ILE PRO ASN ASN ASN PHE PHE ASP PRO LYS LEU SEQRES 14 C 711 MET SER ASP TRP GLU ASP GLU ASP LEU ASP THR ASP ASN SEQRES 15 C 711 ASP ASN ILE PRO ASP SER TYR GLU ARG ASN GLY TYR THR SEQRES 16 C 711 ILE LYS ASP LEU ILE ALA VAL LYS TRP GLU ASP SER PHE SEQRES 17 C 711 ALA GLU GLN GLY TYR LYS LYS TYR VAL SER ASN TYR LEU SEQRES 18 C 711 GLU SER ASN THR ALA GLY ASP PRO TYR THR ASP TYR GLU SEQRES 19 C 711 LYS ALA SER GLY SER PHE ASP LYS ALA ILE LYS THR GLU SEQRES 20 C 711 ALA ARG ASP PRO LEU VAL ALA ALA TYR PRO ILE VAL GLY SEQRES 21 C 711 VAL GLY MET GLU LYS LEU ILE ILE SER THR ASN GLU HIS SEQRES 22 C 711 ALA SER THR ASP GLN GLY LYS THR VAL SER ARG ALA THR SEQRES 23 C 711 THR ASN SER LYS THR GLU SER ASN THR ALA GLY VAL SER SEQRES 24 C 711 VAL ASN VAL GLY TYR GLN ASN GLY PHE THR ALA ASN VAL SEQRES 25 C 711 THR THR ASN TYR SER HIS THR THR ASP ASN SER THR ALA SEQRES 26 C 711 VAL GLN ASP SER ASN GLY GLU SER TRP ASN THR GLY LEU SEQRES 27 C 711 SER ILE ASN LYS GLY GLU SER ALA TYR ILE ASN ALA ASN SEQRES 28 C 711 VAL ARG TYR TYR ASN THR GLY THR ALA PRO MET TYR LYS SEQRES 29 C 711 VAL THR PRO THR THR ASN LEU VAL LEU ASP GLY ASP THR SEQRES 30 C 711 LEU SER THR ILE LYS ALA GLN GLU ASN GLN ILE GLY ASN SEQRES 31 C 711 ASN LEU SER PRO GLY ASP THR TYR PRO LYS LYS GLY LEU SEQRES 32 C 711 SER PRO LEU ALA LEU ASN THR MET ASP GLN PHE SER SER SEQRES 33 C 711 ARG LEU ILE PRO ILE ASN TYR ASP GLN LEU LYS LYS LEU SEQRES 34 C 711 ASP ALA GLY LYS GLN ILE LYS LEU GLU THR THR GLN VAL SEQRES 35 C 711 SER GLY ASN PHE GLY THR LYS ASN SER SER GLY GLN ILE SEQRES 36 C 711 VAL THR GLU GLY ASN SER TRP SER ASP TYR ILE SER GLN SEQRES 37 C 711 ILE ASP SER ILE SER ALA SER ILE ILE LEU ASP THR GLU SEQRES 38 C 711 ASN GLU SER TYR GLU ARG ARG VAL THR ALA LYS ASN LEU SEQRES 39 C 711 GLN ASP PRO GLU ASP LYS THR PRO GLU LEU THR ILE GLY SEQRES 40 C 711 GLU ALA ILE GLU LYS ALA PHE GLY ALA THR LYS LYS ASP SEQRES 41 C 711 GLY LEU LEU TYR PHE ASN ASP ILE PRO ILE ASP GLU SER SEQRES 42 C 711 CYS VAL GLU LEU ILE PHE ASP ASP ASN THR ALA ASN LYS SEQRES 43 C 711 ILE LYS ASP SER LEU LYS THR LEU SER ASP LYS LYS ILE SEQRES 44 C 711 TYR ASN VAL LYS LEU GLU ARG GLY MET ASN ILE LEU ILE SEQRES 45 C 711 LYS THR PRO THR TYR PHE THR ASN PHE ASP ASP TYR ASN SEQRES 46 C 711 ASN TYR PRO SER THR TRP SER ASN VAL ASN THR THR ASN SEQRES 47 C 711 GLN ASP GLY LEU GLN GLY SER ALA ASN LYS LEU ASN GLY SEQRES 48 C 711 GLU THR LYS ILE LYS ILE PRO MET SER GLU LEU LYS PRO SEQRES 49 C 711 TYR LYS ARG TYR VAL PHE SER GLY TYR SER LYS ASP PRO SEQRES 50 C 711 LEU THR SER ASN SER ILE ILE VAL LYS ILE LYS ALA LYS SEQRES 51 C 711 GLU GLU LYS THR ASP TYR LEU VAL PRO GLU GLN GLY TYR SEQRES 52 C 711 THR LYS PHE SER TYR GLU PHE GLU THR THR GLU LYS ASP SEQRES 53 C 711 SER SER ASN ILE GLU ILE THR LEU ILE GLY SER GLY THR SEQRES 54 C 711 THR TYR LEU ASP ASN LEU SER ILE THR GLU LEU ASN SER SEQRES 55 C 711 THR PRO GLU HIS HIS HIS HIS HIS HIS HET CA C 801 1 HET CA C 802 1 HET CA C 803 1 HET NA C 804 1 HETNAM CA CALCIUM ION HETNAM NA SODIUM ION FORMUL 4 CA 3(CA 2+) FORMUL 7 NA NA 1+ FORMUL 8 HOH *259(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ASP A 61 LYS A 64 5 4 HELIX 3 AA3 THR A 73 ALA A 75 5 3 HELIX 4 AA4 LYS A 83 MET A 87 5 5 HELIX 5 AA5 ASN A 97 LEU A 99 5 3 HELIX 6 AA6 SER A 156 SER A 158 5 3 HELIX 7 AA7 PRO A 200 SER A 203 5 4 HELIX 8 AA8 GLN B 79 LEU B 83 5 5 HELIX 9 AA9 SER B 121 SER B 127 1 7 HELIX 10 AB1 LYS B 183 GLU B 187 1 5 HELIX 11 AB2 ASN B 212 CYS B 214 5 3 HELIX 12 AB3 GLU C 82 LYS C 88 1 7 HELIX 13 AB4 PRO C 181 GLU C 183 5 3 HELIX 14 AB5 PRO C 227 GLY C 234 1 8 HELIX 15 AB6 ASP C 247 GLN C 252 1 6 HELIX 16 AB7 THR C 272 SER C 278 1 7 HELIX 17 AB8 LYS C 286 ASP C 291 5 6 HELIX 18 AB9 THR C 332 ALA C 337 1 6 HELIX 19 AC1 SER C 374 LEU C 379 5 6 HELIX 20 AC2 GLN C 425 ILE C 429 5 5 HELIX 21 AC3 ASN C 450 SER C 456 5 7 HELIX 22 AC4 TYR C 464 GLY C 473 1 10 HELIX 23 AC5 TRP C 503 ILE C 513 1 11 HELIX 24 AC6 THR C 546 GLY C 556 1 11 HELIX 25 AC7 ASP C 581 LYS C 593 1 13 HELIX 26 AC8 LYS C 599 VAL C 603 5 5 HELIX 27 AC9 PRO C 659 LEU C 663 5 5 SHEET 1 AA1 4 GLN A 3 GLN A 6 0 SHEET 2 AA1 4 VAL A 18 SER A 25 -1 O LYS A 23 N VAL A 5 SHEET 3 AA1 4 THR A 77 ILE A 82 -1 O LEU A 80 N ILE A 20 SHEET 4 AA1 4 PHE A 67 GLU A 72 -1 N ALA A 68 O GLN A 81 SHEET 1 AA2 7 GLU A 10 LYS A 12 0 SHEET 2 AA2 7 GLY A 33 GLN A 39 0 SHEET 3 AA2 7 LEU A 45 MET A 51 -1 O LYS A 46 N LYS A 38 SHEET 4 AA2 7 PRO A 57 TYR A 59 -1 O THR A 58 N TRP A 50 SHEET 5 AA2 7 ALA A 88 ARG A 95 -1 O ALA A 93 N ASN A 35 SHEET 6 AA2 7 PHE A 100A TRP A 103 -1 O TYR A 102 N ARG A 94 SHEET 7 AA2 7 THR A 107 VAL A 111 -1 O THR A 107 N TYR A 90 SHEET 1 AA3 5 SER A 120 LEU A 124 0 SHEET 2 AA3 5 MET A 135 TYR A 145 -1 O GLY A 139 N LEU A 124 SHEET 3 AA3 5 VAL A 163 THR A 165 0 SHEET 4 AA3 5 VAL A 169 GLN A 171 0 SHEET 5 AA3 5 LEU A 174 PRO A 184 -1 O LEU A 174 N GLN A 171 SHEET 1 AA4 3 THR A 151 TRP A 154 0 SHEET 2 AA4 3 THR A 194 HIS A 199 -1 O ASN A 196 N THR A 153 SHEET 3 AA4 3 THR A 204 LYS A 209 -1 O VAL A 206 N VAL A 197 SHEET 1 AA5 4 MET B 4 GLN B 6 0 SHEET 2 AA5 4 VAL B 19 ALA B 25 -1 O LYS B 24 N THR B 5 SHEET 3 AA5 4 ASP B 70 ILE B 75 -1 O PHE B 73 N ILE B 21 SHEET 4 AA5 4 PHE B 62 SER B 67 -1 N THR B 63 O THR B 74 SHEET 1 AA6 6 PHE B 10 THR B 13 0 SHEET 2 AA6 6 THR B 102 ILE B 106 1 O GLU B 105 N THR B 13 SHEET 3 AA6 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AA6 6 VAL B 33 GLN B 38 -1 N GLY B 34 O GLN B 89 SHEET 5 AA6 6 LYS B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AA6 6 TYR B 53 ARG B 54 -1 O TYR B 53 N TYR B 49 SHEET 1 AA7 4 THR B 114 PHE B 118 0 SHEET 2 AA7 4 GLY B 129 PHE B 139 -1 O PHE B 135 N SER B 116 SHEET 3 AA7 4 TYR B 173 THR B 182 -1 O LEU B 181 N ALA B 130 SHEET 4 AA7 4 VAL B 159 TRP B 163 -1 N LEU B 160 O THR B 178 SHEET 1 AA8 4 SER B 153 ARG B 155 0 SHEET 2 AA8 4 ASN B 145 ILE B 150 -1 N TRP B 148 O ARG B 155 SHEET 3 AA8 4 SER B 191 THR B 197 -1 O GLU B 195 N LYS B 147 SHEET 4 AA8 4 SER B 202 ASN B 210 -1 O ILE B 205 N ALA B 196 SHEET 1 AA9 6 LEU C 55 PHE C 60 0 SHEET 2 AA9 6 LEU C 68 ILE C 74 -1 O ILE C 74 N LEU C 55 SHEET 3 AA9 6 SER C 99 ILE C 106 -1 O ARG C 101 N TYR C 58 SHEET 4 AA9 6 LEU C 124 VAL C 127 0 SHEET 5 AA9 6 TYR C 147 GLN C 154 -1 O GLU C 152 N LEU C 124 SHEET 6 AA9 6 LEU C 185 PHE C 186 -1 O PHE C 186 N ARG C 105 SHEET 1 AB1 4 THR C 136 MET C 141 0 SHEET 2 AB1 4 GLY C 112 THR C 118 -1 N TYR C 114 O VAL C 139 SHEET 3 AB1 4 LEU C 169 LEU C 173 -1 O TYR C 170 N SER C 117 SHEET 4 AB1 4 MET C 176 ILE C 179 -1 O LYS C 178 N TRP C 171 SHEET 1 AB2 2 TYR C 235 LYS C 238 0 SHEET 2 AB2 2 ILE C 241 LYS C 244 -1 O ILE C 241 N LYS C 238 SHEET 1 AB311 VAL C 300 SER C 310 0 SHEET 2 AB311 THR C 322 SER C 330 -1 O VAL C 323 N ILE C 309 SHEET 3 AB311 ASP C 362 VAL C 367 -1 O ALA C 366 N THR C 328 SHEET 4 AB311 SER C 386 ASN C 397 -1 O ASN C 390 N ILE C 308 SHEET 5 AB311 MET C 403 LEU C 414 0 SHEET 6 AB311 ASP C 417 LYS C 423 -1 O ILE C 422 N THR C 410 SHEET 7 AB311 ASN C 432 LEU C 433 -1 O LEU C 433 N MET C 403 SHEET 8 AB311 THR C 438 TYR C 439 -1 O TYR C 439 N TYR C 395 SHEET 9 AB311 LEU C 447 ALA C 448 -1 O LEU C 447 N VAL C 393 SHEET 10 AB311 ILE C 460 ASN C 463 -1 O ILE C 460 N ILE C 389 SHEET 11 AB311 ILE C 476 ASN C 486 -1 O LYS C 477 N VAL C 413 SHEET 1 AB4 5 ASN C 352 VAL C 353 0 SHEET 2 AB4 5 GLU C 577 PHE C 580 1 O PHE C 580 N ASN C 352 SHEET 3 AB4 5 ASN C 610 LYS C 614 -1 O LEU C 612 N ILE C 579 SHEET 4 AB4 5 SER C 514 ASP C 520 1 N ILE C 518 O ILE C 613 SHEET 5 AB4 5 SER C 525 THR C 531 -1 O TYR C 526 N LEU C 519 SHEET 1 AB5 2 THR C 489 ASN C 491 0 SHEET 2 AB5 2 GLN C 495 VAL C 497 -1 O VAL C 497 N THR C 489 SHEET 1 AB6 3 THR C 558 LYS C 560 0 SHEET 2 AB6 3 LEU C 563 PHE C 566 -1 O TYR C 565 N THR C 558 SHEET 3 AB6 3 ILE C 569 PRO C 570 -1 O ILE C 569 N PHE C 566 SHEET 1 AB7 5 TYR C 618 THR C 620 0 SHEET 2 AB7 5 ASN C 648 LEU C 650 0 SHEET 3 AB7 5 LYS C 667 LYS C 676 0 SHEET 4 AB7 5 THR C 705 GLU C 712 -1 O TYR C 709 N PHE C 671 SHEET 5 AB7 5 THR C 731 SER C 743 -1 O ASN C 742 N ARG C 668 SHEET 1 AB8 4 GLU C 653 ILE C 658 0 SHEET 2 AB8 4 ILE C 721 ILE C 726 -1 O ILE C 721 N ILE C 658 SHEET 3 AB8 4 ILE C 684 LYS C 689 -1 N LYS C 687 O THR C 724 SHEET 4 AB8 4 GLU C 693 LEU C 698 -1 O LEU C 698 N ILE C 684 SSBOND 1 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 2 CYS A 140 CYS A 195 1555 1555 2.04 SSBOND 3 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 4 CYS B 134 CYS B 194 1555 1555 2.04 LINK O ASN C 78 NA NA C 804 1555 1555 2.47 LINK O SER C 166 NA NA C 804 1555 1555 2.41 LINK OG SER C 166 NA NA C 804 1555 1555 2.56 LINK O PRO C 167 NA NA C 804 1555 1555 2.49 LINK OD1 ASN C 168 NA NA C 804 1555 1555 2.34 LINK OD1 ASP C 220 CA CA C 802 1555 1555 2.23 LINK OD2 ASP C 222 CA CA C 801 1555 1555 2.49 LINK OD1 ASP C 222 CA CA C 802 1555 1555 2.38 LINK OD2 ASP C 224 CA CA C 801 1555 1555 2.38 LINK OD1 ASP C 224 CA CA C 802 1555 1555 2.36 LINK O ILE C 226 CA CA C 802 1555 1555 2.35 LINK OE1 GLU C 231 CA CA C 801 1555 1555 2.47 LINK OE2 GLU C 231 CA CA C 801 1555 1555 2.62 LINK OE2 GLU C 231 CA CA C 802 1555 1555 2.15 LINK O ASN C 260 CA CA C 801 1555 1555 2.25 LINK O GLU C 263 CA CA C 801 1555 1555 2.32 LINK OD2 ASP C 273 CA CA C 801 1555 1555 2.23 LINK O ASN C 621 CA CA C 803 1555 1555 2.26 LINK OD2 ASP C 623 CA CA C 803 1555 1555 2.64 LINK O GLN C 644 CA CA C 803 1555 1555 2.33 LINK O SER C 646 CA CA C 803 1555 1555 2.38 LINK OD1 ASP C 734 CA CA C 803 1555 1555 2.36 LINK OD2 ASP C 734 CA CA C 803 1555 1555 2.51 CISPEP 1 PHE A 146 PRO A 147 0 -4.47 CISPEP 2 GLU A 148 PRO A 149 0 -1.83 CISPEP 3 TRP A 188 PRO A 189 0 3.81 CISPEP 4 PRO B 94 PRO B 95 0 9.76 CISPEP 5 TYR B 140 PRO B 141 0 0.87 CISPEP 6 TYR C 439 PRO C 440 0 -4.76 CRYST1 70.229 118.480 166.119 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 0.014239 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008440 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006020 0.00000