HEADER IMMUNE SYSTEM 14-FEB-14 4OTX TITLE STRUCTURE OF THE ANTI-FRANCISELLA TULARENSIS O-ANTIGEN ANTIBODY N203 TITLE 2 FAB FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: N203 LIGHT CHAIN; COMPND 3 CHAIN: L, M; COMPND 4 FRAGMENT: FAB; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: N203 HEAVY CHAIN; COMPND 7 CHAIN: H, I; COMPND 8 FRAGMENT: FAB SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_TAXID: 10090; SOURCE 4 STRAIN: BALB/C; SOURCE 5 OTHER_DETAILS: HYBRIDOMA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_TAXID: 10090; SOURCE 9 STRAIN: BALB/C; SOURCE 10 OTHER_DETAILS: HYBRIDOMA KEYWDS ANTIBODY, IMMUNE SYSTEM, LIPOPOLYSACCHARIDE, INTERNAL EPITOPE EXPDTA X-RAY DIFFRACTION AUTHOR Z.LU,M.J.RYNKIEWICZ,C.-Y.YANG,G.MADICO,H.M.PERKINS,M.I.ROCHE, AUTHOR 2 B.A.SEATON,J.SHARON REVDAT 1 10-SEP-14 4OTX 0 JRNL AUTH Z.LU,M.J.RYNKIEWICZ,C.Y.YANG,G.MADICO,H.M.PERKINS,M.I.ROCHE, JRNL AUTH 2 B.A.SEATON,J.SHARON JRNL TITL FUNCTIONAL AND STRUCTURAL CHARACTERIZATION OF FRANCISELLA JRNL TITL 2 TULARENSIS O-ANTIGEN ANTIBODIES AT THE LOW END OF ANTIGEN JRNL TITL 3 REACTIVITY. JRNL REF MONOCLON ANTIB IMMUNODIAGN V. 33 235 2014 JRNL REF 2 IMMUNOTHER JRNL REFN JRNL PMID 25171003 JRNL DOI 10.1089/MAB.2014.0022 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE- REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO, REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH, REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER REMARK 3 : ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.86 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 57003 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.193 REMARK 3 FREE R VALUE : 0.228 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.380 REMARK 3 FREE R VALUE TEST SET COUNT : 1928 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 14.8575 - 5.0007 0.97 4211 152 0.1656 0.1772 REMARK 3 2 5.0007 - 3.9946 0.99 4149 142 0.1431 0.1547 REMARK 3 3 3.9946 - 3.4972 0.99 4099 145 0.1704 0.1952 REMARK 3 4 3.4972 - 3.1808 0.99 4094 147 0.1992 0.2480 REMARK 3 5 3.1808 - 2.9548 0.99 4086 135 0.2254 0.2743 REMARK 3 6 2.9548 - 2.7818 0.98 4009 142 0.2197 0.2673 REMARK 3 7 2.7818 - 2.6433 0.98 3981 142 0.2253 0.2691 REMARK 3 8 2.6433 - 2.5288 0.97 3962 141 0.2172 0.2793 REMARK 3 9 2.5288 - 2.4319 0.96 3892 134 0.2272 0.2603 REMARK 3 10 2.4319 - 2.3483 0.95 3875 133 0.2219 0.2912 REMARK 3 11 2.3483 - 2.2751 0.94 3803 127 0.2191 0.2724 REMARK 3 12 2.2751 - 2.2103 0.93 3795 139 0.2179 0.2777 REMARK 3 13 2.2103 - 2.1523 0.91 3710 125 0.2145 0.2617 REMARK 3 14 2.1523 - 2.0999 0.84 3409 124 0.2153 0.2649 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) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.400 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 27.28 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.02 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 : 0.002 6670 REMARK 3 ANGLE : 0.674 9079 REMARK 3 CHIRALITY : 0.045 1019 REMARK 3 PLANARITY : 0.003 1149 REMARK 3 DIHEDRAL : 9.953 2386 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 4OTX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-14. REMARK 100 THE RCSB ID CODE IS RCSB084943. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-SEP-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58890 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 15.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0 REMARK 200 DATA REDUNDANCY : 4.100 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 0.34900 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: THE LIGHT CHAIN OF PDB CODE 1MCP AND THE HEAVY (H) REMARK 200 CHAIN OF PDB CODE 3CLE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.98 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY STREAK SEEDING REMARK 280 INTO AN OVERNIGHT EQUILIBRATED DROP CONTAINING 0.5 UL OF FAB REMARK 280 (38MG/ML) AND 0.5 UL OF RESERVOIR SOLUTION [0.1 M SODIUM CITRATE REMARK 280 (PH 4.0), 1 M LITHIUM CHLORIDE, 13-16% PEG 6000], VAPOR REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K 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 33.00550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.38200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.16100 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.38200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.00550 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.16100 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: 4200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18960 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H 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 350 REMARK 350 BIOMOLECULE: 2 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: 5450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19180 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -152.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, I 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 THR L 197 REMARK 465 HIS L 198 REMARK 465 LYS L 199 REMARK 465 THR L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 SER L 203 REMARK 465 GLU L 213 REMARK 465 GLY H 129 REMARK 465 ASP H 130 REMARK 465 THR H 131 REMARK 465 THR H 132 REMARK 465 GLY H 133 REMARK 465 SER H 134 REMARK 465 HIS M 198 REMARK 465 LYS M 199 REMARK 465 THR M 200 REMARK 465 SER M 201 REMARK 465 THR M 202 REMARK 465 SER M 203 REMARK 465 GLY I 129 REMARK 465 ASP I 130 REMARK 465 THR I 131 REMARK 465 THR I 132 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 LEU L 47 -60.75 -105.53 REMARK 500 ALA L 51 -40.46 66.25 REMARK 500 ARG H 95 -117.02 55.16 REMARK 500 ASN H 155 -119.06 55.25 REMARK 500 LEU M 47 -60.07 -106.44 REMARK 500 ALA M 51 -36.34 70.40 REMARK 500 LEU M 83 109.68 -56.88 REMARK 500 ARG I 95 -108.57 54.14 REMARK 500 ASN I 155 -120.72 53.50 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 L 506 DISTANCE = 5.10 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL L 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI M 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 304 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 305 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 306 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 307 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 308 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 309 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: CC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL I 304 DBREF 4OTX L 1 213 PDB 4OTX 4OTX 1 213 DBREF 4OTX M 1 213 PDB 4OTX 4OTX 1 213 DBREF 4OTX H 1 213 PDB 4OTX 4OTX 1 213 DBREF 4OTX I 1 213 PDB 4OTX 4OTX 1 213 SEQRES 1 L 219 GLN ILE VAL MET THR GLN SER PRO SER SER LEU THR VAL SEQRES 2 L 219 THR ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 L 219 GLN SER LEU LEU ASN SER GLY ASN GLN LYS ASN TYR LEU SEQRES 4 L 219 THR TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 L 219 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 L 219 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 219 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA VAL SEQRES 8 L 219 TYR TYR CYS GLN ASN ASP TYR SER TYR PRO LEU THR PHE SEQRES 9 L 219 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 L 219 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 L 219 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 L 219 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 L 219 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 L 219 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 L 219 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 L 219 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 L 219 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU SEQRES 1 H 213 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA ARG SEQRES 2 H 213 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 H 213 TYR THR PHE THR SER TYR TRP MET GLN TRP VAL LYS GLN SEQRES 4 H 213 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR SEQRES 5 H 213 PRO GLY ASP GLY ASP THR ARG TYR THR GLN LYS PHE LYS SEQRES 6 H 213 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 213 ALA TYR MET GLN LEU SER SER LEU ALA SER GLU ASP SER SEQRES 8 H 213 ALA VAL TYR TYR CYS ALA ARG ARG TRP ASP TYR TRP GLY SEQRES 9 H 213 GLN GLY THR THR LEU THR VAL SER SER ALA LYS THR THR SEQRES 10 H 213 ALA PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP SEQRES 11 H 213 THR THR GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS SEQRES 12 H 213 GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER SEQRES 13 H 213 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 H 213 LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR SEQRES 15 H 213 VAL THR SER SER THR TRP PRO SER GLN SER ILE THR CYS SEQRES 16 H 213 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS SEQRES 17 H 213 LYS ILE GLU PRO ARG SEQRES 1 M 219 GLN ILE VAL MET THR GLN SER PRO SER SER LEU THR VAL SEQRES 2 M 219 THR ALA GLY GLU LYS VAL THR MET SER CYS LYS SER SER SEQRES 3 M 219 GLN SER LEU LEU ASN SER GLY ASN GLN LYS ASN TYR LEU SEQRES 4 M 219 THR TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 M 219 LEU ILE TYR TRP ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 M 219 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 M 219 LEU THR ILE SER SER VAL GLN ALA GLU ASP LEU ALA VAL SEQRES 8 M 219 TYR TYR CYS GLN ASN ASP TYR SER TYR PRO LEU THR PHE SEQRES 9 M 219 GLY ALA GLY THR LYS LEU GLU LEU LYS ARG ALA ASP ALA SEQRES 10 M 219 ALA PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN SEQRES 11 M 219 LEU THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN SEQRES 12 M 219 ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE SEQRES 13 M 219 ASP GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP SEQRES 14 M 219 THR ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SEQRES 15 M 219 SER THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS SEQRES 16 M 219 ASN SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SEQRES 17 M 219 SER PRO ILE VAL LYS SER PHE ASN ARG ASN GLU SEQRES 1 I 213 PCA VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA ARG SEQRES 2 I 213 PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY SEQRES 3 I 213 TYR THR PHE THR SER TYR TRP MET GLN TRP VAL LYS GLN SEQRES 4 I 213 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR SEQRES 5 I 213 PRO GLY ASP GLY ASP THR ARG TYR THR GLN LYS PHE LYS SEQRES 6 I 213 GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 I 213 ALA TYR MET GLN LEU SER SER LEU ALA SER GLU ASP SER SEQRES 8 I 213 ALA VAL TYR TYR CYS ALA ARG ARG TRP ASP TYR TRP GLY SEQRES 9 I 213 GLN GLY THR THR LEU THR VAL SER SER ALA LYS THR THR SEQRES 10 I 213 ALA PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP SEQRES 11 I 213 THR THR GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS SEQRES 12 I 213 GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER SEQRES 13 I 213 GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 I 213 LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL THR SEQRES 15 I 213 VAL THR SER SER THR TRP PRO SER GLN SER ILE THR CYS SEQRES 16 I 213 ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS SEQRES 17 I 213 LYS ILE GLU PRO ARG MODRES 4OTX PCA H 1 GLU PYROGLUTAMIC ACID MODRES 4OTX PCA I 1 GLU PYROGLUTAMIC ACID HET PCA H 1 8 HET PCA I 1 8 HET CL L 301 1 HET CL L 302 1 HET CL L 303 1 HET CL L 304 1 HET CL H 301 1 HET CL H 302 1 HET AZI M 301 3 HET CL M 302 1 HET CL M 303 1 HET CL M 304 1 HET CL M 305 1 HET CL M 306 1 HET CL M 307 1 HET CL M 308 1 HET CL M 309 1 HET CL I 301 1 HET CL I 302 1 HET CL I 303 1 HET CL I 304 1 HETNAM PCA PYROGLUTAMIC ACID HETNAM CL CHLORIDE ION HETNAM AZI AZIDE ION FORMUL 2 PCA 2(C5 H7 N O3) FORMUL 5 CL 18(CL 1-) FORMUL 11 AZI N3 1- FORMUL 24 HOH *661(H2 O) HELIX 1 1 GLN L 79 LEU L 83 5 5 HELIX 2 2 SER L 121 GLY L 128 1 8 HELIX 3 3 LYS L 183 GLU L 187 1 5 HELIX 4 4 THR H 28 TYR H 32 5 5 HELIX 5 5 GLN H 61 LYS H 64 5 4 HELIX 6 6 ALA H 83 SER H 87 5 5 HELIX 7 7 LEU H 159 SER H 161 5 3 HELIX 8 8 PRO H 200 SER H 203 5 4 HELIX 9 9 GLN M 79 LEU M 83 5 5 HELIX 10 10 SER M 121 GLY M 128 1 8 HELIX 11 11 LYS M 183 HIS M 189 1 7 HELIX 12 12 THR I 28 TYR I 32 5 5 HELIX 13 13 GLN I 61 LYS I 64 5 4 HELIX 14 14 ALA I 83 SER I 87 5 5 HELIX 15 15 LEU I 159 SER I 161 5 3 HELIX 16 16 PRO I 200 SER I 203 5 4 SHEET 1 A 4 MET L 4 SER L 7 0 SHEET 2 A 4 VAL L 19 SER L 25 -1 O SER L 22 N SER L 7 SHEET 3 A 4 ASP L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 A 4 PHE L 62 SER L 67 -1 N THR L 63 O THR L 74 SHEET 1 B12 THR L 53 ARG L 54 0 SHEET 2 B12 LYS L 45 TYR L 49 -1 N TYR L 49 O THR L 53 SHEET 3 B12 LEU L 33 GLN L 38 -1 N TRP L 35 O ILE L 48 SHEET 4 B12 ALA L 84 ASN L 90 -1 O TYR L 87 N TYR L 36 SHEET 5 B12 THR L 102 LYS L 107 -1 O LEU L 104 N ALA L 84 SHEET 6 B12 SER L 10 THR L 14 1 N VAL L 13 O LYS L 107 SHEET 7 B12 SER M 10 THR M 14 -1 O THR M 12 N SER L 10 SHEET 8 B12 THR M 102 LYS M 107 1 O GLU M 105 N LEU M 11 SHEET 9 B12 ALA M 84 ASN M 90 -1 N ALA M 84 O LEU M 104 SHEET 10 B12 LEU M 33 GLN M 38 -1 N TYR M 36 O TYR M 87 SHEET 11 B12 LYS M 45 TYR M 49 -1 O LYS M 45 N GLN M 37 SHEET 12 B12 THR M 53 ARG M 54 -1 O THR M 53 N TYR M 49 SHEET 1 C 2 LEU L 30 ASN L 30A 0 SHEET 2 C 2 LYS L 30F ASN L 31 -1 O LYS L 30F N ASN L 30A SHEET 1 D 4 THR L 114 PHE L 118 0 SHEET 2 D 4 GLY L 129 PHE L 139 -1 O PHE L 135 N SER L 116 SHEET 3 D 4 TYR L 173 THR L 182 -1 O TYR L 173 N PHE L 139 SHEET 4 D 4 VAL L 159 TRP L 163 -1 N LEU L 160 O THR L 178 SHEET 1 E 4 SER L 153 ARG L 155 0 SHEET 2 E 4 LYS L 147 ILE L 150 -1 N ILE L 150 O SER L 153 SHEET 3 E 4 SER L 191 GLU L 195 -1 O THR L 193 N LYS L 149 SHEET 4 E 4 VAL L 206 ASN L 210 -1 O LYS L 207 N CYS L 194 SHEET 1 F 4 GLN H 3 GLN H 6 0 SHEET 2 F 4 VAL H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 F 4 THR H 77 LEU H 82 -1 O MET H 80 N LEU H 20 SHEET 4 F 4 ALA H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 G 6 GLU H 10 ALA H 12 0 SHEET 2 G 6 THR H 107 VAL H 111 1 O THR H 108 N GLU H 10 SHEET 3 G 6 ALA H 88 ARG H 94 -1 N ALA H 88 O LEU H 109 SHEET 4 G 6 MET H 34 GLN H 39 -1 N GLN H 35 O ALA H 93 SHEET 5 G 6 GLU H 46 ILE H 51 -1 O GLU H 46 N LYS H 38 SHEET 6 G 6 THR H 57 TYR H 59 -1 O ARG H 58 N ALA H 50 SHEET 1 H 4 GLU H 10 ALA H 12 0 SHEET 2 H 4 THR H 107 VAL H 111 1 O THR H 108 N GLU H 10 SHEET 3 H 4 ALA H 88 ARG H 94 -1 N ALA H 88 O LEU H 109 SHEET 4 H 4 TYR H 102 TRP H 103 -1 O TYR H 102 N ARG H 94 SHEET 1 I 4 SER H 120 LEU H 124 0 SHEET 2 I 4 VAL H 136 TYR H 145 -1 O LEU H 141 N TYR H 122 SHEET 3 I 4 LEU H 174 VAL H 183 -1 O LEU H 177 N VAL H 142 SHEET 4 I 4 VAL H 163 THR H 165 -1 N HIS H 164 O SER H 180 SHEET 1 J 4 SER H 120 LEU H 124 0 SHEET 2 J 4 VAL H 136 TYR H 145 -1 O LEU H 141 N TYR H 122 SHEET 3 J 4 LEU H 174 VAL H 183 -1 O LEU H 177 N VAL H 142 SHEET 4 J 4 VAL H 169 GLN H 171 -1 N VAL H 169 O THR H 176 SHEET 1 K 3 THR H 151 TRP H 154 0 SHEET 2 K 3 THR H 194 HIS H 199 -1 O ASN H 196 N THR H 153 SHEET 3 K 3 THR H 204 LYS H 209 -1 O LYS H 208 N CYS H 195 SHEET 1 L 4 MET M 4 SER M 7 0 SHEET 2 L 4 VAL M 19 SER M 25 -1 O LYS M 24 N THR M 5 SHEET 3 L 4 ASP M 70 ILE M 75 -1 O PHE M 71 N CYS M 23 SHEET 4 L 4 PHE M 62 SER M 67 -1 N THR M 63 O THR M 74 SHEET 1 M 4 THR M 114 PHE M 118 0 SHEET 2 M 4 GLY M 129 PHE M 139 -1 O PHE M 135 N SER M 116 SHEET 3 M 4 TYR M 173 THR M 182 -1 O LEU M 179 N VAL M 132 SHEET 4 M 4 VAL M 159 TRP M 163 -1 N LEU M 160 O THR M 178 SHEET 1 N 4 SER M 153 ARG M 155 0 SHEET 2 N 4 VAL M 146 ILE M 150 -1 N ILE M 150 O SER M 153 SHEET 3 N 4 SER M 191 ALA M 196 -1 O THR M 193 N LYS M 149 SHEET 4 N 4 ILE M 205 ASN M 210 -1 O LYS M 207 N CYS M 194 SHEET 1 O 4 GLN I 3 GLN I 6 0 SHEET 2 O 4 VAL I 18 SER I 25 -1 O LYS I 23 N GLN I 5 SHEET 3 O 4 THR I 77 LEU I 82 -1 O MET I 80 N LEU I 20 SHEET 4 O 4 ALA I 67 ASP I 72 -1 N THR I 70 O TYR I 79 SHEET 1 P 6 GLU I 10 ALA I 12 0 SHEET 2 P 6 THR I 107 VAL I 111 1 O THR I 110 N ALA I 12 SHEET 3 P 6 ALA I 88 ARG I 94 -1 N ALA I 88 O LEU I 109 SHEET 4 P 6 MET I 34 GLN I 39 -1 N VAL I 37 O TYR I 91 SHEET 5 P 6 LEU I 45 ILE I 51 -1 O GLU I 46 N LYS I 38 SHEET 6 P 6 THR I 57 TYR I 59 -1 O ARG I 58 N ALA I 50 SHEET 1 Q 4 GLU I 10 ALA I 12 0 SHEET 2 Q 4 THR I 107 VAL I 111 1 O THR I 110 N ALA I 12 SHEET 3 Q 4 ALA I 88 ARG I 94 -1 N ALA I 88 O LEU I 109 SHEET 4 Q 4 TYR I 102 TRP I 103 -1 O TYR I 102 N ARG I 94 SHEET 1 R 4 SER I 120 LEU I 124 0 SHEET 2 R 4 SER I 135 TYR I 145 -1 O LEU I 141 N TYR I 122 SHEET 3 R 4 TYR I 175 THR I 184 -1 O LEU I 177 N VAL I 142 SHEET 4 R 4 VAL I 163 THR I 165 -1 N HIS I 164 O SER I 180 SHEET 1 S 4 SER I 120 LEU I 124 0 SHEET 2 S 4 SER I 135 TYR I 145 -1 O LEU I 141 N TYR I 122 SHEET 3 S 4 TYR I 175 THR I 184 -1 O LEU I 177 N VAL I 142 SHEET 4 S 4 VAL I 169 LEU I 170 -1 N VAL I 169 O THR I 176 SHEET 1 T 3 THR I 151 TRP I 154 0 SHEET 2 T 3 THR I 194 HIS I 199 -1 O ASN I 196 N THR I 153 SHEET 3 T 3 THR I 204 LYS I 209 -1 O LYS I 208 N CYS I 195 SSBOND 1 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 2 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 4 CYS H 140 CYS H 195 1555 1555 2.03 SSBOND 5 CYS M 23 CYS M 88 1555 1555 2.04 SSBOND 6 CYS M 134 CYS M 194 1555 1555 2.03 SSBOND 7 CYS I 22 CYS I 92 1555 1555 2.04 SSBOND 8 CYS I 140 CYS I 195 1555 1555 2.03 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 LINK C PCA I 1 N VAL I 2 1555 1555 1.33 CISPEP 1 SER L 7 PRO L 8 0 -1.45 CISPEP 2 TYR L 94 PRO L 95 0 -0.40 CISPEP 3 TYR L 140 PRO L 141 0 1.06 CISPEP 4 PHE H 146 PRO H 147 0 -3.06 CISPEP 5 GLU H 148 PRO H 149 0 0.56 CISPEP 6 TRP H 188 PRO H 189 0 1.82 CISPEP 7 SER M 7 PRO M 8 0 -1.90 CISPEP 8 TYR M 94 PRO M 95 0 0.73 CISPEP 9 TYR M 140 PRO M 141 0 2.51 CISPEP 10 PHE I 146 PRO I 147 0 -5.64 CISPEP 11 GLU I 148 PRO I 149 0 -2.40 CISPEP 12 TRP I 188 PRO I 189 0 2.62 SITE 1 AC1 3 TRP H 47 PHE L 98 HOH L 436 SITE 1 AC2 2 ILE L 117 LYS L 207 SITE 1 AC3 2 ARG L 108 ALA L 109 SITE 1 AC4 2 PRO L 59 ARG L 61 SITE 1 AC5 4 THR H 30 SER I 156 GLY I 157 SER I 158 SITE 1 AC6 2 ALA H 12 ARG H 13 SITE 1 AC7 6 SER L 10 LEU L 11 THR L 12 SER M 10 SITE 2 AC7 6 LEU M 11 THR M 12 SITE 1 AC8 2 TRP I 47 PHE M 98 SITE 1 AC9 3 ARG I 213 HOH I 432 SER M 122 SITE 1 BC1 2 ILE M 117 LYS M 207 SITE 1 BC2 1 ARG M 54 SITE 1 BC3 2 SER M 30B TYR M 92 SITE 1 BC4 5 LYS M 149 ASP M 151 GLY M 152 SER M 191 SITE 2 BC4 5 THR M 193 SITE 1 BC5 2 PRO M 59 ARG M 61 SITE 1 BC6 3 SER M 65 GLY M 66 THR M 72 SITE 1 BC7 1 VAL I 121 SITE 1 BC8 3 TYR I 145 PRO I 149 VAL I 150 SITE 1 BC9 3 TRP I 154 HOH I 415 HOH I 464 SITE 1 CC1 1 ALA I 71 CRYST1 66.011 122.322 124.764 90.00 90.00 90.00 P 21 21 21 8 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 0.015149 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008175 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008015 0.00000