HEADER IMMUNE SYSTEM 28-MAY-24 8ZNT TITLE CATALYTIC ANTIBODY T99_C220A COMPND MOL_ID: 1; COMPND 2 MOLECULE: CATALYTIC ANTIBODY T99_C220A; COMPND 3 CHAIN: A, B, C, D, E, F, G, H; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CATALYTIC ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.KOBAYASHI,H.YOSHIDA,M.TSUYUGUCHI,R.KATO REVDAT 1 28-MAY-25 8ZNT 0 JRNL AUTH T.UDA,R.KATO,Y.SHIGETA,S.HIROTA,J.KOBAYASHI,H.YOSHIDA, JRNL AUTH 2 M.TSUYUGUCHI,K.HENGPHASATPORN,M.TSUJITA,H.TAGUCHI,E.HIFUMI JRNL TITL STRUCTURAL AND BIOCHEMICAL DIFFERENCES BETWEEN NON-CATALYTIC JRNL TITL 2 AND CATALYTIC ANTIBODIES. JRNL REF MABS V. 17 03978 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40356286 JRNL DOI 10.1080/19420862.2025.2503978 REMARK 2 REMARK 2 RESOLUTION. 2.61 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.17.1 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) : 2.61 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.11 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : 66396 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.254 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860 REMARK 3 FREE R VALUE TEST SET COUNT : 3229 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 28.1100 - 7.3800 0.99 2794 145 0.1793 0.2119 REMARK 3 2 7.3800 - 5.8800 0.98 2756 132 0.2085 0.2551 REMARK 3 3 5.8800 - 5.1400 0.99 2729 175 0.1773 0.2358 REMARK 3 4 5.1400 - 4.6700 0.99 2810 141 0.1615 0.2228 REMARK 3 5 4.6700 - 4.3400 0.99 2781 126 0.1536 0.1838 REMARK 3 6 4.3400 - 4.0800 0.99 2789 125 0.1703 0.2376 REMARK 3 7 4.0800 - 3.8800 0.99 2742 138 0.1832 0.2546 REMARK 3 8 3.8800 - 3.7100 0.99 2808 146 0.1896 0.2463 REMARK 3 9 3.7100 - 3.5700 0.99 2761 164 0.1925 0.2534 REMARK 3 10 3.5700 - 3.4500 0.99 2780 134 0.1939 0.2450 REMARK 3 11 3.4500 - 3.3400 0.99 2766 148 0.2006 0.2580 REMARK 3 12 3.3400 - 3.2400 0.99 2760 149 0.2069 0.2810 REMARK 3 13 3.2400 - 3.1600 0.99 2761 132 0.2086 0.2774 REMARK 3 14 3.1600 - 3.0800 0.99 2753 140 0.2057 0.2846 REMARK 3 15 3.0800 - 3.0100 0.99 2762 155 0.2206 0.2902 REMARK 3 16 3.0100 - 2.9500 0.98 2734 150 0.2290 0.2812 REMARK 3 17 2.9500 - 2.8900 0.98 2797 134 0.2334 0.2951 REMARK 3 18 2.8900 - 2.8300 0.98 2739 120 0.2293 0.2940 REMARK 3 19 2.8300 - 2.7800 0.98 2789 144 0.2436 0.3389 REMARK 3 20 2.7800 - 2.7400 0.98 2730 149 0.2560 0.3959 REMARK 3 21 2.7400 - 2.6900 0.98 2775 127 0.2545 0.3419 REMARK 3 22 2.6900 - 2.6500 0.98 2751 128 0.2669 0.3304 REMARK 3 23 2.6500 - 2.6100 0.82 2300 127 0.2613 0.3340 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) : 0.357 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.872 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.34 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.62 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 13926 REMARK 3 ANGLE : 0.568 18793 REMARK 3 CHIRALITY : 0.043 2079 REMARK 3 PLANARITY : 0.003 2405 REMARK 3 DIHEDRAL : 18.624 1979 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 8ZNT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1300047857. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-DEC-17 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 : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66456 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6 REMARK 200 DATA REDUNDANCY : 3.900 REMARK 200 R MERGE (I) : 0.07800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 22.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.44400 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: 4HCR REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.82 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 14%(W/V) PG3350, 0.4 M KSCN, 0.1 M REMARK 280 HEPES(PH7.5), 30%(V/V) GLYCEROL, VAPOR DIFFUSION, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,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 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8 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: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D 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: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E 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: 6 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F 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: 7 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: G 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: 8 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLU A 219 REMARK 465 ALA A 220 REMARK 465 LEU A 221 REMARK 465 GLU A 222 REMARK 465 VAL A 223 REMARK 465 LEU A 224 REMARK 465 PHE A 225 REMARK 465 GLN A 226 REMARK 465 MET B 1 REMARK 465 GLU B 219 REMARK 465 ALA B 220 REMARK 465 LEU B 221 REMARK 465 GLU B 222 REMARK 465 VAL B 223 REMARK 465 LEU B 224 REMARK 465 PHE B 225 REMARK 465 GLN B 226 REMARK 465 GLU C 219 REMARK 465 ALA C 220 REMARK 465 LEU C 221 REMARK 465 GLU C 222 REMARK 465 VAL C 223 REMARK 465 LEU C 224 REMARK 465 PHE C 225 REMARK 465 GLN C 226 REMARK 465 MET D 1 REMARK 465 GLU D 219 REMARK 465 ALA D 220 REMARK 465 LEU D 221 REMARK 465 GLU D 222 REMARK 465 VAL D 223 REMARK 465 LEU D 224 REMARK 465 PHE D 225 REMARK 465 GLN D 226 REMARK 465 LEU E 221 REMARK 465 GLU E 222 REMARK 465 VAL E 223 REMARK 465 LEU E 224 REMARK 465 PHE E 225 REMARK 465 GLN E 226 REMARK 465 MET F 1 REMARK 465 ALA F 220 REMARK 465 LEU F 221 REMARK 465 GLU F 222 REMARK 465 VAL F 223 REMARK 465 LEU F 224 REMARK 465 PHE F 225 REMARK 465 GLN F 226 REMARK 465 MET G 1 REMARK 465 GLU G 219 REMARK 465 ALA G 220 REMARK 465 LEU G 221 REMARK 465 GLU G 222 REMARK 465 VAL G 223 REMARK 465 LEU G 224 REMARK 465 PHE G 225 REMARK 465 GLN G 226 REMARK 465 MET H 1 REMARK 465 PHE H 225 REMARK 465 GLN H 226 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU F 171 CG CD OE1 OE2 REMARK 470 LYS F 196 CG CD CE NZ REMARK 470 GLU G 171 CG CD OE1 OE2 REMARK 470 GLU H 171 CG CD OE1 OE2 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 ASP A 2 98.17 61.46 REMARK 500 ALA A 57 -42.45 65.21 REMARK 500 ASN A 144 74.22 53.64 REMARK 500 LYS A 175 -62.28 -99.37 REMARK 500 LEU B 12 117.47 -161.28 REMARK 500 ALA B 57 -40.23 70.81 REMARK 500 SER B 73 -110.41 -80.38 REMARK 500 ASN B 144 80.61 52.32 REMARK 500 LYS B 175 -73.10 -92.88 REMARK 500 ASP C 34 1.83 -173.91 REMARK 500 ALA C 57 -48.60 70.15 REMARK 500 ARG C 83 82.85 56.13 REMARK 500 ASN C 144 82.56 53.67 REMARK 500 ARG C 217 -79.06 -73.12 REMARK 500 ALA D 57 -50.84 72.18 REMARK 500 SER D 73 -86.37 -82.59 REMARK 500 ARG D 83 107.12 -162.03 REMARK 500 ASN D 144 76.88 53.58 REMARK 500 ALA E 57 -49.98 69.74 REMARK 500 ASN E 144 69.31 61.17 REMARK 500 THR E 170 77.34 -40.60 REMARK 500 GLU E 171 79.00 -171.50 REMARK 500 LYS E 175 -60.07 -106.05 REMARK 500 GLU E 219 -71.29 -68.23 REMARK 500 ALA F 57 -51.68 73.10 REMARK 500 ASN F 144 71.47 60.05 REMARK 500 PRO F 147 -162.05 -79.89 REMARK 500 SER F 162 119.32 -162.82 REMARK 500 ALA G 57 -47.64 69.83 REMARK 500 ASN G 144 73.30 57.11 REMARK 500 PRO G 147 -154.69 -79.67 REMARK 500 SER G 162 100.89 -164.85 REMARK 500 GLU G 171 87.30 -51.97 REMARK 500 GLN G 172 -155.07 59.01 REMARK 500 SER G 174 1.05 -68.58 REMARK 500 ALA H 57 -48.99 64.57 REMARK 500 ARG H 83 71.43 53.81 REMARK 500 ASN H 144 73.77 59.57 REMARK 500 PRO H 147 -164.21 -76.57 REMARK 500 LYS H 196 -55.66 -124.83 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 K A 310 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA A 118 O REMARK 620 2 SER A 120 OG 103.6 REMARK 620 3 ASN A 143 O 88.7 78.2 REMARK 620 4 ASN A 144 O 76.1 135.8 57.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K B 306 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA B 118 O REMARK 620 2 SER B 120 OG 93.5 REMARK 620 3 ASN B 143 O 89.0 84.4 REMARK 620 4 ASN B 144 O 77.3 139.7 56.7 REMARK 620 5 EDO B 304 O2 161.9 68.8 85.7 113.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K C 309 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA C 118 O REMARK 620 2 SER C 120 OG 108.3 REMARK 620 3 ASN C 143 O 88.6 76.2 REMARK 620 4 ASN C 144 O 68.0 131.5 55.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K D 309 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA D 118 O REMARK 620 2 SER D 120 OG 102.2 REMARK 620 3 ASN D 143 O 89.9 89.7 REMARK 620 4 ASN D 144 O 72.0 146.4 57.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K E 310 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA E 118 O REMARK 620 2 SER E 120 OG 106.0 REMARK 620 3 ASN E 143 O 97.0 85.8 REMARK 620 4 ASN E 144 O 78.0 151.5 65.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K F 309 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA F 118 O REMARK 620 2 ASN F 143 O 89.7 REMARK 620 3 ASN F 144 O 74.3 63.2 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K G 312 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA G 118 O REMARK 620 2 SER G 120 OG 105.9 REMARK 620 3 ASN G 143 O 97.1 87.2 REMARK 620 4 ASN G 144 O 79.0 150.1 62.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K H 308 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ALA H 118 O REMARK 620 2 SER H 120 OG 101.6 REMARK 620 3 ASN H 143 O 93.6 77.9 REMARK 620 4 ASN H 144 O 82.0 137.7 59.8 REMARK 620 N 1 2 3 DBREF 8ZNT A 1 226 PDB 8ZNT 8ZNT 1 226 DBREF 8ZNT B 1 226 PDB 8ZNT 8ZNT 1 226 DBREF 8ZNT C 1 226 PDB 8ZNT 8ZNT 1 226 DBREF 8ZNT D 1 226 PDB 8ZNT 8ZNT 1 226 DBREF 8ZNT E 1 226 PDB 8ZNT 8ZNT 1 226 DBREF 8ZNT F 1 226 PDB 8ZNT 8ZNT 1 226 DBREF 8ZNT G 1 226 PDB 8ZNT 8ZNT 1 226 DBREF 8ZNT H 1 226 PDB 8ZNT 8ZNT 1 226 SEQRES 1 A 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 A 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 A 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 A 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 A 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 A 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 A 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 A 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 A 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 A 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 A 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 A 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 A 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 A 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 A 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 A 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 A 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 A 226 GLU VAL LEU PHE GLN SEQRES 1 B 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 B 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 B 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 B 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 B 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 B 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 B 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 B 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 B 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 B 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 B 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 B 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 B 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 B 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 B 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 B 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 B 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 B 226 GLU VAL LEU PHE GLN SEQRES 1 C 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 C 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 C 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 C 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 C 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 C 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 C 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 C 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 C 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 C 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 C 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 C 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 C 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 C 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 C 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 C 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 C 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 C 226 GLU VAL LEU PHE GLN SEQRES 1 D 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 D 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 D 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 D 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 D 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 D 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 D 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 D 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 D 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 D 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 D 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 D 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 D 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 D 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 D 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 D 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 D 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 D 226 GLU VAL LEU PHE GLN SEQRES 1 E 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 E 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 E 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 E 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 E 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 E 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 E 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 E 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 E 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 E 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 E 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 E 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 E 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 E 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 E 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 E 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 E 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 E 226 GLU VAL LEU PHE GLN SEQRES 1 F 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 F 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 F 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 F 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 F 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 F 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 F 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 F 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 F 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 F 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 F 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 F 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 F 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 F 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 F 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 F 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 F 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 F 226 GLU VAL LEU PHE GLN SEQRES 1 G 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 G 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 G 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 G 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 G 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 G 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 G 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 G 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 G 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 G 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 G 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 G 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 G 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 G 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 G 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 G 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 G 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 G 226 GLU VAL LEU PHE GLN SEQRES 1 H 226 MET ASP ILE VAL MET THR GLN THR PRO VAL SER LEU ALA SEQRES 2 H 226 VAL THR PRO GLY GLN SER ALA SER ILE SER CYS ARG SER SEQRES 3 H 226 SER GLN SER LEU LEU HIS GLY ASP GLY ARG SER TYR LEU SEQRES 4 H 226 TYR TRP TYR VAL GLN ARG PRO GLY GLN SER PRO GLN LEU SEQRES 5 H 226 LEU MET TYR GLU ALA SER THR ARG VAL SER GLY VAL PRO SEQRES 6 H 226 ASP ARG PHE THR GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 H 226 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL SEQRES 8 H 226 TYR TYR CYS MET GLN GLY THR HIS TRP PRO GLY THR PHE SEQRES 9 H 226 GLY PRO GLY THR LYS VAL ASP ILE LYS ARG THR VAL ALA SEQRES 10 H 226 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 H 226 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 H 226 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 H 226 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 H 226 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 H 226 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 H 226 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 H 226 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU ALA LEU SEQRES 18 H 226 GLU VAL LEU PHE GLN HET GOL A 301 6 HET EDO A 302 4 HET EDO A 303 4 HET EDO A 304 4 HET EDO A 305 4 HET EDO A 306 4 HET EDO A 307 4 HET EDO A 308 4 HET PEG A 309 7 HET K A 310 1 HET CL A 311 1 HET GOL B 301 6 HET EDO B 302 4 HET EDO B 303 4 HET EDO B 304 4 HET EDO B 305 4 HET K B 306 1 HET K B 307 1 HET CL B 308 1 HET CL B 309 1 HET CL B 310 1 HET GOL C 301 6 HET EDO C 302 4 HET EDO C 303 4 HET EDO C 304 4 HET EDO C 305 4 HET EDO C 306 4 HET EDO C 307 4 HET EDO C 308 4 HET K C 309 1 HET CL C 310 1 HET EDO D 301 4 HET EDO D 302 4 HET EDO D 303 4 HET EDO D 304 4 HET EDO D 305 4 HET EDO D 306 4 HET EDO D 307 4 HET EDO D 308 4 HET K D 309 1 HET CL D 310 1 HET CL D 311 1 HET GOL E 301 6 HET GOL E 302 6 HET GOL E 303 6 HET GOL E 304 6 HET EDO E 305 4 HET EDO E 306 4 HET EDO E 307 4 HET EDO E 308 4 HET EDO E 309 4 HET K E 310 1 HET CL E 311 1 HET CL E 312 1 HET GOL F 301 6 HET GOL F 302 6 HET GOL F 303 6 HET EDO F 304 4 HET EDO F 305 4 HET EDO F 306 4 HET EDO F 307 4 HET EDO F 308 4 HET K F 309 1 HET CL F 310 1 HET GOL G 301 6 HET GOL G 302 6 HET GOL G 303 6 HET GOL G 304 6 HET GOL G 305 6 HET EDO G 306 4 HET EDO G 307 4 HET EDO G 308 4 HET EDO G 309 4 HET EDO G 310 4 HET PEG G 311 7 HET K G 312 1 HET CL G 313 1 HET CL G 314 1 HET GOL H 301 6 HET EDO H 302 4 HET EDO H 303 4 HET EDO H 304 4 HET EDO H 305 4 HET EDO H 306 4 HET EDO H 307 4 HET K H 308 1 HET CL H 309 1 HETNAM GOL GLYCEROL HETNAM EDO 1,2-ETHANEDIOL HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM K POTASSIUM ION HETNAM CL CHLORIDE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 9 GOL 16(C3 H8 O3) FORMUL 10 EDO 47(C2 H6 O2) FORMUL 17 PEG 2(C4 H10 O3) FORMUL 18 K 9(K 1+) FORMUL 19 CL 13(CL 1-) FORMUL 96 HOH *159(H2 O) HELIX 1 AA1 GLU A 85 VAL A 89 5 5 HELIX 2 AA2 SER A 127 SER A 133 1 7 HELIX 3 AA3 LYS A 189 GLU A 193 1 5 HELIX 4 AA4 GLU B 85 VAL B 89 5 5 HELIX 5 AA5 SER B 127 SER B 133 1 7 HELIX 6 AA6 LYS B 189 GLU B 193 1 5 HELIX 7 AA7 GLU C 85 VAL C 89 5 5 HELIX 8 AA8 SER C 127 SER C 133 1 7 HELIX 9 AA9 LYS C 189 GLU C 193 1 5 HELIX 10 AB1 GLU D 85 VAL D 89 5 5 HELIX 11 AB2 SER D 127 LYS D 132 1 6 HELIX 12 AB3 LYS D 189 GLU D 193 1 5 HELIX 13 AB4 GLU E 85 VAL E 89 5 5 HELIX 14 AB5 SER E 127 LYS E 132 1 6 HELIX 15 AB6 LYS E 189 LYS E 194 1 6 HELIX 16 AB7 GLU F 85 VAL F 89 5 5 HELIX 17 AB8 SER F 127 LYS F 132 1 6 HELIX 18 AB9 LYS F 189 GLU F 193 1 5 HELIX 19 AC1 GLU G 85 VAL G 89 5 5 HELIX 20 AC2 SER G 127 LYS G 132 1 6 HELIX 21 AC3 LYS G 189 LYS G 194 1 6 HELIX 22 AC4 GLU H 85 VAL H 89 5 5 HELIX 23 AC5 SER H 127 SER H 133 1 7 HELIX 24 AC6 LYS H 189 LYS H 194 1 6 SHEET 1 AA1 4 MET A 5 THR A 8 0 SHEET 2 AA1 4 ALA A 20 SER A 26 -1 O ARG A 25 N THR A 6 SHEET 3 AA1 4 ASP A 76 ILE A 81 -1 O LEU A 79 N ILE A 22 SHEET 4 AA1 4 PHE A 68 SER A 73 -1 N SER A 71 O THR A 78 SHEET 1 AA2 6 SER A 11 VAL A 14 0 SHEET 2 AA2 6 THR A 108 ILE A 112 1 O LYS A 109 N LEU A 12 SHEET 3 AA2 6 GLY A 90 GLN A 96 -1 N TYR A 92 O THR A 108 SHEET 4 AA2 6 LEU A 39 GLN A 44 -1 N TYR A 42 O TYR A 93 SHEET 5 AA2 6 GLN A 51 TYR A 55 -1 O MET A 54 N TRP A 41 SHEET 6 AA2 6 THR A 59 ARG A 60 -1 O THR A 59 N TYR A 55 SHEET 1 AA3 4 SER A 11 VAL A 14 0 SHEET 2 AA3 4 THR A 108 ILE A 112 1 O LYS A 109 N LEU A 12 SHEET 3 AA3 4 GLY A 90 GLN A 96 -1 N TYR A 92 O THR A 108 SHEET 4 AA3 4 THR A 103 PHE A 104 -1 O THR A 103 N GLN A 96 SHEET 1 AA4 4 SER A 120 PHE A 124 0 SHEET 2 AA4 4 THR A 135 PHE A 145 -1 O LEU A 141 N PHE A 122 SHEET 3 AA4 4 TYR A 179 SER A 188 -1 O LEU A 187 N ALA A 136 SHEET 4 AA4 4 SER A 165 VAL A 169 -1 N GLN A 166 O THR A 184 SHEET 1 AA5 4 ALA A 159 GLN A 161 0 SHEET 2 AA5 4 ALA A 150 VAL A 156 -1 N VAL A 156 O ALA A 159 SHEET 3 AA5 4 VAL A 197 HIS A 204 -1 O GLU A 201 N GLN A 153 SHEET 4 AA5 4 VAL A 211 ASN A 216 -1 O VAL A 211 N VAL A 202 SHEET 1 AA6 4 MET B 5 THR B 8 0 SHEET 2 AA6 4 ALA B 20 SER B 26 -1 O SER B 23 N THR B 8 SHEET 3 AA6 4 ASP B 76 ILE B 81 -1 O LEU B 79 N ILE B 22 SHEET 4 AA6 4 PHE B 68 GLY B 72 -1 N SER B 71 O THR B 78 SHEET 1 AA7 6 SER B 11 VAL B 14 0 SHEET 2 AA7 6 THR B 108 ILE B 112 1 O LYS B 109 N LEU B 12 SHEET 3 AA7 6 GLY B 90 GLN B 96 -1 N GLY B 90 O VAL B 110 SHEET 4 AA7 6 LEU B 39 GLN B 44 -1 N TYR B 42 O TYR B 93 SHEET 5 AA7 6 GLN B 51 TYR B 55 -1 O MET B 54 N TRP B 41 SHEET 6 AA7 6 THR B 59 ARG B 60 -1 O THR B 59 N TYR B 55 SHEET 1 AA8 4 SER B 11 VAL B 14 0 SHEET 2 AA8 4 THR B 108 ILE B 112 1 O LYS B 109 N LEU B 12 SHEET 3 AA8 4 GLY B 90 GLN B 96 -1 N GLY B 90 O VAL B 110 SHEET 4 AA8 4 THR B 103 PHE B 104 -1 O THR B 103 N GLN B 96 SHEET 1 AA9 4 SER B 120 PHE B 124 0 SHEET 2 AA9 4 THR B 135 PHE B 145 -1 O LEU B 141 N PHE B 122 SHEET 3 AA9 4 TYR B 179 SER B 188 -1 O LEU B 185 N VAL B 138 SHEET 4 AA9 4 SER B 165 VAL B 169 -1 N GLN B 166 O THR B 184 SHEET 1 AB1 3 ALA B 150 VAL B 156 0 SHEET 2 AB1 3 VAL B 197 HIS B 204 -1 O GLU B 201 N GLN B 153 SHEET 3 AB1 3 VAL B 211 ASN B 216 -1 O VAL B 211 N VAL B 202 SHEET 1 AB2 4 MET C 5 THR C 8 0 SHEET 2 AB2 4 ALA C 20 SER C 26 -1 O SER C 23 N THR C 8 SHEET 3 AB2 4 ASP C 76 ILE C 81 -1 O LEU C 79 N ILE C 22 SHEET 4 AB2 4 PHE C 68 SER C 73 -1 N SER C 71 O THR C 78 SHEET 1 AB3 6 SER C 11 VAL C 14 0 SHEET 2 AB3 6 THR C 108 ILE C 112 1 O LYS C 109 N LEU C 12 SHEET 3 AB3 6 GLY C 90 GLN C 96 -1 N TYR C 92 O THR C 108 SHEET 4 AB3 6 LEU C 39 ARG C 45 -1 N TYR C 42 O TYR C 93 SHEET 5 AB3 6 GLN C 48 TYR C 55 -1 O MET C 54 N TRP C 41 SHEET 6 AB3 6 THR C 59 ARG C 60 -1 O THR C 59 N TYR C 55 SHEET 1 AB4 4 SER C 11 VAL C 14 0 SHEET 2 AB4 4 THR C 108 ILE C 112 1 O LYS C 109 N LEU C 12 SHEET 3 AB4 4 GLY C 90 GLN C 96 -1 N TYR C 92 O THR C 108 SHEET 4 AB4 4 THR C 103 PHE C 104 -1 O THR C 103 N GLN C 96 SHEET 1 AB5 4 SER C 120 PHE C 124 0 SHEET 2 AB5 4 THR C 135 PHE C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AB5 4 TYR C 179 SER C 188 -1 O LEU C 181 N LEU C 142 SHEET 4 AB5 4 SER C 165 VAL C 169 -1 N GLN C 166 O THR C 184 SHEET 1 AB6 4 ALA C 159 GLN C 161 0 SHEET 2 AB6 4 LYS C 151 VAL C 156 -1 N TRP C 154 O GLN C 161 SHEET 3 AB6 4 VAL C 197 THR C 203 -1 O GLU C 201 N GLN C 153 SHEET 4 AB6 4 VAL C 211 ASN C 216 -1 O VAL C 211 N VAL C 202 SHEET 1 AB7 4 MET D 5 THR D 8 0 SHEET 2 AB7 4 ALA D 20 SER D 26 -1 O ARG D 25 N THR D 6 SHEET 3 AB7 4 ASP D 76 ILE D 81 -1 O LEU D 79 N ILE D 22 SHEET 4 AB7 4 PHE D 68 GLY D 72 -1 N THR D 69 O LYS D 80 SHEET 1 AB8 6 SER D 11 VAL D 14 0 SHEET 2 AB8 6 THR D 108 ILE D 112 1 O LYS D 109 N LEU D 12 SHEET 3 AB8 6 GLY D 90 GLN D 96 -1 N GLY D 90 O VAL D 110 SHEET 4 AB8 6 LEU D 39 GLN D 44 -1 N TYR D 42 O TYR D 93 SHEET 5 AB8 6 GLN D 51 TYR D 55 -1 O GLN D 51 N VAL D 43 SHEET 6 AB8 6 THR D 59 ARG D 60 -1 O THR D 59 N TYR D 55 SHEET 1 AB9 4 SER D 11 VAL D 14 0 SHEET 2 AB9 4 THR D 108 ILE D 112 1 O LYS D 109 N LEU D 12 SHEET 3 AB9 4 GLY D 90 GLN D 96 -1 N GLY D 90 O VAL D 110 SHEET 4 AB9 4 THR D 103 PHE D 104 -1 O THR D 103 N GLN D 96 SHEET 1 AC1 4 SER D 120 PHE D 124 0 SHEET 2 AC1 4 THR D 135 PHE D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AC1 4 TYR D 179 SER D 188 -1 O LEU D 187 N ALA D 136 SHEET 4 AC1 4 SER D 165 VAL D 169 -1 N GLN D 166 O THR D 184 SHEET 1 AC2 3 ALA D 150 VAL D 156 0 SHEET 2 AC2 3 VAL D 197 HIS D 204 -1 O ALA D 199 N LYS D 155 SHEET 3 AC2 3 VAL D 211 ASN D 216 -1 O VAL D 211 N VAL D 202 SHEET 1 AC3 4 MET E 5 THR E 8 0 SHEET 2 AC3 4 ALA E 20 SER E 26 -1 O ARG E 25 N THR E 6 SHEET 3 AC3 4 ASP E 76 ILE E 81 -1 O LEU E 79 N ILE E 22 SHEET 4 AC3 4 PHE E 68 SER E 73 -1 N SER E 71 O THR E 78 SHEET 1 AC4 6 SER E 11 VAL E 14 0 SHEET 2 AC4 6 THR E 108 ILE E 112 1 O ASP E 111 N LEU E 12 SHEET 3 AC4 6 GLY E 90 GLN E 96 -1 N GLY E 90 O VAL E 110 SHEET 4 AC4 6 LEU E 39 ARG E 45 -1 N TYR E 42 O TYR E 93 SHEET 5 AC4 6 GLN E 48 TYR E 55 -1 O MET E 54 N TRP E 41 SHEET 6 AC4 6 THR E 59 ARG E 60 -1 O THR E 59 N TYR E 55 SHEET 1 AC5 4 SER E 11 VAL E 14 0 SHEET 2 AC5 4 THR E 108 ILE E 112 1 O ASP E 111 N LEU E 12 SHEET 3 AC5 4 GLY E 90 GLN E 96 -1 N GLY E 90 O VAL E 110 SHEET 4 AC5 4 THR E 103 PHE E 104 -1 O THR E 103 N GLN E 96 SHEET 1 AC6 4 SER E 120 PHE E 124 0 SHEET 2 AC6 4 THR E 135 PHE E 145 -1 O VAL E 139 N PHE E 124 SHEET 3 AC6 4 TYR E 179 SER E 188 -1 O LEU E 181 N LEU E 142 SHEET 4 AC6 4 SER E 165 SER E 168 -1 N SER E 168 O SER E 182 SHEET 1 AC7 4 ALA E 159 LEU E 160 0 SHEET 2 AC7 4 LYS E 151 VAL E 156 -1 N VAL E 156 O ALA E 159 SHEET 3 AC7 4 VAL E 197 THR E 203 -1 O GLU E 201 N GLN E 153 SHEET 4 AC7 4 VAL E 211 ASN E 216 -1 O LYS E 213 N CYS E 200 SHEET 1 AC8 4 MET F 5 THR F 8 0 SHEET 2 AC8 4 ALA F 20 SER F 26 -1 O ARG F 25 N THR F 6 SHEET 3 AC8 4 ASP F 76 ILE F 81 -1 O LEU F 79 N ILE F 22 SHEET 4 AC8 4 PHE F 68 SER F 73 -1 N SER F 71 O THR F 78 SHEET 1 AC912 THR F 59 ARG F 60 0 SHEET 2 AC912 GLN F 51 TYR F 55 -1 N TYR F 55 O THR F 59 SHEET 3 AC912 LEU F 39 GLN F 44 -1 N TRP F 41 O LEU F 53 SHEET 4 AC912 GLY F 90 GLN F 96 -1 O TYR F 93 N TYR F 42 SHEET 5 AC912 THR F 108 ILE F 112 -1 O VAL F 110 N GLY F 90 SHEET 6 AC912 SER F 11 VAL F 14 1 N LEU F 12 O ASP F 111 SHEET 7 AC912 SER G 11 VAL G 14 -1 O SER G 11 N ALA F 13 SHEET 8 AC912 THR G 108 ILE G 112 1 O ASP G 111 N LEU G 12 SHEET 9 AC912 GLY G 90 GLN G 96 -1 N TYR G 92 O THR G 108 SHEET 10 AC912 LEU G 39 GLN G 44 -1 N GLN G 44 O VAL G 91 SHEET 11 AC912 GLN G 51 TYR G 55 -1 O MET G 54 N TRP G 41 SHEET 12 AC912 THR G 59 ARG G 60 -1 O THR G 59 N TYR G 55 SHEET 1 AD1 8 THR F 103 PHE F 104 0 SHEET 2 AD1 8 GLY F 90 GLN F 96 -1 N GLN F 96 O THR F 103 SHEET 3 AD1 8 THR F 108 ILE F 112 -1 O VAL F 110 N GLY F 90 SHEET 4 AD1 8 SER F 11 VAL F 14 1 N LEU F 12 O ASP F 111 SHEET 5 AD1 8 SER G 11 VAL G 14 -1 O SER G 11 N ALA F 13 SHEET 6 AD1 8 THR G 108 ILE G 112 1 O ASP G 111 N LEU G 12 SHEET 7 AD1 8 GLY G 90 GLN G 96 -1 N TYR G 92 O THR G 108 SHEET 8 AD1 8 THR G 103 PHE G 104 -1 O THR G 103 N GLN G 96 SHEET 1 AD2 4 SER F 120 PHE F 124 0 SHEET 2 AD2 4 THR F 135 PHE F 145 -1 O LEU F 141 N PHE F 122 SHEET 3 AD2 4 TYR F 179 SER F 188 -1 O LEU F 185 N VAL F 138 SHEET 4 AD2 4 SER F 165 VAL F 169 -1 N SER F 168 O SER F 182 SHEET 1 AD3 3 LYS F 151 VAL F 156 0 SHEET 2 AD3 3 VAL F 197 THR F 203 -1 O GLU F 201 N GLN F 153 SHEET 3 AD3 3 VAL F 211 ASN F 216 -1 O VAL F 211 N VAL F 202 SHEET 1 AD4 4 MET G 5 THR G 8 0 SHEET 2 AD4 4 ALA G 20 SER G 26 -1 O ARG G 25 N THR G 6 SHEET 3 AD4 4 ASP G 76 ILE G 81 -1 O LEU G 79 N ILE G 22 SHEET 4 AD4 4 PHE G 68 SER G 73 -1 N SER G 71 O THR G 78 SHEET 1 AD5 4 SER G 120 PHE G 124 0 SHEET 2 AD5 4 THR G 135 PHE G 145 -1 O LEU G 141 N PHE G 122 SHEET 3 AD5 4 TYR G 179 SER G 188 -1 O LEU G 181 N LEU G 142 SHEET 4 AD5 4 SER G 165 THR G 170 -1 N SER G 168 O SER G 182 SHEET 1 AD6 4 ALA G 159 LEU G 160 0 SHEET 2 AD6 4 LYS G 151 VAL G 156 -1 N VAL G 156 O ALA G 159 SHEET 3 AD6 4 VAL G 197 THR G 203 -1 O GLU G 201 N GLN G 153 SHEET 4 AD6 4 VAL G 211 ASN G 216 -1 O VAL G 211 N VAL G 202 SHEET 1 AD7 4 MET H 5 THR H 8 0 SHEET 2 AD7 4 ALA H 20 SER H 26 -1 O ARG H 25 N THR H 6 SHEET 3 AD7 4 ASP H 76 ILE H 81 -1 O ILE H 81 N ALA H 20 SHEET 4 AD7 4 PHE H 68 SER H 73 -1 N SER H 71 O THR H 78 SHEET 1 AD8 6 SER H 11 VAL H 14 0 SHEET 2 AD8 6 THR H 108 ILE H 112 1 O ASP H 111 N LEU H 12 SHEET 3 AD8 6 GLY H 90 GLN H 96 -1 N GLY H 90 O VAL H 110 SHEET 4 AD8 6 TYR H 40 GLN H 44 -1 N TYR H 42 O TYR H 93 SHEET 5 AD8 6 GLN H 51 TYR H 55 -1 O LEU H 53 N TRP H 41 SHEET 6 AD8 6 THR H 59 ARG H 60 -1 O THR H 59 N TYR H 55 SHEET 1 AD9 4 SER H 11 VAL H 14 0 SHEET 2 AD9 4 THR H 108 ILE H 112 1 O ASP H 111 N LEU H 12 SHEET 3 AD9 4 GLY H 90 GLN H 96 -1 N GLY H 90 O VAL H 110 SHEET 4 AD9 4 THR H 103 PHE H 104 -1 O THR H 103 N GLN H 96 SHEET 1 AE1 4 SER H 120 PHE H 124 0 SHEET 2 AE1 4 THR H 135 PHE H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AE1 4 TYR H 179 SER H 188 -1 O LEU H 187 N ALA H 136 SHEET 4 AE1 4 SER H 165 THR H 170 -1 N GLN H 166 O THR H 184 SHEET 1 AE2 4 ALA H 159 LEU H 160 0 SHEET 2 AE2 4 LYS H 151 VAL H 156 -1 N VAL H 156 O ALA H 159 SHEET 3 AE2 4 VAL H 197 THR H 203 -1 O ALA H 199 N LYS H 155 SHEET 4 AE2 4 VAL H 211 ASN H 216 -1 O LYS H 213 N CYS H 200 SSBOND 1 CYS A 24 CYS A 94 1555 1555 2.03 SSBOND 2 CYS A 140 CYS A 200 1555 1555 2.01 SSBOND 3 CYS B 24 CYS B 94 1555 1555 2.03 SSBOND 4 CYS B 140 CYS B 200 1555 1555 2.01 SSBOND 5 CYS C 24 CYS C 94 1555 1555 2.03 SSBOND 6 CYS C 140 CYS C 200 1555 1555 2.03 SSBOND 7 CYS D 24 CYS D 94 1555 1555 2.03 SSBOND 8 CYS D 140 CYS D 200 1555 1555 2.03 SSBOND 9 CYS E 24 CYS E 94 1555 1555 2.03 SSBOND 10 CYS E 140 CYS E 200 1555 1555 2.02 SSBOND 11 CYS F 24 CYS F 94 1555 1555 2.00 SSBOND 12 CYS F 140 CYS F 200 1555 1555 2.02 SSBOND 13 CYS G 24 CYS G 94 1555 1555 2.03 SSBOND 14 CYS G 140 CYS G 200 1555 1555 2.03 SSBOND 15 CYS H 24 CYS H 94 1555 1555 2.03 SSBOND 16 CYS H 140 CYS H 200 1555 1555 2.03 LINK O ALA A 118 K K A 310 1555 1555 2.90 LINK OG SER A 120 K K A 310 1555 1555 3.01 LINK O ASN A 143 K K A 310 1555 1555 3.23 LINK O ASN A 144 K K A 310 1555 1555 2.89 LINK O ALA B 118 K K B 306 1555 1555 2.93 LINK OG SER B 120 K K B 306 1555 1555 3.44 LINK O ASN B 143 K K B 306 1555 1555 3.28 LINK O ASN B 144 K K B 306 1555 1555 2.69 LINK O2 EDO B 304 K K B 306 1555 1555 3.38 LINK O ALA C 118 K K C 309 1555 1555 2.83 LINK OG SER C 120 K K C 309 1555 1555 2.93 LINK O ASN C 143 K K C 309 1555 1555 3.24 LINK O ASN C 144 K K C 309 1555 1555 2.78 LINK O ALA D 118 K K D 309 1555 1555 2.97 LINK OG SER D 120 K K D 309 1555 1555 3.18 LINK O ASN D 143 K K D 309 1555 1555 3.15 LINK O ASN D 144 K K D 309 1555 1555 2.85 LINK O ALA E 118 K K E 310 1555 1555 2.73 LINK OG SER E 120 K K E 310 1555 1555 3.11 LINK O ASN E 143 K K E 310 1555 1555 2.86 LINK O ASN E 144 K K E 310 1555 1555 2.96 LINK O ALA F 118 K K F 309 1555 1555 3.08 LINK O ASN F 143 K K F 309 1555 1555 3.04 LINK O ASN F 144 K K F 309 1555 1555 2.82 LINK O ALA G 118 K K G 312 1555 1555 2.70 LINK OG SER G 120 K K G 312 1555 1555 3.21 LINK O ASN G 143 K K G 312 1555 1555 2.91 LINK O ASN G 144 K K G 312 1555 1555 2.93 LINK O ALA H 118 K K H 308 1555 1555 2.82 LINK OG SER H 120 K K H 308 1555 1555 3.11 LINK O ASN H 143 K K H 308 1555 1555 3.24 LINK O ASN H 144 K K H 308 1555 1555 2.84 CISPEP 1 THR A 8 PRO A 9 0 -1.83 CISPEP 2 TRP A 100 PRO A 101 0 -4.34 CISPEP 3 TYR A 146 PRO A 147 0 0.09 CISPEP 4 THR B 8 PRO B 9 0 -3.34 CISPEP 5 TRP B 100 PRO B 101 0 -3.14 CISPEP 6 TYR B 146 PRO B 147 0 3.06 CISPEP 7 THR C 8 PRO C 9 0 -2.23 CISPEP 8 TRP C 100 PRO C 101 0 -2.97 CISPEP 9 TYR C 146 PRO C 147 0 5.68 CISPEP 10 THR D 8 PRO D 9 0 -0.51 CISPEP 11 TRP D 100 PRO D 101 0 -5.57 CISPEP 12 TYR D 146 PRO D 147 0 3.13 CISPEP 13 THR E 8 PRO E 9 0 -1.78 CISPEP 14 TRP E 100 PRO E 101 0 -7.11 CISPEP 15 TYR E 146 PRO E 147 0 2.31 CISPEP 16 THR F 8 PRO F 9 0 -4.79 CISPEP 17 TRP F 100 PRO F 101 0 -6.47 CISPEP 18 TYR F 146 PRO F 147 0 5.06 CISPEP 19 THR G 8 PRO G 9 0 -2.37 CISPEP 20 TRP G 100 PRO G 101 0 -2.78 CISPEP 21 TYR G 146 PRO G 147 0 0.94 CISPEP 22 THR H 8 PRO H 9 0 -1.52 CISPEP 23 TRP H 100 PRO H 101 0 -5.99 CISPEP 24 TYR H 146 PRO H 147 0 2.64 CRYST1 77.085 85.326 104.580 106.77 91.44 116.91 P 1 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 0.012973 0.006585 0.002698 0.00000 SCALE2 0.000000 0.013143 0.004696 0.00000 SCALE3 0.000000 0.000000 0.010157 0.00000