HEADER IMMUNE SYSTEM 26-SEP-22 8ELN TITLE CRYSTAL STRUCTURE OF NANOBODY VHH222 BOUND TO ITS ANTIGEN PA14 CIF COMPND MOL_ID: 1; COMPND 2 MOLECULE: CFTR INHIBITORY FACTOR; COMPND 3 CHAIN: A, B, E, F, I, J; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: NANOBODY VHH222; COMPND 7 CHAIN: C, D, G, H, K, L; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA PA14; SOURCE 3 ORGANISM_TAXID: 652611; SOURCE 4 GENE: PA2394; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDPM73; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 12 ORGANISM_COMMON: ALPACA; SOURCE 13 ORGANISM_TAXID: 30538; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 16 EXPRESSION_SYSTEM_VARIANT: DE3 RIL; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET16B KEYWDS PSEUDOMONAS AERUGINOSA, NANOBODY VHH, IMMUNOGLOBULIN DOMAIN, CFTR KEYWDS 2 INHIBITORY FACTOR (CIF), IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.R.SIMARD,D.R.MADDEN REVDAT 1 18-OCT-23 8ELN 0 JRNL AUTH A.R.SIMARD,D.R.MADDEN JRNL TITL CRYSTAL STRUCTURE OF NANOBODY VHH222 BOUND TO ITS ANTIGEN JRNL TITL 2 PA14 CIF JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.44 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 101705 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.198 REMARK 3 R VALUE (WORKING SET) : 0.197 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 5080 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 47.4400 - 7.4500 0.99 3194 254 0.1417 0.1543 REMARK 3 2 7.4500 - 5.9200 1.00 3419 0 0.1697 0.0000 REMARK 3 3 5.9200 - 5.1700 0.99 3135 254 0.1681 0.2105 REMARK 3 4 5.1700 - 4.7000 1.00 3156 254 0.1472 0.1550 REMARK 3 5 4.7000 - 4.3600 1.00 3412 0 0.1421 0.0000 REMARK 3 6 4.3600 - 4.1000 1.00 3155 254 0.1529 0.1873 REMARK 3 7 4.1000 - 3.9000 1.00 3134 254 0.1668 0.2028 REMARK 3 8 3.9000 - 3.7300 1.00 3422 0 0.1771 0.0000 REMARK 3 9 3.7300 - 3.5800 1.00 3113 254 0.1858 0.2197 REMARK 3 10 3.5800 - 3.4600 1.00 3139 254 0.1949 0.2432 REMARK 3 11 3.4600 - 3.3500 1.00 3382 0 0.2024 0.0000 REMARK 3 12 3.3500 - 3.2600 1.00 3150 254 0.1987 0.2332 REMARK 3 13 3.2600 - 3.1700 1.00 3090 254 0.2159 0.2385 REMARK 3 14 3.1700 - 3.0900 1.00 3454 0 0.2172 0.0000 REMARK 3 15 3.0900 - 3.0200 1.00 3101 254 0.2357 0.2597 REMARK 3 16 3.0200 - 2.9600 1.00 3152 254 0.2427 0.2851 REMARK 3 17 2.9600 - 2.9000 1.00 3366 0 0.2472 0.0000 REMARK 3 18 2.9000 - 2.8500 1.00 3129 254 0.2550 0.2967 REMARK 3 19 2.8500 - 2.7900 0.99 3117 254 0.2510 0.2983 REMARK 3 20 2.7900 - 2.7500 1.00 3399 0 0.2483 0.0000 REMARK 3 21 2.7500 - 2.7000 1.00 3108 254 0.2451 0.2796 REMARK 3 22 2.7000 - 2.6600 1.00 3141 254 0.2520 0.3057 REMARK 3 23 2.6600 - 2.6200 1.00 3336 0 0.2582 0.0000 REMARK 3 24 2.6200 - 2.5900 1.00 3185 254 0.2683 0.3019 REMARK 3 25 2.5900 - 2.5500 1.00 3084 254 0.2659 0.3035 REMARK 3 26 2.5500 - 2.5200 1.00 3423 0 0.2685 0.0000 REMARK 3 27 2.5200 - 2.4900 1.00 3120 254 0.2774 0.3073 REMARK 3 28 2.4900 - 2.4600 1.00 3077 254 0.2820 0.3439 REMARK 3 29 2.4600 - 2.4300 1.00 3439 0 0.2923 0.0000 REMARK 3 30 2.4300 - 2.4000 1.00 3093 254 0.2880 0.3261 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.308 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.340 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.39 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.27 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 20127 REMARK 3 ANGLE : 0.849 27295 REMARK 3 CHIRALITY : 0.060 2863 REMARK 3 PLANARITY : 0.006 3573 REMARK 3 DIHEDRAL : 14.184 7297 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: AUTHORS STATE THAT THE ATOMS MODELED REMARK 3 WITH ZERO OCCUPANCY COULD NOT BE PLACED WITH CONFIDENCE AND WERE REMARK 3 SELECTED FOR ZERO-OCCUPANCY FLAGGING AFTER MANUAL INSPECTION OF REMARK 3 THE 2FO-FC MAP AT A 0.5-SIGMA CUTOFF. ALTHOUGH THE CORRELATION REMARK 3 IS LOW, RESIDUES LISTED AS RSRZ OUTLIERS HAVE REASONABLE REMARK 3 CONCORDANCE WITH THE 2FO-FC MAP, ARE NOT ROTAMER OUTLIERS, AND REMARK 3 ARE DEVOID OF CLASHES WITH NEIGHBORING ATOMS. REMARK 4 REMARK 4 8ELN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-22. REMARK 100 THE DEPOSITION ID IS D_1000268743. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-OCT-20 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97933 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101735 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 47.440 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : 0.16140 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.8800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6 REMARK 200 DATA REDUNDANCY IN SHELL : 3.60 REMARK 200 R MERGE FOR SHELL (I) : 1.01300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.380 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: 3KD2, 8E1C REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG4000, 200 MM AMMONIUM REMARK 280 ACETATE, 100 MM SODIUM ACETATE, PH 5, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 292.8K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 82.16300 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7200 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 29890 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6900 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30280 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7260 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30430 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 25 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS B 320 REMARK 465 HIS B 321 REMARK 465 HIS B 322 REMARK 465 HIS B 323 REMARK 465 HIS B 324 REMARK 465 HIS B 325 REMARK 465 SER C 121 REMARK 465 GLY C 122 REMARK 465 GLN C 123 REMARK 465 ALA C 124 REMARK 465 GLY C 125 REMARK 465 GLN C 126 REMARK 465 SER D 121 REMARK 465 GLY D 122 REMARK 465 GLN D 123 REMARK 465 ALA D 124 REMARK 465 GLY D 125 REMARK 465 GLN D 126 REMARK 465 HIS E 320 REMARK 465 HIS E 321 REMARK 465 HIS E 322 REMARK 465 HIS E 323 REMARK 465 HIS E 324 REMARK 465 HIS E 325 REMARK 465 ALA F 25 REMARK 465 ARG F 317 REMARK 465 GLY F 318 REMARK 465 ARG F 319 REMARK 465 HIS F 320 REMARK 465 HIS F 321 REMARK 465 HIS F 322 REMARK 465 HIS F 323 REMARK 465 HIS F 324 REMARK 465 HIS F 325 REMARK 465 SER G 121 REMARK 465 GLY G 122 REMARK 465 GLN G 123 REMARK 465 ALA G 124 REMARK 465 GLY G 125 REMARK 465 GLN G 126 REMARK 465 MET H 1 REMARK 465 SER H 121 REMARK 465 GLY H 122 REMARK 465 GLN H 123 REMARK 465 ALA H 124 REMARK 465 GLY H 125 REMARK 465 GLN H 126 REMARK 465 HIS I 320 REMARK 465 HIS I 321 REMARK 465 HIS I 322 REMARK 465 HIS I 323 REMARK 465 HIS I 324 REMARK 465 HIS I 325 REMARK 465 HIS J 321 REMARK 465 HIS J 322 REMARK 465 HIS J 323 REMARK 465 HIS J 324 REMARK 465 HIS J 325 REMARK 465 SER K 121 REMARK 465 GLY K 122 REMARK 465 GLN K 123 REMARK 465 ALA K 124 REMARK 465 GLY K 125 REMARK 465 GLN K 126 REMARK 465 SER L 121 REMARK 465 GLY L 122 REMARK 465 GLN L 123 REMARK 465 ALA L 124 REMARK 465 GLY L 125 REMARK 465 GLN L 126 REMARK 480 REMARK 480 ZERO OCCUPANCY ATOM REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 480 M RES C SSEQI ATOMS REMARK 480 ILE A 84 CD1 REMARK 480 ARG A 224 CZ NH1 NH2 REMARK 480 ARG B 121 CG CD NE CZ NH1 NH2 REMARK 480 LYS C 77 CD CE NZ REMARK 480 LYS D 5 CG CD CE NZ REMARK 480 GLN D 15 CD OE1 NE2 REMARK 480 LYS E 254 NZ REMARK 480 GLN E 258 CD OE1 NE2 REMARK 480 ARG E 317 CZ NH1 NH2 REMARK 480 ARG F 115 CD NE CZ NH1 NH2 REMARK 480 ARG F 217 CD NE CZ NH1 NH2 REMARK 480 ARG F 224 CG CD NE CZ NH1 NH2 REMARK 480 LYS G 5 CE NZ REMARK 480 LYS G 45 NZ REMARK 480 LYS G 77 CD CE NZ REMARK 480 LYS H 5 CG CD CE NZ REMARK 480 LYS H 45 CE NZ REMARK 480 LYS H 77 NZ REMARK 480 GLN H 113 CD OE1 NE2 REMARK 480 ARG I 163 CG CD NE CZ NH1 NH2 REMARK 480 ARG I 217 CD NE CZ NH1 NH2 REMARK 480 GLU I 285 CG CD OE1 OE2 REMARK 480 ARG I 317 CD NE CZ NH1 NH2 REMARK 480 LYS K 66 CG CD CE NZ REMARK 480 GLN K 113 CD OE1 NE2 REMARK 480 GLN L 15 CG CD OE1 NE2 REMARK 480 LYS L 66 CG CD CE NZ 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 129 -131.50 58.98 REMARK 500 ALA A 154 153.82 176.48 REMARK 500 PRO A 157 109.26 -59.85 REMARK 500 ASP B 129 -130.77 58.35 REMARK 500 ALA B 154 149.97 174.64 REMARK 500 ASP E 129 -131.30 58.28 REMARK 500 ASN E 142 50.66 -140.81 REMARK 500 ALA E 154 147.53 172.02 REMARK 500 ASP F 129 -130.85 59.64 REMARK 500 ALA F 154 149.69 175.04 REMARK 500 PRO F 157 108.99 -59.60 REMARK 500 ASP I 129 -130.95 58.42 REMARK 500 ALA I 154 149.54 175.25 REMARK 500 ASP J 129 -130.56 59.65 REMARK 500 ASN J 142 51.38 -140.19 REMARK 500 ALA J 154 150.01 175.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3KD2 RELATED DB: PDB REMARK 900 3KD2 CONTAINS THE APO STRUCTURE OF CIF REMARK 900 RELATED ID: 8E1C RELATED DB: PDB REMARK 900 8E1C CONTAINS THE STRUCTURE OF NANOBODY VHH222 REMARK 900 RELATED ID: 8EE2 RELATED DB: PDB REMARK 900 8EE2 CONTAINS THE CO-CRYSTAL STRUCUTRE OF CIF BOUND BY NANOBODY REMARK 900 VHH219 DBREF1 8ELN A 25 325 UNP A0A0M3KL26_PSEAB DBREF2 8ELN A A0A0M3KL26 1 301 DBREF1 8ELN B 25 325 UNP A0A0M3KL26_PSEAB DBREF2 8ELN B A0A0M3KL26 1 301 DBREF 8ELN C 1 126 PDB 8ELN 8ELN 1 126 DBREF 8ELN D 1 126 PDB 8ELN 8ELN 1 126 DBREF1 8ELN E 25 325 UNP A0A0M3KL26_PSEAB DBREF2 8ELN E A0A0M3KL26 1 301 DBREF1 8ELN F 25 325 UNP A0A0M3KL26_PSEAB DBREF2 8ELN F A0A0M3KL26 1 301 DBREF 8ELN G 1 126 PDB 8ELN 8ELN 1 126 DBREF 8ELN H 1 126 PDB 8ELN 8ELN 1 126 DBREF1 8ELN I 25 325 UNP A0A0M3KL26_PSEAB DBREF2 8ELN I A0A0M3KL26 1 301 DBREF1 8ELN J 25 325 UNP A0A0M3KL26_PSEAB DBREF2 8ELN J A0A0M3KL26 1 301 DBREF 8ELN K 1 126 PDB 8ELN 8ELN 1 126 DBREF 8ELN L 1 126 PDB 8ELN 8ELN 1 126 SEQRES 1 A 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA SEQRES 2 A 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS SEQRES 3 A 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE SEQRES 4 A 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU SEQRES 5 A 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO SEQRES 6 A 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER SEQRES 7 A 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG SEQRES 8 A 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS SEQRES 9 A 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS SEQRES 10 A 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA SEQRES 11 A 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE SEQRES 12 A 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE SEQRES 13 A 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA SEQRES 14 A 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER SEQRES 15 A 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU SEQRES 16 A 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU SEQRES 17 A 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER SEQRES 18 A 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN SEQRES 19 A 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY SEQRES 20 A 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA SEQRES 21 A 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS SEQRES 22 A 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU SEQRES 23 A 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS SEQRES 24 A 301 HIS HIS SEQRES 1 B 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA SEQRES 2 B 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS SEQRES 3 B 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE SEQRES 4 B 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU SEQRES 5 B 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO SEQRES 6 B 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER SEQRES 7 B 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG SEQRES 8 B 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS SEQRES 9 B 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS SEQRES 10 B 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA SEQRES 11 B 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE SEQRES 12 B 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE SEQRES 13 B 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA SEQRES 14 B 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER SEQRES 15 B 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU SEQRES 16 B 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU SEQRES 17 B 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER SEQRES 18 B 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN SEQRES 19 B 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY SEQRES 20 B 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA SEQRES 21 B 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS SEQRES 22 B 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU SEQRES 23 B 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS SEQRES 24 B 301 HIS HIS SEQRES 1 C 126 MET ALA GLN VAL LYS LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 C 126 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SER SEQRES 3 C 126 SER VAL PRO ILE PHE ALA ILE THR VAL MET GLY TRP TYR SEQRES 4 C 126 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA GLY SEQRES 5 C 126 ILE LYS ARG SER GLY ASP THR ASN TYR ALA ASP SER VAL SEQRES 6 C 126 LYS GLY ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN SEQRES 7 C 126 THR VAL PHE LEU GLN MET ASN SER LEU THR THR GLU ASP SEQRES 8 C 126 THR ALA VAL TYR TYR CYS ASN ALA GLN ILE LEU SER TRP SEQRES 9 C 126 MET GLY GLY THR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 C 126 THR VAL SER SER GLY GLN ALA GLY GLN SEQRES 1 D 126 MET ALA GLN VAL LYS LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 D 126 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SER SEQRES 3 D 126 SER VAL PRO ILE PHE ALA ILE THR VAL MET GLY TRP TYR SEQRES 4 D 126 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA GLY SEQRES 5 D 126 ILE LYS ARG SER GLY ASP THR ASN TYR ALA ASP SER VAL SEQRES 6 D 126 LYS GLY ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN SEQRES 7 D 126 THR VAL PHE LEU GLN MET ASN SER LEU THR THR GLU ASP SEQRES 8 D 126 THR ALA VAL TYR TYR CYS ASN ALA GLN ILE LEU SER TRP SEQRES 9 D 126 MET GLY GLY THR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 D 126 THR VAL SER SER GLY GLN ALA GLY GLN SEQRES 1 E 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA SEQRES 2 E 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS SEQRES 3 E 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE SEQRES 4 E 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU SEQRES 5 E 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO SEQRES 6 E 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER SEQRES 7 E 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG SEQRES 8 E 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS SEQRES 9 E 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS SEQRES 10 E 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA SEQRES 11 E 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE SEQRES 12 E 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE SEQRES 13 E 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA SEQRES 14 E 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER SEQRES 15 E 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU SEQRES 16 E 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU SEQRES 17 E 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER SEQRES 18 E 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN SEQRES 19 E 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY SEQRES 20 E 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA SEQRES 21 E 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS SEQRES 22 E 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU SEQRES 23 E 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS SEQRES 24 E 301 HIS HIS SEQRES 1 F 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA SEQRES 2 F 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS SEQRES 3 F 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE SEQRES 4 F 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU SEQRES 5 F 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO SEQRES 6 F 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER SEQRES 7 F 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG SEQRES 8 F 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS SEQRES 9 F 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS SEQRES 10 F 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA SEQRES 11 F 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE SEQRES 12 F 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE SEQRES 13 F 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA SEQRES 14 F 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER SEQRES 15 F 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU SEQRES 16 F 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU SEQRES 17 F 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER SEQRES 18 F 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN SEQRES 19 F 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY SEQRES 20 F 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA SEQRES 21 F 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS SEQRES 22 F 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU SEQRES 23 F 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS SEQRES 24 F 301 HIS HIS SEQRES 1 G 126 MET ALA GLN VAL LYS LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 G 126 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SER SEQRES 3 G 126 SER VAL PRO ILE PHE ALA ILE THR VAL MET GLY TRP TYR SEQRES 4 G 126 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA GLY SEQRES 5 G 126 ILE LYS ARG SER GLY ASP THR ASN TYR ALA ASP SER VAL SEQRES 6 G 126 LYS GLY ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN SEQRES 7 G 126 THR VAL PHE LEU GLN MET ASN SER LEU THR THR GLU ASP SEQRES 8 G 126 THR ALA VAL TYR TYR CYS ASN ALA GLN ILE LEU SER TRP SEQRES 9 G 126 MET GLY GLY THR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 G 126 THR VAL SER SER GLY GLN ALA GLY GLN SEQRES 1 H 126 MET ALA GLN VAL LYS LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 H 126 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SER SEQRES 3 H 126 SER VAL PRO ILE PHE ALA ILE THR VAL MET GLY TRP TYR SEQRES 4 H 126 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA GLY SEQRES 5 H 126 ILE LYS ARG SER GLY ASP THR ASN TYR ALA ASP SER VAL SEQRES 6 H 126 LYS GLY ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN SEQRES 7 H 126 THR VAL PHE LEU GLN MET ASN SER LEU THR THR GLU ASP SEQRES 8 H 126 THR ALA VAL TYR TYR CYS ASN ALA GLN ILE LEU SER TRP SEQRES 9 H 126 MET GLY GLY THR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 H 126 THR VAL SER SER GLY GLN ALA GLY GLN SEQRES 1 I 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA SEQRES 2 I 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS SEQRES 3 I 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE SEQRES 4 I 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU SEQRES 5 I 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO SEQRES 6 I 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER SEQRES 7 I 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG SEQRES 8 I 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS SEQRES 9 I 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS SEQRES 10 I 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA SEQRES 11 I 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE SEQRES 12 I 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE SEQRES 13 I 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA SEQRES 14 I 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER SEQRES 15 I 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU SEQRES 16 I 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU SEQRES 17 I 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER SEQRES 18 I 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN SEQRES 19 I 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY SEQRES 20 I 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA SEQRES 21 I 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS SEQRES 22 I 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU SEQRES 23 I 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS SEQRES 24 I 301 HIS HIS SEQRES 1 J 301 ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA SEQRES 2 J 301 TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS SEQRES 3 J 301 GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE SEQRES 4 J 301 GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU SEQRES 5 J 301 LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO SEQRES 6 J 301 GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER SEQRES 7 J 301 GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG SEQRES 8 J 301 GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS SEQRES 9 J 301 ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS SEQRES 10 J 301 ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLU ALA SEQRES 11 J 301 PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE SEQRES 12 J 301 THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE SEQRES 13 J 301 PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA SEQRES 14 J 301 GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER SEQRES 15 J 301 HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU SEQRES 16 J 301 ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU SEQRES 17 J 301 ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER SEQRES 18 J 301 VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN SEQRES 19 J 301 MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY SEQRES 20 J 301 MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA SEQRES 21 J 301 GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS SEQRES 22 J 301 TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU SEQRES 23 J 301 VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS SEQRES 24 J 301 HIS HIS SEQRES 1 K 126 MET ALA GLN VAL LYS LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 K 126 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SER SEQRES 3 K 126 SER VAL PRO ILE PHE ALA ILE THR VAL MET GLY TRP TYR SEQRES 4 K 126 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA GLY SEQRES 5 K 126 ILE LYS ARG SER GLY ASP THR ASN TYR ALA ASP SER VAL SEQRES 6 K 126 LYS GLY ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN SEQRES 7 K 126 THR VAL PHE LEU GLN MET ASN SER LEU THR THR GLU ASP SEQRES 8 K 126 THR ALA VAL TYR TYR CYS ASN ALA GLN ILE LEU SER TRP SEQRES 9 K 126 MET GLY GLY THR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 K 126 THR VAL SER SER GLY GLN ALA GLY GLN SEQRES 1 L 126 MET ALA GLN VAL LYS LEU GLN GLU SER GLY GLY GLY LEU SEQRES 2 L 126 VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SER SEQRES 3 L 126 SER VAL PRO ILE PHE ALA ILE THR VAL MET GLY TRP TYR SEQRES 4 L 126 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA GLY SEQRES 5 L 126 ILE LYS ARG SER GLY ASP THR ASN TYR ALA ASP SER VAL SEQRES 6 L 126 LYS GLY ARG PHE THR ILE SER ARG ASP ASP ALA LYS ASN SEQRES 7 L 126 THR VAL PHE LEU GLN MET ASN SER LEU THR THR GLU ASP SEQRES 8 L 126 THR ALA VAL TYR TYR CYS ASN ALA GLN ILE LEU SER TRP SEQRES 9 L 126 MET GLY GLY THR ASP TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 L 126 THR VAL SER SER GLY GLN ALA GLY GLN FORMUL 13 HOH *616(H2 O) HELIX 1 AA1 THR A 66 HIS A 71 5 6 HELIX 2 AA2 GLN A 72 ALA A 78 1 7 HELIX 3 AA3 SER A 102 SER A 118 1 17 HELIX 4 AA4 ASP A 129 ASN A 134 1 6 HELIX 5 AA5 THR A 135 ASN A 142 1 8 HELIX 6 AA6 ASP A 158 PHE A 164 5 7 HELIX 7 AA7 TRP A 176 ALA A 183 1 8 HELIX 8 AA8 ARG A 186 ALA A 193 1 8 HELIX 9 AA9 LYS A 195 HIS A 207 1 13 HELIX 10 AB1 SER A 215 ALA A 227 1 13 HELIX 11 AB2 LYS A 228 ALA A 241 1 14 HELIX 12 AB3 ALA A 241 ALA A 253 1 13 HELIX 13 AB4 THR A 274 LYS A 281 1 8 HELIX 14 AB5 TRP A 298 CYS A 303 1 6 HELIX 15 AB6 CYS A 303 ARG A 317 1 15 HELIX 16 AB7 THR B 66 HIS B 71 5 6 HELIX 17 AB8 LEU B 73 ALA B 78 1 6 HELIX 18 AB9 SER B 102 SER B 118 1 17 HELIX 19 AC1 ASP B 129 ASN B 134 1 6 HELIX 20 AC2 THR B 135 ASN B 142 1 8 HELIX 21 AC3 ASP B 158 PHE B 164 5 7 HELIX 22 AC4 TRP B 176 ALA B 183 1 8 HELIX 23 AC5 ARG B 186 ALA B 193 1 8 HELIX 24 AC6 LYS B 195 HIS B 207 1 13 HELIX 25 AC7 ASN B 210 PHE B 214 5 5 HELIX 26 AC8 SER B 215 ALA B 227 1 13 HELIX 27 AC9 LYS B 228 ALA B 241 1 14 HELIX 28 AD1 ALA B 241 ALA B 253 1 13 HELIX 29 AD2 THR B 274 LYS B 281 1 8 HELIX 30 AD3 TRP B 298 CYS B 303 1 6 HELIX 31 AD4 CYS B 303 ARG B 317 1 15 HELIX 32 AD5 PRO C 29 ILE C 33 5 5 HELIX 33 AD6 ASP C 63 LYS C 66 5 4 HELIX 34 AD7 THR C 88 THR C 92 5 5 HELIX 35 AD8 PRO D 29 ILE D 33 5 5 HELIX 36 AD9 ASP D 63 LYS D 66 5 4 HELIX 37 AE1 THR D 88 THR D 92 5 5 HELIX 38 AE2 THR E 66 HIS E 71 5 6 HELIX 39 AE3 GLN E 72 ALA E 78 1 7 HELIX 40 AE4 SER E 102 SER E 118 1 17 HELIX 41 AE5 ASP E 129 ASN E 134 1 6 HELIX 42 AE6 THR E 135 ASN E 142 1 8 HELIX 43 AE7 ASP E 158 PHE E 164 5 7 HELIX 44 AE8 TRP E 176 ALA E 183 1 8 HELIX 45 AE9 ARG E 186 ALA E 193 1 8 HELIX 46 AF1 LYS E 195 HIS E 207 1 13 HELIX 47 AF2 SER E 215 ALA E 227 1 13 HELIX 48 AF3 LYS E 228 ALA E 241 1 14 HELIX 49 AF4 ALA E 241 ALA E 253 1 13 HELIX 50 AF5 THR E 274 LYS E 281 1 8 HELIX 51 AF6 TRP E 298 CYS E 303 1 6 HELIX 52 AF7 CYS E 303 ARG E 317 1 15 HELIX 53 AF8 THR F 66 HIS F 71 5 6 HELIX 54 AF9 GLN F 72 LYS F 79 1 8 HELIX 55 AG1 SER F 102 SER F 118 1 17 HELIX 56 AG2 ASP F 129 ASN F 134 1 6 HELIX 57 AG3 THR F 135 ASN F 142 1 8 HELIX 58 AG4 ASP F 158 PHE F 164 5 7 HELIX 59 AG5 TRP F 176 ALA F 183 1 8 HELIX 60 AG6 ARG F 186 ALA F 193 1 8 HELIX 61 AG7 LYS F 195 HIS F 207 1 13 HELIX 62 AG8 SER F 215 ALA F 227 1 13 HELIX 63 AG9 LYS F 228 ALA F 241 1 14 HELIX 64 AH1 ALA F 241 ALA F 253 1 13 HELIX 65 AH2 THR F 274 LYS F 281 1 8 HELIX 66 AH3 TRP F 298 CYS F 303 1 6 HELIX 67 AH4 CYS F 303 SER F 316 1 14 HELIX 68 AH5 PRO G 29 ILE G 33 5 5 HELIX 69 AH6 ASP G 63 LYS G 66 5 4 HELIX 70 AH7 THR G 88 THR G 92 5 5 HELIX 71 AH8 PRO H 29 ILE H 33 5 5 HELIX 72 AH9 ASP H 63 LYS H 66 5 4 HELIX 73 AI1 THR H 88 THR H 92 5 5 HELIX 74 AI2 THR I 66 HIS I 71 5 6 HELIX 75 AI3 GLN I 72 LYS I 79 1 8 HELIX 76 AI4 SER I 102 SER I 118 1 17 HELIX 77 AI5 ASP I 129 ASN I 134 1 6 HELIX 78 AI6 THR I 135 ASN I 142 1 8 HELIX 79 AI7 ASP I 158 PHE I 164 5 7 HELIX 80 AI8 TRP I 176 ALA I 183 1 8 HELIX 81 AI9 ARG I 186 ALA I 193 1 8 HELIX 82 AJ1 LYS I 195 HIS I 207 1 13 HELIX 83 AJ2 SER I 215 ALA I 227 1 13 HELIX 84 AJ3 LYS I 228 ALA I 241 1 14 HELIX 85 AJ4 ALA I 241 ALA I 253 1 13 HELIX 86 AJ5 THR I 274 ALA I 282 1 9 HELIX 87 AJ6 TRP I 298 CYS I 303 1 6 HELIX 88 AJ7 CYS I 303 ARG I 317 1 15 HELIX 89 AJ8 THR J 66 HIS J 71 5 6 HELIX 90 AJ9 LEU J 73 ALA J 78 1 6 HELIX 91 AK1 SER J 102 SER J 118 1 17 HELIX 92 AK2 ASP J 129 ASN J 134 1 6 HELIX 93 AK3 THR J 135 ASN J 142 1 8 HELIX 94 AK4 ASP J 158 PHE J 164 5 7 HELIX 95 AK5 TRP J 176 ALA J 183 1 8 HELIX 96 AK6 ARG J 186 ALA J 193 1 8 HELIX 97 AK7 LYS J 195 HIS J 207 1 13 HELIX 98 AK8 SER J 215 ALA J 227 1 13 HELIX 99 AK9 LYS J 228 ALA J 241 1 14 HELIX 100 AL1 ALA J 241 ALA J 253 1 13 HELIX 101 AL2 THR J 274 LYS J 281 1 8 HELIX 102 AL3 TRP J 298 CYS J 303 1 6 HELIX 103 AL4 CYS J 303 ARG J 317 1 15 HELIX 104 AL5 PRO K 29 ILE K 33 5 5 HELIX 105 AL6 ASP K 63 LYS K 66 5 4 HELIX 106 AL7 THR K 88 THR K 92 5 5 HELIX 107 AL8 PRO L 29 ILE L 33 5 5 HELIX 108 AL9 THR L 88 THR L 92 5 5 SHEET 1 AA1 8 PHE A 34 VAL A 41 0 SHEET 2 AA1 8 VAL A 44 GLY A 52 -1 O LEU A 46 N ARG A 39 SHEET 3 AA1 8 THR A 82 PRO A 86 -1 O VAL A 83 N GLY A 51 SHEET 4 AA1 8 LEU A 56 VAL A 60 1 N VAL A 57 O ILE A 84 SHEET 5 AA1 8 PHE A 123 HIS A 128 1 O VAL A 126 N VAL A 60 SHEET 6 AA1 8 ILE A 146 MET A 152 1 O ALA A 147 N PHE A 123 SHEET 7 AA1 8 THR A 261 GLY A 266 1 O MET A 262 N LEU A 149 SHEET 8 AA1 8 VAL A 287 LEU A 292 1 O LEU A 292 N ALA A 265 SHEET 1 AA2 2 PHE A 167 THR A 168 0 SHEET 2 AA2 2 GLY A 171 GLU A 172 -1 O GLY A 171 N THR A 168 SHEET 1 AA3 8 PHE B 34 VAL B 41 0 SHEET 2 AA3 8 VAL B 44 GLY B 52 -1 O VAL B 44 N VAL B 41 SHEET 3 AA3 8 THR B 82 PRO B 86 -1 O VAL B 83 N GLY B 51 SHEET 4 AA3 8 LEU B 56 VAL B 60 1 N VAL B 57 O THR B 82 SHEET 5 AA3 8 PHE B 123 HIS B 128 1 O ASP B 124 N MET B 58 SHEET 6 AA3 8 ILE B 146 MET B 152 1 O VAL B 150 N LEU B 125 SHEET 7 AA3 8 THR B 261 GLY B 266 1 O MET B 262 N LEU B 149 SHEET 8 AA3 8 VAL B 287 LEU B 292 1 O LEU B 292 N ALA B 265 SHEET 1 AA4 2 PHE B 167 THR B 168 0 SHEET 2 AA4 2 GLY B 171 GLU B 172 -1 O GLY B 171 N THR B 168 SHEET 1 AA5 4 LEU C 6 SER C 9 0 SHEET 2 AA5 4 LEU C 20 SER C 26 -1 O SER C 23 N SER C 9 SHEET 3 AA5 4 THR C 79 MET C 84 -1 O MET C 84 N LEU C 20 SHEET 4 AA5 4 PHE C 69 ASP C 74 -1 N ASP C 74 O THR C 79 SHEET 1 AA6 6 GLY C 12 VAL C 14 0 SHEET 2 AA6 6 THR C 115 VAL C 119 1 O GLN C 116 N GLY C 12 SHEET 3 AA6 6 ALA C 93 SER C 103 -1 N TYR C 95 O THR C 115 SHEET 4 AA6 6 VAL C 35 GLN C 41 -1 N TYR C 39 O TYR C 96 SHEET 5 AA6 6 GLU C 48 LYS C 54 -1 O ILE C 53 N MET C 36 SHEET 6 AA6 6 THR C 59 TYR C 61 -1 O ASN C 60 N GLY C 52 SHEET 1 AA7 4 GLY C 12 VAL C 14 0 SHEET 2 AA7 4 THR C 115 VAL C 119 1 O GLN C 116 N GLY C 12 SHEET 3 AA7 4 ALA C 93 SER C 103 -1 N TYR C 95 O THR C 115 SHEET 4 AA7 4 GLY C 106 TRP C 111 -1 O TYR C 110 N ALA C 99 SHEET 1 AA8 4 LEU D 6 SER D 9 0 SHEET 2 AA8 4 LEU D 20 SER D 26 -1 O SER D 23 N SER D 9 SHEET 3 AA8 4 THR D 79 MET D 84 -1 O MET D 84 N LEU D 20 SHEET 4 AA8 4 PHE D 69 ASP D 74 -1 N ASP D 74 O THR D 79 SHEET 1 AA9 6 GLY D 12 VAL D 14 0 SHEET 2 AA9 6 THR D 115 VAL D 119 1 O THR D 118 N GLY D 12 SHEET 3 AA9 6 ALA D 93 SER D 103 -1 N TYR D 95 O THR D 115 SHEET 4 AA9 6 VAL D 35 GLN D 41 -1 N TYR D 39 O TYR D 96 SHEET 5 AA9 6 GLU D 48 LYS D 54 -1 O ALA D 51 N TRP D 38 SHEET 6 AA9 6 THR D 59 TYR D 61 -1 O ASN D 60 N GLY D 52 SHEET 1 AB1 4 GLY D 12 VAL D 14 0 SHEET 2 AB1 4 THR D 115 VAL D 119 1 O THR D 118 N GLY D 12 SHEET 3 AB1 4 ALA D 93 SER D 103 -1 N TYR D 95 O THR D 115 SHEET 4 AB1 4 GLY D 106 TRP D 111 -1 O TYR D 110 N ALA D 99 SHEET 1 AB2 8 PHE E 34 VAL E 41 0 SHEET 2 AB2 8 VAL E 44 GLY E 52 -1 O LEU E 46 N ARG E 39 SHEET 3 AB2 8 THR E 82 PRO E 86 -1 O VAL E 83 N GLY E 51 SHEET 4 AB2 8 LEU E 56 VAL E 60 1 N VAL E 57 O THR E 82 SHEET 5 AB2 8 PHE E 123 HIS E 128 1 O VAL E 126 N VAL E 60 SHEET 6 AB2 8 ILE E 146 MET E 152 1 O VAL E 150 N LEU E 125 SHEET 7 AB2 8 THR E 261 GLY E 266 1 O MET E 262 N TYR E 151 SHEET 8 AB2 8 VAL E 287 LEU E 292 1 O LEU E 292 N ALA E 265 SHEET 1 AB3 2 PHE E 167 THR E 168 0 SHEET 2 AB3 2 GLY E 171 GLU E 172 -1 O GLY E 171 N THR E 168 SHEET 1 AB4 8 PHE F 34 VAL F 41 0 SHEET 2 AB4 8 VAL F 44 GLY F 51 -1 O LYS F 50 N GLU F 35 SHEET 3 AB4 8 THR F 82 PRO F 86 -1 O VAL F 83 N GLY F 51 SHEET 4 AB4 8 LEU F 56 VAL F 60 1 N VAL F 57 O THR F 82 SHEET 5 AB4 8 PHE F 123 HIS F 128 1 O VAL F 126 N VAL F 60 SHEET 6 AB4 8 ILE F 146 MET F 152 1 O ALA F 147 N PHE F 123 SHEET 7 AB4 8 THR F 261 GLY F 266 1 O MET F 262 N LEU F 149 SHEET 8 AB4 8 VAL F 287 LEU F 292 1 O LEU F 292 N ALA F 265 SHEET 1 AB5 2 PHE F 167 THR F 168 0 SHEET 2 AB5 2 GLY F 171 GLU F 172 -1 O GLY F 171 N THR F 168 SHEET 1 AB6 4 LEU G 6 SER G 9 0 SHEET 2 AB6 4 LEU G 20 SER G 26 -1 O ALA G 25 N GLN G 7 SHEET 3 AB6 4 THR G 79 MET G 84 -1 O MET G 84 N LEU G 20 SHEET 4 AB6 4 PHE G 69 ASP G 74 -1 N THR G 70 O GLN G 83 SHEET 1 AB7 6 GLY G 12 VAL G 14 0 SHEET 2 AB7 6 THR G 115 VAL G 119 1 O GLN G 116 N GLY G 12 SHEET 3 AB7 6 ALA G 93 SER G 103 -1 N TYR G 95 O THR G 115 SHEET 4 AB7 6 VAL G 35 GLN G 41 -1 N TYR G 39 O TYR G 96 SHEET 5 AB7 6 GLU G 48 LYS G 54 -1 O ILE G 53 N MET G 36 SHEET 6 AB7 6 THR G 59 TYR G 61 -1 O ASN G 60 N GLY G 52 SHEET 1 AB8 4 GLY G 12 VAL G 14 0 SHEET 2 AB8 4 THR G 115 VAL G 119 1 O GLN G 116 N GLY G 12 SHEET 3 AB8 4 ALA G 93 SER G 103 -1 N TYR G 95 O THR G 115 SHEET 4 AB8 4 GLY G 106 TRP G 111 -1 O TYR G 110 N ALA G 99 SHEET 1 AB9 4 LEU H 6 SER H 9 0 SHEET 2 AB9 4 LEU H 20 SER H 26 -1 O ALA H 25 N GLN H 7 SHEET 3 AB9 4 THR H 79 MET H 84 -1 O MET H 84 N LEU H 20 SHEET 4 AB9 4 PHE H 69 ASP H 74 -1 N THR H 70 O GLN H 83 SHEET 1 AC1 6 GLY H 12 VAL H 14 0 SHEET 2 AC1 6 THR H 115 VAL H 119 1 O GLN H 116 N GLY H 12 SHEET 3 AC1 6 ALA H 93 LEU H 102 -1 N TYR H 95 O THR H 115 SHEET 4 AC1 6 VAL H 35 GLN H 41 -1 N VAL H 35 O GLN H 100 SHEET 5 AC1 6 GLU H 48 LYS H 54 -1 O ALA H 51 N TRP H 38 SHEET 6 AC1 6 THR H 59 TYR H 61 -1 O ASN H 60 N GLY H 52 SHEET 1 AC2 4 GLY H 12 VAL H 14 0 SHEET 2 AC2 4 THR H 115 VAL H 119 1 O GLN H 116 N GLY H 12 SHEET 3 AC2 4 ALA H 93 LEU H 102 -1 N TYR H 95 O THR H 115 SHEET 4 AC2 4 GLY H 107 TRP H 111 -1 O TYR H 110 N ALA H 99 SHEET 1 AC3 8 PHE I 34 VAL I 41 0 SHEET 2 AC3 8 VAL I 44 GLY I 52 -1 O VAL I 44 N VAL I 41 SHEET 3 AC3 8 THR I 82 PRO I 86 -1 O VAL I 83 N GLY I 51 SHEET 4 AC3 8 LEU I 56 VAL I 60 1 N VAL I 57 O THR I 82 SHEET 5 AC3 8 PHE I 123 HIS I 128 1 O VAL I 126 N VAL I 60 SHEET 6 AC3 8 ILE I 146 MET I 152 1 O VAL I 150 N LEU I 125 SHEET 7 AC3 8 THR I 261 GLY I 266 1 O MET I 262 N LEU I 149 SHEET 8 AC3 8 VAL I 287 LEU I 292 1 O LEU I 292 N ALA I 265 SHEET 1 AC4 2 PHE I 167 THR I 168 0 SHEET 2 AC4 2 GLY I 171 GLU I 172 -1 O GLY I 171 N THR I 168 SHEET 1 AC5 8 PHE J 34 VAL J 41 0 SHEET 2 AC5 8 VAL J 44 GLY J 52 -1 O LEU J 46 N ARG J 39 SHEET 3 AC5 8 THR J 82 PRO J 86 -1 O VAL J 83 N GLY J 51 SHEET 4 AC5 8 LEU J 56 VAL J 60 1 N VAL J 57 O THR J 82 SHEET 5 AC5 8 PHE J 123 HIS J 128 1 O VAL J 126 N VAL J 60 SHEET 6 AC5 8 ILE J 146 MET J 152 1 O VAL J 150 N LEU J 125 SHEET 7 AC5 8 THR J 261 GLY J 266 1 O MET J 262 N TYR J 151 SHEET 8 AC5 8 VAL J 287 LEU J 292 1 O LEU J 292 N ALA J 265 SHEET 1 AC6 2 PHE J 167 THR J 168 0 SHEET 2 AC6 2 GLY J 171 GLU J 172 -1 O GLY J 171 N THR J 168 SHEET 1 AC7 4 LEU K 6 SER K 9 0 SHEET 2 AC7 4 LEU K 20 SER K 26 -1 O SER K 23 N SER K 9 SHEET 3 AC7 4 THR K 79 MET K 84 -1 O MET K 84 N LEU K 20 SHEET 4 AC7 4 PHE K 69 ASP K 74 -1 N THR K 70 O GLN K 83 SHEET 1 AC8 6 GLY K 12 VAL K 14 0 SHEET 2 AC8 6 THR K 115 VAL K 119 1 O THR K 118 N GLY K 12 SHEET 3 AC8 6 ALA K 93 LEU K 102 -1 N TYR K 95 O THR K 115 SHEET 4 AC8 6 VAL K 35 GLN K 41 -1 N TYR K 39 O TYR K 96 SHEET 5 AC8 6 GLU K 48 LYS K 54 -1 O ILE K 53 N MET K 36 SHEET 6 AC8 6 THR K 59 TYR K 61 -1 O ASN K 60 N GLY K 52 SHEET 1 AC9 4 GLY K 12 VAL K 14 0 SHEET 2 AC9 4 THR K 115 VAL K 119 1 O THR K 118 N GLY K 12 SHEET 3 AC9 4 ALA K 93 LEU K 102 -1 N TYR K 95 O THR K 115 SHEET 4 AC9 4 GLY K 107 TRP K 111 -1 O TYR K 110 N ALA K 99 SHEET 1 AD1 4 LEU L 6 GLU L 8 0 SHEET 2 AD1 4 LEU L 20 SER L 26 -1 O ALA L 25 N GLN L 7 SHEET 3 AD1 4 THR L 79 MET L 84 -1 O MET L 84 N LEU L 20 SHEET 4 AD1 4 PHE L 69 ASP L 74 -1 N THR L 70 O GLN L 83 SHEET 1 AD2 6 GLY L 12 VAL L 14 0 SHEET 2 AD2 6 THR L 115 VAL L 119 1 O THR L 118 N VAL L 14 SHEET 3 AD2 6 ALA L 93 SER L 103 -1 N TYR L 95 O THR L 115 SHEET 4 AD2 6 VAL L 35 GLN L 41 -1 N TYR L 39 O TYR L 96 SHEET 5 AD2 6 GLU L 48 LYS L 54 -1 O VAL L 50 N TRP L 38 SHEET 6 AD2 6 THR L 59 TYR L 61 -1 O ASN L 60 N GLY L 52 SHEET 1 AD3 4 GLY L 12 VAL L 14 0 SHEET 2 AD3 4 THR L 115 VAL L 119 1 O THR L 118 N VAL L 14 SHEET 3 AD3 4 ALA L 93 SER L 103 -1 N TYR L 95 O THR L 115 SHEET 4 AD3 4 GLY L 106 TRP L 111 -1 O GLY L 106 N SER L 103 SSBOND 1 CYS A 295 CYS A 303 1555 1555 2.02 SSBOND 2 CYS B 295 CYS B 303 1555 1555 2.03 SSBOND 3 CYS C 24 CYS C 97 1555 1555 2.03 SSBOND 4 CYS D 24 CYS D 97 1555 1555 2.03 SSBOND 5 CYS E 295 CYS E 303 1555 1555 2.02 SSBOND 6 CYS F 295 CYS F 303 1555 1555 2.03 SSBOND 7 CYS G 24 CYS G 97 1555 1555 2.03 SSBOND 8 CYS H 24 CYS H 97 1555 1555 2.02 SSBOND 9 CYS I 295 CYS I 303 1555 1555 2.02 SSBOND 10 CYS J 295 CYS J 303 1555 1555 2.02 SSBOND 11 CYS K 24 CYS K 97 1555 1555 2.02 SSBOND 12 CYS L 24 CYS L 97 1555 1555 2.02 CRYST1 76.222 164.326 107.291 90.00 97.54 90.00 P 1 21 1 12 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 0.013120 0.000000 0.001737 0.00000 SCALE2 0.000000 0.006085 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009402 0.00000