HEADER VIRAL PROTEIN 05-NOV-24 9KFB TITLE RABV-G-ECTO/NM57-SCFV COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: NM57-SCFV LIGHT CHAIN, NM57-SCFV HEAVY CHAIN; COMPND 3 CHAIN: A, M, X; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RABV-G-ECTO; COMPND 7 CHAIN: B, K, F; COMPND 8 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; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: RABIES VIRUS CVS-11; SOURCE 8 ORGANISM_TAXID: 11294; SOURCE 9 EXPRESSION_SYSTEM: BACULOVIRUS EXPRESSION VECTOR PFASTBAC1-HM; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 274590 KEYWDS RABIES VIRUS, GLYCOPROTEIN, NEUTRALIZING ANTIBODY, SO57, VIRAL KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.LU,F.YANG,S.LIN REVDAT 1 23-APR-25 9KFB 0 JRNL AUTH F.YANG,L.ZHAI,K.YIN,S.LIN,J.YANG,F.YE,Z.CHEN,S.SHU,Y.YU, JRNL AUTH 2 L.GUO,B.HE,W.WANG,H.YE,Y.CAO,J.GAO,G.LU JRNL TITL MOLECULAR BASIS OF TWO BROAD-SPECTRUM ANTIBODIES JRNL TITL 2 NEUTRALIZING RABIES VIRUS AND OTHER PHYLOGROUP-I JRNL TITL 3 LYSSAVIRUSES BY BLOCKING STRUCTURAL TRANSITION BETWEEN THE JRNL TITL 4 PLECKSTRIN-HOMOLOGY AND FUSION DOMAINS IN THE GLYCOPROTEIN. JRNL REF INT.J.BIOL.MACROMOL. V. 308 42570 2025 JRNL REFN ISSN 0141-8130 JRNL PMID 40154685 JRNL DOI 10.1016/J.IJBIOMAC.2025.142570 REMARK 2 REMARK 2 RESOLUTION. 4.30 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.64 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 19516 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.263 REMARK 3 R VALUE (WORKING SET) : 0.261 REMARK 3 FREE R VALUE : 0.314 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600 REMARK 3 FREE R VALUE TEST SET COUNT : 897 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 36.6400 - 7.7900 1.00 3281 156 0.2146 0.2726 REMARK 3 2 7.7900 - 6.2000 1.00 3115 155 0.3121 0.3578 REMARK 3 3 6.2000 - 5.4200 1.00 3088 150 0.3019 0.3538 REMARK 3 4 5.4200 - 4.9200 1.00 3051 152 0.2829 0.3282 REMARK 3 5 4.9200 - 4.5700 1.00 3065 135 0.2806 0.3300 REMARK 3 6 4.5700 - 4.3000 1.00 3019 149 0.3058 0.3584 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) : 0.650 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.380 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 12947 REMARK 3 ANGLE : 1.102 17525 REMARK 3 CHIRALITY : 0.056 1924 REMARK 3 PLANARITY : 0.009 2225 REMARK 3 DIHEDRAL : 8.189 1740 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 14.5221 10.4411 -1.8016 REMARK 3 T TENSOR REMARK 3 T11: 1.4486 T22: 1.3975 REMARK 3 T33: 1.4162 T12: 0.0893 REMARK 3 T13: 0.0017 T23: 0.1204 REMARK 3 L TENSOR REMARK 3 L11: 0.7424 L22: 0.7964 REMARK 3 L33: 0.6767 L12: -0.1819 REMARK 3 L13: 0.1804 L23: 0.2421 REMARK 3 S TENSOR REMARK 3 S11: 0.0507 S12: 0.1012 S13: -0.0795 REMARK 3 S21: -0.1319 S22: -0.0614 S23: 0.0527 REMARK 3 S31: -0.0324 S32: 0.0312 S33: 0.0155 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 9KFB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300053441. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-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 : SSRF REMARK 200 BEAMLINE : BL17U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97925 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19823 REMARK 200 RESOLUTION RANGE HIGH (A) : 4.280 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 24.50 REMARK 200 R MERGE (I) : 0.22600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 24.9600 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.45 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.84700 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM REMARK 280 ACETATE (PH 5.5), 10 % W/V PEG 2000 MME, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.69600 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 78.80950 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 78.80950 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.34800 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 78.80950 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 78.80950 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 166.04400 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 78.80950 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 78.80950 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 55.34800 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 78.80950 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 78.80950 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 166.04400 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 110.69600 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, M 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, X REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 0 REMARK 465 GLN A 1 REMARK 465 SER A 13 REMARK 465 PRO A 14 REMARK 465 GLY A 15 REMARK 465 GLN A 16 REMARK 465 GLN A 81 REMARK 465 LEU A 112 REMARK 465 GLY A 113 REMARK 465 GLN A 114 REMARK 465 PRO A 115 REMARK 465 LYS A 116 REMARK 465 GLY A 117 REMARK 465 GLY A 118 REMARK 465 GLY A 119 REMARK 465 GLY A 120 REMARK 465 SER A 121 REMARK 465 GLY A 122 REMARK 465 GLY A 123 REMARK 465 GLY A 124 REMARK 465 GLY A 125 REMARK 465 SER A 126 REMARK 465 GLY A 127 REMARK 465 GLY A 128 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 SER A 131 REMARK 465 GLY A 132 REMARK 465 GLY A 133 REMARK 465 GLY A 134 REMARK 465 GLY A 135 REMARK 465 SER A 136 REMARK 465 GLN A 137 REMARK 465 VAL A 138 REMARK 465 SER A 161 REMARK 465 GLY A 162 REMARK 465 ALA A 208 REMARK 465 ASP A 209 REMARK 465 GLU A 210 REMARK 465 SER A 263 REMARK 465 THR B 68 REMARK 465 GLU B 69 REMARK 465 ALA B 70 REMARK 465 GLU B 71 REMARK 465 THR B 72 REMARK 465 TYR B 73 REMARK 465 THR B 74 REMARK 465 GLY B 75 REMARK 465 GLY B 76 REMARK 465 SER B 77 REMARK 465 GLY B 78 REMARK 465 GLY B 79 REMARK 465 THR B 80 REMARK 465 THR B 81 REMARK 465 PHE B 82 REMARK 465 LYS B 83 REMARK 465 ARG B 84 REMARK 465 LYS B 85 REMARK 465 HIS B 86 REMARK 465 PHE B 87 REMARK 465 GLY B 104 REMARK 465 GLU B 114 REMARK 465 SER B 115 REMARK 465 LEU B 116 REMARK 465 HIS B 117 REMARK 465 ASN B 118 REMARK 465 PRO B 119 REMARK 465 TYR B 120 REMARK 465 GLY B 121 REMARK 465 GLY B 122 REMARK 465 SER B 123 REMARK 465 GLY B 124 REMARK 465 GLY B 125 REMARK 465 ARG B 264 REMARK 465 SER B 265 REMARK 465 ASP B 266 REMARK 465 GLU B 267 REMARK 465 ILE B 268 REMARK 465 PRO B 394 REMARK 465 LEU B 395 REMARK 465 MET B 396 REMARK 465 HIS B 397 REMARK 465 PRO B 398 REMARK 465 LEU B 399 REMARK 465 ALA B 400 REMARK 465 ASP B 401 REMARK 465 PRO B 402 REMARK 465 SER B 403 REMARK 465 THR B 404 REMARK 465 VAL B 405 REMARK 465 PHE B 406 REMARK 465 LYS B 407 REMARK 465 GLU B 408 REMARK 465 GLY B 409 REMARK 465 ASP B 410 REMARK 465 GLU B 411 REMARK 465 ALA B 412 REMARK 465 GLU B 413 REMARK 465 ASP B 414 REMARK 465 PHE B 415 REMARK 465 VAL B 416 REMARK 465 GLU B 417 REMARK 465 VAL B 418 REMARK 465 HIS B 419 REMARK 465 LEU B 420 REMARK 465 PRO B 421 REMARK 465 ASP B 422 REMARK 465 VAL B 423 REMARK 465 TYR B 424 REMARK 465 LYS B 425 REMARK 465 GLN B 426 REMARK 465 ILE B 427 REMARK 465 SER B 428 REMARK 465 GLY B 429 REMARK 465 VAL B 430 REMARK 465 ASP B 431 REMARK 465 LEU B 432 REMARK 465 GLY B 433 REMARK 465 LEU B 434 REMARK 465 PRO B 435 REMARK 465 ASN B 436 REMARK 465 TRP B 437 REMARK 465 GLY B 438 REMARK 465 LYS B 439 REMARK 465 THR K 64 REMARK 465 GLY K 65 REMARK 465 VAL K 66 REMARK 465 VAL K 67 REMARK 465 THR K 68 REMARK 465 GLU K 69 REMARK 465 ALA K 70 REMARK 465 GLU K 71 REMARK 465 THR K 72 REMARK 465 TYR K 73 REMARK 465 THR K 74 REMARK 465 GLY K 75 REMARK 465 GLY K 76 REMARK 465 SER K 77 REMARK 465 GLY K 78 REMARK 465 GLY K 79 REMARK 465 THR K 80 REMARK 465 THR K 81 REMARK 465 PHE K 82 REMARK 465 LYS K 83 REMARK 465 ARG K 84 REMARK 465 LYS K 85 REMARK 465 HIS K 86 REMARK 465 MET K 102 REMARK 465 ALA K 103 REMARK 465 GLY K 104 REMARK 465 ASP K 105 REMARK 465 GLU K 114 REMARK 465 SER K 115 REMARK 465 LEU K 116 REMARK 465 HIS K 117 REMARK 465 ASN K 118 REMARK 465 PRO K 119 REMARK 465 TYR K 120 REMARK 465 GLY K 121 REMARK 465 GLY K 122 REMARK 465 SER K 123 REMARK 465 GLY K 124 REMARK 465 GLY K 125 REMARK 465 ARG K 126 REMARK 465 THR K 127 REMARK 465 THR K 128 REMARK 465 LYS K 129 REMARK 465 GLU K 130 REMARK 465 SER K 131 REMARK 465 LEU K 132 REMARK 465 ILE K 133 REMARK 465 GLY K 203 REMARK 465 ASN K 204 REMARK 465 ASN K 259 REMARK 465 LEU K 260 REMARK 465 HIS K 261 REMARK 465 ASP K 262 REMARK 465 PHE K 263 REMARK 465 ARG K 264 REMARK 465 SER K 265 REMARK 465 ASP K 266 REMARK 465 GLU K 267 REMARK 465 ILE K 268 REMARK 465 GLU K 269 REMARK 465 LEU K 395 REMARK 465 MET K 396 REMARK 465 HIS K 397 REMARK 465 PRO K 398 REMARK 465 LEU K 399 REMARK 465 ALA K 400 REMARK 465 ASP K 401 REMARK 465 PRO K 402 REMARK 465 SER K 403 REMARK 465 THR K 404 REMARK 465 VAL K 405 REMARK 465 PHE K 406 REMARK 465 LYS K 407 REMARK 465 GLU K 408 REMARK 465 GLY K 409 REMARK 465 ASP K 410 REMARK 465 GLU K 411 REMARK 465 ALA K 412 REMARK 465 GLU K 413 REMARK 465 ASP K 414 REMARK 465 PHE K 415 REMARK 465 VAL K 416 REMARK 465 GLU K 417 REMARK 465 VAL K 418 REMARK 465 HIS K 419 REMARK 465 LEU K 420 REMARK 465 PRO K 421 REMARK 465 ASP K 422 REMARK 465 VAL K 423 REMARK 465 TYR K 424 REMARK 465 LYS K 425 REMARK 465 GLN K 426 REMARK 465 ILE K 427 REMARK 465 SER K 428 REMARK 465 GLY K 429 REMARK 465 VAL K 430 REMARK 465 ASP K 431 REMARK 465 LEU K 432 REMARK 465 GLY K 433 REMARK 465 LEU K 434 REMARK 465 PRO K 435 REMARK 465 ASN K 436 REMARK 465 TRP K 437 REMARK 465 GLY K 438 REMARK 465 LYS K 439 REMARK 465 MET M 0 REMARK 465 GLN M 1 REMARK 465 SER M 2 REMARK 465 GLU M 83 REMARK 465 ASP M 84 REMARK 465 GLU M 85 REMARK 465 ALA M 86 REMARK 465 ASP M 87 REMARK 465 TYR M 88 REMARK 465 TYR M 89 REMARK 465 LYS M 108 REMARK 465 LEU M 109 REMARK 465 THR M 110 REMARK 465 VAL M 111 REMARK 465 LEU M 112 REMARK 465 GLY M 113 REMARK 465 GLN M 114 REMARK 465 PRO M 115 REMARK 465 LYS M 116 REMARK 465 GLY M 117 REMARK 465 GLY M 118 REMARK 465 GLY M 119 REMARK 465 GLY M 120 REMARK 465 SER M 121 REMARK 465 GLY M 122 REMARK 465 GLY M 123 REMARK 465 GLY M 124 REMARK 465 GLY M 125 REMARK 465 SER M 126 REMARK 465 GLY M 127 REMARK 465 GLY M 128 REMARK 465 GLY M 129 REMARK 465 GLY M 130 REMARK 465 SER M 131 REMARK 465 GLY M 132 REMARK 465 GLY M 133 REMARK 465 GLY M 134 REMARK 465 GLY M 135 REMARK 465 SER M 136 REMARK 465 GLN M 137 REMARK 465 VAL M 138 REMARK 465 GLN M 139 REMARK 465 GLY M 162 REMARK 465 GLY M 163 REMARK 465 THR M 164 REMARK 465 PHE M 165 REMARK 465 ALA M 208 REMARK 465 ASP M 209 REMARK 465 GLU M 210 REMARK 465 SER M 211 REMARK 465 THR M 212 REMARK 465 SER M 240 REMARK 465 GLY M 241 REMARK 465 THR M 242 REMARK 465 VAL M 261 REMARK 465 SER M 262 REMARK 465 SER M 263 REMARK 465 VAL F 66 REMARK 465 VAL F 67 REMARK 465 THR F 68 REMARK 465 GLU F 69 REMARK 465 ALA F 70 REMARK 465 GLU F 71 REMARK 465 THR F 72 REMARK 465 TYR F 73 REMARK 465 THR F 74 REMARK 465 GLY F 75 REMARK 465 GLY F 76 REMARK 465 SER F 77 REMARK 465 GLY F 78 REMARK 465 GLY F 79 REMARK 465 THR F 80 REMARK 465 THR F 81 REMARK 465 PHE F 82 REMARK 465 LYS F 83 REMARK 465 ARG F 84 REMARK 465 LYS F 85 REMARK 465 HIS F 86 REMARK 465 GLY F 108 REMARK 465 ASP F 109 REMARK 465 PRO F 110 REMARK 465 ARG F 111 REMARK 465 TYR F 112 REMARK 465 GLU F 113 REMARK 465 GLU F 114 REMARK 465 SER F 115 REMARK 465 LEU F 116 REMARK 465 HIS F 117 REMARK 465 ASN F 118 REMARK 465 PRO F 119 REMARK 465 TYR F 120 REMARK 465 GLY F 121 REMARK 465 GLY F 122 REMARK 465 SER F 123 REMARK 465 GLY F 124 REMARK 465 GLY F 125 REMARK 465 ARG F 126 REMARK 465 THR F 127 REMARK 465 THR F 128 REMARK 465 LYS F 129 REMARK 465 GLU F 130 REMARK 465 SER F 131 REMARK 465 LEU F 132 REMARK 465 ILE F 133 REMARK 465 ARG F 213 REMARK 465 GLY F 214 REMARK 465 LEU F 260 REMARK 465 HIS F 261 REMARK 465 ASP F 262 REMARK 465 PHE F 263 REMARK 465 ARG F 264 REMARK 465 SER F 265 REMARK 465 ASP F 266 REMARK 465 HIS F 397 REMARK 465 PRO F 398 REMARK 465 LEU F 399 REMARK 465 ALA F 400 REMARK 465 ASP F 401 REMARK 465 PRO F 402 REMARK 465 SER F 403 REMARK 465 THR F 404 REMARK 465 VAL F 405 REMARK 465 PHE F 406 REMARK 465 LYS F 407 REMARK 465 GLU F 408 REMARK 465 GLY F 409 REMARK 465 ASP F 410 REMARK 465 GLU F 411 REMARK 465 ALA F 412 REMARK 465 GLU F 413 REMARK 465 ASP F 414 REMARK 465 PHE F 415 REMARK 465 VAL F 416 REMARK 465 GLU F 417 REMARK 465 VAL F 418 REMARK 465 HIS F 419 REMARK 465 LEU F 420 REMARK 465 PRO F 421 REMARK 465 ASP F 422 REMARK 465 VAL F 423 REMARK 465 TYR F 424 REMARK 465 LYS F 425 REMARK 465 GLN F 426 REMARK 465 ILE F 427 REMARK 465 SER F 428 REMARK 465 GLY F 429 REMARK 465 VAL F 430 REMARK 465 ASP F 431 REMARK 465 LEU F 432 REMARK 465 GLY F 433 REMARK 465 LEU F 434 REMARK 465 PRO F 435 REMARK 465 ASN F 436 REMARK 465 TRP F 437 REMARK 465 GLY F 438 REMARK 465 LYS F 439 REMARK 465 MET X 0 REMARK 465 GLN X 1 REMARK 465 SER X 2 REMARK 465 SER X 11 REMARK 465 GLY X 12 REMARK 465 SER X 13 REMARK 465 PRO X 14 REMARK 465 GLY X 15 REMARK 465 GLN X 16 REMARK 465 SER X 17 REMARK 465 VAL X 18 REMARK 465 THR X 19 REMARK 465 ILE X 20 REMARK 465 ASP X 62 REMARK 465 ARG X 63 REMARK 465 PHE X 64 REMARK 465 SER X 65 REMARK 465 LEU X 75 REMARK 465 THR X 76 REMARK 465 ILE X 77 REMARK 465 SER X 78 REMARK 465 GLY X 79 REMARK 465 LEU X 80 REMARK 465 GLN X 81 REMARK 465 ALA X 82 REMARK 465 GLU X 83 REMARK 465 ASP X 84 REMARK 465 GLU X 85 REMARK 465 ALA X 86 REMARK 465 ASP X 87 REMARK 465 TYR X 88 REMARK 465 TYR X 89 REMARK 465 LYS X 108 REMARK 465 LEU X 109 REMARK 465 THR X 110 REMARK 465 VAL X 111 REMARK 465 LEU X 112 REMARK 465 GLY X 113 REMARK 465 GLN X 114 REMARK 465 PRO X 115 REMARK 465 LYS X 116 REMARK 465 GLY X 117 REMARK 465 GLY X 118 REMARK 465 GLY X 119 REMARK 465 GLY X 120 REMARK 465 SER X 121 REMARK 465 GLY X 122 REMARK 465 GLY X 123 REMARK 465 GLY X 124 REMARK 465 GLY X 125 REMARK 465 SER X 126 REMARK 465 GLY X 127 REMARK 465 GLY X 128 REMARK 465 GLY X 129 REMARK 465 GLY X 130 REMARK 465 SER X 131 REMARK 465 GLY X 132 REMARK 465 GLY X 133 REMARK 465 GLY X 134 REMARK 465 GLY X 135 REMARK 465 SER X 136 REMARK 465 GLN X 137 REMARK 465 GLY X 162 REMARK 465 ALA X 208 REMARK 465 ASP X 209 REMARK 465 GLU X 210 REMARK 465 SER X 211 REMARK 465 SER X 240 REMARK 465 GLY X 241 REMARK 465 THR X 242 REMARK 465 TYR X 243 REMARK 465 GLN X 255 REMARK 465 SER X 262 REMARK 465 SER X 263 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 ASP F 369 CG OD1 OD2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O SER A 152 CD1 LEU A 222 1.96 REMARK 500 NH2 ARG K 224 OE1 GLN M 198 2.10 REMARK 500 NH2 ARG X 174 OE2 GLU X 182 2.11 REMARK 500 O LEU B 260 O ASP B 262 2.11 REMARK 500 O GLN M 175 N VAL M 229 2.11 REMARK 500 O THR K 187 N CYS K 189 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 SER A 153 N - CA - CB ANGL. DEV. = -11.4 DEGREES REMARK 500 GLN A 179 N - CA - C ANGL. DEV. = -16.3 DEGREES REMARK 500 GLU A 235 CB - CA - C ANGL. DEV. = -12.2 DEGREES REMARK 500 ASN A 236 N - CA - CB ANGL. DEV. = -15.6 DEGREES REMARK 500 LEU A 237 N - CA - CB ANGL. DEV. = 16.6 DEGREES REMARK 500 ASN B 26 N - CA - C ANGL. DEV. = -21.5 DEGREES REMARK 500 ASN B 27 N - CA - CB ANGL. DEV. = 11.2 DEGREES REMARK 500 VAL B 153 CB - CA - C ANGL. DEV. = 21.5 DEGREES REMARK 500 VAL B 153 N - CA - C ANGL. DEV. = -26.4 DEGREES REMARK 500 PHE B 154 N - CA - C ANGL. DEV. = -16.6 DEGREES REMARK 500 LEU B 257 CB - CA - C ANGL. DEV. = -13.1 DEGREES REMARK 500 VAL B 358 CB - CA - C ANGL. DEV. = 18.8 DEGREES REMARK 500 PHE B 359 CB - CA - C ANGL. DEV. = -12.1 DEGREES REMARK 500 PHE B 359 N - CA - C ANGL. DEV. = -18.5 DEGREES REMARK 500 TYR K 108 N - CA - CB ANGL. DEV. = 11.2 DEGREES REMARK 500 PRO K 144 N - CA - CB ANGL. DEV. = -9.5 DEGREES REMARK 500 ARG K 152 CB - CA - C ANGL. DEV. = -15.5 DEGREES REMARK 500 VAL K 153 N - CA - CB ANGL. DEV. = -15.8 DEGREES REMARK 500 VAL K 153 N - CA - C ANGL. DEV. = 24.0 DEGREES REMARK 500 PRO K 180 CB - CA - C ANGL. DEV. = -21.5 DEGREES REMARK 500 PRO K 180 N - CA - C ANGL. DEV. = -16.3 DEGREES REMARK 500 GLU K 181 N - CA - CB ANGL. DEV. = -17.6 DEGREES REMARK 500 ASN K 319 CB - CA - C ANGL. DEV. = -16.8 DEGREES REMARK 500 LYS K 320 CB - CA - C ANGL. DEV. = 12.2 DEGREES REMARK 500 LYS K 320 N - CA - CB ANGL. DEV. = 13.8 DEGREES REMARK 500 LYS K 320 N - CA - C ANGL. DEV. = -16.3 DEGREES REMARK 500 GLN K 377 N - CA - C ANGL. DEV. = -17.1 DEGREES REMARK 500 ALA M 94 CB - CA - C ANGL. DEV. = -25.9 DEGREES REMARK 500 ALA M 94 N - CA - C ANGL. DEV. = -20.6 DEGREES REMARK 500 SER M 153 N - CA - CB ANGL. DEV. = 9.2 DEGREES REMARK 500 VAL M 173 N - CA - CB ANGL. DEV. = -24.9 DEGREES REMARK 500 VAL M 173 N - CA - C ANGL. DEV. = 32.8 DEGREES REMARK 500 THR M 257 N - CA - C ANGL. DEV. = -16.7 DEGREES REMARK 500 LEU M 258 N - CA - C ANGL. DEV. = -16.4 DEGREES REMARK 500 ASN F 26 CB - CA - C ANGL. DEV. = 15.1 DEGREES REMARK 500 ASN F 26 N - CA - C ANGL. DEV. = -18.5 DEGREES REMARK 500 SER F 148 N - CA - C ANGL. DEV. = -17.3 DEGREES REMARK 500 LEU F 149 N - CA - CB ANGL. DEV. = 13.0 DEGREES REMARK 500 VAL F 153 CB - CA - C ANGL. DEV. = 14.6 DEGREES REMARK 500 HIS F 270 N - CA - C ANGL. DEV. = 16.6 DEGREES REMARK 500 VAL F 355 CB - CA - C ANGL. DEV. = -13.3 DEGREES REMARK 500 GLN X 179 CB - CA - C ANGL. DEV. = -15.0 DEGREES REMARK 500 GLY X 180 N - CA - C ANGL. DEV. = 15.4 DEGREES REMARK 500 GLU X 218 N - CA - C ANGL. DEV. = -18.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA A 3 -69.12 -97.17 REMARK 500 LEU A 4 -163.80 -109.86 REMARK 500 ASP A 28 -161.71 -71.35 REMARK 500 ALA A 53 -54.02 68.90 REMARK 500 PHE A 64 -4.79 84.32 REMARK 500 ASP A 96 -65.24 -100.88 REMARK 500 LYS A 108 92.91 -68.43 REMARK 500 GLN A 142 -165.89 -123.39 REMARK 500 SER A 152 -162.90 -117.24 REMARK 500 CYS A 158 77.79 -158.55 REMARK 500 PHE A 165 -12.24 78.08 REMARK 500 PRO A 177 105.94 -49.31 REMARK 500 GLU A 182 105.09 -164.91 REMARK 500 THR A 205 88.35 -151.00 REMARK 500 SER A 221 101.37 -166.83 REMARK 500 SER A 224 -35.62 65.46 REMARK 500 ALA A 228 -167.27 -166.34 REMARK 500 ASP A 238 -64.79 -95.96 REMARK 500 ASP B 32 105.31 -59.74 REMARK 500 ASN B 37 108.65 -59.57 REMARK 500 PHE B 41 -179.21 -173.20 REMARK 500 THR B 128 168.57 60.13 REMARK 500 SER B 138 -150.05 -128.93 REMARK 500 ASP B 141 -151.21 -110.69 REMARK 500 HIS B 150 87.87 -153.94 REMARK 500 PRO B 155 -46.86 -16.05 REMARK 500 LYS B 158 -180.00 67.33 REMARK 500 CYS B 159 -113.63 -139.46 REMARK 500 SER B 160 -153.78 -161.31 REMARK 500 THR B 171 -149.76 -125.05 REMARK 500 HIS B 173 -149.74 52.92 REMARK 500 ILE B 177 -74.60 -127.42 REMARK 500 MET B 179 64.30 -154.88 REMARK 500 PRO B 185 96.61 -48.12 REMARK 500 ASN B 202 -150.52 -96.40 REMARK 500 ALA B 222 -153.33 -95.04 REMARK 500 THR B 245 98.62 -47.85 REMARK 500 PRO B 254 16.61 -66.41 REMARK 500 LEU B 260 -75.87 -112.41 REMARK 500 HIS B 261 -119.39 37.71 REMARK 500 HIS B 270 -63.80 -107.48 REMARK 500 LYS B 294 16.67 52.76 REMARK 500 ASN B 319 -76.36 -124.34 REMARK 500 LYS B 342 -119.13 43.03 REMARK 500 SER B 378 50.08 -91.41 REMARK 500 LEU B 380 31.14 71.73 REMARK 500 GLU B 386 68.77 -116.21 REMARK 500 LEU B 387 -23.30 -140.49 REMARK 500 CYS K 35 62.37 -69.03 REMARK 500 THR K 36 -129.99 43.87 REMARK 500 REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 9KFB A 0 136 PDB 9KFB 9KFB 0 136 DBREF 9KFB A 137 263 PDB 9KFB 9KFB 137 263 DBREF 9KFB B 1 439 PDB 9KFB 9KFB 1 439 DBREF 9KFB K 1 439 PDB 9KFB 9KFB 1 439 DBREF 9KFB M 0 136 PDB 9KFB 9KFB 0 136 DBREF 9KFB M 137 263 PDB 9KFB 9KFB 137 263 DBREF 9KFB F 1 439 PDB 9KFB 9KFB 1 439 DBREF 9KFB X 0 136 PDB 9KFB 9KFB 0 136 DBREF 9KFB X 137 263 PDB 9KFB 9KFB 137 263 SEQRES 1 A 264 MET GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SEQRES 2 A 264 SER PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SEQRES 3 A 264 SER SER ASP ILE GLY GLY TYR ASN PHE VAL SER TRP TYR SEQRES 4 A 264 GLN GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR SEQRES 5 A 264 ASP ALA THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SEQRES 6 A 264 SER GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SEQRES 7 A 264 SER GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 A 264 CYS SER TYR ALA GLY ASP TYR THR PRO GLY VAL VAL PHE SEQRES 9 A 264 GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS SEQRES 10 A 264 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY SEQRES 11 A 264 GLY SER GLY GLY GLY GLY SER GLN VAL GLN LEU VAL GLN SEQRES 12 A 264 SER GLY ALA GLU VAL LYS LYS PRO GLY SER SER VAL LYS SEQRES 13 A 264 VAL SER CYS LYS ALA SER GLY GLY THR PHE ASN ARG TYR SEQRES 14 A 264 THR VAL ASN TRP VAL ARG GLN ALA PRO GLY GLN GLY LEU SEQRES 15 A 264 GLU TRP MET GLY GLY ILE ILE PRO ILE PHE GLY THR ALA SEQRES 16 A 264 ASN TYR ALA GLN ARG PHE GLN GLY ARG LEU THR ILE THR SEQRES 17 A 264 ALA ASP GLU SER THR SER THR ALA TYR MET GLU LEU SER SEQRES 18 A 264 SER LEU ARG SER ASP ASP THR ALA VAL TYR PHE CYS ALA SEQRES 19 A 264 ARG GLU ASN LEU ASP ASN SER GLY THR TYR TYR TYR PHE SEQRES 20 A 264 SER GLY TRP PHE ASP PRO TRP GLY GLN GLY THR LEU VAL SEQRES 21 A 264 THR VAL SER SER SEQRES 1 B 433 LYS PHE PRO ILE TYR THR ILE PRO ASP GLU LEU GLY PRO SEQRES 2 B 433 TRP SER PRO ILE ASP ILE HIS HIS LEU SER CYS PRO ASN SEQRES 3 B 433 ASN LEU VAL VAL GLU ASP GLU GLY CYS THR ASN LEU SER SEQRES 4 B 433 GLU PHE SER TYR MET GLU LEU LYS VAL GLY TYR ILE SER SEQRES 5 B 433 ALA ILE LYS VAL ASN GLY PHE THR CYS THR GLY VAL VAL SEQRES 6 B 433 THR GLU ALA GLU THR TYR THR GLY GLY SER GLY GLY THR SEQRES 7 B 433 THR PHE LYS ARG LYS HIS PHE ARG PRO THR PRO ASP ALA SEQRES 8 B 433 CYS ARG ALA ALA TYR ASN TRP LYS MET ALA GLY ASP PRO SEQRES 9 B 433 ARG TYR GLU GLU SER LEU HIS ASN PRO TYR GLY GLY SER SEQRES 10 B 433 GLY GLY ARG THR THR LYS GLU SER LEU ILE ILE ILE SER SEQRES 11 B 433 PRO SER VAL THR ASP LEU ASP PRO TYR ASP LYS SER LEU SEQRES 12 B 433 HIS SER ARG VAL PHE PRO GLY GLY LYS CYS SER GLY ILE SEQRES 13 B 433 THR VAL SER SER THR TYR CYS SER THR ASN HIS ASP TYR SEQRES 14 B 433 THR ILE TRP MET PRO GLU ASN PRO ARG PRO ARG THR PRO SEQRES 15 B 433 CYS ASP ILE PHE THR ASN SER ARG GLY LYS ARG ALA SER SEQRES 16 B 433 ASN GLY ASN LYS THR CYS GLY PHE VAL ASP GLU ARG GLY SEQRES 17 B 433 LEU TYR LYS SER LEU LYS GLY ALA CYS ARG LEU LYS LEU SEQRES 18 B 433 CYS GLY VAL LEU GLY LEU ARG LEU MET ASP GLY THR TRP SEQRES 19 B 433 VAL ALA MET GLN THR SER ASP GLU THR LYS TRP CYS PRO SEQRES 20 B 433 PRO ASP GLN LEU VAL ASN LEU HIS ASP PHE ARG SER ASP SEQRES 21 B 433 GLU ILE GLU HIS LEU VAL VAL GLU GLU LEU VAL LYS LYS SEQRES 22 B 433 ARG GLU GLU CYS LEU ASP ALA LEU GLU SER ILE MET THR SEQRES 23 B 433 THR LYS SER VAL SER PHE ARG ARG LEU SER HIS LEU ARG SEQRES 24 B 433 LYS LEU VAL PRO GLY PHE GLY LYS ALA TYR THR ILE PHE SEQRES 25 B 433 ASN LYS THR LEU MET GLU ALA ASP ALA HIS TYR LYS SER SEQRES 26 B 433 VAL ARG THR TRP ASN GLU ILE ILE PRO SER LYS GLY CYS SEQRES 27 B 433 LEU LYS VAL GLY GLY ARG CYS HIS PRO HIS VAL ASN GLY SEQRES 28 B 433 VAL PHE PHE ASN GLY ILE ILE LEU GLY PRO ASP ASP HIS SEQRES 29 B 433 VAL LEU ILE PRO GLU MET GLN SER SER LEU LEU GLN GLN SEQRES 30 B 433 HIS MET GLU LEU LEU LYS SER SER VAL ILE PRO LEU MET SEQRES 31 B 433 HIS PRO LEU ALA ASP PRO SER THR VAL PHE LYS GLU GLY SEQRES 32 B 433 ASP GLU ALA GLU ASP PHE VAL GLU VAL HIS LEU PRO ASP SEQRES 33 B 433 VAL TYR LYS GLN ILE SER GLY VAL ASP LEU GLY LEU PRO SEQRES 34 B 433 ASN TRP GLY LYS SEQRES 1 K 433 LYS PHE PRO ILE TYR THR ILE PRO ASP GLU LEU GLY PRO SEQRES 2 K 433 TRP SER PRO ILE ASP ILE HIS HIS LEU SER CYS PRO ASN SEQRES 3 K 433 ASN LEU VAL VAL GLU ASP GLU GLY CYS THR ASN LEU SER SEQRES 4 K 433 GLU PHE SER TYR MET GLU LEU LYS VAL GLY TYR ILE SER SEQRES 5 K 433 ALA ILE LYS VAL ASN GLY PHE THR CYS THR GLY VAL VAL SEQRES 6 K 433 THR GLU ALA GLU THR TYR THR GLY GLY SER GLY GLY THR SEQRES 7 K 433 THR PHE LYS ARG LYS HIS PHE ARG PRO THR PRO ASP ALA SEQRES 8 K 433 CYS ARG ALA ALA TYR ASN TRP LYS MET ALA GLY ASP PRO SEQRES 9 K 433 ARG TYR GLU GLU SER LEU HIS ASN PRO TYR GLY GLY SER SEQRES 10 K 433 GLY GLY ARG THR THR LYS GLU SER LEU ILE ILE ILE SER SEQRES 11 K 433 PRO SER VAL THR ASP LEU ASP PRO TYR ASP LYS SER LEU SEQRES 12 K 433 HIS SER ARG VAL PHE PRO GLY GLY LYS CYS SER GLY ILE SEQRES 13 K 433 THR VAL SER SER THR TYR CYS SER THR ASN HIS ASP TYR SEQRES 14 K 433 THR ILE TRP MET PRO GLU ASN PRO ARG PRO ARG THR PRO SEQRES 15 K 433 CYS ASP ILE PHE THR ASN SER ARG GLY LYS ARG ALA SER SEQRES 16 K 433 ASN GLY ASN LYS THR CYS GLY PHE VAL ASP GLU ARG GLY SEQRES 17 K 433 LEU TYR LYS SER LEU LYS GLY ALA CYS ARG LEU LYS LEU SEQRES 18 K 433 CYS GLY VAL LEU GLY LEU ARG LEU MET ASP GLY THR TRP SEQRES 19 K 433 VAL ALA MET GLN THR SER ASP GLU THR LYS TRP CYS PRO SEQRES 20 K 433 PRO ASP GLN LEU VAL ASN LEU HIS ASP PHE ARG SER ASP SEQRES 21 K 433 GLU ILE GLU HIS LEU VAL VAL GLU GLU LEU VAL LYS LYS SEQRES 22 K 433 ARG GLU GLU CYS LEU ASP ALA LEU GLU SER ILE MET THR SEQRES 23 K 433 THR LYS SER VAL SER PHE ARG ARG LEU SER HIS LEU ARG SEQRES 24 K 433 LYS LEU VAL PRO GLY PHE GLY LYS ALA TYR THR ILE PHE SEQRES 25 K 433 ASN LYS THR LEU MET GLU ALA ASP ALA HIS TYR LYS SER SEQRES 26 K 433 VAL ARG THR TRP ASN GLU ILE ILE PRO SER LYS GLY CYS SEQRES 27 K 433 LEU LYS VAL GLY GLY ARG CYS HIS PRO HIS VAL ASN GLY SEQRES 28 K 433 VAL PHE PHE ASN GLY ILE ILE LEU GLY PRO ASP ASP HIS SEQRES 29 K 433 VAL LEU ILE PRO GLU MET GLN SER SER LEU LEU GLN GLN SEQRES 30 K 433 HIS MET GLU LEU LEU LYS SER SER VAL ILE PRO LEU MET SEQRES 31 K 433 HIS PRO LEU ALA ASP PRO SER THR VAL PHE LYS GLU GLY SEQRES 32 K 433 ASP GLU ALA GLU ASP PHE VAL GLU VAL HIS LEU PRO ASP SEQRES 33 K 433 VAL TYR LYS GLN ILE SER GLY VAL ASP LEU GLY LEU PRO SEQRES 34 K 433 ASN TRP GLY LYS SEQRES 1 M 264 MET GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SEQRES 2 M 264 SER PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SEQRES 3 M 264 SER SER ASP ILE GLY GLY TYR ASN PHE VAL SER TRP TYR SEQRES 4 M 264 GLN GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR SEQRES 5 M 264 ASP ALA THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SEQRES 6 M 264 SER GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SEQRES 7 M 264 SER GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 M 264 CYS SER TYR ALA GLY ASP TYR THR PRO GLY VAL VAL PHE SEQRES 9 M 264 GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS SEQRES 10 M 264 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY SEQRES 11 M 264 GLY SER GLY GLY GLY GLY SER GLN VAL GLN LEU VAL GLN SEQRES 12 M 264 SER GLY ALA GLU VAL LYS LYS PRO GLY SER SER VAL LYS SEQRES 13 M 264 VAL SER CYS LYS ALA SER GLY GLY THR PHE ASN ARG TYR SEQRES 14 M 264 THR VAL ASN TRP VAL ARG GLN ALA PRO GLY GLN GLY LEU SEQRES 15 M 264 GLU TRP MET GLY GLY ILE ILE PRO ILE PHE GLY THR ALA SEQRES 16 M 264 ASN TYR ALA GLN ARG PHE GLN GLY ARG LEU THR ILE THR SEQRES 17 M 264 ALA ASP GLU SER THR SER THR ALA TYR MET GLU LEU SER SEQRES 18 M 264 SER LEU ARG SER ASP ASP THR ALA VAL TYR PHE CYS ALA SEQRES 19 M 264 ARG GLU ASN LEU ASP ASN SER GLY THR TYR TYR TYR PHE SEQRES 20 M 264 SER GLY TRP PHE ASP PRO TRP GLY GLN GLY THR LEU VAL SEQRES 21 M 264 THR VAL SER SER SEQRES 1 F 433 LYS PHE PRO ILE TYR THR ILE PRO ASP GLU LEU GLY PRO SEQRES 2 F 433 TRP SER PRO ILE ASP ILE HIS HIS LEU SER CYS PRO ASN SEQRES 3 F 433 ASN LEU VAL VAL GLU ASP GLU GLY CYS THR ASN LEU SER SEQRES 4 F 433 GLU PHE SER TYR MET GLU LEU LYS VAL GLY TYR ILE SER SEQRES 5 F 433 ALA ILE LYS VAL ASN GLY PHE THR CYS THR GLY VAL VAL SEQRES 6 F 433 THR GLU ALA GLU THR TYR THR GLY GLY SER GLY GLY THR SEQRES 7 F 433 THR PHE LYS ARG LYS HIS PHE ARG PRO THR PRO ASP ALA SEQRES 8 F 433 CYS ARG ALA ALA TYR ASN TRP LYS MET ALA GLY ASP PRO SEQRES 9 F 433 ARG TYR GLU GLU SER LEU HIS ASN PRO TYR GLY GLY SER SEQRES 10 F 433 GLY GLY ARG THR THR LYS GLU SER LEU ILE ILE ILE SER SEQRES 11 F 433 PRO SER VAL THR ASP LEU ASP PRO TYR ASP LYS SER LEU SEQRES 12 F 433 HIS SER ARG VAL PHE PRO GLY GLY LYS CYS SER GLY ILE SEQRES 13 F 433 THR VAL SER SER THR TYR CYS SER THR ASN HIS ASP TYR SEQRES 14 F 433 THR ILE TRP MET PRO GLU ASN PRO ARG PRO ARG THR PRO SEQRES 15 F 433 CYS ASP ILE PHE THR ASN SER ARG GLY LYS ARG ALA SER SEQRES 16 F 433 ASN GLY ASN LYS THR CYS GLY PHE VAL ASP GLU ARG GLY SEQRES 17 F 433 LEU TYR LYS SER LEU LYS GLY ALA CYS ARG LEU LYS LEU SEQRES 18 F 433 CYS GLY VAL LEU GLY LEU ARG LEU MET ASP GLY THR TRP SEQRES 19 F 433 VAL ALA MET GLN THR SER ASP GLU THR LYS TRP CYS PRO SEQRES 20 F 433 PRO ASP GLN LEU VAL ASN LEU HIS ASP PHE ARG SER ASP SEQRES 21 F 433 GLU ILE GLU HIS LEU VAL VAL GLU GLU LEU VAL LYS LYS SEQRES 22 F 433 ARG GLU GLU CYS LEU ASP ALA LEU GLU SER ILE MET THR SEQRES 23 F 433 THR LYS SER VAL SER PHE ARG ARG LEU SER HIS LEU ARG SEQRES 24 F 433 LYS LEU VAL PRO GLY PHE GLY LYS ALA TYR THR ILE PHE SEQRES 25 F 433 ASN LYS THR LEU MET GLU ALA ASP ALA HIS TYR LYS SER SEQRES 26 F 433 VAL ARG THR TRP ASN GLU ILE ILE PRO SER LYS GLY CYS SEQRES 27 F 433 LEU LYS VAL GLY GLY ARG CYS HIS PRO HIS VAL ASN GLY SEQRES 28 F 433 VAL PHE PHE ASN GLY ILE ILE LEU GLY PRO ASP ASP HIS SEQRES 29 F 433 VAL LEU ILE PRO GLU MET GLN SER SER LEU LEU GLN GLN SEQRES 30 F 433 HIS MET GLU LEU LEU LYS SER SER VAL ILE PRO LEU MET SEQRES 31 F 433 HIS PRO LEU ALA ASP PRO SER THR VAL PHE LYS GLU GLY SEQRES 32 F 433 ASP GLU ALA GLU ASP PHE VAL GLU VAL HIS LEU PRO ASP SEQRES 33 F 433 VAL TYR LYS GLN ILE SER GLY VAL ASP LEU GLY LEU PRO SEQRES 34 F 433 ASN TRP GLY LYS SEQRES 1 X 264 MET GLN SER ALA LEU THR GLN PRO ARG SER VAL SER GLY SEQRES 2 X 264 SER PRO GLY GLN SER VAL THR ILE SER CYS THR GLY THR SEQRES 3 X 264 SER SER ASP ILE GLY GLY TYR ASN PHE VAL SER TRP TYR SEQRES 4 X 264 GLN GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR SEQRES 5 X 264 ASP ALA THR LYS ARG PRO SER GLY VAL PRO ASP ARG PHE SEQRES 6 X 264 SER GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SEQRES 7 X 264 SER GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS SEQRES 8 X 264 CYS SER TYR ALA GLY ASP TYR THR PRO GLY VAL VAL PHE SEQRES 9 X 264 GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS SEQRES 10 X 264 GLY GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY SEQRES 11 X 264 GLY SER GLY GLY GLY GLY SER GLN VAL GLN LEU VAL GLN SEQRES 12 X 264 SER GLY ALA GLU VAL LYS LYS PRO GLY SER SER VAL LYS SEQRES 13 X 264 VAL SER CYS LYS ALA SER GLY GLY THR PHE ASN ARG TYR SEQRES 14 X 264 THR VAL ASN TRP VAL ARG GLN ALA PRO GLY GLN GLY LEU SEQRES 15 X 264 GLU TRP MET GLY GLY ILE ILE PRO ILE PHE GLY THR ALA SEQRES 16 X 264 ASN TYR ALA GLN ARG PHE GLN GLY ARG LEU THR ILE THR SEQRES 17 X 264 ALA ASP GLU SER THR SER THR ALA TYR MET GLU LEU SER SEQRES 18 X 264 SER LEU ARG SER ASP ASP THR ALA VAL TYR PHE CYS ALA SEQRES 19 X 264 ARG GLU ASN LEU ASP ASN SER GLY THR TYR TYR TYR PHE SEQRES 20 X 264 SER GLY TRP PHE ASP PRO TRP GLY GLN GLY THR LEU VAL SEQRES 21 X 264 THR VAL SER SER HELIX 1 AA1 ASP B 18 LEU B 22 5 5 HELIX 2 AA2 THR B 90 ALA B 103 1 14 HELIX 3 AA3 HIS B 270 ARG B 280 1 11 HELIX 4 AA4 GLU B 281 THR B 292 1 12 HELIX 5 AA5 SER B 297 HIS B 303 1 7 HELIX 6 AA6 THR B 334 ILE B 338 5 5 HELIX 7 AA7 THR K 90 ALA K 97 1 8 HELIX 8 AA8 TYR K 98 LYS K 101 5 4 HELIX 9 AA9 VAL K 272 THR K 292 1 21 HELIX 10 AB1 ARG K 299 ARG K 305 5 7 HELIX 11 AB2 THR K 334 ILE K 338 5 5 HELIX 12 AB3 ASP F 18 LEU F 22 5 5 HELIX 13 AB4 THR F 90 ARG F 95 1 6 HELIX 14 AB5 ARG F 95 LYS F 101 1 7 HELIX 15 AB6 HIS F 270 ARG F 280 1 11 HELIX 16 AB7 GLU F 281 THR F 292 1 12 HELIX 17 AB8 SER F 297 SER F 302 1 6 HELIX 18 AB9 HIS F 303 ARG F 305 5 3 HELIX 19 AC1 THR F 334 ILE F 338 5 5 SHEET 1 AA1 2 SER A 9 SER A 11 0 SHEET 2 AA1 2 LYS A 108 THR A 110 1 O THR A 110 N VAL A 10 SHEET 1 AA2 3 THR A 19 SER A 21 0 SHEET 2 AA2 3 ALA A 73 THR A 76 -1 O LEU A 75 N ILE A 20 SHEET 3 AA2 3 SER A 67 LYS A 68 -1 N SER A 67 O SER A 74 SHEET 1 AA3 3 LYS A 47 ILE A 50 0 SHEET 2 AA3 3 TRP A 37 GLN A 40 -1 N GLN A 39 O LYS A 47 SHEET 3 AA3 3 ASP A 87 TYR A 89 -1 O TYR A 89 N TYR A 38 SHEET 1 AA4 6 GLU A 146 VAL A 147 0 SHEET 2 AA4 6 THR A 257 THR A 260 1 O LEU A 258 N GLU A 146 SHEET 3 AA4 6 VAL A 229 ASN A 236 -1 N TYR A 230 O THR A 257 SHEET 4 AA4 6 TYR A 168 GLN A 175 -1 N ASN A 171 O ALA A 233 SHEET 5 AA4 6 TRP A 183 ILE A 188 -1 O ILE A 187 N VAL A 170 SHEET 6 AA4 6 THR A 193 TYR A 196 -1 O ASN A 195 N GLY A 186 SHEET 1 AA5 2 LYS A 155 LYS A 159 0 SHEET 2 AA5 2 THR A 214 GLU A 218 -1 O MET A 217 N VAL A 156 SHEET 1 AA6 3 TYR B 5 LEU B 11 0 SHEET 2 AA6 3 LEU B 322 VAL B 332 -1 O LYS B 330 N ILE B 7 SHEET 3 AA6 3 SER B 15 ILE B 17 -1 N ILE B 17 O LEU B 322 SHEET 1 AA7 3 TYR B 5 LEU B 11 0 SHEET 2 AA7 3 LEU B 322 VAL B 332 -1 O LYS B 330 N ILE B 7 SHEET 3 AA7 3 GLY B 310 ILE B 317 -1 N ALA B 314 O ALA B 325 SHEET 1 AA8 7 TYR B 216 LYS B 217 0 SHEET 2 AA8 7 THR B 206 VAL B 210 -1 N PHE B 209 O LYS B 217 SHEET 3 AA8 7 PHE B 192 SER B 201 -1 N ALA B 200 O GLY B 208 SHEET 4 AA8 7 SER B 39 TYR B 50 -1 N SER B 39 O ARG B 199 SHEET 5 AA8 7 THR B 239 VAL B 241 -1 O TRP B 240 N LEU B 46 SHEET 6 AA8 7 VAL B 230 ARG B 234 -1 N LEU B 233 O VAL B 241 SHEET 7 AA8 7 CYS B 223 LEU B 227 -1 N LEU B 225 O GLY B 232 SHEET 1 AA9 2 ILE B 364 LEU B 365 0 SHEET 2 AA9 2 VAL B 371 LEU B 372 -1 O LEU B 372 N ILE B 364 SHEET 1 AB1 3 TYR K 5 LEU K 11 0 SHEET 2 AB1 3 LEU K 322 VAL K 332 -1 O LYS K 330 N ILE K 7 SHEET 3 AB1 3 SER K 15 ILE K 17 -1 N SER K 15 O GLU K 324 SHEET 1 AB2 3 TYR K 5 LEU K 11 0 SHEET 2 AB2 3 LEU K 322 VAL K 332 -1 O LYS K 330 N ILE K 7 SHEET 3 AB2 3 GLY K 310 ILE K 317 -1 N GLY K 312 O ALA K 327 SHEET 1 AB3 5 PHE K 192 LYS K 198 0 SHEET 2 AB3 5 GLU K 40 TYR K 50 -1 N PHE K 41 O GLY K 197 SHEET 3 AB3 5 THR K 239 VAL K 241 -1 O TRP K 240 N GLY K 49 SHEET 4 AB3 5 LEU K 231 ARG K 234 -1 N LEU K 233 O VAL K 241 SHEET 5 AB3 5 CYS K 223 LYS K 226 -1 N CYS K 223 O ARG K 234 SHEET 1 AB4 2 PHE K 209 VAL K 210 0 SHEET 2 AB4 2 TYR K 216 LYS K 217 -1 O LYS K 217 N PHE K 209 SHEET 1 AB5 2 VAL K 296 SER K 297 0 SHEET 2 AB5 2 LEU K 388 LYS K 389 -1 O LYS K 389 N VAL K 296 SHEET 1 AB6 2 LEU K 345 VAL K 347 0 SHEET 2 AB6 2 ARG K 350 HIS K 352 -1 O ARG K 350 N VAL K 347 SHEET 1 AB7 2 ILE K 364 LEU K 365 0 SHEET 2 AB7 2 VAL K 371 LEU K 372 -1 O LEU K 372 N ILE K 364 SHEET 1 AB8 3 VAL M 18 THR M 23 0 SHEET 2 AB8 3 THR M 72 ILE M 77 -1 O ILE M 77 N VAL M 18 SHEET 3 AB8 3 SER M 67 LYS M 68 -1 N SER M 67 O SER M 74 SHEET 1 AB9 2 TRP M 37 TYR M 38 0 SHEET 2 AB9 2 LEU M 48 ILE M 50 -1 O ILE M 50 N TRP M 37 SHEET 1 AC1 2 CYS M 91 TYR M 93 0 SHEET 2 AC1 2 VAL M 101 PHE M 103 -1 O VAL M 102 N SER M 92 SHEET 1 AC2 2 VAL M 141 GLN M 142 0 SHEET 2 AC2 2 CYS M 158 LYS M 159 -1 O LYS M 159 N VAL M 141 SHEET 1 AC3 2 GLY M 185 ILE M 188 0 SHEET 2 AC3 2 THR M 193 TYR M 196 -1 O THR M 193 N ILE M 188 SHEET 1 AC4 2 ALA M 228 TYR M 230 0 SHEET 2 AC4 2 THR M 257 VAL M 259 -1 O VAL M 259 N ALA M 228 SHEET 1 AC5 3 THR F 6 LEU F 11 0 SHEET 2 AC5 3 THR F 321 SER F 331 -1 O HIS F 328 N ASP F 9 SHEET 3 AC5 3 SER F 15 PRO F 16 -1 N SER F 15 O GLU F 324 SHEET 1 AC6 3 THR F 6 LEU F 11 0 SHEET 2 AC6 3 THR F 321 SER F 331 -1 O HIS F 328 N ASP F 9 SHEET 3 AC6 3 GLY F 310 PHE F 318 -1 N THR F 316 O MET F 323 SHEET 1 AC7 2 SER F 39 LEU F 46 0 SHEET 2 AC7 2 PHE F 192 ARG F 199 -1 O GLY F 197 N PHE F 41 SHEET 1 AC8 2 ASP F 143 PRO F 144 0 SHEET 2 AC8 2 HIS F 150 SER F 151 -1 O SER F 151 N ASP F 143 SHEET 1 AC9 3 ALA F 222 LEU F 227 0 SHEET 2 AC9 3 VAL F 230 LEU F 235 -1 O ARG F 234 N CYS F 223 SHEET 3 AC9 3 TRP F 240 VAL F 241 -1 O VAL F 241 N LEU F 233 SHEET 1 AD1 2 SER F 295 VAL F 296 0 SHEET 2 AD1 2 LYS F 389 SER F 390 -1 O LYS F 389 N VAL F 296 SHEET 1 AD2 2 ILE F 364 LEU F 365 0 SHEET 2 AD2 2 VAL F 371 LEU F 372 -1 O LEU F 372 N ILE F 364 SHEET 1 AD3 2 TYR X 38 GLN X 39 0 SHEET 2 AD3 2 LYS X 47 LEU X 48 -1 O LYS X 47 N GLN X 39 SHEET 1 AD4 2 VAL X 141 GLN X 142 0 SHEET 2 AD4 2 CYS X 158 LYS X 159 -1 O LYS X 159 N VAL X 141 SHEET 1 AD5 2 VAL X 154 LYS X 155 0 SHEET 2 AD5 2 GLU X 218 LEU X 219 -1 O LEU X 219 N VAL X 154 SHEET 1 AD6 4 THR X 193 TYR X 196 0 SHEET 2 AD6 4 GLN X 179 ILE X 188 -1 N GLY X 186 O ASN X 195 SHEET 3 AD6 4 VAL X 170 ALA X 176 -1 N ALA X 176 O GLN X 179 SHEET 4 AD6 4 PHE X 231 ALA X 233 -1 O ALA X 233 N ASN X 171 SSBOND 1 CYS A 22 CYS A 90 1555 1555 2.04 SSBOND 2 CYS A 158 CYS A 232 1555 1555 2.04 SSBOND 3 CYS B 24 CYS B 283 1555 1555 2.04 SSBOND 4 CYS B 35 CYS B 207 1555 1555 2.03 SSBOND 5 CYS B 61 CYS B 94 1555 1555 2.03 SSBOND 6 CYS B 159 CYS B 169 1555 1555 2.04 SSBOND 7 CYS B 189 CYS B 228 1555 1555 2.03 SSBOND 8 CYS B 223 CYS B 252 1555 1555 2.03 SSBOND 9 CYS B 344 CYS B 351 1555 1555 2.03 SSBOND 10 CYS K 24 CYS K 283 1555 1555 2.04 SSBOND 11 CYS K 35 CYS K 207 1555 1555 2.03 SSBOND 12 CYS K 61 CYS K 94 1555 1555 2.04 SSBOND 13 CYS K 159 CYS K 169 1555 1555 2.04 SSBOND 14 CYS K 189 CYS K 228 1555 1555 2.02 SSBOND 15 CYS K 223 CYS K 252 1555 1555 2.03 SSBOND 16 CYS K 344 CYS K 351 1555 1555 2.03 SSBOND 17 CYS M 22 CYS M 90 1555 1555 2.03 SSBOND 18 CYS M 158 CYS M 232 1555 1555 2.04 SSBOND 19 CYS F 24 CYS F 283 1555 1555 2.04 SSBOND 20 CYS F 35 CYS F 207 1555 1555 2.03 SSBOND 21 CYS F 61 CYS F 94 1555 1555 2.03 SSBOND 22 CYS F 159 CYS F 169 1555 1555 2.04 SSBOND 23 CYS F 189 CYS F 228 1555 1555 2.04 SSBOND 24 CYS F 223 CYS F 252 1555 1555 2.03 SSBOND 25 CYS F 344 CYS F 351 1555 1555 2.03 SSBOND 26 CYS X 22 CYS X 90 1555 1555 2.04 SSBOND 27 CYS X 158 CYS X 232 1555 1555 2.03 CRYST1 157.619 157.619 221.392 90.00 90.00 90.00 P 41 21 2 24 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 0.006344 0.000000 0.000000 0.00000 SCALE2 0.000000 0.006344 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004517 0.00000