HEADER IMMUNE SYSTEM 18-AUG-24 9D7Y TITLE CRYSTAL STRUCTURE OF SCFV CORRESPONDING TO HUMAN AUTOANTIBODY B96.11 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SCFV CORRESPONDING TO HUMAN AUTOANTIBODY B96.11; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293; SOURCE 9 EXPRESSION_SYSTEM_ORGAN: KIDNEY; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1(-) KEYWDS AUTOANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR A.M.BUCKLE,S.MCGOWAN REVDAT 1 06-NOV-24 9D7Y 0 JRNL AUTH S.H.D.STANDER,C.F.REBOUL,S.N.LE,D.E.WILLIAMS,P.G.CHANDLER, JRNL AUTH 2 M.G.S.COSTA,D.E.HOKE,J.D.T.JIMMA,J.FODOR,G.FENALTI, JRNL AUTH 3 S.I.MANNERING,B.T.POREBSKI,P.SCHOFIELD,D.CHRIST,M.BUCKLE, JRNL AUTH 4 S.MCGOWAN,D.ELMLUND,K.D.RAND,A.M.BUCKLE JRNL TITL STRUCTURE AND DYNAMICS OF THE AUTOANTIGEN GAD65 IN COMPLEX JRNL TITL 2 WITH THE HUMAN AUTOIMMUNE POLYENDOCRINE SYNDROME TYPE JRNL TITL 3 2-ASSOCIATED AUTOANTIBODY B96.11 JRNL REF BIORXIV 2024 JRNL REFN ISSN 2692-8205 JRNL DOI 10.1101/2024.03.18.585568 REMARK 2 REMARK 2 RESOLUTION. 2.60 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) : 2.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.77 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 86.7 REMARK 3 NUMBER OF REFLECTIONS : 23377 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.233 REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.301 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.730 REMARK 3 FREE R VALUE TEST SET COUNT : 1806 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 45.7700 - 6.1100 0.92 1882 165 0.2153 0.2851 REMARK 3 2 6.1100 - 4.8500 0.94 1858 155 0.1966 0.2524 REMARK 3 3 4.8500 - 4.2400 0.94 1814 148 0.1660 0.2238 REMARK 3 4 4.2400 - 3.8500 0.95 1817 158 0.1922 0.2772 REMARK 3 5 3.8500 - 3.5800 0.93 1776 155 0.2115 0.2600 REMARK 3 6 3.5800 - 3.3700 0.94 1805 135 0.2206 0.3078 REMARK 3 7 3.3600 - 3.2000 0.88 1679 149 0.2461 0.3168 REMARK 3 8 3.2000 - 3.0600 0.86 1617 130 0.2590 0.3673 REMARK 3 9 3.0600 - 2.9400 0.82 1547 133 0.2786 0.3590 REMARK 3 10 2.9400 - 2.8400 0.81 1526 123 0.3018 0.3919 REMARK 3 11 2.8400 - 2.7500 0.80 1510 124 0.3184 0.4257 REMARK 3 12 2.7500 - 2.6700 0.77 1433 121 0.3321 0.4231 REMARK 3 13 2.6700 - 2.6000 0.69 1307 110 0.3298 0.3878 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) : 0.425 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.293 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32.73 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.10 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 : 0.010 5500 REMARK 3 ANGLE : 1.316 7473 REMARK 3 CHIRALITY : 0.073 790 REMARK 3 PLANARITY : 0.009 959 REMARK 3 DIHEDRAL : 17.009 778 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 : 1 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 2 or REMARK 3 (resid 3 and (name N or name CA or name C REMARK 3 or name O or name CB )) or resid 4 REMARK 3 through 12 or (resid 13 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 14 through 15 or (resid 16 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 17 through 42 or REMARK 3 (resid 43 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 44 REMARK 3 through 53 or (resid 54 through 57 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 58 or (resid 59 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 60 or (resid 61 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 62 through 64 or REMARK 3 (resid 65 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 66 REMARK 3 through 90 or (resid 91 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 92 through 107 or (resid 108 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 109 through 193 or REMARK 3 (resid 194 and (name N or name CA or name REMARK 3 C or name O or name CB or name CG or name REMARK 3 CD )) or resid 195 through 242 or (resid REMARK 3 243 and (name N or name CA or name C or REMARK 3 name O or name CB )) or resid 244 through REMARK 3 257)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and ((resid 1 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 2 through 42 or (resid 43 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 44 through 53 or REMARK 3 (resid 54 through 57 and (name N or name REMARK 3 CA or name C or name O or name CB )) or REMARK 3 resid 58 through 60 or (resid 61 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 62 through 107 or REMARK 3 (resid 108 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 109 REMARK 3 through 159 or (resid 160 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 161 through 162 or (resid 163 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 164 through 190 REMARK 3 or (resid 191 through 192 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 193 through 229 or (resid 230 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 231 through 242 REMARK 3 or (resid 243 and (name N or name CA or REMARK 3 name C or name O or name CB )) or resid REMARK 3 244 through 257)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and ((resid 1 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 2 through 12 or (resid 13 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 14 through 15 or REMARK 3 (resid 16 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 17 REMARK 3 through 55 or (resid 56 through 57 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 58 or (resid 59 and REMARK 3 (name N or name CA or name C or name O or REMARK 3 name CB )) or resid 60 through 66 or REMARK 3 (resid 67 and (name N or name CA or name REMARK 3 C or name O or name CB )) or resid 68 REMARK 3 through 90 or (resid 91 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 92 through 127 or resid 150 REMARK 3 through 159 or (resid 160 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 161 through 162 or (resid 163 REMARK 3 and (name N or name CA or name C or name REMARK 3 O or name CB )) or resid 164 through 190 REMARK 3 or (resid 191 through 192 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or (resid 193 through 194 and (name N or REMARK 3 name CA or name C or name O or name CB or REMARK 3 name CG or name CD )) or resid 195 REMARK 3 through 229 or (resid 230 and (name N or REMARK 3 name CA or name C or name O or name CB )) REMARK 3 or resid 231 through 257)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9D7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1000287490. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-AUG-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 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 : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26242 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600 REMARK 200 RESOLUTION RANGE LOW (A) : 45.770 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 85.7 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : 0.13720 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.9200 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) : 2.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 70.1 REMARK 200 DATA REDUNDANCY IN SHELL : 1.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.680 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.84 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: THE HANGING DROP CONTAINED 1 REMARK 280 MICROLITER OF MOTHER LIQUOR COMBINED WITH 1 MICROLITER OF 20 MG/ REMARK 280 ML B96.11 SCFV PROTEIN SOLUTION. CRYSTALS FORMED AS SHARDS REMARK 280 WITHIN 24 HOURS AT 293 K, WITH FINAL CRYSTALS BEING SELECTED REMARK 280 FROM WELL CONDITIONS CONTAINING 0.1M BIS-TRIS PH 6.5, 2.5M (NH4) REMARK 280 2SO4, VAPOR DIFFUSION, HANGING DROP REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 48.27200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.54400 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.98150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.54400 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.27200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 51.98150 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 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: 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 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 SER A 128 REMARK 465 GLY A 129 REMARK 465 GLY A 130 REMARK 465 GLY A 131 REMARK 465 GLY A 132 REMARK 465 SER A 133 REMARK 465 GLY A 134 REMARK 465 GLY A 135 REMARK 465 GLY A 136 REMARK 465 GLY A 137 REMARK 465 SER A 138 REMARK 465 GLY A 139 REMARK 465 GLY A 140 REMARK 465 GLY A 141 REMARK 465 GLY A 142 REMARK 465 SER A 143 REMARK 465 GLY A 144 REMARK 465 GLY A 145 REMARK 465 GLY A 146 REMARK 465 GLY A 147 REMARK 465 GLN A 148 REMARK 465 SER A 149 REMARK 465 LEU A 258 REMARK 465 GLY A 259 REMARK 465 HIS A 260 REMARK 465 HIS A 261 REMARK 465 HIS A 262 REMARK 465 HIS A 263 REMARK 465 HIS A 264 REMARK 465 ASP B 0 REMARK 465 SER B 128 REMARK 465 GLY B 129 REMARK 465 GLY B 130 REMARK 465 GLY B 131 REMARK 465 GLY B 132 REMARK 465 SER B 133 REMARK 465 GLY B 134 REMARK 465 GLY B 135 REMARK 465 GLY B 136 REMARK 465 GLY B 137 REMARK 465 SER B 138 REMARK 465 GLY B 139 REMARK 465 GLY B 140 REMARK 465 GLY B 141 REMARK 465 GLY B 142 REMARK 465 SER B 143 REMARK 465 GLY B 144 REMARK 465 GLY B 145 REMARK 465 GLY B 146 REMARK 465 GLY B 147 REMARK 465 GLN B 148 REMARK 465 SER B 149 REMARK 465 HIS B 260 REMARK 465 HIS B 261 REMARK 465 HIS B 262 REMARK 465 HIS B 263 REMARK 465 HIS B 264 REMARK 465 ASP C 0 REMARK 465 SER C 128 REMARK 465 GLY C 129 REMARK 465 GLY C 130 REMARK 465 GLY C 131 REMARK 465 GLY C 132 REMARK 465 SER C 133 REMARK 465 GLY C 134 REMARK 465 GLY C 135 REMARK 465 GLY C 136 REMARK 465 GLY C 137 REMARK 465 SER C 138 REMARK 465 GLY C 139 REMARK 465 GLY C 140 REMARK 465 GLY C 141 REMARK 465 GLY C 142 REMARK 465 SER C 143 REMARK 465 GLY C 144 REMARK 465 GLY C 145 REMARK 465 GLY C 146 REMARK 465 GLY C 147 REMARK 465 GLY C 259 REMARK 465 HIS C 260 REMARK 465 HIS C 261 REMARK 465 HIS C 262 REMARK 465 HIS C 263 REMARK 465 HIS C 264 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 A 0 OD1 OD2 REMARK 470 GLU A 1 CG CD OE1 OE2 REMARK 470 ASP A 57 CG OD1 OD2 REMARK 470 LYS A 67 CG CD CE NZ REMARK 470 SER A 160 OG REMARK 470 GLN A 163 CG CD OE1 NE2 REMARK 470 LYS A 191 CG CD CE NZ REMARK 470 GLU A 230 CG CD OE1 OE2 REMARK 470 GLN B 3 CG CD OE1 NE2 REMARK 470 GLN B 13 CG CD OE1 NE2 REMARK 470 ARG B 16 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 56 CG1 CG2 CD1 REMARK 470 THR B 59 OG1 CG2 REMARK 470 SER B 65 OG REMARK 470 LYS B 67 CG CD CE NZ REMARK 470 GLU B 91 CG CD OE1 OE2 REMARK 470 LYS B 191 CD CE NZ REMARK 470 LYS B 194 CE NZ REMARK 470 LEU B 258 CG CD1 CD2 REMARK 470 GLN C 3 CG CD OE1 NE2 REMARK 470 LYS C 43 CG CD CE NZ REMARK 470 ARG C 54 CG CD NE CZ NH1 NH2 REMARK 470 ASP C 57 CG OD1 OD2 REMARK 470 GLN C 61 CG CD OE1 NE2 REMARK 470 SER C 65 OG REMARK 470 GLU C 108 CG CD OE1 OE2 REMARK 470 GLN C 148 CG CD OE1 NE2 REMARK 470 SER C 149 OG REMARK 470 SER C 243 OG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLY A 206 O HOH A 401 1.90 REMARK 500 O ALA A 192 O HOH A 402 1.92 REMARK 500 O GLY C 44 O HOH C 401 1.93 REMARK 500 O PHE A 109 O HOH A 403 1.96 REMARK 500 OE2 GLU C 199 O HOH C 402 2.00 REMARK 500 O PHE B 105 O HOH B 401 2.01 REMARK 500 O VAL A 5 O HOH A 404 2.01 REMARK 500 ND2 ASN C 251 O HOH C 403 2.04 REMARK 500 O TRP C 106 O HOH C 404 2.04 REMARK 500 O3 SO4 A 302 O HOH A 405 2.05 REMARK 500 O HOH A 405 O HOH A 417 2.05 REMARK 500 O GLY C 30 OG SER C 53 2.06 REMARK 500 OG SER A 65 O HOH A 406 2.06 REMARK 500 O HOH A 409 O HOH A 416 2.06 REMARK 500 O HOH C 428 O HOH C 445 2.07 REMARK 500 OG SER C 164 O HOH C 405 2.09 REMARK 500 OD1 ASP B 57 O HOH B 402 2.09 REMARK 500 O GLY A 250 O HOH A 407 2.09 REMARK 500 NH2 ARG B 100 O HOH B 403 2.10 REMARK 500 O HOH A 418 O HOH A 447 2.10 REMARK 500 O HOH B 403 O HOH B 416 2.11 REMARK 500 O GLY B 44 O HOH B 404 2.12 REMARK 500 O ARG A 112 OH TYR A 247 2.12 REMARK 500 NE2 HIS A 187 O HOH A 408 2.13 REMARK 500 O HOH A 444 O HOH A 448 2.14 REMARK 500 O HOH A 446 O HOH A 453 2.15 REMARK 500 N ALA B 241 O PHE B 246 2.15 REMARK 500 O HOH C 415 O HOH C 429 2.16 REMARK 500 O GLU B 1 O HOH B 405 2.16 REMARK 500 N ALA C 40 O HOH C 401 2.17 REMARK 500 ND2 ASN A 251 O HOH A 409 2.17 REMARK 500 OE2 GLU C 230 O HOH C 406 2.18 REMARK 500 OH TYR B 97 O HOH B 406 2.18 REMARK 500 O HOH A 452 O HOH A 456 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 434 O HOH B 414 3646 2.08 REMARK 500 N ASP A 209 OD2 ASP C 209 2664 2.09 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 ARG A 16 CG - CD - NE ANGL. DEV. = -15.1 DEGREES REMARK 500 ASP C 209 CB - CG - OD2 ANGL. DEV. = -6.4 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 GLU A 1 146.94 103.75 REMARK 500 ALA A 55 20.36 -73.77 REMARK 500 ILE A 56 -49.25 -140.28 REMARK 500 ASP A 57 -58.35 -178.00 REMARK 500 ASP A 175 -93.25 -140.25 REMARK 500 VAL A 200 -51.07 73.63 REMARK 500 ASP A 209 -4.52 -56.21 REMARK 500 LEU A 227 162.09 -47.23 REMARK 500 PHE A 246 -91.77 62.42 REMARK 500 PRO B 14 -124.93 -13.57 REMARK 500 ILE B 56 -49.97 -146.11 REMARK 500 ASP B 57 -142.25 40.89 REMARK 500 THR B 59 134.03 76.69 REMARK 500 ALA B 64 -59.83 -29.23 REMARK 500 LYS B 67 -112.25 -73.85 REMARK 500 GLU B 91 0.09 -69.84 REMARK 500 TYR B 103 140.58 88.59 REMARK 500 GLN B 119 -24.15 -148.95 REMARK 500 SER B 126 -105.79 -64.53 REMARK 500 ASP B 175 -99.75 -139.79 REMARK 500 VAL B 200 -55.04 73.50 REMARK 500 ASP B 209 -4.57 -59.93 REMARK 500 LEU B 227 165.51 -49.64 REMARK 500 PHE B 246 -91.34 59.19 REMARK 500 VAL C 2 85.14 90.14 REMARK 500 ILE C 56 -52.90 -145.56 REMARK 500 ASP C 57 -116.76 30.32 REMARK 500 GLU C 91 2.78 -69.50 REMARK 500 SER C 149 86.64 -176.14 REMARK 500 ALA C 150 173.63 179.88 REMARK 500 ASP C 175 -101.57 -134.20 REMARK 500 VAL C 200 -52.25 72.85 REMARK 500 ASP C 209 -8.27 -53.18 REMARK 500 PHE C 246 -92.29 51.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 GLU C 6 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 457 DISTANCE = 7.93 ANGSTROMS DBREF 9D7Y A 0 264 PDB 9D7Y 9D7Y 0 264 DBREF 9D7Y B 0 264 PDB 9D7Y 9D7Y 0 264 DBREF 9D7Y C 0 264 PDB 9D7Y 9D7Y 0 264 SEQRES 1 A 265 ASP GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 A 265 GLN PRO GLY ARG SER LEU ARG LEU SER CYS SER ALA SER SEQRES 3 A 265 GLY PHE THR PHE GLY ASP TYR ALA MET SER TRP PHE ARG SEQRES 4 A 265 LEU ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY LEU ILE SEQRES 5 A 265 LYS SER ARG ALA ILE ASP GLY THR PRO GLN TYR ALA ALA SEQRES 6 A 265 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER SEQRES 7 A 265 ASN SER ILE ALA TYR LEU GLN MET ASN SER LEU THR THR SEQRES 8 A 265 GLU ASP THR ALA ILE TYR TYR CYS ALA ARG ASP PHE TYR SEQRES 9 A 265 ASP PHE TRP ASN GLU PHE SER HIS ARG THR PHE ASP PHE SEQRES 10 A 265 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SER GLY SEQRES 11 A 265 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 12 A 265 SER GLY GLY GLY GLY GLN SER ALA LEU THR GLN PRO ALA SEQRES 13 A 265 SER ALA SER GLY SER PRO GLY GLN SER VAL THR ILE THR SEQRES 14 A 265 CYS THR GLY SER SER SER ASP VAL GLY GLY TYR LYS TYR SEQRES 15 A 265 VAL SER TRP TYR GLN HIS HIS PRO GLY LYS ALA PRO LYS SEQRES 16 A 265 LEU MET ILE TYR GLU VAL SER LYS ARG PRO SER GLY VAL SEQRES 17 A 265 PRO ASP ARG PHE SER GLY SER LYS SER GLY ASN MET ALA SEQRES 18 A 265 SER LEU THR VAL SER GLY LEU GLN ALA GLU ASP GLU ALA SEQRES 19 A 265 ASP TYR TYR CYS SER SER TYR ALA GLY SER TYR ASN PHE SEQRES 20 A 265 TYR VAL PHE GLY ASN GLY THR LYS VAL THR VAL LEU GLY SEQRES 21 A 265 HIS HIS HIS HIS HIS SEQRES 1 B 265 ASP GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 B 265 GLN PRO GLY ARG SER LEU ARG LEU SER CYS SER ALA SER SEQRES 3 B 265 GLY PHE THR PHE GLY ASP TYR ALA MET SER TRP PHE ARG SEQRES 4 B 265 LEU ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY LEU ILE SEQRES 5 B 265 LYS SER ARG ALA ILE ASP GLY THR PRO GLN TYR ALA ALA SEQRES 6 B 265 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER SEQRES 7 B 265 ASN SER ILE ALA TYR LEU GLN MET ASN SER LEU THR THR SEQRES 8 B 265 GLU ASP THR ALA ILE TYR TYR CYS ALA ARG ASP PHE TYR SEQRES 9 B 265 ASP PHE TRP ASN GLU PHE SER HIS ARG THR PHE ASP PHE SEQRES 10 B 265 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SER GLY SEQRES 11 B 265 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 12 B 265 SER GLY GLY GLY GLY GLN SER ALA LEU THR GLN PRO ALA SEQRES 13 B 265 SER ALA SER GLY SER PRO GLY GLN SER VAL THR ILE THR SEQRES 14 B 265 CYS THR GLY SER SER SER ASP VAL GLY GLY TYR LYS TYR SEQRES 15 B 265 VAL SER TRP TYR GLN HIS HIS PRO GLY LYS ALA PRO LYS SEQRES 16 B 265 LEU MET ILE TYR GLU VAL SER LYS ARG PRO SER GLY VAL SEQRES 17 B 265 PRO ASP ARG PHE SER GLY SER LYS SER GLY ASN MET ALA SEQRES 18 B 265 SER LEU THR VAL SER GLY LEU GLN ALA GLU ASP GLU ALA SEQRES 19 B 265 ASP TYR TYR CYS SER SER TYR ALA GLY SER TYR ASN PHE SEQRES 20 B 265 TYR VAL PHE GLY ASN GLY THR LYS VAL THR VAL LEU GLY SEQRES 21 B 265 HIS HIS HIS HIS HIS SEQRES 1 C 265 ASP GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL SEQRES 2 C 265 GLN PRO GLY ARG SER LEU ARG LEU SER CYS SER ALA SER SEQRES 3 C 265 GLY PHE THR PHE GLY ASP TYR ALA MET SER TRP PHE ARG SEQRES 4 C 265 LEU ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY LEU ILE SEQRES 5 C 265 LYS SER ARG ALA ILE ASP GLY THR PRO GLN TYR ALA ALA SEQRES 6 C 265 SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER SEQRES 7 C 265 ASN SER ILE ALA TYR LEU GLN MET ASN SER LEU THR THR SEQRES 8 C 265 GLU ASP THR ALA ILE TYR TYR CYS ALA ARG ASP PHE TYR SEQRES 9 C 265 ASP PHE TRP ASN GLU PHE SER HIS ARG THR PHE ASP PHE SEQRES 10 C 265 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SER GLY SEQRES 11 C 265 GLY GLY GLY SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 12 C 265 SER GLY GLY GLY GLY GLN SER ALA LEU THR GLN PRO ALA SEQRES 13 C 265 SER ALA SER GLY SER PRO GLY GLN SER VAL THR ILE THR SEQRES 14 C 265 CYS THR GLY SER SER SER ASP VAL GLY GLY TYR LYS TYR SEQRES 15 C 265 VAL SER TRP TYR GLN HIS HIS PRO GLY LYS ALA PRO LYS SEQRES 16 C 265 LEU MET ILE TYR GLU VAL SER LYS ARG PRO SER GLY VAL SEQRES 17 C 265 PRO ASP ARG PHE SER GLY SER LYS SER GLY ASN MET ALA SEQRES 18 C 265 SER LEU THR VAL SER GLY LEU GLN ALA GLU ASP GLU ALA SEQRES 19 C 265 ASP TYR TYR CYS SER SER TYR ALA GLY SER TYR ASN PHE SEQRES 20 C 265 TYR VAL PHE GLY ASN GLY THR LYS VAL THR VAL LEU GLY SEQRES 21 C 265 HIS HIS HIS HIS HIS HET SO4 A 301 5 HET SO4 A 302 5 HET SO4 B 301 5 HET SO4 C 301 5 HETNAM SO4 SULFATE ION FORMUL 4 SO4 4(O4 S 2-) FORMUL 8 HOH *157(H2 O) HELIX 1 AA1 THR A 28 TYR A 32 5 5 HELIX 2 AA2 ALA A 64 LYS A 67 5 4 HELIX 3 AA3 THR A 89 THR A 93 5 5 HELIX 4 AA4 ASP A 175 TYR A 179 5 5 HELIX 5 AA5 GLN A 228 GLU A 232 5 5 HELIX 6 AA6 ALA A 241 PHE A 246 1 6 HELIX 7 AA7 THR B 28 TYR B 32 5 5 HELIX 8 AA8 THR B 89 THR B 93 5 5 HELIX 9 AA9 GLN B 228 GLU B 232 5 5 HELIX 10 AB1 ALA B 241 PHE B 246 1 6 HELIX 11 AB2 THR C 28 TYR C 32 5 5 HELIX 12 AB3 ALA C 64 LYS C 67 5 4 HELIX 13 AB4 ASP C 76 ASN C 78 5 3 HELIX 14 AB5 THR C 89 THR C 93 5 5 HELIX 15 AB6 GLN C 228 GLU C 232 5 5 HELIX 16 AB7 ALA C 241 PHE C 246 1 6 SHEET 1 AA1 4 GLN A 3 SER A 7 0 SHEET 2 AA1 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AA1 4 ILE A 80 MET A 85 -1 O LEU A 83 N LEU A 20 SHEET 4 AA1 4 PHE A 70 ASP A 75 -1 N SER A 73 O TYR A 82 SHEET 1 AA2 6 LEU A 11 VAL A 12 0 SHEET 2 AA2 6 THR A 121 VAL A 125 1 O THR A 124 N VAL A 12 SHEET 3 AA2 6 ALA A 94 ASP A 101 -1 N ALA A 94 O VAL A 123 SHEET 4 AA2 6 MET A 34 LEU A 39 -1 N LEU A 39 O ILE A 95 SHEET 5 AA2 6 LEU A 45 ILE A 51 -1 O VAL A 48 N TRP A 36 SHEET 6 AA2 6 GLN A 61 TYR A 62 -1 O GLN A 61 N LEU A 50 SHEET 1 AA3 4 LEU A 11 VAL A 12 0 SHEET 2 AA3 4 THR A 121 VAL A 125 1 O THR A 124 N VAL A 12 SHEET 3 AA3 4 ALA A 94 ASP A 101 -1 N ALA A 94 O VAL A 123 SHEET 4 AA3 4 PHE A 114 ASP A 115 -1 O ASP A 115 N ARG A 100 SHEET 1 AA4 5 SER A 156 SER A 158 0 SHEET 2 AA4 5 THR A 253 THR A 256 1 O LYS A 254 N ALA A 157 SHEET 3 AA4 5 ASP A 234 TYR A 240 -1 N TYR A 235 O THR A 253 SHEET 4 AA4 5 VAL A 182 HIS A 187 -1 N TYR A 185 O TYR A 236 SHEET 5 AA4 5 LYS A 194 ILE A 197 -1 O MET A 196 N TRP A 184 SHEET 1 AA5 4 SER A 156 SER A 158 0 SHEET 2 AA5 4 THR A 253 THR A 256 1 O LYS A 254 N ALA A 157 SHEET 3 AA5 4 ASP A 234 TYR A 240 -1 N TYR A 235 O THR A 253 SHEET 4 AA5 4 TYR A 247 PHE A 249 -1 O VAL A 248 N SER A 239 SHEET 1 AA6 3 VAL A 165 THR A 170 0 SHEET 2 AA6 3 MET A 219 VAL A 224 -1 O LEU A 222 N ILE A 167 SHEET 3 AA6 3 PHE A 211 SER A 216 -1 N SER A 214 O SER A 221 SHEET 1 AA7 4 GLN B 3 SER B 7 0 SHEET 2 AA7 4 LEU B 18 SER B 25 -1 O SER B 25 N GLN B 3 SHEET 3 AA7 4 ILE B 80 MET B 85 -1 O LEU B 83 N LEU B 20 SHEET 4 AA7 4 PHE B 70 ASP B 75 -1 N SER B 73 O TYR B 82 SHEET 1 AA8 6 GLY B 10 VAL B 12 0 SHEET 2 AA8 6 THR B 121 VAL B 125 1 O THR B 124 N VAL B 12 SHEET 3 AA8 6 ALA B 94 ASP B 101 -1 N ALA B 94 O VAL B 123 SHEET 4 AA8 6 MET B 34 LEU B 39 -1 N PHE B 37 O TYR B 97 SHEET 5 AA8 6 LEU B 45 ILE B 51 -1 O ILE B 51 N MET B 34 SHEET 6 AA8 6 GLN B 61 TYR B 62 -1 O GLN B 61 N LEU B 50 SHEET 1 AA9 4 GLY B 10 VAL B 12 0 SHEET 2 AA9 4 THR B 121 VAL B 125 1 O THR B 124 N VAL B 12 SHEET 3 AA9 4 ALA B 94 ASP B 101 -1 N ALA B 94 O VAL B 123 SHEET 4 AA9 4 PHE B 114 ASP B 115 -1 O ASP B 115 N ARG B 100 SHEET 1 AB1 5 SER B 156 GLY B 159 0 SHEET 2 AB1 5 THR B 253 VAL B 257 1 O THR B 256 N ALA B 157 SHEET 3 AB1 5 ALA B 233 TYR B 240 -1 N ALA B 233 O VAL B 255 SHEET 4 AB1 5 VAL B 182 HIS B 187 -1 N HIS B 187 O ASP B 234 SHEET 5 AB1 5 LYS B 194 ILE B 197 -1 O MET B 196 N TRP B 184 SHEET 1 AB2 4 SER B 156 GLY B 159 0 SHEET 2 AB2 4 THR B 253 VAL B 257 1 O THR B 256 N ALA B 157 SHEET 3 AB2 4 ALA B 233 TYR B 240 -1 N ALA B 233 O VAL B 255 SHEET 4 AB2 4 TYR B 247 PHE B 249 -1 O VAL B 248 N SER B 239 SHEET 1 AB3 3 VAL B 165 THR B 170 0 SHEET 2 AB3 3 MET B 219 VAL B 224 -1 O ALA B 220 N CYS B 169 SHEET 3 AB3 3 PHE B 211 SER B 216 -1 N SER B 212 O THR B 223 SHEET 1 AB4 4 GLN C 3 SER C 7 0 SHEET 2 AB4 4 LEU C 18 SER C 25 -1 O SER C 23 N VAL C 5 SHEET 3 AB4 4 ILE C 80 MET C 85 -1 O MET C 85 N LEU C 18 SHEET 4 AB4 4 PHE C 70 ASP C 75 -1 N SER C 73 O TYR C 82 SHEET 1 AB5 6 LEU C 11 VAL C 12 0 SHEET 2 AB5 6 THR C 121 VAL C 125 1 O THR C 124 N VAL C 12 SHEET 3 AB5 6 ALA C 94 ASP C 101 -1 N ALA C 94 O VAL C 123 SHEET 4 AB5 6 MET C 34 LEU C 39 -1 N PHE C 37 O TYR C 97 SHEET 5 AB5 6 LEU C 45 ILE C 51 -1 O VAL C 48 N TRP C 36 SHEET 6 AB5 6 GLN C 61 TYR C 62 -1 O GLN C 61 N LEU C 50 SHEET 1 AB6 4 LEU C 11 VAL C 12 0 SHEET 2 AB6 4 THR C 121 VAL C 125 1 O THR C 124 N VAL C 12 SHEET 3 AB6 4 ALA C 94 ASP C 101 -1 N ALA C 94 O VAL C 123 SHEET 4 AB6 4 PHE C 114 ASP C 115 -1 O ASP C 115 N ARG C 100 SHEET 1 AB7 5 SER C 156 GLY C 159 0 SHEET 2 AB7 5 THR C 253 VAL C 257 1 O LYS C 254 N ALA C 157 SHEET 3 AB7 5 ASP C 234 TYR C 240 -1 N TYR C 235 O THR C 253 SHEET 4 AB7 5 VAL C 182 HIS C 187 -1 N HIS C 187 O ASP C 234 SHEET 5 AB7 5 LYS C 194 ILE C 197 -1 O MET C 196 N TRP C 184 SHEET 1 AB8 4 SER C 156 GLY C 159 0 SHEET 2 AB8 4 THR C 253 VAL C 257 1 O LYS C 254 N ALA C 157 SHEET 3 AB8 4 ASP C 234 TYR C 240 -1 N TYR C 235 O THR C 253 SHEET 4 AB8 4 TYR C 247 PHE C 249 -1 O VAL C 248 N SER C 239 SHEET 1 AB9 3 VAL C 165 THR C 170 0 SHEET 2 AB9 3 MET C 219 VAL C 224 -1 O ALA C 220 N CYS C 169 SHEET 3 AB9 3 PHE C 211 SER C 216 -1 N SER C 214 O SER C 221 SSBOND 1 CYS A 22 CYS A 98 1555 1555 2.04 SSBOND 2 CYS A 169 CYS A 237 1555 1555 2.04 SSBOND 3 CYS B 22 CYS B 98 1555 1555 2.05 SSBOND 4 CYS B 169 CYS B 237 1555 1555 2.04 SSBOND 5 CYS C 22 CYS C 98 1555 1555 2.05 SSBOND 6 CYS C 169 CYS C 237 1555 1555 2.05 CRYST1 96.544 103.963 85.088 90.00 90.00 90.00 P 21 21 21 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 0.010358 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009619 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011753 0.00000 MTRIX1 1 0.529311 0.017400 -0.848250 75.94912 1 MTRIX2 1 0.021672 0.999186 0.034019 13.22963 1 MTRIX3 1 0.848151 -0.036389 0.528503 -52.40415 1 MTRIX1 2 -0.473017 0.026831 -0.880645 163.77930 1 MTRIX2 2 0.034615 0.999330 0.011855 31.51600 1 MTRIX3 2 0.880373 -0.024876 -0.473629 73.05561 1