HEADER SIGNALING PROTEIN 13-DEC-23 8VC7 TITLE CRYSTAL STRUCTURE OF HUMAN BTN2A1 ECTODOMAIN IN COMPLEX WITH TITLE 2 ANTAGONIST 2A1.9 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUMAN IGG1 FRAGMENT ANTIBODY LIGHT CHAIN; COMPND 3 CHAIN: D, A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: LIGHT CHAIN OF HERCEPTIN FAB SCAFFOLD WITH CDR LOOPS COMPND 6 MODIFIED THROUGH PHAGE-DISPLAY EVOLUTION. (CDR1: VSSAV) (CDR2: COMPND 7 IYSASSLY) (CDR3: SSSSLIT). N-TERMINAL (S) RESIDUE IS A COMPND 8 LINKER/RESTRICTION ENZYME ARTIFACT, DISORDERED AND NOT MODELED.; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: HUMAN IGG1 FRAGMENT ANTIBODY HEAVY CHAIN; COMPND 11 CHAIN: J, B; COMPND 12 ENGINEERED: YES; COMPND 13 OTHER_DETAILS: HEAVY CHAIN OF HERCEPTIN FAB SCAFFOLD WITH CDR LOOPS COMPND 14 MODIFIED THROUGH PHAGE-DISPLAY EVOLUTION. (CDR1: NLYSSSI) (CDR2: COMPND 15 YIYPSSGYTS) (CDR3: YYYTRGYPDGMDY). N-TERMINAL (EISE) IS A COMPND 16 LINKER/RESTRICTION ENZYME ARTIFACT AND FIRST RESIDUE OF FAB, AND COMPND 17 DISORDERED AND NOT MODELED. MIDDLE (SSKSTSG) AND C-TERMINAL COMPND 18 (KSCDKTHT) RESIDUES WERE DISORDERED AND NOT MODELED.; COMPND 19 MOL_ID: 3; COMPND 20 MOLECULE: BUTYROPHILIN SUBFAMILY 2 MEMBER A1; COMPND 21 CHAIN: C, E; COMPND 22 ENGINEERED: YES; COMPND 23 MUTATION: YES; COMPND 24 OTHER_DETAILS: BTN2A1 ECTODOMAIN WITH C219S MUTATION, AND N- AND C- COMPND 25 TERMINAL LINKERS. N-TERMINAL (ADL) AND C-TERMINAL (VSPSGSGLEVLFQ) COMPND 26 RESIDUES ARE DISORDERED AND NOT MODELED. 3 GLYCANS ARE DENOTED AS COMPND 27 NAG. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: RH2.2; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: RH2.2; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: BTN2A1, BT2.1, BTF1; SOURCE 20 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 22 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS; SOURCE 23 EXPRESSION_SYSTEM_PLASMID: PAC-GP67A KEYWDS INHIBITOR, COMPLEX, ANTIBODY, IMMUNE RECOGNITION, SIGNALING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.RAMESH,S.ROY,E.ADAMS REVDAT 1 18-DEC-24 8VC7 0 JRNL AUTH A.RAMESH,S.ROY,T.SLEZAK,A.A.KOSSIAKOFF,E.J.ADAMS JRNL TITL MAPPING THE EXTRACELLULAR MOLECULAR ARCHITECTURE OF THE JRNL TITL 2 PAG-SIGNALING COMPLEX WITH ANTI-BUTYROPHILIN ANTIBODIES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.76 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5015 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) : 2.76 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.46 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 49406 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.219 REMARK 3 R VALUE (WORKING SET) : 0.218 REMARK 3 FREE R VALUE : 0.261 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.040 REMARK 3 FREE R VALUE TEST SET COUNT : 1998 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 39.4600 - 6.6400 0.99 3620 154 0.2049 0.2419 REMARK 3 2 6.6400 - 5.2800 1.00 3503 145 0.1934 0.2282 REMARK 3 3 5.2800 - 4.6100 0.99 3404 147 0.1538 0.1727 REMARK 3 4 4.6100 - 4.1900 1.00 3391 147 0.1523 0.2034 REMARK 3 5 4.1900 - 3.8900 1.00 3401 137 0.1916 0.2272 REMARK 3 6 3.8900 - 3.6600 1.00 3365 142 0.2087 0.2577 REMARK 3 7 3.6600 - 3.4800 1.00 3339 143 0.2188 0.2869 REMARK 3 8 3.4800 - 3.3300 0.99 3374 142 0.2251 0.2397 REMARK 3 9 3.3300 - 3.2000 1.00 3298 147 0.2878 0.3299 REMARK 3 10 3.2000 - 3.0900 1.00 3377 141 0.2780 0.3031 REMARK 3 11 3.0900 - 2.9900 1.00 3287 129 0.2883 0.3768 REMARK 3 12 2.9900 - 2.9100 1.00 3400 142 0.2882 0.3665 REMARK 3 13 2.9100 - 2.8300 1.00 3274 146 0.3113 0.3831 REMARK 3 14 2.8300 - 2.7600 1.00 3375 136 0.3396 0.3815 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) : 0.420 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.330 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 : 0.008 NULL REMARK 3 ANGLE : 1.130 NULL REMARK 3 CHIRALITY : 0.068 1558 REMARK 3 PLANARITY : 0.009 1752 REMARK 3 DIHEDRAL : 15.898 3534 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8VC7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-23. REMARK 100 THE DEPOSITION ID IS D_1000279865. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 31-AUG-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.3 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.1950 REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL REMARK 200 OPTICS : MIRROR: FLAT BENT COLLIMATING RH REMARK 200 COATED MIRROR, TOROIDAL REMARK 200 FOCUSSING MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49431 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.760 REMARK 200 RESOLUTION RANGE LOW (A) : 39.460 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 8.900 REMARK 200 R MERGE (I) : 0.25800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.76 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 9.30 REMARK 200 R MERGE FOR SHELL (I) : 1.42400 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: OVERLAPPING LARGE PLATES REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.75 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: OPTIMIZED WELL-G9 FROM MORPHEUS MIDAS REMARK 280 MD1-76-HT SCREEN: - 0.1M BUFFER SYSTEM 3, PH 8.3 (BUFFER SYSTEM REMARK 280 3 1M STOCK: 50.3% 1M BICINE, 49.7% 1M TRIS) - 0.1M CARBOXYLIC REMARK 280 ACIDS MIX (CARBOXYLIC ACIDS MIX 1M STOCK: 0.2M SODIUM FORMATE; REMARK 280 0.2M AMMONIUM ACETATE; 0.2M SODIUM CITRATE TRIBASIC DIHYDRATE; REMARK 280 0.2M POTASSIUM SODIUM TARTRATE TETRAHYDRATE; 0.2M SODIUM OXAMATE) REMARK 280 - 20% PRECIPITANT MIX 1 (PRECIPITANT MIX 1 60% STOCK: 40% V/V REMARK 280 PEG500 MME; 20% W/V PEG20000), VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 298K 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 22.45750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.34200 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 100.48800 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.34200 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.45750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 100.48800 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 D 1 REMARK 465 GLU J 1 REMARK 465 ILE J 2 REMARK 465 SER J 3 REMARK 465 GLU J 4 REMARK 465 SER J 140 REMARK 465 LYS J 141 REMARK 465 SER J 142 REMARK 465 THR J 143 REMARK 465 SER J 144 REMARK 465 GLY J 145 REMARK 465 LYS J 226 REMARK 465 SER J 227 REMARK 465 CYS J 228 REMARK 465 ASP J 229 REMARK 465 LYS J 230 REMARK 465 THR J 231 REMARK 465 HIS J 232 REMARK 465 THR J 233 REMARK 465 ALA C -2 REMARK 465 ASP C -1 REMARK 465 LEU C 0 REMARK 465 VAL C 216 REMARK 465 SER C 217 REMARK 465 PRO C 218 REMARK 465 SER C 219 REMARK 465 GLY C 220 REMARK 465 SER C 221 REMARK 465 GLY C 222 REMARK 465 LEU C 223 REMARK 465 GLU C 224 REMARK 465 VAL C 225 REMARK 465 LEU C 226 REMARK 465 PHE C 227 REMARK 465 GLN C 228 REMARK 465 SER A 1 REMARK 465 GLU B 1 REMARK 465 ILE B 2 REMARK 465 SER B 3 REMARK 465 SER B 139 REMARK 465 SER B 140 REMARK 465 LYS B 141 REMARK 465 SER B 142 REMARK 465 THR B 143 REMARK 465 SER B 144 REMARK 465 GLY B 145 REMARK 465 LYS B 226 REMARK 465 SER B 227 REMARK 465 CYS B 228 REMARK 465 ASP B 229 REMARK 465 LYS B 230 REMARK 465 THR B 231 REMARK 465 HIS B 232 REMARK 465 THR B 233 REMARK 465 ALA E -2 REMARK 465 ASP E -1 REMARK 465 LEU E 0 REMARK 465 VAL E 216 REMARK 465 SER E 217 REMARK 465 PRO E 218 REMARK 465 SER E 219 REMARK 465 GLY E 220 REMARK 465 SER E 221 REMARK 465 GLY E 222 REMARK 465 LEU E 223 REMARK 465 GLU E 224 REMARK 465 VAL E 225 REMARK 465 LEU E 226 REMARK 465 PHE E 227 REMARK 465 GLN E 228 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 LYS D 43 CG CD CE NZ REMARK 470 LYS D 127 CG CD CE NZ REMARK 470 LYS D 189 CG CD CE NZ REMARK 470 LYS J 46 CG CD CE NZ REMARK 470 LYS J 213 CG CD CE NZ REMARK 470 LYS J 218 CG CD CE NZ REMARK 470 LYS C 29 CG CD CE NZ REMARK 470 GLU C 32 CG CD OE1 OE2 REMARK 470 LYS C 51 CG CD CE NZ REMARK 470 GLU C 62 CG CD OE1 OE2 REMARK 470 LYS C 73 CG CD CE NZ REMARK 470 ARG C 77 CG CD NE CZ NH1 NH2 REMARK 470 TYR C 154 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS C 184 CG CD CE NZ REMARK 470 LYS C 201 CG CD CE NZ REMARK 470 LYS A 43 CG CD CE NZ REMARK 470 LYS A 46 CG CD CE NZ REMARK 470 SER A 57 OG REMARK 470 LYS A 127 CG CD CE NZ REMARK 470 LYS A 146 CG CD CE NZ REMARK 470 SER A 157 OG REMARK 470 LYS A 170 CG CD CE NZ REMARK 470 LYS A 184 CG CD CE NZ REMARK 470 GLU A 188 CG CD OE1 OE2 REMARK 470 LYS B 46 CG CD CE NZ REMARK 470 GLN B 117 CG CD OE1 NE2 REMARK 470 LYS B 213 CG CD CE NZ REMARK 470 GLN E 1 CG CD OE1 NE2 REMARK 470 LYS E 29 CG CD CE NZ REMARK 470 GLN E 42 CG CD OE1 NE2 REMARK 470 GLU E 62 CG CD OE1 OE2 REMARK 470 LYS E 73 CG CD CE NZ REMARK 470 ARG E 140 CG CD NE CZ NH1 NH2 REMARK 470 LYS E 184 CG CD CE NZ REMARK 470 VAL E 186 CG1 CG2 REMARK 470 SER E 215 OG 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 GLU C 58 CG CD OE1 OE2 REMARK 480 ARG C 140 CD NE CZ NH1 NH2 REMARK 480 THR C 196 OG1 CG2 REMARK 480 LYS E 51 CD CE NZ REMARK 480 GLU E 58 CG CD OE1 OE2 REMARK 480 THR E 196 OG1 CG2 REMARK 480 LYS E 201 CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 CYS B 99 CB CYS B 99 SG -0.098 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 SER D 31 -129.97 52.29 REMARK 500 LEU D 48 -61.18 -102.89 REMARK 500 ALA D 52 -36.08 71.53 REMARK 500 SER D 53 -2.44 -141.37 REMARK 500 ALA D 85 -170.74 -172.06 REMARK 500 LYS D 191 -55.47 -123.78 REMARK 500 SER J 34 43.85 -109.61 REMARK 500 GLU C 28 93.56 71.11 REMARK 500 ARG C 40 -108.94 -124.72 REMARK 500 PRO C 144 -158.57 -79.61 REMARK 500 PRO C 214 -152.67 -61.60 REMARK 500 SER A 31 -131.19 53.28 REMARK 500 LEU A 48 -60.74 -102.99 REMARK 500 ALA A 52 -34.92 69.67 REMARK 500 ALA A 85 -169.07 -171.60 REMARK 500 ASN A 139 70.29 47.39 REMARK 500 LYS A 191 -52.80 -125.63 REMARK 500 VAL B 5 106.43 43.39 REMARK 500 SER B 34 48.74 -109.49 REMARK 500 VAL B 51 -60.40 -102.72 REMARK 500 PRO B 161 97.85 -65.89 REMARK 500 SER E 26 -71.21 -58.44 REMARK 500 GLU E 28 100.55 -45.57 REMARK 500 ARG E 40 -107.27 -122.12 REMARK 500 ASP E 130 -131.16 57.65 REMARK 500 PRO E 144 -155.68 -78.55 REMARK 500 LYS E 184 0.50 -67.16 REMARK 500 ARG E 187 -37.69 81.75 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 ARG C 54 0.13 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 8VC7 D 1 215 PDB 8VC7 8VC7 1 215 DBREF 8VC7 J 1 233 PDB 8VC7 8VC7 1 233 DBREF 8VC7 C 1 219 UNP Q7KYR7 BT2A1_HUMAN 29 247 DBREF 8VC7 A 1 215 PDB 8VC7 8VC7 1 215 DBREF 8VC7 B 1 233 PDB 8VC7 8VC7 1 233 DBREF 8VC7 E 1 219 UNP Q7KYR7 BT2A1_HUMAN 29 247 SEQADV 8VC7 ALA C -2 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 ASP C -1 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 LEU C 0 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 SER C 219 UNP Q7KYR7 CYS 247 ENGINEERED MUTATION SEQADV 8VC7 GLY C 220 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 SER C 221 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 GLY C 222 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 LEU C 223 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 GLU C 224 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 VAL C 225 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 LEU C 226 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 PHE C 227 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 GLN C 228 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 ALA E -2 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 ASP E -1 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 LEU E 0 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 SER E 219 UNP Q7KYR7 CYS 247 ENGINEERED MUTATION SEQADV 8VC7 GLY E 220 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 SER E 221 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 GLY E 222 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 LEU E 223 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 GLU E 224 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 VAL E 225 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 LEU E 226 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 PHE E 227 UNP Q7KYR7 EXPRESSION TAG SEQADV 8VC7 GLN E 228 UNP Q7KYR7 EXPRESSION TAG SEQRES 1 D 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 D 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 D 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 D 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 D 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 D 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 D 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 D 215 SER SER SER SER LEU ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 D 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 D 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 D 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 D 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 D 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 D 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 D 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 D 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 J 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 J 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 J 233 ALA SER GLY PHE ASN LEU TYR SER SER SER ILE HIS TRP SEQRES 4 J 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 J 233 TYR ILE TYR PRO SER SER GLY TYR THR SER TYR ALA ASP SEQRES 6 J 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 J 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 J 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR SEQRES 9 J 233 THR ARG GLY TYR PRO ASP GLY MET ASP TYR TRP GLY GLN SEQRES 10 J 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 J 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 J 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 J 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 J 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 J 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 J 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 J 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 J 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 C 231 ALA ASP LEU GLN PHE ILE VAL VAL GLY PRO THR ASP PRO SEQRES 2 C 231 ILE LEU ALA THR VAL GLY GLU ASN THR THR LEU ARG CYS SEQRES 3 C 231 HIS LEU SER PRO GLU LYS ASN ALA GLU ASP MET GLU VAL SEQRES 4 C 231 ARG TRP PHE ARG SER GLN PHE SER PRO ALA VAL PHE VAL SEQRES 5 C 231 TYR LYS GLY GLY ARG GLU ARG THR GLU GLU GLN MET GLU SEQRES 6 C 231 GLU TYR ARG GLY ARG THR THR PHE VAL SER LYS ASP ILE SEQRES 7 C 231 SER ARG GLY SER VAL ALA LEU VAL ILE HIS ASN ILE THR SEQRES 8 C 231 ALA GLN GLU ASN GLY THR TYR ARG CYS TYR PHE GLN GLU SEQRES 9 C 231 GLY ARG SER TYR ASP GLU ALA ILE LEU HIS LEU VAL VAL SEQRES 10 C 231 ALA GLY LEU GLY SER LYS PRO LEU ILE SER MET ARG GLY SEQRES 11 C 231 HIS GLU ASP GLY GLY ILE ARG LEU GLU CYS ILE SER ARG SEQRES 12 C 231 GLY TRP TYR PRO LYS PRO LEU THR VAL TRP ARG ASP PRO SEQRES 13 C 231 TYR GLY GLY VAL ALA PRO ALA LEU LYS GLU VAL SER MET SEQRES 14 C 231 PRO ASP ALA ASP GLY LEU PHE MET VAL THR THR ALA VAL SEQRES 15 C 231 ILE ILE ARG ASP LYS SER VAL ARG ASN MET SER CYS SER SEQRES 16 C 231 ILE ASN ASN THR LEU LEU GLY GLN LYS LYS GLU SER VAL SEQRES 17 C 231 ILE PHE ILE PRO GLU SER PHE MET PRO SER VAL SER PRO SEQRES 18 C 231 SER GLY SER GLY LEU GLU VAL LEU PHE GLN SEQRES 1 A 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 A 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 A 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 A 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 A 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 A 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 A 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 A 215 SER SER SER SER LEU ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 A 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 A 215 ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER GLY THR SEQRES 11 A 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 A 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 A 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 A 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 A 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 A 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 A 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 B 233 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 B 233 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 B 233 ALA SER GLY PHE ASN LEU TYR SER SER SER ILE HIS TRP SEQRES 4 B 233 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 B 233 TYR ILE TYR PRO SER SER GLY TYR THR SER TYR ALA ASP SEQRES 6 B 233 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 B 233 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 B 233 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG TYR TYR TYR SEQRES 9 B 233 THR ARG GLY TYR PRO ASP GLY MET ASP TYR TRP GLY GLN SEQRES 10 B 233 GLY THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 B 233 PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SEQRES 12 B 233 SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 B 233 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 B 233 ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 B 233 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 B 233 VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS SEQRES 17 B 233 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 B 233 LYS VAL GLU PRO LYS SER CYS ASP LYS THR HIS THR SEQRES 1 E 231 ALA ASP LEU GLN PHE ILE VAL VAL GLY PRO THR ASP PRO SEQRES 2 E 231 ILE LEU ALA THR VAL GLY GLU ASN THR THR LEU ARG CYS SEQRES 3 E 231 HIS LEU SER PRO GLU LYS ASN ALA GLU ASP MET GLU VAL SEQRES 4 E 231 ARG TRP PHE ARG SER GLN PHE SER PRO ALA VAL PHE VAL SEQRES 5 E 231 TYR LYS GLY GLY ARG GLU ARG THR GLU GLU GLN MET GLU SEQRES 6 E 231 GLU TYR ARG GLY ARG THR THR PHE VAL SER LYS ASP ILE SEQRES 7 E 231 SER ARG GLY SER VAL ALA LEU VAL ILE HIS ASN ILE THR SEQRES 8 E 231 ALA GLN GLU ASN GLY THR TYR ARG CYS TYR PHE GLN GLU SEQRES 9 E 231 GLY ARG SER TYR ASP GLU ALA ILE LEU HIS LEU VAL VAL SEQRES 10 E 231 ALA GLY LEU GLY SER LYS PRO LEU ILE SER MET ARG GLY SEQRES 11 E 231 HIS GLU ASP GLY GLY ILE ARG LEU GLU CYS ILE SER ARG SEQRES 12 E 231 GLY TRP TYR PRO LYS PRO LEU THR VAL TRP ARG ASP PRO SEQRES 13 E 231 TYR GLY GLY VAL ALA PRO ALA LEU LYS GLU VAL SER MET SEQRES 14 E 231 PRO ASP ALA ASP GLY LEU PHE MET VAL THR THR ALA VAL SEQRES 15 E 231 ILE ILE ARG ASP LYS SER VAL ARG ASN MET SER CYS SER SEQRES 16 E 231 ILE ASN ASN THR LEU LEU GLY GLN LYS LYS GLU SER VAL SEQRES 17 E 231 ILE PHE ILE PRO GLU SER PHE MET PRO SER VAL SER PRO SEQRES 18 E 231 SER GLY SER GLY LEU GLU VAL LEU PHE GLN HET NAG C 301 14 HET NAG C 302 14 HET NAG C 303 14 HET NAG E 301 14 HET NAG E 302 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE FORMUL 7 NAG 5(C8 H15 N O6) HELIX 1 AA1 GLN D 80 PHE D 84 5 5 HELIX 2 AA2 SER D 122 SER D 128 1 7 HELIX 3 AA3 LYS D 184 LYS D 189 1 6 HELIX 4 AA4 ASN J 31 TYR J 33 5 3 HELIX 5 AA5 ARG J 90 THR J 94 5 5 HELIX 6 AA6 SER J 168 ALA J 170 5 3 HELIX 7 AA7 SER J 199 GLY J 202 5 4 HELIX 8 AA8 LYS J 213 ASN J 216 5 4 HELIX 9 AA9 THR C 57 GLN C 60 5 4 HELIX 10 AB1 MET C 61 ARG C 65 5 5 HELIX 11 AB2 ASP C 74 ARG C 77 5 4 HELIX 12 AB3 THR C 88 ASN C 92 5 5 HELIX 13 AB4 PRO C 209 MET C 213 5 5 HELIX 14 AB5 GLN A 80 PHE A 84 5 5 HELIX 15 AB6 SER A 122 LYS A 127 1 6 HELIX 16 AB7 LYS A 184 LYS A 189 1 6 HELIX 17 AB8 ASN B 31 TYR B 33 5 3 HELIX 18 AB9 ARG B 90 THR B 94 5 5 HELIX 19 AC1 SER B 168 ALA B 170 5 3 HELIX 20 AC2 SER B 199 GLY B 202 5 4 HELIX 21 AC3 LYS B 213 ASN B 216 5 4 HELIX 22 AC4 THR E 57 GLN E 60 5 4 HELIX 23 AC5 MET E 61 ARG E 65 5 5 HELIX 24 AC6 ILE E 75 ARG E 77 5 3 HELIX 25 AC7 THR E 88 ASN E 92 5 5 HELIX 26 AC8 PRO E 209 MET E 213 5 5 SHEET 1 AA1 4 MET D 5 SER D 8 0 SHEET 2 AA1 4 VAL D 20 ALA D 26 -1 O ARG D 25 N THR D 6 SHEET 3 AA1 4 ASP D 71 ILE D 76 -1 O ILE D 76 N VAL D 20 SHEET 4 AA1 4 PHE D 63 SER D 68 -1 N SER D 64 O THR D 75 SHEET 1 AA2 6 SER D 11 ALA D 14 0 SHEET 2 AA2 6 THR D 103 ILE D 107 1 O GLU D 106 N ALA D 14 SHEET 3 AA2 6 THR D 86 GLN D 91 -1 N TYR D 87 O THR D 103 SHEET 4 AA2 6 VAL D 34 GLN D 39 -1 N GLN D 39 O THR D 86 SHEET 5 AA2 6 LYS D 46 TYR D 50 -1 O LEU D 48 N TRP D 36 SHEET 6 AA2 6 SER D 54 LEU D 55 -1 O SER D 54 N TYR D 50 SHEET 1 AA3 4 SER D 11 ALA D 14 0 SHEET 2 AA3 4 THR D 103 ILE D 107 1 O GLU D 106 N ALA D 14 SHEET 3 AA3 4 THR D 86 GLN D 91 -1 N TYR D 87 O THR D 103 SHEET 4 AA3 4 THR D 98 PHE D 99 -1 O THR D 98 N GLN D 91 SHEET 1 AA4 4 SER D 115 PHE D 119 0 SHEET 2 AA4 4 THR D 130 PHE D 140 -1 O ASN D 138 N SER D 115 SHEET 3 AA4 4 TYR D 174 SER D 183 -1 O TYR D 174 N PHE D 140 SHEET 4 AA4 4 SER D 160 VAL D 164 -1 N GLN D 161 O THR D 179 SHEET 1 AA5 4 ALA D 154 LEU D 155 0 SHEET 2 AA5 4 ALA D 145 VAL D 151 -1 N VAL D 151 O ALA D 154 SHEET 3 AA5 4 VAL D 192 HIS D 199 -1 O ALA D 194 N LYS D 150 SHEET 4 AA5 4 VAL D 206 ASN D 211 -1 O VAL D 206 N VAL D 197 SHEET 1 AA6 4 GLN J 6 SER J 10 0 SHEET 2 AA6 4 LEU J 21 SER J 28 -1 O SER J 24 N SER J 10 SHEET 3 AA6 4 THR J 81 MET J 86 -1 O MET J 86 N LEU J 21 SHEET 4 AA6 4 PHE J 71 ASP J 76 -1 N ASP J 76 O THR J 81 SHEET 1 AA7 6 LEU J 14 VAL J 15 0 SHEET 2 AA7 6 THR J 119 VAL J 123 1 O THR J 122 N VAL J 15 SHEET 3 AA7 6 ALA J 95 TYR J 103 -1 N TYR J 97 O THR J 119 SHEET 4 AA7 6 SER J 35 GLN J 42 -1 N VAL J 40 O TYR J 98 SHEET 5 AA7 6 LEU J 48 ILE J 54 -1 O VAL J 51 N TRP J 39 SHEET 6 AA7 6 THR J 61 TYR J 63 -1 O SER J 62 N TYR J 53 SHEET 1 AA8 4 LEU J 14 VAL J 15 0 SHEET 2 AA8 4 THR J 119 VAL J 123 1 O THR J 122 N VAL J 15 SHEET 3 AA8 4 ALA J 95 TYR J 103 -1 N TYR J 97 O THR J 119 SHEET 4 AA8 4 TYR J 114 TRP J 115 -1 O TYR J 114 N ARG J 101 SHEET 1 AA9 4 SER J 132 LEU J 136 0 SHEET 2 AA9 4 THR J 147 TYR J 157 -1 O LYS J 155 N SER J 132 SHEET 3 AA9 4 TYR J 188 PRO J 197 -1 O TYR J 188 N TYR J 157 SHEET 4 AA9 4 VAL J 175 THR J 177 -1 N HIS J 176 O VAL J 193 SHEET 1 AB1 4 SER J 132 LEU J 136 0 SHEET 2 AB1 4 THR J 147 TYR J 157 -1 O LYS J 155 N SER J 132 SHEET 3 AB1 4 TYR J 188 PRO J 197 -1 O TYR J 188 N TYR J 157 SHEET 4 AB1 4 VAL J 181 LEU J 182 -1 N VAL J 181 O SER J 189 SHEET 1 AB2 3 THR J 163 TRP J 166 0 SHEET 2 AB2 3 ILE J 207 HIS J 212 -1 O ASN J 209 N SER J 165 SHEET 3 AB2 3 THR J 217 LYS J 222 -1 O THR J 217 N HIS J 212 SHEET 1 AB3 4 VAL C 4 VAL C 5 0 SHEET 2 AB3 4 THR C 19 LEU C 25 -1 O HIS C 24 N VAL C 5 SHEET 3 AB3 4 SER C 79 ILE C 84 -1 O LEU C 82 N LEU C 21 SHEET 4 AB3 4 THR C 68 VAL C 71 -1 N THR C 69 O VAL C 83 SHEET 1 AB4 6 ILE C 11 THR C 14 0 SHEET 2 AB4 6 SER C 104 ALA C 115 1 O VAL C 113 N ILE C 11 SHEET 3 AB4 6 GLY C 93 GLU C 101 -1 N GLY C 93 O LEU C 112 SHEET 4 AB4 6 GLU C 35 PHE C 39 -1 N ARG C 37 O TYR C 98 SHEET 5 AB4 6 PHE C 48 LYS C 51 -1 O TYR C 50 N VAL C 36 SHEET 6 AB4 6 ARG C 54 GLU C 55 -1 O ARG C 54 N LYS C 51 SHEET 1 AB5 4 LEU C 122 GLU C 129 0 SHEET 2 AB5 4 GLY C 132 TRP C 142 -1 O ARG C 134 N GLY C 127 SHEET 3 AB5 4 PHE C 173 ILE C 181 -1 O VAL C 179 N LEU C 135 SHEET 4 AB5 4 LYS C 162 PRO C 167 -1 N MET C 166 O MET C 174 SHEET 1 AB6 4 VAL C 157 ALA C 158 0 SHEET 2 AB6 4 LEU C 147 ARG C 151 -1 N TRP C 150 O ALA C 158 SHEET 3 AB6 4 ASN C 188 ASN C 195 -1 O SER C 190 N ARG C 151 SHEET 4 AB6 4 GLN C 200 PHE C 207 -1 O GLN C 200 N ASN C 195 SHEET 1 AB7 4 MET A 5 SER A 8 0 SHEET 2 AB7 4 VAL A 20 ALA A 26 -1 O ARG A 25 N THR A 6 SHEET 3 AB7 4 ASP A 71 ILE A 76 -1 O ILE A 76 N VAL A 20 SHEET 4 AB7 4 PHE A 63 SER A 68 -1 N SER A 64 O THR A 75 SHEET 1 AB8 6 SER A 11 ALA A 14 0 SHEET 2 AB8 6 THR A 103 ILE A 107 1 O GLU A 106 N LEU A 12 SHEET 3 AB8 6 THR A 86 GLN A 91 -1 N TYR A 87 O THR A 103 SHEET 4 AB8 6 VAL A 34 GLN A 39 -1 N GLN A 39 O THR A 86 SHEET 5 AB8 6 LYS A 46 TYR A 50 -1 O LEU A 48 N TRP A 36 SHEET 6 AB8 6 SER A 54 LEU A 55 -1 O SER A 54 N TYR A 50 SHEET 1 AB9 4 SER A 11 ALA A 14 0 SHEET 2 AB9 4 THR A 103 ILE A 107 1 O GLU A 106 N LEU A 12 SHEET 3 AB9 4 THR A 86 GLN A 91 -1 N TYR A 87 O THR A 103 SHEET 4 AB9 4 THR A 98 PHE A 99 -1 O THR A 98 N GLN A 91 SHEET 1 AC1 4 SER A 115 PHE A 119 0 SHEET 2 AC1 4 THR A 130 PHE A 140 -1 O ASN A 138 N SER A 115 SHEET 3 AC1 4 TYR A 174 SER A 183 -1 O SER A 178 N CYS A 135 SHEET 4 AC1 4 SER A 160 VAL A 164 -1 N GLN A 161 O THR A 179 SHEET 1 AC2 3 ALA A 145 VAL A 151 0 SHEET 2 AC2 3 VAL A 192 HIS A 199 -1 O GLU A 196 N GLN A 148 SHEET 3 AC2 3 VAL A 206 ASN A 211 -1 O VAL A 206 N VAL A 197 SHEET 1 AC3 4 GLN B 6 SER B 10 0 SHEET 2 AC3 4 LEU B 21 SER B 28 -1 O ALA B 26 N VAL B 8 SHEET 3 AC3 4 THR B 81 MET B 86 -1 O LEU B 84 N LEU B 23 SHEET 4 AC3 4 PHE B 71 ASP B 76 -1 N SER B 74 O TYR B 83 SHEET 1 AC4 6 LEU B 14 VAL B 15 0 SHEET 2 AC4 6 THR B 119 VAL B 123 1 O THR B 122 N VAL B 15 SHEET 3 AC4 6 ALA B 95 TYR B 103 -1 N TYR B 97 O THR B 119 SHEET 4 AC4 6 SER B 35 GLN B 42 -1 N VAL B 40 O TYR B 98 SHEET 5 AC4 6 GLU B 49 ILE B 54 -1 O GLU B 49 N ARG B 41 SHEET 6 AC4 6 THR B 61 TYR B 63 -1 O SER B 62 N TYR B 53 SHEET 1 AC5 4 LEU B 14 VAL B 15 0 SHEET 2 AC5 4 THR B 119 VAL B 123 1 O THR B 122 N VAL B 15 SHEET 3 AC5 4 ALA B 95 TYR B 103 -1 N TYR B 97 O THR B 119 SHEET 4 AC5 4 TYR B 114 TRP B 115 -1 O TYR B 114 N ARG B 101 SHEET 1 AC6 4 SER B 132 LEU B 136 0 SHEET 2 AC6 4 THR B 147 TYR B 157 -1 O LYS B 155 N SER B 132 SHEET 3 AC6 4 TYR B 188 PRO B 197 -1 O TYR B 188 N TYR B 157 SHEET 4 AC6 4 VAL B 175 THR B 177 -1 N HIS B 176 O VAL B 193 SHEET 1 AC7 4 SER B 132 LEU B 136 0 SHEET 2 AC7 4 THR B 147 TYR B 157 -1 O LYS B 155 N SER B 132 SHEET 3 AC7 4 TYR B 188 PRO B 197 -1 O TYR B 188 N TYR B 157 SHEET 4 AC7 4 VAL B 181 LEU B 182 -1 N VAL B 181 O SER B 189 SHEET 1 AC8 3 THR B 163 TRP B 166 0 SHEET 2 AC8 3 TYR B 206 HIS B 212 -1 O ASN B 209 N SER B 165 SHEET 3 AC8 3 THR B 217 VAL B 223 -1 O THR B 217 N HIS B 212 SHEET 1 AC9 4 VAL E 4 VAL E 5 0 SHEET 2 AC9 4 THR E 19 LEU E 25 -1 O HIS E 24 N VAL E 5 SHEET 3 AC9 4 SER E 79 ILE E 84 -1 O LEU E 82 N LEU E 21 SHEET 4 AC9 4 THR E 68 ASP E 74 -1 N VAL E 71 O ALA E 81 SHEET 1 AD1 6 ILE E 11 THR E 14 0 SHEET 2 AD1 6 SER E 104 ALA E 115 1 O VAL E 113 N ILE E 11 SHEET 3 AD1 6 GLY E 93 GLU E 101 -1 N PHE E 99 O ASP E 106 SHEET 4 AD1 6 GLU E 35 PHE E 39 -1 N ARG E 37 O TYR E 98 SHEET 5 AD1 6 PHE E 48 LYS E 51 -1 O TYR E 50 N VAL E 36 SHEET 6 AD1 6 ARG E 54 GLU E 55 -1 O ARG E 54 N LYS E 51 SHEET 1 AD2 4 LEU E 122 GLU E 129 0 SHEET 2 AD2 4 GLY E 132 TRP E 142 -1 O ARG E 134 N GLY E 127 SHEET 3 AD2 4 PHE E 173 ILE E 181 -1 O PHE E 173 N TRP E 142 SHEET 4 AD2 4 LYS E 162 PRO E 167 -1 N MET E 166 O MET E 174 SHEET 1 AD3 4 VAL E 157 ALA E 158 0 SHEET 2 AD3 4 LEU E 147 ARG E 151 -1 N TRP E 150 O ALA E 158 SHEET 3 AD3 4 ASN E 188 ASN E 195 -1 O ASN E 194 N LEU E 147 SHEET 4 AD3 4 GLN E 200 PHE E 207 -1 O GLN E 200 N ASN E 195 SSBOND 1 CYS D 24 CYS D 89 1555 1555 2.06 SSBOND 2 CYS D 135 CYS D 195 1555 1555 2.04 SSBOND 3 CYS J 25 CYS J 99 1555 1555 2.06 SSBOND 4 CYS J 152 CYS J 208 1555 1555 2.04 SSBOND 5 CYS C 23 CYS C 97 1555 1555 2.06 SSBOND 6 CYS C 137 CYS C 191 1555 1555 2.07 SSBOND 7 CYS A 24 CYS A 89 1555 1555 2.07 SSBOND 8 CYS A 135 CYS A 195 1555 1555 2.02 SSBOND 9 CYS B 25 CYS B 99 1555 1555 2.06 SSBOND 10 CYS B 152 CYS B 208 1555 1555 2.04 SSBOND 11 CYS E 23 CYS E 97 1555 1555 2.04 SSBOND 12 CYS E 137 CYS E 191 1555 1555 2.07 LINK ND2 ASN C 18 C1 NAG C 301 1555 1555 1.44 LINK ND2 ASN C 86 C1 NAG C 302 1555 1555 1.47 LINK ND2 ASN C 92 C1 NAG C 303 1555 1555 1.44 LINK ND2 ASN E 18 C1 NAG E 301 1555 1555 1.47 LINK ND2 ASN E 92 C1 NAG E 302 1555 1555 1.44 CISPEP 1 SER D 8 PRO D 9 0 1.22 CISPEP 2 TYR D 141 PRO D 142 0 6.29 CISPEP 3 PHE J 158 PRO J 159 0 3.33 CISPEP 4 GLU J 160 PRO J 161 0 -14.87 CISPEP 5 SER C 44 PRO C 45 0 6.00 CISPEP 6 TYR C 143 PRO C 144 0 -3.22 CISPEP 7 SER A 8 PRO A 9 0 -0.61 CISPEP 8 TYR A 141 PRO A 142 0 6.73 CISPEP 9 PHE B 158 PRO B 159 0 6.29 CISPEP 10 SER E 44 PRO E 45 0 5.94 CISPEP 11 TYR E 143 PRO E 144 0 -3.38 CRYST1 44.915 200.976 206.684 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.022264 0.000000 0.000000 0.00000 SCALE2 0.000000 0.004976 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004838 0.00000