HEADER IMMUNE SYSTEM 22-DEC-16 5UCB TITLE STRUCTURE OF ANTIGEN-FAB COMPLEX WITH ENGINEERED SWITCH RESIDUE TITLE 2 REGION. COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HISTONE CHAPERONE ASF1; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: ANTI-SILENCING FUNCTION PROTEIN 1,YASF1; COMPND 13 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: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 / SOURCE 13 S288C); SOURCE 14 ORGANISM_COMMON: BAKER'S YEAST; SOURCE 15 ORGANISM_TAXID: 559292; SOURCE 16 STRAIN: ATCC 204508 / S288C; SOURCE 17 GENE: ASF1, CIA1, YJL115W, J0755; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, FAB, ASF1, HISTONE CHAPERONE, STRUCTURAL GENOMICS, PSI- KEYWDS 2 BIOLOGY, CHAPERONE-ENABLED STUDIES OF EPIGENETIC REGULATION ENZYMES, KEYWDS 3 CEBS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR L.J.BAILEY,A.A.KOSSIAKOFF,CHAPERONE-ENABLED STUDIES OF EPIGENETIC AUTHOR 2 REGULATION ENZYMES (CEBS) REVDAT 1 27-DEC-17 5UCB 0 JRNL AUTH L.J.BAILEY,A.A.KOSSIAKOFF JRNL TITL ANTIBODY SWITCH RESIDUE ENGINEERING FOR IMPROVED JRNL TITL 2 CRYSTALLIZATION CHAPERONES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.52 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???) 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) : 1.52 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.59 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 3 NUMBER OF REFLECTIONS : 100518 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.140 REMARK 3 R VALUE (WORKING SET) : 0.138 REMARK 3 FREE R VALUE : 0.169 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 5020 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 35.5990 - 4.7240 0.90 2981 177 0.1681 0.1881 REMARK 3 2 4.7240 - 3.7509 0.96 3241 141 0.1253 0.1491 REMARK 3 3 3.7509 - 3.2771 0.98 3231 177 0.1364 0.1658 REMARK 3 4 3.2771 - 2.9777 0.98 3294 187 0.1425 0.1506 REMARK 3 5 2.9777 - 2.7643 0.98 3237 195 0.1467 0.1673 REMARK 3 6 2.7643 - 2.6014 0.98 3249 174 0.1485 0.2027 REMARK 3 7 2.6014 - 2.4712 0.98 3279 162 0.1471 0.1826 REMARK 3 8 2.4712 - 2.3636 0.98 3216 155 0.1384 0.1865 REMARK 3 9 2.3636 - 2.2726 0.97 3251 157 0.1394 0.1676 REMARK 3 10 2.2726 - 2.1942 0.98 3295 159 0.1264 0.1450 REMARK 3 11 2.1942 - 2.1256 0.97 3167 190 0.1298 0.1586 REMARK 3 12 2.1256 - 2.0649 0.97 3185 172 0.1312 0.1796 REMARK 3 13 2.0649 - 2.0105 0.97 3273 152 0.1302 0.1518 REMARK 3 14 2.0105 - 1.9615 0.97 3150 180 0.1285 0.1743 REMARK 3 15 1.9615 - 1.9169 0.96 3282 163 0.1274 0.1726 REMARK 3 16 1.9169 - 1.8761 0.96 3161 171 0.1267 0.1465 REMARK 3 17 1.8761 - 1.8386 0.96 3178 146 0.1244 0.1771 REMARK 3 18 1.8386 - 1.8039 0.96 3229 162 0.1261 0.1714 REMARK 3 19 1.8039 - 1.7717 0.96 3177 177 0.1194 0.1623 REMARK 3 20 1.7717 - 1.7416 0.95 3147 160 0.1220 0.1634 REMARK 3 21 1.7416 - 1.7135 0.95 3238 169 0.1162 0.1787 REMARK 3 22 1.7135 - 1.6872 0.95 3089 162 0.1091 0.1652 REMARK 3 23 1.6872 - 1.6624 0.95 3185 170 0.1152 0.1602 REMARK 3 24 1.6624 - 1.6389 0.96 3163 169 0.1207 0.1632 REMARK 3 25 1.6389 - 1.6168 0.94 3139 172 0.1242 0.1723 REMARK 3 26 1.6168 - 1.5958 0.95 3159 169 0.1291 0.1959 REMARK 3 27 1.5958 - 1.5758 0.95 3093 160 0.1252 0.1911 REMARK 3 28 1.5758 - 1.5569 0.94 3152 166 0.1317 0.1784 REMARK 3 29 1.5569 - 1.5388 0.94 3093 186 0.1412 0.1904 REMARK 3 30 1.5388 - 1.5215 0.87 2964 140 0.1470 0.2078 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) : 0.130 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.700 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 26.76 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 4568 REMARK 3 ANGLE : 0.950 6228 REMARK 3 CHIRALITY : 0.064 704 REMARK 3 PLANARITY : 0.006 794 REMARK 3 DIHEDRAL : 10.174 2724 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 5UCB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-17. REMARK 100 THE DEPOSITION ID IS D_1000225635. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUN-15 REMARK 200 TEMPERATURE (KELVIN) : 193 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 21-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 100518 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.521 REMARK 200 RESOLUTION RANGE LOW (A) : 35.589 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 32.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL 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: NULL REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG3350,, VAPOR DIFFUSION, HANGING REMARK 280 DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 25030 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU H 85 CG CD OE1 OE2 REMARK 470 GLN L 27 CG CD OE1 NE2 REMARK 470 GLU B 120 CG CD OE1 OE2 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 HG CYS H 22 HG CYS H 92 0.56 REMARK 500 HG CYS H 22 SG CYS H 92 0.99 REMARK 500 SG CYS H 22 HG CYS H 92 1.13 REMARK 500 HE21 GLN L 79 O HOH L 304 1.52 REMARK 500 O HOH B 238 O HOH B 351 1.97 REMARK 500 O HOH H 407 O HOH L 372 2.00 REMARK 500 O HOH B 203 O HOH B 363 2.01 REMARK 500 O HOH H 305 O HOH H 498 2.08 REMARK 500 O HOH L 304 O HOH L 309 2.11 REMARK 500 O HOH B 388 O HOH B 394 2.12 REMARK 500 O HOH H 485 O HOH H 520 2.15 REMARK 500 O HOH L 330 O HOH L 377 2.17 REMARK 500 OE1 GLU L 187 O HOH L 301 2.17 REMARK 500 O SER L 7 O HOH L 302 2.19 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 H 312 O HOH B 236 1565 2.03 REMARK 500 O HOH H 491 O HOH L 350 1565 2.07 REMARK 500 O HOH L 401 O HOH B 356 1554 2.09 REMARK 500 O HOH H 498 O HOH L 476 1565 2.16 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 TYR H 53 -46.45 74.13 REMARK 500 ALA H 88 164.85 178.60 REMARK 500 THR H 191 -62.18 -120.78 REMARK 500 ALA L 51 -40.57 71.79 REMARK 500 ARG L 211 -175.87 146.30 REMARK 500 TRP B 152 -108.49 -99.63 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASN L 210 ARG L 211 147.70 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 H 549 DISTANCE = 5.83 ANGSTROMS REMARK 525 HOH B 397 DISTANCE = 5.85 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5UEK RELATED DB: PDB REMARK 900 RELATED ID: 5UEA RELATED DB: PDB DBREF 5UCB H 1 214 PDB 5UCB 5UCB 1 214 DBREF 5UCB L 3 212 PDB 5UCB 5UCB 3 212 DBREF 5UCB B 1 153 UNP P32447 ASF1_YEAST 2 154 SEQRES 1 H 217 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 H 217 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 217 PHE ASN VAL SER TYR TYR SER ILE HIS TRP VAL ARG GLN SEQRES 4 H 217 ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SER ILE TYR SEQRES 5 H 217 PRO TYR TYR GLY SER THR SER TYR ALA ASP SER VAL LYS SEQRES 6 H 217 GLY ARG PHE THR ILE SER ALA ASP THR SER LYS ASN THR SEQRES 7 H 217 ALA TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 217 ALA VAL TYR TYR CYS ALA ARG GLY TYR GLY TRP ALA LEU SEQRES 9 H 217 ASP TYR TRP GLY GLN GLY THR LEU VAL THR VAL PHE ASN SEQRES 10 H 217 GLN ILE LYS PRO PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 11 H 217 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 12 H 217 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 13 H 217 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 14 H 217 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 15 H 217 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 16 H 217 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 17 H 217 LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 1 L 210 GLN MET THR GLN SER PRO SER SER LEU SER ALA SER VAL SEQRES 2 L 210 GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER GLN SER SEQRES 3 L 210 VAL SER SER ALA VAL ALA TRP TYR GLN GLN LYS PRO GLY SEQRES 4 L 210 LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER SER LEU SEQRES 5 L 210 TYR SER GLY VAL PRO SER ARG PHE SER GLY SER ARG SER SEQRES 6 L 210 GLY THR ASP TYR THR LEU THR ILE SER SER LEU GLN PRO SEQRES 7 L 210 GLU ASP PHE ALA THR TYR TYR CYS GLN GLN ASP GLY TRP SEQRES 8 L 210 SER LEU ILE THR PHE GLY GLN GLY THR LYS VAL GLU ILE SEQRES 9 L 210 LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE PRO SEQRES 10 L 210 PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER VAL SEQRES 11 L 210 VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS SEQRES 12 L 210 VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SEQRES 13 L 210 SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SER SEQRES 14 L 210 THR TYR SER LEU SER SER THR LEU THR LEU SER LYS ALA SEQRES 15 L 210 ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL THR SEQRES 16 L 210 HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE ASN SEQRES 17 L 210 ARG GLY SEQRES 1 B 153 SER ILE VAL SER LEU LEU GLY ILE LYS VAL LEU ASN ASN SEQRES 2 B 153 PRO ALA LYS PHE THR ASP PRO TYR GLU PHE GLU ILE THR SEQRES 3 B 153 PHE GLU CYS LEU GLU SER LEU LYS HIS ASP LEU GLU TRP SEQRES 4 B 153 LYS LEU THR TYR VAL GLY SER SER ARG SER LEU ASP HIS SEQRES 5 B 153 ASP GLN GLU LEU ASP SER ILE LEU VAL GLY PRO VAL PRO SEQRES 6 B 153 VAL GLY VAL ASN LYS PHE VAL PHE SER ALA ASP PRO PRO SEQRES 7 B 153 SER ALA GLU LEU ILE PRO ALA SER GLU LEU VAL SER VAL SEQRES 8 B 153 THR VAL ILE LEU LEU SER CYS SER TYR ASP GLY ARG GLU SEQRES 9 B 153 PHE VAL ARG VAL GLY TYR TYR VAL ASN ASN GLU TYR ASP SEQRES 10 B 153 GLU GLU GLU LEU ARG GLU ASN PRO PRO ALA LYS VAL GLN SEQRES 11 B 153 VAL ASP HIS ILE VAL ARG ASN ILE LEU ALA GLU LYS PRO SEQRES 12 B 153 ARG VAL THR ARG PHE ASN ILE VAL TRP ASP FORMUL 4 HOH *641(H2 O) HELIX 1 AA1 ASN H 28 TYR H 32 5 5 HELIX 2 AA2 ARG H 83 THR H 87 5 5 HELIX 3 AA3 SER H 156 ALA H 158 5 3 HELIX 4 AA4 SER H 187 LEU H 189 5 3 HELIX 5 AA5 LYS H 201 ASN H 204 5 4 HELIX 6 AA6 VAL L 29 SER L 31 5 3 HELIX 7 AA7 GLN L 79 PHE L 83 5 5 HELIX 8 AA8 SER L 121 SER L 127 1 7 HELIX 9 AA9 LYS L 183 LYS L 188 1 6 HELIX 10 AB1 SER B 79 ILE B 83 5 5 HELIX 11 AB2 PRO B 84 VAL B 89 1 6 HELIX 12 AB3 GLU B 118 ASN B 124 1 7 HELIX 13 AB4 GLN B 130 ASP B 132 5 3 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AA1 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 TYR H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA2 6 ILE H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O SER H 58 N SER H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 TYR H 96 -1 N TYR H 90 O THR H 107 SHEET 4 AA3 4 ALA H 99 TRP H 103 -1 O ALA H 99 N TYR H 96 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 ASP L 70 ILE L 75 -1 O TYR L 71 N CYS L 23 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 SER L 10 ALA L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA8 6 THR L 85 ASP L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 VAL L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 ALA L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AA9 4 THR L 85 ASP L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 ILE L 96 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O ASN L 137 N SER L 114 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SHEET 1 AB3 3 VAL B 3 VAL B 10 0 SHEET 2 AB3 3 TYR B 21 CYS B 29 -1 O GLU B 24 N LYS B 9 SHEET 3 AB3 3 GLY B 67 ALA B 75 -1 O GLY B 67 N CYS B 29 SHEET 1 AB4 6 ALA B 15 LYS B 16 0 SHEET 2 AB4 6 ILE B 134 ILE B 138 -1 O ARG B 136 N ALA B 15 SHEET 3 AB4 6 ARG B 103 TYR B 116 -1 N GLU B 115 O VAL B 135 SHEET 4 AB4 6 VAL B 91 TYR B 100 -1 N LEU B 96 O VAL B 108 SHEET 5 AB4 6 LEU B 37 SER B 46 -1 N VAL B 44 O VAL B 93 SHEET 6 AB4 6 ASP B 51 VAL B 61 -1 O HIS B 52 N GLY B 45 SHEET 1 AB5 4 ALA B 15 LYS B 16 0 SHEET 2 AB5 4 ILE B 134 ILE B 138 -1 O ARG B 136 N ALA B 15 SHEET 3 AB5 4 ARG B 103 TYR B 116 -1 N GLU B 115 O VAL B 135 SHEET 4 AB5 4 ARG B 144 ARG B 147 -1 O ARG B 144 N GLY B 109 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.10 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.05 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.06 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.04 CISPEP 1 PHE H 146 PRO H 147 0 -7.48 CISPEP 2 GLU H 148 PRO H 149 0 -2.03 CISPEP 3 SER L 7 PRO L 8 0 -4.41 CISPEP 4 TYR L 140 PRO L 141 0 0.10 CISPEP 5 ASN B 13 PRO B 14 0 -5.78 CISPEP 6 GLY B 62 PRO B 63 0 -1.37 CRYST1 45.378 49.180 84.707 106.29 95.71 100.13 P 1 1 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 0.022037 0.003937 0.003570 0.00000 SCALE2 0.000000 0.020655 0.006595 0.00000 SCALE3 0.000000 0.000000 0.012454 0.00000