HEADER PROTEIN BINDING 26-MAR-24 9ETL TITLE MOUSE CNPASE CATALYTIC DOMAIN WITH NANOBODY 8D COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHAINS: D,C; COMPND 3 CHAIN: D, C; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: ANTI-CNPASE NANOBODY 8D; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; COMPND 8 CHAIN: A, B; COMPND 9 SYNONYM: CNP,CNPASE; COMPND 10 EC: 3.1.4.37; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: MOUSE CNPASE CATALYTIC DOMAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 3 ORGANISM_TAXID: 30538; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 9 ORGANISM_TAXID: 10090; SOURCE 10 GENE: CNP, CNP1; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CNPASE, MYELIN, NANOBODY, SINGLE-DOMAIN ANTIBODY, COMPLEX, PROTEIN KEYWDS 2 BINDING EXPDTA X-RAY DIFFRACTION AUTHOR M.SCHRODER,S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA REVDAT 1 11-DEC-24 9ETL 0 JRNL AUTH M.SCHRODER,S.MARKUSSON,A.RAASAKKA,F.OPAZO,P.KURSULA JRNL TITL MOUSE CNPASE CATALYTIC DOMAIN WITH NANOBODY 8D JRNL REF TO BE PUBLISHED JRNL REFN REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN, REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY, REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON, REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL, REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS, REMARK 1 AUTH 6 P.D.ADAMS REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS, REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX REMARK 1 REF ACTA CRYSTALLOGR., SECT. D: V. 75 861 2019 REMARK 1 REF 2 BIOL. CRYSTALLOGR. REMARK 1 REFN ISSN 0907-4449 REMARK 1 PMID 31588918 REMARK 1 DOI 10.1107/S2059798319011471 REMARK 2 REMARK 2 RESOLUTION. 1.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 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) : 1.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.05 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960 REMARK 3 COMPLETENESS FOR RANGE (%) : 81.4 REMARK 3 NUMBER OF REFLECTIONS : 179148 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.180 REMARK 3 R VALUE (WORKING SET) : 0.179 REMARK 3 FREE R VALUE : 0.229 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.080 REMARK 3 FREE R VALUE TEST SET COUNT : 3731 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 45.0500 - 4.5000 0.89 7105 151 0.1756 0.2199 REMARK 3 2 4.5000 - 3.5700 0.83 6582 143 0.1462 0.1592 REMARK 3 3 3.5700 - 3.1200 0.89 7154 155 0.1458 0.1859 REMARK 3 4 3.1200 - 2.8300 0.90 7223 155 0.1645 0.2464 REMARK 3 5 2.8300 - 2.6300 0.90 7189 149 0.1515 0.1853 REMARK 3 6 2.6300 - 2.4800 0.91 7196 163 0.1659 0.2766 REMARK 3 7 2.4800 - 2.3500 0.76 6083 130 0.1499 0.2329 REMARK 3 8 2.3500 - 2.2500 0.84 6675 138 0.1521 0.2059 REMARK 3 9 2.2500 - 2.1600 0.86 7000 153 0.1435 0.2341 REMARK 3 10 2.1600 - 2.0900 0.89 7010 138 0.1504 0.2044 REMARK 3 11 2.0900 - 2.0200 0.88 7011 163 0.1613 0.2214 REMARK 3 12 2.0200 - 1.9600 0.90 7196 143 0.1893 0.2951 REMARK 3 13 1.9600 - 1.9100 0.89 7201 147 0.1998 0.2755 REMARK 3 14 1.9100 - 1.8700 0.90 7164 174 0.2194 0.2710 REMARK 3 15 1.8700 - 1.8200 0.90 7241 131 0.2330 0.2877 REMARK 3 16 1.8200 - 1.7900 0.90 7187 171 0.2490 0.2685 REMARK 3 17 1.7900 - 1.7500 0.80 6367 128 0.2688 0.2956 REMARK 3 18 1.7500 - 1.7200 0.79 6334 137 0.2936 0.3996 REMARK 3 19 1.7200 - 1.6900 0.83 6652 137 0.3129 0.4088 REMARK 3 20 1.6900 - 1.6600 0.85 6615 144 0.3364 0.3561 REMARK 3 21 1.6600 - 1.6300 0.85 6825 149 0.3495 0.4110 REMARK 3 22 1.6300 - 1.6100 0.84 6746 136 0.3525 0.4010 REMARK 3 23 1.6100 - 1.5800 0.81 6535 141 0.3553 0.3645 REMARK 3 24 1.5800 - 1.5600 0.76 6066 107 0.3614 0.3969 REMARK 3 25 1.5600 - 1.5400 0.66 5354 113 0.3609 0.4246 REMARK 3 26 1.5400 - 1.5200 0.49 3931 99 0.3674 0.3604 REMARK 3 27 1.5200 - 1.5000 0.23 1775 36 0.3687 0.3548 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) : 0.286 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.742 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.15 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.35 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 : 0.011 5202 REMARK 3 ANGLE : 1.006 7017 REMARK 3 CHIRALITY : 0.081 763 REMARK 3 PLANARITY : 0.009 895 REMARK 3 DIHEDRAL : 12.970 1907 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 : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 162 through 218 or REMARK 3 resid 220 through 296 or resid 298 REMARK 3 through 361 or resid 363 through 378)) 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 162 through 218 or REMARK 3 resid 220 through 361 or resid 363 REMARK 3 through 378)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and resid 2 through 122) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "D" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9ETL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1292137572. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 19-FEB-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.2 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, DESY REMARK 200 BEAMLINE : P11 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 EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 190179 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500 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 (%) : 89.7 REMARK 200 DATA REDUNDANCY : 2.700 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59 REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4 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 : 0.500 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 (%): 47.93 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M PHOSPHATE-CITRATE PH 4.2, 18% REMARK 280 PEG8000, 0.35M NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 277K 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, 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 GLU D 1 REMARK 465 GLY A 159 REMARK 465 LEU A 160 REMARK 465 GLU A 161 REMARK 465 SER A 207 REMARK 465 GLY A 208 REMARK 465 ASP A 209 REMARK 465 GLU A 210 REMARK 465 PRO A 211 REMARK 465 LYS A 212 REMARK 465 ASP A 292 REMARK 465 LEU A 293 REMARK 465 ASP A 294 REMARK 465 LYS A 295 REMARK 465 GLY B 159 REMARK 465 LEU B 160 REMARK 465 GLU B 161 REMARK 465 SER B 207 REMARK 465 GLY B 208 REMARK 465 ASP B 209 REMARK 465 GLU B 210 REMARK 465 PRO B 211 REMARK 465 LYS B 212 REMARK 465 ASP B 292 REMARK 465 LEU B 293 REMARK 465 ASP B 294 REMARK 465 LYS B 295 REMARK 465 ALA B 296 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 SER B 297 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 HZ2 LYS A 162 OE1 GLU A 245 1.56 REMARK 500 O HOH B 402 O HOH B 407 1.80 REMARK 500 O HOH A 512 O HOH A 521 1.86 REMARK 500 O HOH B 547 O HOH B 548 1.87 REMARK 500 O HOH B 474 O HOH B 492 1.92 REMARK 500 OE1 GLU A 216 O HOH A 401 2.01 REMARK 500 O HOH B 537 O HOH B 540 2.04 REMARK 500 O HOH B 464 O HOH B 546 2.05 REMARK 500 NZ LYS A 262 O HOH A 402 2.05 REMARK 500 O HOH B 515 O HOH B 527 2.05 REMARK 500 O ALA C 75 O HOH C 201 2.08 REMARK 500 O HOH A 497 O HOH A 522 2.10 REMARK 500 O HOH B 531 O HOH B 540 2.15 REMARK 500 NZ LYS A 162 OE1 GLU A 245 2.15 REMARK 500 O HOH A 489 O HOH A 514 2.15 REMARK 500 O HOH A 453 O HOH A 479 2.16 REMARK 500 O HOH B 507 O HOH B 528 2.16 REMARK 500 O HOH B 524 O HOH B 538 2.17 REMARK 500 NZ LYS B 176 O HOH B 401 2.17 REMARK 500 NE2 GLN A 284 O HOH A 403 2.19 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 VAL D 48 -62.41 -124.58 REMARK 500 ALA D 92 169.50 179.73 REMARK 500 ASP D 99 178.66 74.92 REMARK 500 THR D 104 24.59 46.26 REMARK 500 THR A 233 -67.66 -101.38 REMARK 500 THR B 233 -67.78 -100.32 REMARK 500 VAL C 48 -62.40 -125.33 REMARK 500 ALA C 92 170.02 179.04 REMARK 500 ASP C 99 -179.55 73.05 REMARK 500 THR C 104 23.69 48.65 REMARK 500 REMARK 500 REMARK: NULL DBREF 9ETL D 1 122 PDB 9ETL 9ETL 1 122 DBREF 9ETL A 159 378 UNP P16330 CN37_MOUSE 179 398 DBREF 9ETL B 159 378 UNP P16330 CN37_MOUSE 179 398 DBREF 9ETL C 1 122 PDB 9ETL 9ETL 1 122 SEQADV 9ETL ALA A 296 UNP P16330 PRO 316 CONFLICT SEQADV 9ETL ALA B 296 UNP P16330 PRO 316 CONFLICT SEQRES 1 D 122 GLU VAL GLN LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 122 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 122 PHE THR PHE SER SER TYR VAL MET SER TRP VAL ARG GLN SEQRES 4 D 122 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE ASN SEQRES 5 D 122 SER GLY GLY SER ARG THR TYR TYR THR ASP SER VAL LYS SEQRES 6 D 122 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 D 122 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 D 122 ALA VAL TYR TYR CYS ALA ARG ASP SER LEU LEU SER THR SEQRES 9 D 122 ARG TYR LEU HIS THR SER GLU ARG GLY GLN GLY THR GLN SEQRES 10 D 122 VAL THR VAL SER SER SEQRES 1 A 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 A 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 A 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 A 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 A 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 A 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 A 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 A 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 A 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 A 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 A 220 TRP PRO SER ASP LEU ASP LYS ALA SER ALA SER GLU GLY SEQRES 12 A 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 A 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 A 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 A 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 A 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 A 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY SEQRES 1 B 220 GLY LEU GLU LYS ASP PHE LEU PRO LEU TYR PHE GLY TRP SEQRES 2 B 220 PHE LEU THR LYS LYS SER SER GLU THR LEU ARG LYS ALA SEQRES 3 B 220 GLY GLN VAL PHE LEU GLU GLU LEU GLY ASN HIS LYS ALA SEQRES 4 B 220 PHE LYS LYS GLU LEU ARG HIS PHE ILE SER GLY ASP GLU SEQRES 5 B 220 PRO LYS GLU LYS LEU GLU LEU VAL SER TYR PHE GLY LYS SEQRES 6 B 220 ARG PRO PRO GLY VAL LEU HIS CYS THR THR LYS PHE CYS SEQRES 7 B 220 ASP TYR GLY LYS ALA ALA GLY ALA GLU GLU TYR ALA GLN SEQRES 8 B 220 GLN GLU VAL VAL LYS ARG SER TYR GLY LYS ALA PHE LYS SEQRES 9 B 220 LEU SER ILE SER ALA LEU PHE VAL THR PRO LYS THR ALA SEQRES 10 B 220 GLY ALA GLN VAL VAL LEU THR ASP GLN GLU LEU GLN LEU SEQRES 11 B 220 TRP PRO SER ASP LEU ASP LYS ALA SER ALA SER GLU GLY SEQRES 12 B 220 LEU PRO PRO GLY SER ARG ALA HIS VAL THR LEU GLY CYS SEQRES 13 B 220 ALA ALA ASP VAL GLN PRO VAL GLN THR GLY LEU ASP LEU SEQRES 14 B 220 LEU ASP ILE LEU GLN GLN VAL LYS GLY GLY SER GLN GLY SEQRES 15 B 220 GLU ALA VAL GLY GLU LEU PRO ARG GLY LYS LEU TYR SER SEQRES 16 B 220 LEU GLY LYS GLY ARG TRP MET LEU SER LEU THR LYS LYS SEQRES 17 B 220 MET GLU VAL LYS ALA ILE PHE THR GLY TYR TYR GLY SEQRES 1 C 122 GLU VAL GLN LEU GLU GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 122 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 122 PHE THR PHE SER SER TYR VAL MET SER TRP VAL ARG GLN SEQRES 4 C 122 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE ASN SEQRES 5 C 122 SER GLY GLY SER ARG THR TYR TYR THR ASP SER VAL LYS SEQRES 6 C 122 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 122 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 C 122 ALA VAL TYR TYR CYS ALA ARG ASP SER LEU LEU SER THR SEQRES 9 C 122 ARG TYR LEU HIS THR SER GLU ARG GLY GLN GLY THR GLN SEQRES 10 C 122 VAL THR VAL SER SER FORMUL 5 HOH *347(H2 O) HELIX 1 AA1 THR D 28 TYR D 32 5 5 HELIX 2 AA2 ASN D 74 LYS D 76 5 3 HELIX 3 AA3 LYS D 87 THR D 91 5 5 HELIX 4 AA4 THR D 104 ARG D 112 5 9 HELIX 5 AA5 THR A 174 HIS A 195 1 22 HELIX 6 AA6 HIS A 195 GLU A 201 1 7 HELIX 7 AA7 LEU A 202 PHE A 205 5 4 HELIX 8 AA8 GLU A 216 PHE A 221 1 6 HELIX 9 AA9 ASP A 237 LYS A 240 5 4 HELIX 10 AB1 GLY A 243 GLN A 249 1 7 HELIX 11 AB2 GLN A 250 TYR A 257 1 8 HELIX 12 AB3 THR A 282 GLN A 287 1 6 HELIX 13 AB4 ALA A 296 GLU A 300 5 5 HELIX 14 AB5 VAL A 321 GLY A 336 1 16 HELIX 15 AB6 THR B 174 ASN B 194 1 21 HELIX 16 AB7 HIS B 195 GLU B 201 1 7 HELIX 17 AB8 LEU B 202 PHE B 205 5 4 HELIX 18 AB9 GLU B 216 PHE B 221 1 6 HELIX 19 AC1 ASP B 237 LYS B 240 5 4 HELIX 20 AC2 GLY B 243 GLN B 249 1 7 HELIX 21 AC3 GLN B 250 TYR B 257 1 8 HELIX 22 AC4 THR B 282 GLN B 287 1 6 HELIX 23 AC5 VAL B 321 GLY B 336 1 16 HELIX 24 AC6 THR C 28 TYR C 32 5 5 HELIX 25 AC7 ASN C 74 LYS C 76 5 3 HELIX 26 AC8 LYS C 87 THR C 91 5 5 HELIX 27 AC9 THR C 104 ARG C 112 5 9 SHEET 1 AA1 4 GLN D 3 SER D 7 0 SHEET 2 AA1 4 LEU D 18 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AA1 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA1 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AA2 6 GLY D 10 VAL D 12 0 SHEET 2 AA2 6 THR D 116 VAL D 120 1 O THR D 119 N VAL D 12 SHEET 3 AA2 6 ALA D 92 ARG D 98 -1 N TYR D 94 O THR D 116 SHEET 4 AA2 6 MET D 34 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AA2 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AA2 6 THR D 58 TYR D 60 -1 O TYR D 59 N ASP D 50 SHEET 1 AA3 6 HIS A 230 PHE A 235 0 SHEET 2 AA3 6 TYR A 168 LEU A 173 -1 N TRP A 171 O CYS A 231 SHEET 3 AA3 6 ARG A 358 TYR A 376 -1 O TYR A 376 N TYR A 168 SHEET 4 AA3 6 ALA A 260 VAL A 270 -1 N ILE A 265 O MET A 367 SHEET 5 AA3 6 THR A 274 VAL A 280 -1 O GLN A 278 N ALA A 267 SHEET 6 AA3 6 HIS A 309 CYS A 314 -1 O LEU A 312 N ALA A 275 SHEET 1 AA4 5 HIS A 230 PHE A 235 0 SHEET 2 AA4 5 TYR A 168 LEU A 173 -1 N TRP A 171 O CYS A 231 SHEET 3 AA4 5 ARG A 358 TYR A 376 -1 O TYR A 376 N TYR A 168 SHEET 4 AA4 5 GLY A 349 GLY A 355 -1 N TYR A 352 O MET A 360 SHEET 5 AA4 5 GLY A 344 LEU A 346 -1 N LEU A 346 O GLY A 349 SHEET 1 AA5 6 HIS B 230 PHE B 235 0 SHEET 2 AA5 6 TYR B 168 LEU B 173 -1 N PHE B 169 O THR B 233 SHEET 3 AA5 6 ARG B 358 TYR B 376 -1 O THR B 374 N GLY B 170 SHEET 4 AA5 6 ALA B 260 VAL B 270 -1 N ILE B 265 O MET B 367 SHEET 5 AA5 6 THR B 274 VAL B 280 -1 O GLN B 278 N ALA B 267 SHEET 6 AA5 6 HIS B 309 CYS B 314 -1 O LEU B 312 N ALA B 275 SHEET 1 AA6 5 HIS B 230 PHE B 235 0 SHEET 2 AA6 5 TYR B 168 LEU B 173 -1 N PHE B 169 O THR B 233 SHEET 3 AA6 5 ARG B 358 TYR B 376 -1 O THR B 374 N GLY B 170 SHEET 4 AA6 5 GLY B 349 GLY B 355 -1 N LYS B 350 O SER B 362 SHEET 5 AA6 5 GLY B 344 LEU B 346 -1 N LEU B 346 O GLY B 349 SHEET 1 AA7 4 GLN C 3 SER C 7 0 SHEET 2 AA7 4 LEU C 18 SER C 25 -1 O SER C 21 N SER C 7 SHEET 3 AA7 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 18 SHEET 4 AA7 4 PHE C 68 ASP C 73 -1 N THR C 69 O GLN C 82 SHEET 1 AA8 6 GLY C 10 VAL C 12 0 SHEET 2 AA8 6 THR C 116 VAL C 120 1 O THR C 119 N VAL C 12 SHEET 3 AA8 6 ALA C 92 ARG C 98 -1 N ALA C 92 O VAL C 118 SHEET 4 AA8 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 95 SHEET 5 AA8 6 GLU C 46 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AA8 6 THR C 58 TYR C 60 -1 O TYR C 59 N ASP C 50 SSBOND 1 CYS D 22 CYS D 96 1555 1555 2.06 SSBOND 2 CYS C 22 CYS C 96 1555 1555 2.07 CRYST1 42.300 46.541 91.976 95.66 100.11 90.08 P 1 2 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 0.023641 0.000032 0.004241 0.00000 SCALE2 0.000000 0.021486 0.002167 0.00000 SCALE3 0.000000 0.000000 0.011100 0.00000 MTRIX1 1 -0.999977 0.001994 0.006494 34.25254 1 MTRIX2 1 0.001951 0.999977 -0.006561 23.10855 1 MTRIX3 1 -0.006507 -0.006548 -0.999957 -50.23061 1 MTRIX1 2 -0.999975 -0.004474 -0.005417 34.09829 1 MTRIX2 2 -0.004284 0.999393 -0.034585 -24.79390 1 MTRIX3 2 0.005568 -0.034561 -0.999387 -49.66235 1