HEADER VIRAL PROTEIN 11-APR-24 9BDI TITLE CRYSTAL STRUCTURE OF HIV-1 MPER SCAFFOLD IN COMPLEX WITH ANTIBODY FAB TITLE 2 AB45.2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GT10.2 GLYCAN KO; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB 45.2 HEAVY CHAIN; COMPND 7 CHAIN: C, H; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: FAB 45.2 LIGHT CHAIN; COMPND 11 CHAIN: D, L; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 9 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 10 ORGANISM_TAXID: 10090; SOURCE 11 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 15 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 16 ORGANISM_TAXID: 10090; SOURCE 17 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS MEMBRANE-PROXIMAL EXTERNAL REGION (MPER), HIV-1, GERMLINE TARGETING, KEYWDS 2 B CELL, GERMINAL CENTER, VIRAL PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR C.C.D.LEE,I.A.WILSON REVDAT 1 19-FEB-25 9BDI 0 JRNL AUTH R.RAY,T.SCHIFFNER,X.WANG,Y.YAN,K.RANTALAINEN,C.D.LEE, JRNL AUTH 2 S.PARIKH,R.A.REYES,G.A.DALE,Y.C.LIN,S.PECETTA,S.GIGUERE, JRNL AUTH 3 O.SWANSON,S.KRATOCHVIL,E.MELZI,I.PHUNG,L.MADUNGWE, JRNL AUTH 4 O.KALYUZHNIY,J.WARNER,S.R.WELDON,R.TINGLE,E.LAMPERTI, JRNL AUTH 5 K.H.KIRSCH,N.PHELPS,E.GEORGESON,Y.ADACHI,M.KUBITZ,U.NAIR, JRNL AUTH 6 S.CROTTY,I.A.WILSON,W.R.SCHIEF,F.D.BATISTA JRNL TITL AFFINITY GAPS AMONG B CELLS IN GERMINAL CENTERS DRIVE THE JRNL TITL 2 SELECTION OF MPER PRECURSORS. JRNL REF NAT.IMMUNOL. V. 25 1083 2024 JRNL REFN ESSN 1529-2916 JRNL PMID 38816616 JRNL DOI 10.1038/S41590-024-01844-7 REMARK 2 REMARK 2 RESOLUTION. 2.07 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) : 2.07 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.47 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970 REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8 REMARK 3 NUMBER OF REFLECTIONS : 61615 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.238 REMARK 3 R VALUE (WORKING SET) : 0.235 REMARK 3 FREE R VALUE : 0.283 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.880 REMARK 3 FREE R VALUE TEST SET COUNT : 3009 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 44.4700 - 5.7100 0.83 2690 157 0.1670 0.1800 REMARK 3 2 5.7100 - 4.5300 0.75 2413 154 0.1495 0.2036 REMARK 3 3 4.5300 - 3.9600 0.85 2784 115 0.1520 0.1933 REMARK 3 4 3.9600 - 3.6000 0.89 2873 172 0.1770 0.2098 REMARK 3 5 3.6000 - 3.3400 0.91 2923 151 0.1914 0.2433 REMARK 3 6 3.3400 - 3.1400 0.91 2957 148 0.2163 0.2576 REMARK 3 7 3.1400 - 2.9800 0.92 3070 138 0.2346 0.3006 REMARK 3 8 2.9800 - 2.8500 0.79 2585 117 0.2491 0.3727 REMARK 3 9 2.8500 - 2.7400 0.75 2425 109 0.2606 0.3165 REMARK 3 10 2.7400 - 2.6500 0.84 2751 138 0.2685 0.3831 REMARK 3 11 2.6500 - 2.5700 0.86 2819 144 0.2722 0.2979 REMARK 3 12 2.5700 - 2.4900 0.87 2776 146 0.2720 0.3543 REMARK 3 13 2.4900 - 2.4300 0.87 2851 162 0.2884 0.2824 REMARK 3 14 2.4300 - 2.3700 0.88 2848 138 0.2929 0.3653 REMARK 3 15 2.3700 - 2.3200 0.89 2878 150 0.3029 0.3869 REMARK 3 16 2.3200 - 2.2700 0.88 2913 157 0.3087 0.3739 REMARK 3 17 2.2700 - 2.2200 0.90 2833 157 0.3232 0.3518 REMARK 3 18 2.2200 - 2.1800 0.89 2994 147 0.3325 0.3817 REMARK 3 19 2.1800 - 2.1400 0.88 2838 139 0.3366 0.3953 REMARK 3 20 2.1400 - 2.1000 0.87 2805 140 0.3623 0.4089 REMARK 3 21 2.1000 - 2.0700 0.79 2580 130 0.3801 0.4159 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) : 0.230 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 44.980 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.61 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.87 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 : 0.003 9522 REMARK 3 ANGLE : 0.611 12940 REMARK 3 CHIRALITY : 0.044 1442 REMARK 3 PLANARITY : 0.004 1654 REMARK 3 DIHEDRAL : 16.778 3448 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 9BDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-24. REMARK 100 THE DEPOSITION ID IS D_1000283134. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-OCT-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0337 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63266 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070 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 (%) : 88.6 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.07 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11 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: 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 (%): 46.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M PHOSPHATE REMARK 280 CITRATE AND 20% PEG8000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 295K 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L 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: B, C, D 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 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 OE2 GLU A 29 O HOH A 201 2.09 REMARK 500 OE2 GLU B 29 O HOH B 201 2.10 REMARK 500 O HOH B 204 O HOH B 252 2.19 REMARK 500 O HOH D 306 O HOH D 385 2.19 REMARK 500 OE1 GLU H 166 O HOH H 301 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 NE2 GLN A 80 O HIS L 30 1655 2.10 REMARK 500 NZ LYS A 106 OH TYR H 105 1655 2.12 REMARK 500 NE2 GLN B 80 O HIS D 30 1655 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 ASP A 83 91.44 58.23 REMARK 500 SER A 144 -39.01 -27.51 REMARK 500 LYS B 45 -96.90 57.24 REMARK 500 SER B 144 -38.73 -27.75 REMARK 500 GLU C 116 42.15 -87.35 REMARK 500 ASN D 31 9.55 58.50 REMARK 500 ALA D 51 -26.42 69.24 REMARK 500 GLU D 213 -151.80 -76.51 REMARK 500 GLU H 116 42.67 -86.14 REMARK 500 ASP H 162 70.21 57.83 REMARK 500 ALA L 51 -27.07 69.25 REMARK 500 ASN L 158 20.96 -141.76 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 C 450 DISTANCE = 6.31 ANGSTROMS DBREF 9BDI A 4 156 PDB 9BDI 9BDI 4 156 DBREF 9BDI B 4 156 PDB 9BDI 9BDI 4 156 DBREF 9BDI C 1 234 PDB 9BDI 9BDI 1 234 DBREF 9BDI D 1 214 PDB 9BDI 9BDI 1 214 DBREF 9BDI H 1 234 PDB 9BDI 9BDI 1 234 DBREF 9BDI L 1 214 PDB 9BDI 9BDI 1 214 SEQRES 1 A 153 VAL THR GLN GLU ASP ILE ILE ARG ALA LEU ALA SER PRO SEQRES 2 A 153 LEU ILE LYS ASP GLY MET VAL ASP GLU ASP PHE ALA GLU SEQRES 3 A 153 TYR VAL ILE ALA ARG GLU ASP ARG SER PRO THR GLY LEU SEQRES 4 A 153 GLN ALA LYS GLY VAL GLY VAL ALA ILE PRO HIS THR LEU SEQRES 5 A 153 GLY ASP TYR VAL ARG ASP ASN ALA ILE SER VAL GLY ILE SEQRES 6 A 153 LEU ASP LYS PRO VAL ASN PHE GLU GLY TRP TYR GLN SER SEQRES 7 A 153 PRO ASP PRO VAL PRO VAL ARG VAL VAL PHE MET LEU ALA SEQRES 8 A 153 GLY ARG THR TRP ASP ASP ILE VAL ILE VAL LEU LYS TRP SEQRES 9 A 153 LEU LYS ASP VAL ILE LEU ASP GLU GLU PHE MET LYS ARG SEQRES 10 A 153 LEU LEU THR MET SER ASP GLU GLU ILE TYR ARG GLN ILE SEQRES 11 A 153 TYR THR ARG ILE SER LYS ALA PRO GLN LEU SER GLY ILE SEQRES 12 A 153 ASN PHE LYS ARG GLU TYR VAL ARG HIS LEU SEQRES 1 B 153 VAL THR GLN GLU ASP ILE ILE ARG ALA LEU ALA SER PRO SEQRES 2 B 153 LEU ILE LYS ASP GLY MET VAL ASP GLU ASP PHE ALA GLU SEQRES 3 B 153 TYR VAL ILE ALA ARG GLU ASP ARG SER PRO THR GLY LEU SEQRES 4 B 153 GLN ALA LYS GLY VAL GLY VAL ALA ILE PRO HIS THR LEU SEQRES 5 B 153 GLY ASP TYR VAL ARG ASP ASN ALA ILE SER VAL GLY ILE SEQRES 6 B 153 LEU ASP LYS PRO VAL ASN PHE GLU GLY TRP TYR GLN SER SEQRES 7 B 153 PRO ASP PRO VAL PRO VAL ARG VAL VAL PHE MET LEU ALA SEQRES 8 B 153 GLY ARG THR TRP ASP ASP ILE VAL ILE VAL LEU LYS TRP SEQRES 9 B 153 LEU LYS ASP VAL ILE LEU ASP GLU GLU PHE MET LYS ARG SEQRES 10 B 153 LEU LEU THR MET SER ASP GLU GLU ILE TYR ARG GLN ILE SEQRES 11 B 153 TYR THR ARG ILE SER LYS ALA PRO GLN LEU SER GLY ILE SEQRES 12 B 153 ASN PHE LYS ARG GLU TYR VAL ARG HIS LEU SEQRES 1 C 234 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 C 234 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 234 PHE THR PHE SER ASN ALA TRP MET SER TRP VAL ARG GLN SEQRES 4 C 234 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ARG ILE LYS SEQRES 5 C 234 SER LYS THR ASP GLY GLY THR THR ASP CYS ALA ALA PRO SEQRES 6 C 234 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 C 234 ASN THR LEU TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 C 234 ASP THR ALA VAL TYR TYR CYS THR ARG SER ALA GLU PHE SEQRES 9 C 234 TYR ASP PHE TRP SER GLY TYR TYR THR GLY LEU GLU TYR SEQRES 10 C 234 PHE GLN HIS TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 C 234 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 C 234 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 C 234 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 C 234 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 C 234 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 C 234 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 C 234 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 C 234 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 1 D 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 D 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 214 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS SEQRES 5 D 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 D 214 GLN PRO GLU ASP VAL GLY SER TYR TYR CYS GLN TYR PHE SEQRES 8 D 214 TRP SER ILE PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 D 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 D 214 PHE ASN ARG GLY GLU CYS SEQRES 1 H 234 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 234 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 234 PHE THR PHE SER ASN ALA TRP MET SER TRP VAL ARG GLN SEQRES 4 H 234 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ARG ILE LYS SEQRES 5 H 234 SER LYS THR ASP GLY GLY THR THR ASP CYS ALA ALA PRO SEQRES 6 H 234 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 H 234 ASN THR LEU TYR LEU GLN MET ASN SER LEU LYS THR GLU SEQRES 8 H 234 ASP THR ALA VAL TYR TYR CYS THR ARG SER ALA GLU PHE SEQRES 9 H 234 TYR ASP PHE TRP SER GLY TYR TYR THR GLY LEU GLU TYR SEQRES 10 H 234 PHE GLN HIS TRP GLY GLN GLY THR LEU VAL THR VAL SER SEQRES 11 H 234 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 12 H 234 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 13 H 234 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 14 H 234 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 15 H 234 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 16 H 234 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 17 H 234 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 18 H 234 ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO ALA SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY GLU THR VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLY ASN ILE HIS ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 214 GLN GLY LYS SER PRO GLN LEU LEU VAL TYR ASN ALA LYS SEQRES 5 L 214 THR LEU ALA ASP GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR GLN TYR SER LEU LYS ILE ASN SER LEU SEQRES 7 L 214 GLN PRO GLU ASP VAL GLY SER TYR TYR CYS GLN TYR PHE SEQRES 8 L 214 TRP SER ILE PRO TYR THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS FORMUL 7 HOH *692(H2 O) HELIX 1 AA1 THR A 5 ASP A 20 1 16 HELIX 2 AA2 ASP A 26 SER A 38 1 13 HELIX 3 AA3 THR A 97 ASP A 114 1 18 HELIX 4 AA4 ASP A 114 LEU A 122 1 9 HELIX 5 AA5 SER A 125 LYS A 139 1 15 HELIX 6 AA6 LYS A 149 GLU A 151 5 3 HELIX 7 AA7 THR B 5 ASP B 20 1 16 HELIX 8 AA8 ASP B 26 SER B 38 1 13 HELIX 9 AA9 THR B 97 ASP B 114 1 18 HELIX 10 AB1 ASP B 114 MET B 124 1 11 HELIX 11 AB2 SER B 125 LYS B 139 1 15 HELIX 12 AB3 LYS B 149 GLU B 151 5 3 HELIX 13 AB4 THR C 28 ALA C 32 5 5 HELIX 14 AB5 SER C 53 GLY C 57 5 5 HELIX 15 AB6 LYS C 89 THR C 93 5 5 HELIX 16 AB7 SER C 145 THR C 149 5 5 HELIX 17 AB8 SER C 174 ALA C 176 5 3 HELIX 18 AB9 SER C 205 LEU C 207 5 3 HELIX 19 AC1 LYS C 219 ASN C 222 5 4 HELIX 20 AC2 GLN D 79 VAL D 83 5 5 HELIX 21 AC3 SER D 121 SER D 127 1 7 HELIX 22 AC4 LYS D 183 HIS D 189 1 7 HELIX 23 AC5 THR H 28 ALA H 32 5 5 HELIX 24 AC6 SER H 53 GLY H 57 5 5 HELIX 25 AC7 LYS H 89 THR H 93 5 5 HELIX 26 AC8 SER H 145 THR H 149 5 5 HELIX 27 AC9 SER H 174 ALA H 176 5 3 HELIX 28 AD1 SER H 205 LEU H 207 5 3 HELIX 29 AD2 LYS H 219 ASN H 222 5 4 HELIX 30 AD3 GLN L 79 VAL L 83 5 5 HELIX 31 AD4 SER L 121 SER L 127 1 7 HELIX 32 AD5 LYS L 183 HIS L 189 1 7 SHEET 1 AA1 5 LEU A 42 ALA A 44 0 SHEET 2 AA1 5 VAL A 47 ALA A 50 -1 O VAL A 49 N LEU A 42 SHEET 3 AA1 5 VAL A 85 ALA A 94 1 O PHE A 91 N ALA A 50 SHEET 4 AA1 5 ALA A 63 PHE A 75 -1 N SER A 65 O MET A 92 SHEET 5 AA1 5 VAL A 153 LEU A 156 1 O LEU A 156 N ILE A 68 SHEET 1 AA2 5 LEU B 42 ALA B 44 0 SHEET 2 AA2 5 VAL B 47 ALA B 50 -1 O VAL B 49 N LEU B 42 SHEET 3 AA2 5 VAL B 85 ALA B 94 1 O PHE B 91 N ALA B 50 SHEET 4 AA2 5 ALA B 63 PHE B 75 -1 N SER B 65 O MET B 92 SHEET 5 AA2 5 VAL B 153 LEU B 156 1 O LEU B 156 N ILE B 68 SHEET 1 AA3 4 GLN C 3 SER C 7 0 SHEET 2 AA3 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AA3 4 THR C 80 MET C 85 -1 O MET C 85 N LEU C 18 SHEET 4 AA3 4 PHE C 70 ASP C 75 -1 N THR C 71 O GLN C 84 SHEET 1 AA4 6 LEU C 11 VAL C 12 0 SHEET 2 AA4 6 THR C 125 VAL C 129 1 O THR C 128 N VAL C 12 SHEET 3 AA4 6 ALA C 94 TYR C 105 -1 N TYR C 96 O THR C 125 SHEET 4 AA4 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 97 SHEET 5 AA4 6 LEU C 45 ILE C 51 -1 O ILE C 51 N MET C 34 SHEET 6 AA4 6 THR C 60 CYS C 62 -1 O ASP C 61 N ARG C 50 SHEET 1 AA5 4 LEU C 11 VAL C 12 0 SHEET 2 AA5 4 THR C 125 VAL C 129 1 O THR C 128 N VAL C 12 SHEET 3 AA5 4 ALA C 94 TYR C 105 -1 N TYR C 96 O THR C 125 SHEET 4 AA5 4 TYR C 112 TRP C 121 -1 O THR C 113 N PHE C 104 SHEET 1 AA6 4 SER C 138 LEU C 142 0 SHEET 2 AA6 4 THR C 153 TYR C 163 -1 O LEU C 159 N PHE C 140 SHEET 3 AA6 4 TYR C 194 PRO C 203 -1 O LEU C 196 N VAL C 160 SHEET 4 AA6 4 VAL C 181 THR C 183 -1 N HIS C 182 O VAL C 199 SHEET 1 AA7 4 SER C 138 LEU C 142 0 SHEET 2 AA7 4 THR C 153 TYR C 163 -1 O LEU C 159 N PHE C 140 SHEET 3 AA7 4 TYR C 194 PRO C 203 -1 O LEU C 196 N VAL C 160 SHEET 4 AA7 4 VAL C 187 LEU C 188 -1 N VAL C 187 O SER C 195 SHEET 1 AA8 3 THR C 169 TRP C 172 0 SHEET 2 AA8 3 ILE C 213 HIS C 218 -1 O ASN C 215 N SER C 171 SHEET 3 AA8 3 THR C 223 ARG C 228 -1 O VAL C 225 N VAL C 216 SHEET 1 AA9 4 MET D 4 SER D 7 0 SHEET 2 AA9 4 VAL D 19 ALA D 25 -1 O THR D 22 N SER D 7 SHEET 3 AA9 4 GLN D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AA9 4 PHE D 62 SER D 67 -1 N SER D 63 O LYS D 74 SHEET 1 AB1 6 SER D 10 SER D 14 0 SHEET 2 AB1 6 THR D 102 LYS D 107 1 O GLU D 105 N LEU D 11 SHEET 3 AB1 6 GLY D 84 TYR D 90 -1 N GLY D 84 O LEU D 104 SHEET 4 AB1 6 LEU D 33 GLN D 38 -1 N TYR D 36 O TYR D 87 SHEET 5 AB1 6 GLN D 45 TYR D 49 -1 O GLN D 45 N GLN D 37 SHEET 6 AB1 6 THR D 53 LEU D 54 -1 O THR D 53 N TYR D 49 SHEET 1 AB2 4 SER D 114 PHE D 118 0 SHEET 2 AB2 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AB2 4 TYR D 173 SER D 182 -1 O LEU D 175 N LEU D 136 SHEET 4 AB2 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AB3 4 ALA D 153 LEU D 154 0 SHEET 2 AB3 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AB3 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AB3 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SHEET 1 AB4 4 GLN H 3 SER H 7 0 SHEET 2 AB4 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AB4 4 THR H 80 MET H 85 -1 O MET H 85 N LEU H 18 SHEET 4 AB4 4 PHE H 70 ASP H 75 -1 N THR H 71 O GLN H 84 SHEET 1 AB5 6 LEU H 11 VAL H 12 0 SHEET 2 AB5 6 THR H 125 VAL H 129 1 O THR H 128 N VAL H 12 SHEET 3 AB5 6 ALA H 94 TYR H 105 -1 N TYR H 96 O THR H 125 SHEET 4 AB5 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 97 SHEET 5 AB5 6 GLU H 46 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AB5 6 THR H 60 CYS H 62 -1 O ASP H 61 N ARG H 50 SHEET 1 AB6 4 LEU H 11 VAL H 12 0 SHEET 2 AB6 4 THR H 125 VAL H 129 1 O THR H 128 N VAL H 12 SHEET 3 AB6 4 ALA H 94 TYR H 105 -1 N TYR H 96 O THR H 125 SHEET 4 AB6 4 TYR H 112 TRP H 121 -1 O THR H 113 N PHE H 104 SHEET 1 AB7 4 SER H 138 LEU H 142 0 SHEET 2 AB7 4 THR H 153 TYR H 163 -1 O LEU H 159 N PHE H 140 SHEET 3 AB7 4 TYR H 194 PRO H 203 -1 O LEU H 196 N VAL H 160 SHEET 4 AB7 4 VAL H 181 THR H 183 -1 N HIS H 182 O VAL H 199 SHEET 1 AB8 4 SER H 138 LEU H 142 0 SHEET 2 AB8 4 THR H 153 TYR H 163 -1 O LEU H 159 N PHE H 140 SHEET 3 AB8 4 TYR H 194 PRO H 203 -1 O LEU H 196 N VAL H 160 SHEET 4 AB8 4 VAL H 187 LEU H 188 -1 N VAL H 187 O SER H 195 SHEET 1 AB9 3 THR H 169 TRP H 172 0 SHEET 2 AB9 3 ILE H 213 HIS H 218 -1 O ASN H 215 N SER H 171 SHEET 3 AB9 3 THR H 223 ARG H 228 -1 O VAL H 225 N VAL H 216 SHEET 1 AC1 4 MET L 4 SER L 7 0 SHEET 2 AC1 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AC1 4 GLN L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AC1 4 PHE L 62 SER L 67 -1 N SER L 63 O LYS L 74 SHEET 1 AC2 6 SER L 10 SER L 14 0 SHEET 2 AC2 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AC2 6 GLY L 84 TYR L 90 -1 N GLY L 84 O LEU L 104 SHEET 4 AC2 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AC2 6 GLN L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AC2 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AC3 4 SER L 114 PHE L 118 0 SHEET 2 AC3 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AC3 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AC3 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AC4 4 ALA L 153 LEU L 154 0 SHEET 2 AC4 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AC4 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AC4 4 VAL L 205 ASN L 210 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS C 22 CYS C 98 1555 1555 2.04 SSBOND 2 CYS C 158 CYS C 214 1555 1555 2.03 SSBOND 3 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 4 CYS D 134 CYS D 194 1555 1555 2.04 SSBOND 5 CYS H 22 CYS H 98 1555 1555 2.04 SSBOND 6 CYS H 158 CYS H 214 1555 1555 2.03 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 8 CYS L 134 CYS L 194 1555 1555 2.04 CISPEP 1 PHE C 164 PRO C 165 0 -7.15 CISPEP 2 GLU C 166 PRO C 167 0 1.58 CISPEP 3 SER D 7 PRO D 8 0 -2.63 CISPEP 4 ILE D 94 PRO D 95 0 5.06 CISPEP 5 TYR D 140 PRO D 141 0 2.54 CISPEP 6 PHE H 164 PRO H 165 0 -4.87 CISPEP 7 GLU H 166 PRO H 167 0 -1.94 CISPEP 8 SER L 7 PRO L 8 0 -3.17 CISPEP 9 ILE L 94 PRO L 95 0 3.52 CISPEP 10 TYR L 140 PRO L 141 0 4.28 CRYST1 37.617 46.638 178.352 86.67 86.76 77.04 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 0.026584 -0.006116 -0.001221 0.00000 SCALE2 0.000000 0.022002 -0.001027 0.00000 SCALE3 0.000000 0.000000 0.005622 0.00000