HEADER IMMUNE SYSTEM 09-JAN-25 9MRZ TITLE STRUCTURE OF HCV BROADLY NEUTRALIZING ANTIBODY RM1-73 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RM1-73 FAB LIGHT CHAIN; COMPND 3 CHAIN: l, L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: RM1-73 FAB HEAVY CHAIN; COMPND 7 CHAIN: h, H; COMPND 8 ENGINEERED: YES; COMPND 9 OTHER_DETAILS: Q1(PCA) SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 4 ORGANISM_TAXID: 9544; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 10 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 11 ORGANISM_TAXID: 9544; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS MONKEY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR T.K.Y.NGUYEN,R.L.STANFIELD,I.A.WILSON REVDAT 1 14-JAN-26 9MRZ 0 JRNL AUTH T.K.Y.NGUYEN,R.L.STANFIELD,I.A.WILSON JRNL TITL STRUCTURE OF HCV BROADLY NEUTRALIZING ANTIBODY RM1-73 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.03 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) : 2.03 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.79 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 80798 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.171 REMARK 3 R VALUE (WORKING SET) : 0.170 REMARK 3 FREE R VALUE : 0.196 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4040 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 44.7900 - 6.2300 0.99 2801 153 0.1705 0.1894 REMARK 3 2 6.2300 - 4.9500 1.00 2752 139 0.1531 0.1629 REMARK 3 3 4.9500 - 4.3200 0.99 2726 159 0.1268 0.1594 REMARK 3 4 4.3200 - 3.9300 1.00 2719 156 0.1351 0.1524 REMARK 3 5 3.9300 - 3.6500 0.99 2701 133 0.1547 0.1538 REMARK 3 6 3.6500 - 3.4300 0.99 2702 147 0.1615 0.1798 REMARK 3 7 3.4300 - 3.2600 0.99 2705 145 0.1709 0.1825 REMARK 3 8 3.2600 - 3.1200 0.99 2672 137 0.1809 0.2090 REMARK 3 9 3.1200 - 3.0000 0.99 2673 146 0.1779 0.2257 REMARK 3 10 3.0000 - 2.8900 0.99 2678 150 0.1920 0.1913 REMARK 3 11 2.8900 - 2.8000 0.98 2639 140 0.1868 0.2204 REMARK 3 12 2.8000 - 2.7200 0.98 2686 133 0.1885 0.2271 REMARK 3 13 2.7200 - 2.6500 0.98 2638 144 0.1945 0.2414 REMARK 3 14 2.6500 - 2.5900 0.98 2683 118 0.1923 0.2235 REMARK 3 15 2.5900 - 2.5300 0.98 2612 127 0.1968 0.2603 REMARK 3 16 2.5300 - 2.4700 0.98 2678 125 0.1932 0.2339 REMARK 3 17 2.4700 - 2.4300 0.97 2645 134 0.1750 0.1861 REMARK 3 18 2.4300 - 2.3800 0.97 2611 134 0.1882 0.2009 REMARK 3 19 2.3800 - 2.3400 0.98 2631 142 0.1812 0.2381 REMARK 3 20 2.3400 - 2.3000 0.97 2615 131 0.1819 0.2256 REMARK 3 21 2.3000 - 2.2600 0.97 2629 141 0.1827 0.2148 REMARK 3 22 2.2600 - 2.2300 0.97 2591 156 0.1763 0.2611 REMARK 3 23 2.2300 - 2.1900 0.96 2621 126 0.1859 0.2318 REMARK 3 24 2.1900 - 2.1600 0.97 2587 132 0.1828 0.2148 REMARK 3 25 2.1600 - 2.1300 0.96 2602 159 0.1824 0.2263 REMARK 3 26 2.1300 - 2.1000 0.96 2575 145 0.1868 0.2302 REMARK 3 27 2.1000 - 2.0800 0.96 2591 118 0.1938 0.2319 REMARK 3 28 2.0800 - 2.0500 0.96 2593 143 0.1915 0.2812 REMARK 3 29 2.0500 - 2.0300 0.90 2402 127 0.2958 0.3008 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) : 0.209 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.903 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 31.17 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.11 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 : 0.004 6834 REMARK 3 ANGLE : 0.670 9300 REMARK 3 CHIRALITY : 0.050 1065 REMARK 3 PLANARITY : 0.006 1179 REMARK 3 DIHEDRAL : 11.886 2438 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 9MRZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291428. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-SEP-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : ROTATING ANODE REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : RIGAKU REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.54 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80829 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030 REMARK 200 RESOLUTION RANGE LOW (A) : 44.790 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 26.4300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.33000 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: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.89 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CHES, PH 9.5, 0.2 M SODIUM REMARK 280 CHLORIDE, 1.26 M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.66450 REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4760 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19720 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: l, h 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4580 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19470 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 CYS h 216 REMARK 465 ASP h 217 REMARK 465 LYS h 218 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS l 194 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 CYS L 194 CA - CB - SG ANGL. DEV. = 7.2 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LYS l 30 -125.10 54.37 REMARK 500 ALA l 51 -37.49 71.52 REMARK 500 ALA l 84 -179.05 -171.59 REMARK 500 ARG h 66 10.61 -141.50 REMARK 500 ALA h 100c -122.65 -128.86 REMARK 500 ALA h 100d -105.59 -116.79 REMARK 500 ALA H 100d -82.83 -76.28 REMARK 500 LYS L 30 -120.20 51.64 REMARK 500 ALA L 51 -39.19 71.85 REMARK 500 ALA L 84 172.31 172.83 REMARK 500 ASN L 138 68.29 61.60 REMARK 500 REMARK 500 REMARK: NULL DBREF 9MRZ l 1 212 PDB 9MRZ 9MRZ 1 212 DBREF 9MRZ h 1 218 PDB 9MRZ 9MRZ 1 218 DBREF 9MRZ H 1 218 PDB 9MRZ 9MRZ 1 218 DBREF 9MRZ L 1 212 PDB 9MRZ 9MRZ 1 212 SEQRES 1 l 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 l 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 l 212 GLU ASN VAL LYS ASN TYR LEU HIS TRP TYR GLN GLN LYS SEQRES 4 l 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 l 212 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 l 212 GLY SER GLY THR ASP PHE ILE LEU THR ILE SER SER LEU SEQRES 7 l 212 GLN SER GLU ASP VAL ALA THR TYR TYR CYS GLN HIS SER SEQRES 8 l 212 TYR ASP THR PRO TYR SER PHE GLY GLN GLY THR LYS VAL SEQRES 9 l 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 l 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 l 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 l 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 l 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 l 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 l 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 l 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 l 212 ARG GLY GLU CYS SEQRES 1 h 235 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 h 235 PRO GLY ALA SER VAL ARG LEU SER CYS LYS ALA SER GLY SEQRES 3 h 235 PHE THR PHE SER ILE SER ALA ILE GLY TRP VAL ARG GLN SEQRES 4 h 235 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE ILE SEQRES 5 h 235 PRO LEU VAL GLY ILE THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 h 235 GLY ARG VAL THR ILE THR ALA ASP THR SER THR SER THR SEQRES 7 h 235 ALA TYR MET ASP LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 h 235 ALA VAL TYR TYR CYS ALA ARG GLY ASP SER LYS LEU GLN SEQRES 9 h 235 SER VAL ALA ALA GLY GLY THR GLU GLY GLY ASN GLY LEU SEQRES 10 h 235 ASP SER TRP GLY GLN GLY VAL VAL VAL THR VAL SER SER SEQRES 11 h 235 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 h 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 h 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 h 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 h 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 h 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 h 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 h 235 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 19 h 235 LYS SEQRES 1 H 235 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 235 PRO GLY ALA SER VAL ARG LEU SER CYS LYS ALA SER GLY SEQRES 3 H 235 PHE THR PHE SER ILE SER ALA ILE GLY TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE ILE SEQRES 5 H 235 PRO LEU VAL GLY ILE THR ASN TYR ALA GLN LYS PHE GLN SEQRES 6 H 235 GLY ARG VAL THR ILE THR ALA ASP THR SER THR SER THR SEQRES 7 H 235 ALA TYR MET ASP LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 235 ALA VAL TYR TYR CYS ALA ARG GLY ASP SER LYS LEU GLN SEQRES 9 H 235 SER VAL ALA ALA GLY GLY THR GLU GLY GLY ASN GLY LEU SEQRES 10 H 235 ASP SER TRP GLY GLN GLY VAL VAL VAL THR VAL SER SER SEQRES 11 H 235 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 H 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 H 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 H 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 H 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 H 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 H 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 H 235 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS ASP SEQRES 19 H 235 LYS SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLU ASN VAL LYS ASN TYR LEU HIS TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 L 212 THR LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR ASP PHE ILE LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN SER GLU ASP VAL ALA THR TYR TYR CYS GLN HIS SER SEQRES 8 L 212 TYR ASP THR PRO TYR SER PHE GLY GLN GLY THR LYS VAL SEQRES 9 L 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 L 212 ARG GLY GLU CYS HET PCA h 1 8 HET PCA H 1 8 HET SO4 l 301 5 HET SO4 l 302 5 HET NHE h 301 13 HET SO4 h 302 5 HET NHE H 301 13 HET SO4 H 302 5 HET SO4 H 303 5 HET SO4 L 301 5 HET SO4 L 302 5 HET SO4 L 303 5 HETNAM PCA PYROGLUTAMIC ACID HETNAM SO4 SULFATE ION HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID HETSYN NHE N-CYCLOHEXYLTAURINE; CHES FORMUL 2 PCA 2(C5 H7 N O3) FORMUL 5 SO4 8(O4 S 2-) FORMUL 7 NHE 2(C8 H17 N O3 S) FORMUL 15 HOH *729(H2 O) HELIX 1 AA1 GLN l 79 VAL l 83 5 5 HELIX 2 AA2 SER l 121 LYS l 126 1 6 HELIX 3 AA3 LYS l 183 LYS l 188 1 6 HELIX 4 AA4 THR h 28 SER h 32 5 5 HELIX 5 AA5 GLN h 61 GLN h 64 5 4 HELIX 6 AA6 ARG h 83 THR h 87 5 5 HELIX 7 AA7 SER h 156 ALA h 158 5 3 HELIX 8 AA8 SER h 187 LEU h 189 5 3 HELIX 9 AA9 LYS h 201 ASN h 204 5 4 HELIX 10 AB1 GLN H 61 GLN H 64 5 4 HELIX 11 AB2 ARG H 83 THR H 87 5 5 HELIX 12 AB3 SER H 156 ALA H 158 5 3 HELIX 13 AB4 SER H 187 LEU H 189 5 3 HELIX 14 AB5 LYS H 201 ASN H 204 5 4 HELIX 15 AB6 GLN L 79 VAL L 83 5 5 HELIX 16 AB7 SER L 121 LYS L 126 1 6 HELIX 17 AB8 LYS L 183 HIS L 189 1 7 SHEET 1 AA1 4 MET l 4 SER l 7 0 SHEET 2 AA1 4 VAL l 19 ALA l 25 -1 O ARG l 24 N THR l 5 SHEET 3 AA1 4 ASP l 70 ILE l 75 -1 O LEU l 73 N ILE l 21 SHEET 4 AA1 4 PHE l 62 GLY l 66 -1 N SER l 63 O THR l 74 SHEET 1 AA2 6 SER l 10 ALA l 13 0 SHEET 2 AA2 6 THR l 102 ILE l 106 1 O GLU l 105 N LEU l 11 SHEET 3 AA2 6 THR l 85 HIS l 90 -1 N TYR l 86 O THR l 102 SHEET 4 AA2 6 LEU l 33 GLN l 38 -1 N TYR l 36 O TYR l 87 SHEET 5 AA2 6 LYS l 45 TYR l 49 -1 O ILE l 48 N TRP l 35 SHEET 6 AA2 6 THR l 53 LEU l 54 -1 O THR l 53 N TYR l 49 SHEET 1 AA3 4 SER l 10 ALA l 13 0 SHEET 2 AA3 4 THR l 102 ILE l 106 1 O GLU l 105 N LEU l 11 SHEET 3 AA3 4 THR l 85 HIS l 90 -1 N TYR l 86 O THR l 102 SHEET 4 AA3 4 SER l 97 PHE l 98 -1 O SER l 97 N HIS l 90 SHEET 1 AA4 4 SER l 114 PHE l 118 0 SHEET 2 AA4 4 THR l 129 PHE l 139 -1 O LEU l 135 N PHE l 116 SHEET 3 AA4 4 TYR l 173 SER l 182 -1 O LEU l 181 N ALA l 130 SHEET 4 AA4 4 SER l 159 VAL l 163 -1 N SER l 162 O SER l 176 SHEET 1 AA5 4 ALA l 153 LEU l 154 0 SHEET 2 AA5 4 LYS l 145 VAL l 150 -1 N VAL l 150 O ALA l 153 SHEET 3 AA5 4 VAL l 191 GLN l 198 -1 O GLU l 195 N GLN l 147 SHEET 4 AA5 4 THR l 201 ASN l 208 -1 O VAL l 203 N VAL l 196 SHEET 1 AA6 4 GLN h 3 GLN h 6 0 SHEET 2 AA6 4 VAL h 18 SER h 25 -1 O LYS h 23 N VAL h 5 SHEET 3 AA6 4 THR h 77 LEU h 82 -1 O MET h 80 N LEU h 20 SHEET 4 AA6 4 VAL h 67 ASP h 72 -1 N THR h 70 O TYR h 79 SHEET 1 AA7 6 GLU h 10 LYS h 12 0 SHEET 2 AA7 6 VAL h 107 VAL h 111 1 O THR h 110 N LYS h 12 SHEET 3 AA7 6 ALA h 88 SER h 97 -1 N TYR h 90 O VAL h 107 SHEET 4 AA7 6 ALA h 33 GLN h 39 -1 N VAL h 37 O TYR h 91 SHEET 5 AA7 6 LEU h 45 ILE h 52 -1 O ILE h 51 N ILE h 34 SHEET 6 AA7 6 ILE h 56 TYR h 59 -1 O ASN h 58 N GLU h 50 SHEET 1 AA8 4 GLU h 10 LYS h 12 0 SHEET 2 AA8 4 VAL h 107 VAL h 111 1 O THR h 110 N LYS h 12 SHEET 3 AA8 4 ALA h 88 SER h 97 -1 N TYR h 90 O VAL h 107 SHEET 4 AA8 4 GLU h 100H TRP h 103 -1 O GLY h 100I N ASP h 96 SHEET 1 AA9 4 SER h 120 LEU h 124 0 SHEET 2 AA9 4 THR h 135 TYR h 145 -1 O LEU h 141 N PHE h 122 SHEET 3 AA9 4 TYR h 176 PRO h 185 -1 O LEU h 178 N VAL h 142 SHEET 4 AA9 4 VAL h 163 THR h 165 -1 N HIS h 164 O VAL h 181 SHEET 1 AB1 4 SER h 120 LEU h 124 0 SHEET 2 AB1 4 THR h 135 TYR h 145 -1 O LEU h 141 N PHE h 122 SHEET 3 AB1 4 TYR h 176 PRO h 185 -1 O LEU h 178 N VAL h 142 SHEET 4 AB1 4 VAL h 169 LEU h 170 -1 N VAL h 169 O SER h 177 SHEET 1 AB2 3 THR h 151 TRP h 154 0 SHEET 2 AB2 3 ILE h 195 HIS h 200 -1 O ASN h 197 N SER h 153 SHEET 3 AB2 3 THR h 205 LYS h 210 -1 O VAL h 207 N VAL h 198 SHEET 1 AB3 4 GLN H 3 GLN H 6 0 SHEET 2 AB3 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AB3 4 THR H 77 LEU H 82 -1 O MET H 80 N LEU H 20 SHEET 4 AB3 4 VAL H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AB4 6 GLU H 10 LYS H 12 0 SHEET 2 AB4 6 VAL H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AB4 6 ALA H 88 ASP H 96 -1 N TYR H 90 O VAL H 107 SHEET 4 AB4 6 SER H 32 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AB4 6 GLU H 46 ILE H 51 -1 O ILE H 51 N ILE H 34 SHEET 6 AB4 6 THR H 57 TYR H 59 -1 O ASN H 58 N GLU H 50 SHEET 1 AB5 4 GLU H 10 LYS H 12 0 SHEET 2 AB5 4 VAL H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AB5 4 ALA H 88 ASP H 96 -1 N TYR H 90 O VAL H 107 SHEET 4 AB5 4 SER H 102 TRP H 103 -1 O SER H 102 N ARG H 94 SHEET 1 AB6 4 SER H 120 LEU H 124 0 SHEET 2 AB6 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB6 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB6 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AB7 4 SER H 120 LEU H 124 0 SHEET 2 AB7 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AB7 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AB7 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AB8 3 THR H 151 TRP H 154 0 SHEET 2 AB8 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AB8 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AB9 4 MET L 4 SER L 7 0 SHEET 2 AB9 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB9 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB9 4 PHE L 62 GLY L 66 -1 N SER L 63 O THR L 74 SHEET 1 AC1 6 SER L 10 SER L 14 0 SHEET 2 AC1 6 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AC1 6 ALA L 84 HIS L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AC1 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AC1 6 LYS L 45 TYR L 49 -1 O ILE L 48 N TRP L 35 SHEET 6 AC1 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AC2 4 SER L 10 SER L 14 0 SHEET 2 AC2 4 THR L 102 LYS L 107 1 O GLU L 105 N LEU L 11 SHEET 3 AC2 4 ALA L 84 HIS L 90 -1 N ALA L 84 O VAL L 104 SHEET 4 AC2 4 SER L 97 PHE L 98 -1 O SER L 97 N HIS L 90 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 181 N ALA L 130 SHEET 4 AC3 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 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 GLN L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AC4 4 THR L 201 ASN L 208 -1 O VAL L 203 N VAL L 196 SSBOND 1 CYS l 23 CYS l 88 1555 1555 2.06 SSBOND 2 CYS l 134 CYS l 194 1555 1555 2.02 SSBOND 3 CYS h 22 CYS h 92 1555 1555 2.05 SSBOND 4 CYS h 140 CYS h 196 1555 1555 2.03 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.06 SSBOND 6 CYS H 140 CYS H 196 1555 1555 2.04 SSBOND 7 CYS L 23 CYS L 88 1555 1555 2.08 SSBOND 8 CYS L 134 CYS L 194 1555 1555 2.05 LINK C PCA h 1 N VAL h 2 1555 1555 1.33 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 CISPEP 1 SER l 7 PRO l 8 0 -7.53 CISPEP 2 THR l 94 PRO l 95 0 -0.96 CISPEP 3 TYR l 140 PRO l 141 0 0.67 CISPEP 4 PHE h 146 PRO h 147 0 -8.24 CISPEP 5 GLU h 148 PRO h 149 0 0.25 CISPEP 6 PHE H 146 PRO H 147 0 -7.74 CISPEP 7 GLU H 148 PRO H 149 0 0.77 CISPEP 8 SER L 7 PRO L 8 0 -5.62 CISPEP 9 THR L 94 PRO L 95 0 -0.83 CISPEP 10 TYR L 140 PRO L 141 0 -2.07 CRYST1 88.889 73.329 99.685 90.00 94.23 90.00 P 1 21 1 4 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 0.011250 0.000000 0.000831 0.00000 SCALE2 0.000000 0.013637 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010059 0.00000