HEADER IMMUNE SYSTEM 26-MAR-15 4Z0X TITLE STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 ANTIGENIC TITLE 2 REGION 434-446 BOUND TO THE BROADLY NEUTRALIZING ANTIBODY HC26AM COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTIBODY HC26AM LIGHT CHAIN VARIABLE DOMAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTIBODY HC26AM HEAVY CHAIN VARIABLE DOMAIN; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HCV E2 ANTIGEN (RESIDUES 432-446); COMPND 11 CHAIN: C; COMPND 12 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: 469008; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 13 MOL_ID: 3; SOURCE 14 SYNTHETIC: YES; SOURCE 15 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS; SOURCE 16 ORGANISM_TAXID: 11103 KEYWDS HCV, BROADLY NEUTRALIZING ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR S.RANGARAJAN,R.A.MARIUZZA REVDAT 1 20-JUL-16 4Z0X 0 JRNL AUTH S.RANGARAJAN,R.A.MARIUZZA JRNL TITL STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 JRNL TITL 2 ANTIGENIC REGION 434-446 BOUND TO THE BROADLY NEUTRALIZING JRNL TITL 3 ANTIBODY HC26AM JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.19 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1 REMARK 3 NUMBER OF REFLECTIONS : 12367 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.230 REMARK 3 R VALUE (WORKING SET) : 0.226 REMARK 3 FREE R VALUE : 0.270 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.910 REMARK 3 FREE R VALUE TEST SET COUNT : 1226 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 4.1589 - 3.3015 1.00 1294 143 0.2065 0.2420 REMARK 3 2 3.3015 - 2.8843 1.00 1268 139 0.2147 0.2598 REMARK 3 3 2.8843 - 2.6206 0.98 1238 139 0.2274 0.2667 REMARK 3 4 2.6206 - 2.4328 0.97 1227 136 0.2457 0.3520 REMARK 3 5 2.4328 - 2.2894 0.96 1230 126 0.2442 0.2844 REMARK 3 6 2.2894 - 2.1747 0.96 1185 138 0.2276 0.2671 REMARK 3 7 2.1747 - 2.0801 0.94 1193 131 0.2364 0.3268 REMARK 3 8 2.0801 - 2.0000 0.92 1134 120 0.2381 0.2831 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) : 0.260 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.420 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 1849 REMARK 3 ANGLE : 1.392 2514 REMARK 3 CHIRALITY : 0.073 272 REMARK 3 PLANARITY : 0.005 323 REMARK 3 DIHEDRAL : 12.579 648 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 4Z0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-15. REMARK 100 THE DEPOSITION ID IS D_1000204735. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 10-SEP-14 REMARK 200 TEMPERATURE (KELVIN) : 298 REMARK 200 PH : 4-4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS REMARK 200 BEAMLINE : X29A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.075 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15612 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 41.190 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 12.70 REMARK 200 R MERGE (I) : 0.14500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.8000 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: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 30.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.73 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHAT MONOBASIC, POTASSIUM REMARK 280 PHOSPHATE DIBASIC, SODIUM PHOSPHATE DIBASIC/CITRIC ACID, PH 4.2, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.36000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.83000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.53500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.83000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.36000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.53500 REMARK 290 SMTRY3 4 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: 2670 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 11010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 O HOH B 229 O HOH B 230 0.33 REMARK 500 HZ2 LYS C 446 O HOH C 501 1.28 REMARK 500 H SER B 146 O HOH B 201 1.28 REMARK 500 O HOH A 263 O HOH A 268 1.88 REMARK 500 NE ARG A 38 O HOH A 201 1.91 REMARK 500 N SER B 146 O HOH B 201 1.93 REMARK 500 N SER B 32 O HOH B 202 1.95 REMARK 500 NH2 ARG A 38 O HOH A 201 1.96 REMARK 500 SD MET A 80 O HOH A 260 1.97 REMARK 500 NZ LYS C 446 O HOH C 501 1.99 REMARK 500 CZ ARG A 38 O HOH A 201 2.00 REMARK 500 O HOH B 207 O HOH B 224 2.09 REMARK 500 O GLY B 88 O HOH B 203 2.14 REMARK 500 OE1 GLU B 71 O HOH B 204 2.16 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 OE1 GLN A 16 O VAL B 30 3544 2.19 REMARK 500 REMARK 500 REMARK: NULL 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 GLY A 67 N - CA - C ANGL. DEV. = -17.6 DEGREES REMARK 500 VAL B 30 CB - CA - C ANGL. DEV. = -21.0 DEGREES REMARK 500 GLN B 31 N - CA - CB ANGL. DEV. = -11.6 DEGREES REMARK 500 GLN B 31 N - CA - C ANGL. DEV. = 24.9 DEGREES REMARK 500 CYS B 121 CA - CB - SG ANGL. DEV. = 10.2 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 ASP A 50 -51.99 70.52 REMARK 500 VAL B 30 139.28 70.18 REMARK 500 SER B 50 -123.28 126.52 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 SER B 50 GLY B 51 -149.24 REMARK 500 REMARK 500 REMARK: NULL DBREF 4Z0X A 2 106 PDB 4Z0X 4Z0X 2 106 DBREF 4Z0X B 27 147 PDB 4Z0X 4Z0X 27 147 DBREF 4Z0X C 435 446 PDB 4Z0X 4Z0X 435 446 SEQRES 1 A 105 TYR VAL LEU THR GLN PRO PRO SER VAL SER VAL ALA PRO SEQRES 2 A 105 GLY GLN THR ALA SER ILE THR CYS SER GLY ASP LYS LEU SEQRES 3 A 105 GLY ASP LYS TYR VAL SER TRP TYR GLN GLN ARG PRO GLY SEQRES 4 A 105 GLN SER PRO VAL LEU VAL LEU TYR GLN ASP SER LYS ARG SEQRES 5 A 105 PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SER SEQRES 6 A 105 GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN ALA SEQRES 7 A 105 MET ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP SER SEQRES 8 A 105 SER ALA LEU VAL PHE GLY GLY GLY THR LYS LEU THR VAL SEQRES 9 A 105 LEU SEQRES 1 B 121 VAL GLN PRO VAL GLN SER GLY ALA GLU VAL LYS LYS PRO SEQRES 2 B 121 GLY SER SER VAL LYS VAL SER CYS GLU ALA SER GLY GLY SEQRES 3 B 121 THR HIS SER ASN TYR VAL ILE THR TRP VAL ARG GLN ALA SEQRES 4 B 121 PRO GLY GLN GLY LEU GLU TRP MET GLY GLY PHE ILE PRO SEQRES 5 B 121 ASP PHE ARG THR ALA MET TYR ALA GLN GLY PHE GLN GLY SEQRES 6 B 121 ARG VAL THR ILE THR ALA ASP GLU SER THR SER LEU ALA SEQRES 7 B 121 TYR MET GLU LEU THR ASN LEU ARG SER GLU ASP THR ALA SEQRES 8 B 121 VAL TYR TYR CYS ALA ARG GLY PRO LEU SER ARG GLY TYR SEQRES 9 B 121 TYR ASP TYR TRP GLY PRO GLY THR LEU VAL THR VAL SER SEQRES 10 B 121 SER GLY SER THR SEQRES 1 C 12 THR GLY TRP LEU ALA GLY LEU PHE TYR GLN HIS LYS FORMUL 4 HOH *120(H2 O) HELIX 1 AA1 LYS A 26 LYS A 30 5 5 HELIX 2 AA2 GLN A 78 GLU A 82 5 5 HELIX 3 AA3 ARG B 112 THR B 116 5 5 HELIX 4 AA4 GLY C 436 TYR C 443 1 8 SHEET 1 AA1 5 SER A 9 VAL A 12 0 SHEET 2 AA1 5 THR A 101 VAL A 105 1 O THR A 104 N VAL A 12 SHEET 3 AA1 5 ALA A 83 TRP A 90 -1 N ALA A 83 O LEU A 103 SHEET 4 AA1 5 SER A 33 GLN A 37 -1 N GLN A 37 O ASP A 84 SHEET 5 AA1 5 VAL A 44 LEU A 47 -1 O VAL A 44 N GLN A 36 SHEET 1 AA2 4 SER A 9 VAL A 12 0 SHEET 2 AA2 4 THR A 101 VAL A 105 1 O THR A 104 N VAL A 12 SHEET 3 AA2 4 ALA A 83 TRP A 90 -1 N ALA A 83 O LEU A 103 SHEET 4 AA2 4 LEU A 95 PHE A 97 -1 O VAL A 96 N ALA A 89 SHEET 1 AA3 3 ALA A 18 SER A 23 0 SHEET 2 AA3 3 THR A 69 ILE A 74 -1 O ILE A 74 N ALA A 18 SHEET 3 AA3 3 PHE A 61 SER A 66 -1 N SER A 62 O THR A 73 SHEET 1 AA4 6 ALA B 34 LYS B 37 0 SHEET 2 AA4 6 THR B 138 VAL B 142 1 O LEU B 139 N GLU B 35 SHEET 3 AA4 6 ALA B 117 ARG B 123 -1 N ALA B 117 O VAL B 140 SHEET 4 AA4 6 ILE B 59 GLN B 64 -1 N VAL B 62 O TYR B 120 SHEET 5 AA4 6 LEU B 70 PHE B 76 -1 O PHE B 76 N ILE B 59 SHEET 6 AA4 6 ALA B 83 TYR B 85 -1 O MET B 84 N GLY B 75 SHEET 1 AA5 4 ALA B 34 LYS B 37 0 SHEET 2 AA5 4 THR B 138 VAL B 142 1 O LEU B 139 N GLU B 35 SHEET 3 AA5 4 ALA B 117 ARG B 123 -1 N ALA B 117 O VAL B 140 SHEET 4 AA5 4 TYR B 133 TRP B 134 -1 O TYR B 133 N ARG B 123 SHEET 1 AA6 3 VAL B 43 SER B 46 0 SHEET 2 AA6 3 ALA B 104 LEU B 108 -1 O MET B 106 N VAL B 45 SHEET 3 AA6 3 VAL B 93 ALA B 97 -1 N THR B 96 O TYR B 105 SSBOND 1 CYS A 22 CYS A 87 1555 1555 2.03 SSBOND 2 CYS B 47 CYS B 121 1555 1555 1.85 CRYST1 50.720 51.070 69.660 90.00 90.00 90.00 P 21 21 21 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 0.019716 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019581 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014355 0.00000