HEADER IMMUNE SYSTEM 30-MAR-13 4BH8 TITLE CRYSTAL STRUCTURE OF GERMLINE ANTIBODY 36-65 IN COMPLEX TITLE 2 WITH PEPTIDE GDPRPSYISHLL COMPND MOL_ID: 1; COMPND 2 MOLECULE: ANTI-ARS MURINE GERMLINE MONOCLONAL ANTIBODY 36-65; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: ANTIGEN BINDING FRAGMENT; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: ANTI-ARS MURINE GERMLINE MONOCLONAL ANTIBODY 36-65; COMPND 7 CHAIN: B; COMPND 8 FRAGMENT: ANTIGEN BINDING FRAGMENT; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: DODECAPEPTIDE ANTIGEN; COMPND 11 CHAIN: P SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 STRAIN: BALB/C; SOURCE 6 CELL_LINE: 36-65 HYBRIDOMA; SOURCE 7 ORGAN: SPLEEN; SOURCE 8 CELL: B CELL; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 11 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 12 ORGANISM_TAXID: 10090; SOURCE 13 STRAIN: BALB/C; SOURCE 14 CELL_LINE: 36-65 HYBRIDOMA; SOURCE 15 ORGAN: SPLEEN; SOURCE 16 CELL: B CELL; SOURCE 17 MOL_ID: 3; SOURCE 18 SYNTHETIC: YES; SOURCE 19 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 20 ORGANISM_TAXID: 32630 KEYWDS IMMUNE SYSTEM, GERMLINE ANTIBODY, ANTIBODY POLYSPECIFICTY EXPDTA X-RAY DIFFRACTION AUTHOR T.KHAN,D.M.SALUNKE REVDAT 1 16-APR-14 4BH8 0 JRNL AUTH T.KHAN,D.M.SALUNKE JRNL TITL ADJUSTABLE LOCKS AND FLEXIBLE KEYS: PLASTICITY OF EPITOPE- JRNL TITL 2 PARATOPE INTERACTIONS IN GERMLINE ANTIBODIES. JRNL REF J.IMMUNOL. 2014 JRNL REFN ESSN 1550-6606 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS 1.2 REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.4 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 18818 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.2305 REMARK 3 FREE R VALUE : 0.2510 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.8 REMARK 3 FREE R VALUE TEST SET COUNT : 1842 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 6 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.4 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.55 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.5 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2664 REMARK 3 BIN R VALUE (WORKING SET) : 0.34 REMARK 3 BIN FREE R VALUE : 0.35 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.8 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 291 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3379 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 190 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 32 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.042 REMARK 3 B22 (A**2) : 3.742 REMARK 3 B33 (A**2) : -1.700 REMARK 3 B12 (A**2) : 0.000 REMARK 3 B13 (A**2) : -1.607 REMARK 3 B23 (A**2) : 0.000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25 REMARK 3 ESD FROM SIGMAA (A) : 0.23 REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.0 REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27 REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007262 REMARK 3 BOND ANGLES (DEGREES) : 1.69316 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.6 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.06 REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.4 REMARK 3 BSOL : 21.262 REMARK 3 REMARK 3 NCS MODEL : NULL REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 2 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 3 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 4 POSITIONAL (A) : NULL ; NULL REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP REMARK 3 TOPOLOGY FILE 2 : WATER.TOP REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 4BH8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-13. REMARK 100 THE PDBE ID CODE IS EBI-53332. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-APR-09 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : 6.7 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 RU300 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418 REMARK 200 MONOCHROMATOR : NI FILTER CMF12 38CU-6 REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19076 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.40 REMARK 200 RESOLUTION RANGE LOW (A) : 58.00 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 4.5 REMARK 200 R MERGE (I) : 0.10 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.00 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.5 REMARK 200 R MERGE FOR SHELL (I) : 0.40 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.20 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 2A6J REMARK 200 REMARK 200 REMARK: NO REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.4 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M SODIUM CACODYLATE, PH REMARK 280 6.7, 21% PEG 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 38.48500 REMARK 290 SMTRY3 2 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: 5340 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 24360 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.2 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P 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 ALA B 138 REMARK 465 GLN B 139 REMARK 465 THR B 140 REMARK 465 ASN B 141 REMARK 465 GLY P -2 REMARK 465 ASP P -1 REMARK 465 PRO P 0 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 CYS A 214 CB SG REMARK 470 ALA B 137 CB REMARK 470 LEU B 178 CG CD1 CD2 REMARK 470 THR B 200 CG2 REMARK 470 LEU P 9 CA C O CB CG CD1 CD2 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 ASN A 31 N GLY A 51 2.15 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 THR A 43 N - CA - C ANGL. DEV. = 18.4 DEGREES REMARK 500 SER P 3 N - CA - C ANGL. DEV. = 20.5 DEGREES REMARK 500 TYR P 4 N - CA - C ANGL. DEV. = -24.5 DEGREES REMARK 500 ILE P 5 N - CA - C ANGL. DEV. = 19.4 DEGREES REMARK 500 HIS P 7 N - CA - C ANGL. DEV. = 16.6 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 CYS A 23 134.46 -170.90 REMARK 500 ASP A 41 -51.45 -127.32 REMARK 500 THR A 43 -70.64 49.84 REMARK 500 TYR A 50 113.31 64.17 REMARK 500 SER A 56 -25.23 -149.68 REMARK 500 THR A 77 73.27 57.02 REMARK 500 ALA A 84 -172.82 -173.13 REMARK 500 LYS A 169 -66.62 -93.36 REMARK 500 ASN A 190 -61.16 -108.84 REMARK 500 PRO B 41 -21.91 -39.35 REMARK 500 GLN B 43 -75.19 124.85 REMARK 500 ALA B 92 -179.97 -172.36 REMARK 500 SER B 105 -159.32 -131.80 REMARK 500 GLN B 179 76.84 -109.66 REMARK 500 SER B 180 65.45 73.27 REMARK 500 ASP B 181 -8.34 68.72 REMARK 500 ARG B 221 161.13 99.61 REMARK 500 PRO P 2 -154.19 -106.43 REMARK 500 SER P 3 -142.98 6.55 REMARK 500 TYR P 4 112.31 96.44 REMARK 500 ILE P 5 -60.84 -129.58 REMARK 500 HIS P 7 141.78 22.79 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CHIRAL CENTERS REMARK 500 REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16) REMARK 500 REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS REMARK 500 THR A 43 20.1 L L OUTSIDE RANGE REMARK 500 VAL A 44 24.0 L L OUTSIDE RANGE REMARK 500 SER P 3 20.5 L L OUTSIDE RANGE REMARK 500 TYR P 4 45.4 L L OUTSIDE RANGE REMARK 500 ILE P 5 21.5 L L OUTSIDE RANGE REMARK 500 HIS P 7 23.4 L L OUTSIDE RANGE REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4BH7 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF GERMLINE ANTIBODY 36-65 IN REMARK 900 COMPLEX WITH PEPTIDE PPYPAWHAPGNI DBREF 4BH8 A 1 214 PDB 4BH8 4BH8 1 214 DBREF 4BH8 B 1 222 PDB 4BH8 4BH8 1 222 DBREF 4BH8 P -2 9 PDB 4BH8 4BH8 -2 9 SEQRES 1 A 214 ASP ILE SER MET THR GLN GLY THR SER SER LEU SER ALA SEQRES 2 A 214 ARG LEU GLY ASP ARG VAL THR ILE SER CYS ARG ALA SER SEQRES 3 A 214 GLN ASP ILE SER ASN TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 A 214 PRO ASP GLY THR VAL SER LEU LEU ILE TYR TYR GLY SER SEQRES 5 A 214 ARG LEU HIS SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 214 GLY SER GLY THR ASP TYR SER LEU THR ILE SER THR LEU SEQRES 7 A 214 GLU GLN GLU ASP ILE ALA THR TYR PHE CYS GLN GLN GLY SEQRES 8 A 214 ASN THR LEU PRO ARG THR PHE GLY GLY GLY THR LYS LEU SEQRES 9 A 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE SEQRES 10 A 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SEQRES 11 A 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP SEQRES 12 A 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN SEQRES 13 A 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS SEQRES 14 A 214 ASP LYS THR TYR SER MET SER SER THR LEU THR LEU THR SEQRES 15 A 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU SEQRES 16 A 214 ALA THR HIS LYS LYS SER THR SER PRO ILE VAL LYS SER SEQRES 17 A 214 PHE ASN ARG ASN GLU CYS SEQRES 1 B 222 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 B 222 ALA GLY SER SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 B 222 TYR THR PHE THR SER TYR GLY ILE ASN TRP VAL LYS GLN SEQRES 4 B 222 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN SEQRES 5 B 222 PRO GLY ASN GLY TYR THR LYS TYR ASN GLU LYS PHE LYS SEQRES 6 B 222 GLY LYS THR THR LEU THR VAL ASP LYS SER SER SER THR SEQRES 7 B 222 ALA TYR MET GLN LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 B 222 ALA VAL TYR PHE CYS ALA ARG SER VAL TYR TYR GLY GLY SEQRES 9 B 222 SER TYR TYR PHE ASP TYR TRP GLY GLN GLY THR THR LEU SEQRES 10 B 222 THR VAL SER SER ALA LYS THR THR PRO PRO SER VAL TYR SEQRES 11 B 222 PRO LEU ALA PRO GLY SER ALA ALA GLN THR ASN SER MET SEQRES 12 B 222 VAL THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SEQRES 13 B 222 PRO VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SEQRES 14 B 222 GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU SEQRES 15 B 222 TYR THR LEU SER SER SER VAL THR VAL PRO SER SER PRO SEQRES 16 B 222 ARG PRO SER GLU THR VAL THR CYS ASN VAL ALA HIS PRO SEQRES 17 B 222 ALA SER SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG SEQRES 18 B 222 ASP SEQRES 1 P 12 GLY ASP PRO ARG PRO SER TYR ILE SER HIS LEU LEU FORMUL 4 HOH *190(H2 O) HELIX 1 1 GLU A 79 ILE A 83 5 5 HELIX 2 2 SER A 121 THR A 126 1 6 HELIX 3 3 LYS A 183 ARG A 188 1 6 HELIX 4 4 THR B 28 TYR B 32 5 5 HELIX 5 5 GLU B 62 PHE B 64 5 3 HELIX 6 6 THR B 87 SER B 91 5 5 HELIX 7 7 SER B 164 SER B 166 5 3 HELIX 8 8 PRO B 208 SER B 211 5 4 SHEET 1 AA 4 MET A 4 THR A 5 0 SHEET 2 AA 4 VAL A 19 ALA A 25 -1 O ARG A 24 N THR A 5 SHEET 3 AA 4 ASP A 70 ILE A 75 -1 O TYR A 71 N CYS A 23 SHEET 4 AA 4 PHE A 62 SER A 67 -1 O SER A 63 N THR A 74 SHEET 1 AB 4 SER A 10 ALA A 13 0 SHEET 2 AB 4 THR A 102 ILE A 106 1 O LYS A 103 N LEU A 11 SHEET 3 AB 4 THR A 85 GLN A 90 -1 O TYR A 86 N THR A 102 SHEET 4 AB 4 THR A 97 PHE A 98 1 O THR A 97 N GLN A 90 SHEET 1 AC 5 SER A 10 ALA A 13 0 SHEET 2 AC 5 THR A 102 ILE A 106 1 O LYS A 103 N LEU A 11 SHEET 3 AC 5 THR A 85 GLN A 90 -1 O TYR A 86 N THR A 102 SHEET 4 AC 5 LEU A 33 GLN A 38 -1 O ASN A 34 N GLN A 89 SHEET 5 AC 5 VAL A 44 ILE A 48 -1 O SER A 45 N GLN A 37 SHEET 1 AD 2 THR A 97 PHE A 98 0 SHEET 2 AD 2 THR A 85 GLN A 90 1 O GLN A 90 N THR A 97 SHEET 1 AE 4 THR A 114 PHE A 118 0 SHEET 2 AE 4 GLY A 129 PHE A 139 -1 O VAL A 133 N PHE A 118 SHEET 3 AE 4 TYR A 173 THR A 182 -1 O TYR A 173 N PHE A 139 SHEET 4 AE 4 VAL A 159 TRP A 163 -1 O LEU A 160 N THR A 178 SHEET 1 AF 4 SER A 153 ARG A 155 0 SHEET 2 AF 4 ASN A 145 ILE A 150 -1 O TRP A 148 N ARG A 155 SHEET 3 AF 4 SER A 191 THR A 197 -1 O THR A 193 N LYS A 149 SHEET 4 AF 4 ILE A 205 ASN A 210 -1 O ILE A 205 N ALA A 196 SHEET 1 BA 4 GLN B 3 GLN B 6 0 SHEET 2 BA 4 VAL B 18 SER B 25 -1 O LYS B 23 N GLN B 5 SHEET 3 BA 4 THR B 78 LEU B 83 -1 O ALA B 79 N CYS B 22 SHEET 4 BA 4 THR B 68 ASP B 73 -1 O THR B 69 N GLN B 82 SHEET 1 BB 4 GLU B 10 VAL B 12 0 SHEET 2 BB 4 THR B 115 VAL B 119 -1 O THR B 116 N GLU B 10 SHEET 3 BB 4 ALA B 92 TYR B 102 -1 O ALA B 92 N LEU B 117 SHEET 4 BB 4 SER B 105 TRP B 111 -1 O SER B 105 N TYR B 102 SHEET 1 BC 6 GLU B 10 VAL B 12 0 SHEET 2 BC 6 THR B 115 VAL B 119 -1 O THR B 116 N GLU B 10 SHEET 3 BC 6 ALA B 92 TYR B 102 -1 O ALA B 92 N LEU B 117 SHEET 4 BC 6 ILE B 34 GLN B 39 -1 O ASN B 35 N ALA B 97 SHEET 5 BC 6 GLU B 46 ASN B 52 -1 O GLU B 46 N LYS B 38 SHEET 6 BC 6 TYR B 57 TYR B 60 -1 O TYR B 57 N ASN B 52 SHEET 1 BD 2 SER B 105 TRP B 111 0 SHEET 2 BD 2 ALA B 92 TYR B 102 -1 O ARG B 98 N ASP B 109 SHEET 1 BE 4 SER B 128 LEU B 132 0 SHEET 2 BE 4 MET B 143 TYR B 153 -1 O GLY B 147 N LEU B 132 SHEET 3 BE 4 TYR B 183 PRO B 192 -1 O TYR B 183 N TYR B 153 SHEET 4 BE 4 VAL B 177 LEU B 178 1 O VAL B 177 N THR B 184 SHEET 1 BF 4 SER B 128 LEU B 132 0 SHEET 2 BF 4 MET B 143 TYR B 153 -1 O GLY B 147 N LEU B 132 SHEET 3 BF 4 TYR B 183 PRO B 192 -1 O TYR B 183 N TYR B 153 SHEET 4 BF 4 VAL B 171 THR B 173 -1 O HIS B 172 N SER B 188 SHEET 1 BG 2 VAL B 177 LEU B 178 0 SHEET 2 BG 2 TYR B 183 PRO B 192 1 O THR B 184 N VAL B 177 SHEET 1 BH 3 THR B 159 TRP B 162 0 SHEET 2 BH 3 THR B 202 HIS B 207 -1 O ASN B 204 N THR B 161 SHEET 3 BH 3 THR B 212 LYS B 217 -1 O THR B 212 N HIS B 207 SSBOND 1 CYS A 23 CYS A 88 1555 1555 2.04 SSBOND 2 CYS A 134 CYS A 194 1555 1555 2.03 SSBOND 3 CYS B 22 CYS B 96 1555 1555 2.04 SSBOND 4 CYS B 148 CYS B 203 1555 1555 2.03 CISPEP 1 LEU A 94 PRO A 95 0 -0.13 CISPEP 2 TYR A 140 PRO A 141 0 0.42 CISPEP 3 PHE B 154 PRO B 155 0 -0.05 CISPEP 4 GLU B 156 PRO B 157 0 0.37 CISPEP 5 ARG B 196 PRO B 197 0 1.96 CISPEP 6 ARG P 1 PRO P 2 0 -0.03 CRYST1 54.410 76.970 59.260 90.00 101.74 90.00 P 1 21 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 0.018379 0.000000 0.003819 0.00000 SCALE2 0.000000 0.012992 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017235 0.00000