HEADER IMMUNE SYSTEM 26-APR-04 1T3F TITLE THREE DIMENSIONAL STRUCTURE OF A HUMANIZED ANTI-IFN-GAMMA TITLE 2 FAB (HUZAF) IN P21 21 21 SPACE GROUP COMPND MOL_ID: 1; COMPND 2 MOLECULE: HUZAF ANTIBODY LIGHT CHAIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: THE SOURCE IS ENGINEERED HUMAN CONSTANT AND COMPND 6 FRAMEWORK REGIONS WITH CDRS FROM MOUSE; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HUZAF ANTIBODY HEAVY CHAIN; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: THE SOURCE IS ENGINEERED HUMAN CONSTANT AND COMPND 12 FRAMEWORK REGIONS WITH CDRS FROM MOUSE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 6 ORGANISM_COMMON: HUMAN KEYWDS ANTIBODY ENGINEERING, HUMANIZED AND CHIMERIC ANTIBODY, FAB, KEYWDS 2 X-RAY STRUCTURE, GAMMA-INTERFERON, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR P.C.BOURNE,S.S.TERZYAN,G.CLOUD,N.F.LANDOLFI,M.VASQUEZ, AUTHOR 2 A.B.EDMUNDSON REVDAT 1 05-OCT-04 1T3F 0 JRNL AUTH P.C.BOURNE,S.S.TERZYAN,G.CLOUD,N.F.LANDOLFI, JRNL AUTH 2 M.VASQUEZ,A.B.EDMUNDSON JRNL TITL THREE-DIMENSIONAL STRUCTURES OF A HUMANIZED JRNL TITL 2 ANTI-IFN-GAMMA FAB (HUZAF) IN TWO CRYSTAL FORMS. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 1761 2004 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.1.24 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4 REMARK 3 NUMBER OF REFLECTIONS : 29067 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 + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.172 REMARK 3 FREE R VALUE : 0.222 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1547 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH : 2.00 REMARK 3 BIN RESOLUTION RANGE LOW : 2.05 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2213 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2000 REMARK 3 BIN FREE R VALUE SET COUNT : 121 REMARK 3 BIN FREE R VALUE : 0.2660 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 ALL ATOMS : 3702 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 25.13 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.07 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.05000 REMARK 3 B22 (A**2) : -0.68000 REMARK 3 B33 (A**2) : 0.64000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.186 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.168 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.796 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3384 ; 0.015 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): 2909 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4610 ; 1.504 ; 1.949 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6842 ; 0.846 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 432 ; 6.813 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 518 ; 0.093 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3767 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 654 ; 0.003 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 567 ; 0.209 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3381 ; 0.259 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 1977 ; 0.085 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 318 ; 0.169 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 8 ; 0.168 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 36 ; 0.326 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.166 ; 0.200 REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2161 ; 0.871 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3506 ; 1.616 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1223 ; 2.317 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1104 ; 3.840 ; 4.500 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 0 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 0 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1T3F COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB . REMARK 100 THE RCSB ID CODE IS RCSB022262. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : NULL REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 5.00 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) : 1.54 REMARK 200 MONOCHROMATOR : OSMIC BLUE OPTICS REMARK 200 OPTICS : OSMIC BLUE OPTICS REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30615 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 88.5 REMARK 200 DATA REDUNDANCY : 3.000 REMARK 200 R MERGE (I) : 0.05500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.31300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.150 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: PDB ENTRY 1B4J REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.60 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, SODIUM CITRATE, PH 5, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K 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 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-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 SMTRY1 2 -1.000000 0.000000 0.000000 32.19500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.32150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.13700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.32150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.19500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.13700 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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE 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 APPLY THE FOLLOWING TO CHAINS: A, B 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 REMARK 500 OE1 GLN A 147 O HOH 394 2.16 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 ASN A 138 CG ASN A 138 OD1 0.099 REMARK 500 ASN A 138 CG ASN A 138 ND2 -0.115 REMARK 500 VAL B 20 CB VAL B 20 CG1 -0.104 REMARK 500 THR B 78 CB THR B 78 CG2 -0.138 REMARK 500 MET B 81 SD MET B 81 CE -0.182 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 M RES CSSEQI PSI PHI REMARK 500 ALA A 51 -35.76 76.32 REMARK 500 GLU A 213 -76.55 144.39 REMARK 500 SER B 134 -112.94 166.05 REMARK 500 THR B 135 -163.88 22.97 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1T04 RELATED DB: PDB REMARK 900 STRUCTURE OF A HUMANIZED ANTI-IFN-GAMMA FAB (HUZAF) IN C2 REMARK 900 RELATED ID: 1B2W RELATED DB: PDB REMARK 900 HUMANIZED FAB OF AN ANTI-GAMMA-INTERFERON ANTIBODY REMARK 900 RELATED ID: 1B4J RELATED DB: PDB REMARK 900 CHIMERIC FAB OF AN ANTI-GAMMA-INTERFERON ANTIBODY REMARK 999 REMARK 999 SEQUENCE REMARK 999 THERE IS NO SEQUENCE DATABASE REFERENCE FOR THIS ENTRY. REMARK 999 THE SEQUENCE WAS DETERMINED IN THE PROTEIN DESIGN REMARK 999 LABORATORY. SEQRES 1 A 214 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 A 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER SEQRES 3 A 214 GLU ASN VAL ASP THR TYR VAL SER TRP TYR GLN GLN LYS SEQRES 4 A 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR GLY ALA SER SEQRES 5 A 214 ASN ARG TYR THR GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 A 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 A 214 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLY GLN SER SEQRES 8 A 214 TYR ASN TYR PRO PHE THR PHE GLY GLN GLY THR LYS VAL SEQRES 9 A 214 GLU VAL LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 A 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 A 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 A 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 A 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 A 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 A 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 A 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 A 214 PHE ASN ARG GLY GLU CYS SEQRES 1 B 220 PCA VAL GLN LEU VAL GLN SER GLY ALA GLU LEU LYS LYS SEQRES 2 B 220 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 B 220 TYR ILE PHE THR SER SER TRP ILE ASN TRP VAL LYS GLN SEQRES 4 B 220 ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP SEQRES 5 B 220 PRO SER ASP GLY GLU VAL HIS TYR ASN GLN ASP PHE LYS SEQRES 6 B 220 ASP LYS ALA THR LEU THR VAL ASP LYS SER THR ASN THR SEQRES 7 B 220 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 B 220 ALA VAL TYR TYR CYS ALA ARG GLY PHE LEU PRO TRP PHE SEQRES 9 B 220 ALA ASP TRP GLY GLN GLY THR LEU VAL THR VAL SER SER SEQRES 10 B 220 ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SEQRES 11 B 220 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 12 B 220 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 13 B 220 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 14 B 220 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 15 B 220 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 16 B 220 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 17 B 220 THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS MODRES 1T3F PCA B 1 GLU PYROGLUTAMIC ACID HET PCA B 1 8 HETNAM PCA PYROGLUTAMIC ACID FORMUL 2 PCA C5 H7 N O3 FORMUL 3 HOH *403(H2 O) HELIX 1 1 GLN A 79 PHE A 83 5 5 HELIX 2 2 SER A 121 LYS A 126 1 6 HELIX 3 3 LYS A 183 GLU A 187 1 5 HELIX 4 4 ILE B 28 SER B 32 5 5 HELIX 5 5 GLN B 62 LYS B 65 5 4 HELIX 6 6 LYS B 74 THR B 76 5 3 HELIX 7 7 ARG B 87 THR B 91 5 5 HELIX 8 8 SER B 160 ALA B 162 5 3 HELIX 9 9 SER B 191 THR B 195 5 5 HELIX 10 10 LYS B 205 ASN B 208 5 4 SHEET 1 A 4 MET A 4 SER A 7 0 SHEET 2 A 4 VAL A 19 ALA A 25 -1 O THR A 22 N SER A 7 SHEET 3 A 4 ASP A 70 ILE A 75 -1 O LEU A 73 N ILE A 21 SHEET 4 A 4 PHE A 62 SER A 67 -1 N SER A 63 O THR A 74 SHEET 1 B 6 THR A 10 ALA A 13 0 SHEET 2 B 6 THR A 102 VAL A 106 1 O LYS A 103 N LEU A 11 SHEET 3 B 6 ALA A 84 GLN A 90 -1 N ALA A 84 O VAL A 104 SHEET 4 B 6 VAL A 33 GLN A 38 -1 N GLN A 38 O THR A 85 SHEET 5 B 6 LYS A 45 TYR A 49 -1 O LEU A 47 N TRP A 35 SHEET 6 B 6 ASN A 53 ARG A 54 -1 O ASN A 53 N TYR A 49 SHEET 1 C 4 THR A 10 ALA A 13 0 SHEET 2 C 4 THR A 102 VAL A 106 1 O LYS A 103 N LEU A 11 SHEET 3 C 4 ALA A 84 GLN A 90 -1 N ALA A 84 O VAL A 104 SHEET 4 C 4 THR A 97 PHE A 98 -1 O THR A 97 N GLN A 90 SHEET 1 D 4 SER A 114 PHE A 118 0 SHEET 2 D 4 THR A 129 PHE A 139 -1 O LEU A 135 N PHE A 116 SHEET 3 D 4 TYR A 173 SER A 182 -1 O TYR A 173 N PHE A 139 SHEET 4 D 4 SER A 159 VAL A 163 -1 N GLN A 160 O THR A 178 SHEET 1 E 4 ALA A 153 LEU A 154 0 SHEET 2 E 4 LYS A 145 VAL A 150 -1 N VAL A 150 O ALA A 153 SHEET 3 E 4 VAL A 191 THR A 197 -1 O GLU A 195 N GLN A 147 SHEET 4 E 4 VAL A 205 ASN A 210 -1 O VAL A 205 N VAL A 196 SHEET 1 F 4 GLN B 3 GLN B 6 0 SHEET 2 F 4 VAL B 18 SER B 25 -1 O LYS B 23 N VAL B 5 SHEET 3 F 4 THR B 78 LEU B 83 -1 O MET B 81 N VAL B 20 SHEET 4 F 4 ALA B 68 ASP B 73 -1 N THR B 71 O TYR B 80 SHEET 1 G 6 GLU B 10 LYS B 12 0 SHEET 2 G 6 THR B 111 VAL B 115 1 O THR B 114 N GLU B 10 SHEET 3 G 6 ALA B 92 GLY B 99 -1 N ALA B 92 O VAL B 113 SHEET 4 G 6 TRP B 33 GLN B 39 -1 N ASN B 35 O ALA B 97 SHEET 5 G 6 GLU B 46 ILE B 51 -1 O GLU B 46 N LYS B 38 SHEET 6 G 6 VAL B 58 TYR B 60 -1 O HIS B 59 N ARG B 50 SHEET 1 H 4 GLU B 10 LYS B 12 0 SHEET 2 H 4 THR B 111 VAL B 115 1 O THR B 114 N GLU B 10 SHEET 3 H 4 ALA B 92 GLY B 99 -1 N ALA B 92 O VAL B 113 SHEET 4 H 4 PHE B 104 TRP B 107 -1 O ASP B 106 N ARG B 98 SHEET 1 I 4 SER B 124 LEU B 128 0 SHEET 2 I 4 THR B 139 TYR B 149 -1 O LEU B 145 N PHE B 126 SHEET 3 I 4 TYR B 180 PRO B 189 -1 O LEU B 182 N VAL B 146 SHEET 4 I 4 VAL B 167 THR B 169 -1 N HIS B 168 O VAL B 185 SHEET 1 J 4 SER B 124 LEU B 128 0 SHEET 2 J 4 THR B 139 TYR B 149 -1 O LEU B 145 N PHE B 126 SHEET 3 J 4 TYR B 180 PRO B 189 -1 O LEU B 182 N VAL B 146 SHEET 4 J 4 VAL B 173 LEU B 174 -1 N VAL B 173 O SER B 181 SHEET 1 K 3 THR B 155 TRP B 158 0 SHEET 2 K 3 ILE B 199 HIS B 204 -1 O ASN B 201 N SER B 157 SHEET 3 K 3 THR B 209 LYS B 214 -1 O VAL B 211 N VAL B 202 SSBOND 1 CYS A 23 CYS A 88 SSBOND 2 CYS A 134 CYS A 194 SSBOND 3 CYS A 214 CYS B 220 SSBOND 4 CYS B 22 CYS B 96 SSBOND 5 CYS B 144 CYS B 200 CISPEP 1 SER A 7 PRO A 8 0 -5.78 CISPEP 2 TYR A 94 PRO A 95 0 -0.01 CISPEP 3 TYR A 140 PRO A 141 0 1.46 CISPEP 4 PHE B 150 PRO B 151 0 -12.75 CISPEP 5 GLU B 152 PRO B 153 0 -5.76 CRYST1 64.390 74.274 104.643 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 0.015530 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013464 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009556 0.00000