HEADER PROTEIN BINDING 06-SEP-19 6SS2 TITLE STRUCTURE OF ARGINASE-2 IN COMPLEX WITH THE INHIBITORY HUMAN ANTIGEN- TITLE 2 BINDING FRAGMENT FAB C0021158 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARGINASE-2, MITOCHONDRIAL; COMPND 3 CHAIN: AAA; COMPND 4 SYNONYM: ARGINASE II,KIDNEY-TYPE ARGINASE,NON-HEPATIC ARGINASE,TYPE COMPND 5 II ARGINASE; COMPND 6 EC: 3.5.3.1; COMPND 7 ENGINEERED: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: FAB C0021158 HEAVY CHAIN (IGG1); COMPND 10 CHAIN: HHH; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 13 NUMBERING SCHEME.; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: FAB C0021158 LIGHT CHAIN (IGG1); COMPND 16 CHAIN: LLL; COMPND 17 ENGINEERED: YES; COMPND 18 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 19 NUMBERING SCHEME. RESIDUE 10 WOULD NOT BE PRESENT IN THE KABAT COMPND 20 SCHEME, BUT DUE TO PROBLEMS WITH NON-CONTINUOUS NUMBERING IN L- COMPND 21 PEPTIDES, WE INCLUDED IT. THEREFORE, RESIDUES 2-10 SHOULD BE READ AS COMPND 22 1-9, PER KABAT. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ARG2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 EXPRESSION_SYSTEM_VARIANT: EXPICHO; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 23 EXPRESSION_SYSTEM_VARIANT: EXPICHO; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 25 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB KEYWDS ARGINASE-2 INHIBITOR, IGG, ANTIGEN-BINDING FRAGMENT, PROTEIN BINDING EXPDTA X-RAY DIFFRACTION AUTHOR D.BURSCHOWSKY,A.ADDYMAN,S.FIEDLER,M.GROVES,S.HAYNES,C.SEEWOORUTHUN, AUTHOR 2 M.CARR JRNL AUTH M.AUSTIN,D.BURSCHOWSKY,D.T.Y.CHAN,L.JENKINSON,S.HAYNES, JRNL AUTH 2 A.DIAMANDAKIS,C.SEEWOORUTHUN,A.ADDYMAN,S.FIEDLER,S.RYMAN, JRNL AUTH 3 J.WHITEHOUSE,L.H.SLATER,A.V.HADJINICOLAOU,U.GILEADI, JRNL AUTH 4 E.GOWANS,Y.SHIBATA,M.BARNARD,T.KASERER,P.SHARMA,N.M.LUHESHI, JRNL AUTH 5 R.W.WILKINSON,T.J.VAUGHAN,S.V.HOLT,V.CERUNDOLO,M.D.CARR, JRNL AUTH 6 M.A.T.GROVES JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF C0021158, A JRNL TITL 2 HIGH-AFFINITY MONOCLONAL ANTIBODY THAT INHIBITS ARGINASE 2 JRNL TITL 3 FUNCTION VIA A NOVEL NON-COMPETITIVE MECHANISM OF ACTION. JRNL REF MABS V. 12 01230 JRNL REFN ESSN 1942-0870 JRNL PMID 32880207 JRNL DOI 10.1080/19420862.2020.1801230 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0253 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.37 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 39901 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.254 REMARK 3 FREE R VALUE : 0.284 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.952 REMARK 3 FREE R VALUE TEST SET COUNT : 1976 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2818 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0 REMARK 3 BIN R VALUE (WORKING SET) : 0.8470 REMARK 3 BIN FREE R VALUE SET COUNT : 160 REMARK 3 BIN FREE R VALUE : 0.7690 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5680 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 207 REMARK 3 SOLVENT ATOMS : 59 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.54 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.96900 REMARK 3 B22 (A**2) : 1.96900 REMARK 3 B33 (A**2) : -3.93800 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): 0.085 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.058 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.128 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.443 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5993 ; 0.005 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 5436 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8128 ; 1.413 ; 1.638 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12664 ; 1.137 ; 1.570 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 752 ; 7.536 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 251 ;34.509 ;22.550 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 915 ;17.550 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;12.136 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.054 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6525 ; 0.005 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1153 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 980 ; 0.189 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 60 ; 0.212 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2718 ; 0.156 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 164 ; 0.166 ; 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): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL 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): 3017 ; 1.026 ; 3.238 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3016 ; 1.023 ; 3.238 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3766 ; 1.704 ; 4.854 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3767 ; 1.704 ; 4.855 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2975 ; 1.393 ; 3.477 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2906 ; 1.122 ; 3.370 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4361 ; 1.593 ; 5.127 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4260 ; 1.418 ; 4.969 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL 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 : NULL REMARK 3 REMARK 3 TWIN DETAILS REMARK 3 NUMBER OF TWIN DOMAINS : 2 REMARK 3 TWIN DOMAIN : 1 REMARK 3 TWIN OPERATOR : H, K, L REMARK 3 TWIN FRACTION : 0.8011 REMARK 3 TWIN DOMAIN : 2 REMARK 3 TWIN OPERATOR : K, H, -L REMARK 3 TWIN FRACTION : 0.1989 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : AA 22 AA 341 REMARK 3 ORIGIN FOR THE GROUP (A): -10.4685 -21.2699 10.8871 REMARK 3 T TENSOR REMARK 3 T11: 0.0219 T22: 0.0199 REMARK 3 T33: 0.1948 T12: 0.0017 REMARK 3 T13: 0.0118 T23: 0.0336 REMARK 3 L TENSOR REMARK 3 L11: 0.8445 L22: 1.4106 REMARK 3 L33: 1.6565 L12: 0.1494 REMARK 3 L13: 0.3189 L23: 0.1752 REMARK 3 S TENSOR REMARK 3 S11: -0.0104 S12: -0.1096 S13: -0.1344 REMARK 3 S21: 0.1185 S22: 0.0416 S23: 0.0895 REMARK 3 S31: 0.1376 S32: -0.0934 S33: -0.0311 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : HH 1 HH 215 REMARK 3 ORIGIN FOR THE GROUP (A): -19.8956 -19.3957 -43.1582 REMARK 3 T TENSOR REMARK 3 T11: 0.2600 T22: 0.3058 REMARK 3 T33: 0.3648 T12: -0.0234 REMARK 3 T13: 0.0206 T23: 0.0051 REMARK 3 L TENSOR REMARK 3 L11: 0.3919 L22: 0.2333 REMARK 3 L33: 3.1571 L12: 0.1800 REMARK 3 L13: 0.8115 L23: 0.1157 REMARK 3 S TENSOR REMARK 3 S11: -0.1194 S12: 0.2777 S13: 0.0142 REMARK 3 S21: -0.2063 S22: 0.1414 S23: -0.0902 REMARK 3 S31: -0.1543 S32: 0.2397 S33: -0.0221 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : LL 2 LL 210 REMARK 3 ORIGIN FOR THE GROUP (A): -34.4796 -12.6966 -38.6427 REMARK 3 T TENSOR REMARK 3 T11: 0.1117 T22: 0.1293 REMARK 3 T33: 0.3227 T12: 0.0116 REMARK 3 T13: -0.0255 T23: 0.0027 REMARK 3 L TENSOR REMARK 3 L11: 0.4299 L22: 0.6833 REMARK 3 L33: 1.9416 L12: 0.3760 REMARK 3 L13: 0.8272 L23: 0.4636 REMARK 3 S TENSOR REMARK 3 S11: -0.1419 S12: 0.0148 S13: 0.0757 REMARK 3 S21: -0.1448 S22: 0.0517 S23: -0.0131 REMARK 3 S31: -0.3137 S32: -0.1066 S33: 0.0902 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 6SS2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292104106. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-JAN-19 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 : BESSY REMARK 200 BEAMLINE : 14.1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39908 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 45.370 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.17000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.0000 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) : 2.49 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 5.40 REMARK 200 R MERGE FOR SHELL (I) : 1.72000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 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: 6SS4, 6SRX REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 60.39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISATION CONDITION: 2 M REMARK 280 (NH4)2SO4 SEED CONDITION (APPROX. FINAL CONC.) 20 MM MIB REMARK 280 (MALONATE, IMIDAZOLE, BORIC ACID) 4% GLYCEROL 2% PEG4000 9 MM REMARK 280 NANO3 9 MM NA2HPO4 9 MM (NH4)2SO4, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 X+2/3,Y+1/3,Z+1/3 REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 7555 X+1/3,Y+2/3,Z+2/3 REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 74.53050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.03020 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.09567 REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 74.53050 REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 43.03020 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 41.09567 REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 74.53050 REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 43.03020 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 41.09567 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 86.06041 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 82.19133 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 86.06041 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 82.19133 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 86.06041 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 82.19133 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: NONAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: NONAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 43650 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 93610 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -766.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, HHH, LLL 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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 350 BIOMT3 3 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 SER A 342 REMARK 465 PRO A 343 REMARK 465 ASP A 344 REMARK 465 GLU A 345 REMARK 465 SER A 346 REMARK 465 GLU A 347 REMARK 465 ASN A 348 REMARK 465 GLN A 349 REMARK 465 ALA A 350 REMARK 465 ARG A 351 REMARK 465 VAL A 352 REMARK 465 ARG A 353 REMARK 465 ILE A 354 REMARK 465 HIS A 355 REMARK 465 HIS A 356 REMARK 465 HIS A 357 REMARK 465 HIS A 358 REMARK 465 HIS A 359 REMARK 465 HIS A 360 REMARK 465 GLY H -3 REMARK 465 ALA H -2 REMARK 465 HIS H -1 REMARK 465 SER H 0 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 THR H 219 REMARK 465 HIS H 220 REMARK 465 ALA H 221 REMARK 465 ALA H 222 REMARK 465 GLY L -2 REMARK 465 VAL L -1 REMARK 465 HIS L 0 REMARK 465 SER L 1 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 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 HH22 ARGHH 96 HO2 GOLHH 301 1.03 REMARK 500 HD1 HISAA 120 MN MNAA 414 1.15 REMARK 500 HD1 HISAA 145 MN MNAA 415 1.26 REMARK 500 H LEUHH 108 O1 SO4HH 305 1.59 REMARK 500 OD1 ASPAA 251 O4 SO4AA 422 2.11 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 GLNAA 37 -131.22 62.96 REMARK 500 ARGAA 199 4.01 -154.32 REMARK 500 GLUAA 296 20.05 81.61 REMARK 500 ASPAA 335 -71.84 -96.15 REMARK 500 PROAA 340 -71.56 -28.33 REMARK 500 VALHH 2 117.63 -177.17 REMARK 500 VALHH 48 -67.46 -109.52 REMARK 500 ALAHH 88 156.73 175.59 REMARK 500 ASPHH 98 -100.57 -130.20 REMARK 500 THRHH 116 79.59 -62.19 REMARK 500 SERHH 127 123.65 -35.00 REMARK 500 SERHH 130 72.46 19.88 REMARK 500 ASPHH 144 77.11 61.31 REMARK 500 ASNHH 204 78.17 64.02 REMARK 500 PROHH 213 -178.09 -68.81 REMARK 500 SERLL 3 43.96 90.30 REMARK 500 ASNLL 27B -101.35 -117.31 REMARK 500 ASNLL 51 -43.94 76.07 REMARK 500 SERLL 52 13.80 -152.61 REMARK 500 GLULL 83 97.36 -60.46 REMARK 500 LYSLL 111 118.29 -36.06 REMARK 500 ASNLL 129 36.56 71.51 REMARK 500 ASPLL 152 -105.34 54.31 REMARK 500 ASNLL 171 -3.85 85.82 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN A 414 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 120 ND1 REMARK 620 2 ASP A 143 OD2 88.3 REMARK 620 3 ASP A 147 OD2 88.6 81.7 REMARK 620 4 ASP A 251 OD1 113.3 92.1 157.2 REMARK 620 5 SO4 A 422 O4 163.9 107.3 97.3 63.5 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN A 415 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 143 OD1 REMARK 620 2 HIS A 145 ND1 97.6 REMARK 620 3 ASP A 251 OD1 76.1 156.6 REMARK 620 4 ASP A 253 OD1 82.9 108.0 93.8 REMARK 620 5 ASP A 253 OD2 147.1 99.2 97.9 65.0 REMARK 620 6 SO4 A 422 O4 92.1 94.6 63.6 157.3 114.5 REMARK 620 N 1 2 3 4 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6SRV RELATED DB: PDB REMARK 900 RELATED ID: 6SRX RELATED DB: PDB REMARK 900 RELATED ID: 6SS0 RELATED DB: PDB REMARK 900 RELATED ID: 6SS4 RELATED DB: PDB REMARK 900 RELATED ID: 6SS5 RELATED DB: PDB REMARK 900 RELATED ID: 6SS6 RELATED DB: PDB REMARK 900 RELATED ID: 6TUL RELATED DB: PDB DBREF 6SS2AA 23 354 UNP P78540 ARGI2_HUMAN 23 354 DBREF 6SS2HH -3 222 PDB 6SS2 6SS2 -3 222 DBREF 6SS2LL -2 213 PDB 6SS2 6SS2 -2 213 SEQADV 6SS2 METAA 22 UNP P78540 INITIATING METHIONINE SEQADV 6SS2 HISAA 355 UNP P78540 EXPRESSION TAG SEQADV 6SS2 HISAA 356 UNP P78540 EXPRESSION TAG SEQADV 6SS2 HISAA 357 UNP P78540 EXPRESSION TAG SEQADV 6SS2 HISAA 358 UNP P78540 EXPRESSION TAG SEQADV 6SS2 HISAA 359 UNP P78540 EXPRESSION TAG SEQADV 6SS2 HISAA 360 UNP P78540 EXPRESSION TAG SEQRES 1AA 339 MET VAL HIS SER VAL ALA VAL ILE GLY ALA PRO PHE SER SEQRES 2AA 339 GLN GLY GLN LYS ARG LYS GLY VAL GLU HIS GLY PRO ALA SEQRES 3AA 339 ALA ILE ARG GLU ALA GLY LEU MET LYS ARG LEU SER SER SEQRES 4AA 339 LEU GLY CYS HIS LEU LYS ASP PHE GLY ASP LEU SER PHE SEQRES 5AA 339 THR PRO VAL PRO LYS ASP ASP LEU TYR ASN ASN LEU ILE SEQRES 6AA 339 VAL ASN PRO ARG SER VAL GLY LEU ALA ASN GLN GLU LEU SEQRES 7AA 339 ALA GLU VAL VAL SER ARG ALA VAL SER ASP GLY TYR SER SEQRES 8AA 339 CYS VAL THR LEU GLY GLY ASP HIS SER LEU ALA ILE GLY SEQRES 9AA 339 THR ILE SER GLY HIS ALA ARG HIS CSO PRO ASP LEU CYS SEQRES 10AA 339 VAL VAL TRP VAL ASP ALA HIS ALA ASP ILE ASN THR PRO SEQRES 11AA 339 LEU THR THR SER SER GLY ASN LEU HIS GLY GLN PRO VAL SEQRES 12AA 339 SER PHE LEU LEU ARG GLU LEU GLN ASP LYS VAL PRO GLN SEQRES 13AA 339 LEU PRO GLY PHE SER TRP ILE LYS PRO CYS ILE SER SER SEQRES 14AA 339 ALA SER ILE VAL TYR ILE GLY LEU ARG ASP VAL ASP PRO SEQRES 15AA 339 PRO GLU HIS PHE ILE LEU LYS ASN TYR ASP ILE GLN TYR SEQRES 16AA 339 PHE SER MET ARG ASP ILE ASP ARG LEU GLY ILE GLN LYS SEQRES 17AA 339 VAL MET GLU ARG THR PHE ASP LEU LEU ILE GLY LYS ARG SEQRES 18AA 339 GLN ARG PRO ILE HIS LEU SER PHE ASP ILE ASP ALA PHE SEQRES 19AA 339 ASP PRO THR LEU ALA PRO ALA THR GLY THR PRO VAL VAL SEQRES 20AA 339 GLY GLY LEU THR TYR ARG GLU GLY MET TYR ILE ALA GLU SEQRES 21AA 339 GLU ILE HIS ASN THR GLY LEU LEU SER ALA LEU ASP LEU SEQRES 22AA 339 VAL GLU VAL ASN PRO GLN LEU ALA THR SER GLU GLU GLU SEQRES 23AA 339 ALA LYS THR THR ALA ASN LEU ALA VAL ASP VAL ILE ALA SEQRES 24AA 339 SER SER PHE GLY GLN THR ARG GLU GLY GLY HIS ILE VAL SEQRES 25AA 339 TYR ASP GLN LEU PRO THR PRO SER SER PRO ASP GLU SER SEQRES 26AA 339 GLU ASN GLN ALA ARG VAL ARG ILE HIS HIS HIS HIS HIS SEQRES 27AA 339 HIS SEQRES 1HH 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2HH 233 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3HH 233 ALA ALA SER GLY PHE THR PHE ARG TYR GLU VAL ALA ALA SEQRES 4HH 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5HH 233 SER ALA ILE SER GLY PRO ILE PRO LYS GLY TYR TYR ALA SEQRES 6HH 233 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7HH 233 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG SEQRES 8HH 233 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LEU ARG SEQRES 9HH 233 ALA ASP LEU GLY LEU TYR MET ASP LEU TRP GLY ARG GLY SEQRES 10HH 233 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11HH 233 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12HH 233 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13HH 233 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14HH 233 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15HH 233 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16HH 233 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17HH 233 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18HH 233 VAL GLU PRO LYS SER CYS ASP LYS THR HIS ALA ALA SEQRES 1LL 220 GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO PRO SER SEQRES 2LL 220 VAL SER ALA ALA PRO GLY GLN LYS VAL THR ILE SER CYS SEQRES 3LL 220 SER GLY SER SER SER ASN ILE GLY ASN HIS TYR VAL SER SEQRES 4LL 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5LL 220 ILE TYR ASP ASN SER GLU ARG THR ALA GLY VAL PRO ASP SEQRES 6LL 220 ARG PHE SER GLY SER LYS SER GLY THR SER ALA THR LEU SEQRES 7LL 220 GLY ILE THR GLY LEU GLN THR GLY ASP GLU ALA ASP TYR SEQRES 8LL 220 TYR CYS GLY THR TRP ASP GLU LEU THR SER ASN LEU VAL SEQRES 9LL 220 PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO SEQRES 10LL 220 LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11LL 220 GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU SEQRES 12LL 220 ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP SEQRES 13LL 220 LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR SEQRES 14LL 220 THR THR PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SEQRES 15LL 220 SER SER TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER SEQRES 16LL 220 HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU GLY SER SEQRES 17LL 220 THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SER MODRES 6SS2 CSOAA 134 CYS MODIFIED RESIDUE HET CSO AA 134 12 HET GOL AA 401 14 HET GOL AA 402 14 HET GOL AA 403 14 HET GOL AA 404 14 HET GOL AA 405 14 HET GOL AA 406 14 HET GOL AA 407 14 HET GOL AA 408 14 HET GOL AA 409 14 HET GOL AA 410 14 HET GOL AA 411 14 HET GOL AA 412 14 HET GOL AA 413 14 HET MN AA 414 1 HET MN AA 415 1 HET SO4 AA 416 5 HET SO4 AA 417 5 HET SO4 AA 418 5 HET SO4 AA 419 5 HET SO4 AA 420 5 HET SO4 AA 421 5 HET SO4 AA 422 5 HET SO4 AA 423 5 HET SO4 AA 424 5 HET GOL HH 301 14 HET GOL HH 302 14 HET GOL HH 303 14 HET SO4 HH 304 5 HET SO4 HH 305 5 HET GOL LL 301 14 HET GOL LL 302 14 HET GOL LL 303 14 HET GOL LL 304 14 HET SO4 LL 305 5 HET SO4 LL 306 5 HET SO4 LL 307 5 HET SO4 LL 308 5 HET SO4 LL 309 5 HET SO4 LL 310 5 HETNAM CSO S-HYDROXYCYSTEINE HETNAM GOL GLYCEROL HETNAM MN MANGANESE (II) ION HETNAM SO4 SULFATE ION HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 1 CSO C3 H7 N O3 S FORMUL 4 GOL 20(C3 H8 O3) FORMUL 17 MN 2(MN 2+) FORMUL 19 SO4 17(O4 S 2-) FORMUL 43 HOH *59(H2 O) HELIX 1 AA1 GLYAA 36 GLUAA 43 5 8 HELIX 2 AA2 HISAA 44 ALAAA 52 1 9 HELIX 3 AA3 GLYAA 53 LEUAA 61 1 9 HELIX 4 AA4 ASPAA 80 ILEAA 86 1 7 HELIX 5 AA5 ASNAA 88 ASPAA 109 1 22 HELIX 6 AA6 ASPAA 119 SERAA 121 5 3 HELIX 7 AA7 LEUAA 122 CSOAA 134 1 13 HELIX 8 AA8 ASNAA 158 GLYAA 161 5 4 HELIX 9 AA9 GLNAA 162 LEUAA 168 1 7 HELIX 10 AB1 LEUAA 171 VALAA 175 5 5 HELIX 11 AB2 ASPAA 202 TYRAA 212 1 11 HELIX 12 AB3 METAA 219 GLYAA 226 1 8 HELIX 13 AB4 GLYAA 226 GLYAA 240 1 15 HELIX 14 AB5 ASPAA 253 PHEAA 255 5 3 HELIX 15 AB6 THRAA 272 GLYAA 287 1 16 HELIX 16 AB7 ASNAA 298 ALAAA 302 5 5 HELIX 17 AB8 SERAA 304 PHEAA 323 1 20 HELIX 18 AB9 THRHH 28 GLUHH 32 5 5 HELIX 19 AC1 ARGHH 83 THRHH 87 5 5 HELIX 20 AC2 ASNLL 27B HISLL 31 5 5 HELIX 21 AC3 GLNLL 79 GLULL 83 5 5 HELIX 22 AC4 SERLL 122 ALALL 128 1 7 HELIX 23 AC5 THRLL 182 SERLL 188 1 7 SHEET 1 AA1 8 HISAA 64 ASPAA 70 0 SHEET 2 AA1 8 SERAA 25 ALAAA 31 1 N GLYAA 30 O GLYAA 69 SHEET 3 AA1 8 SERAA 112 GLYAA 117 1 O VALAA 114 N ALAAA 27 SHEET 4 AA1 8 LEUAA 289 VALAA 295 1 O LEUAA 292 N CYSAA 113 SHEET 5 AA1 8 ILEAA 246 ASPAA 251 1 N LEUAA 248 O ASPAA 293 SHEET 6 AA1 8 CYSAA 138 VALAA 142 1 N VALAA 142 O ASPAA 251 SHEET 7 AA1 8 ILEAA 193 LEUAA 198 1 O ILEAA 196 N TRPAA 141 SHEET 8 AA1 8 GLNAA 215 SERAA 218 1 O PHEAA 217 N TYRAA 195 SHEET 1 AA2 4 GLNHH 3 SERHH 7 0 SHEET 2 AA2 4 LEUHH 18 SERHH 25 -1 O SERHH 21 N SERHH 7 SHEET 3 AA2 4 THRHH 77 METHH 82 -1 O LEUHH 78 N CYSHH 22 SHEET 4 AA2 4 PHEHH 67 ASPHH 72 -1 N THRHH 68 O GLNHH 81 SHEET 1 AA3 6 GLYHH 10 VALHH 12 0 SHEET 2 AA3 6 THRHH 107 VALHH 111 1 O THRHH 110 N GLYHH 10 SHEET 3 AA3 6 ALAHH 88 ALAHH 97 -1 N TYRHH 90 O THRHH 107 SHEET 4 AA3 6 VALHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 91 SHEET 5 AA3 6 GLUHH 46 SERHH 52 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AA3 6 LYSHH 56 TYRHH 59 -1 O TYRHH 58 N ALAHH 50 SHEET 1 AA4 4 GLYHH 10 VALHH 12 0 SHEET 2 AA4 4 THRHH 107 VALHH 111 1 O THRHH 110 N GLYHH 10 SHEET 3 AA4 4 ALAHH 88 ALAHH 97 -1 N TYRHH 90 O THRHH 107 SHEET 4 AA4 4 LEUHH 100A TRPHH 103 -1 O TYRHH 100B N ARGHH 96 SHEET 1 AA5 4 SERHH 120 LEUHH 124 0 SHEET 2 AA5 4 ALAHH 136 TYRHH 145 -1 O LEUHH 141 N PHEHH 122 SHEET 3 AA5 4 TYRHH 176 VALHH 184 -1 O TYRHH 176 N TYRHH 145 SHEET 4 AA5 4 HISHH 164 THRHH 165 -1 N HISHH 164 O VALHH 181 SHEET 1 AA6 4 SERHH 120 LEUHH 124 0 SHEET 2 AA6 4 ALAHH 136 TYRHH 145 -1 O LEUHH 141 N PHEHH 122 SHEET 3 AA6 4 TYRHH 176 VALHH 184 -1 O TYRHH 176 N TYRHH 145 SHEET 4 AA6 4 VALHH 169 LEUHH 170 -1 N VALHH 169 O SERHH 177 SHEET 1 AA7 3 THRHH 151 TRPHH 154 0 SHEET 2 AA7 3 TYRHH 194 HISHH 200 -1 O ASNHH 197 N SERHH 153 SHEET 3 AA7 3 THRHH 205 VALHH 211 -1 O THRHH 205 N HISHH 200 SHEET 1 AA8 6 SERLL 10 ALALL 13 0 SHEET 2 AA8 6 THRLL 102 VALLL 106 1 O LYSLL 103 N VALLL 11 SHEET 3 AA8 6 ASPLL 85 ASPLL 92 -1 N TYRLL 86 O THRLL 102 SHEET 4 AA8 6 SERLL 34 GLNLL 38 -1 N TYRLL 36 O TYRLL 87 SHEET 5 AA8 6 LYSLL 45 TYRLL 49 -1 O LEULL 47 N TRPLL 35 SHEET 6 AA8 6 GLULL 53 ARGLL 54 -1 O GLULL 53 N TYRLL 49 SHEET 1 AA9 4 SERLL 10 ALALL 13 0 SHEET 2 AA9 4 THRLL 102 VALLL 106 1 O LYSLL 103 N VALLL 11 SHEET 3 AA9 4 ASPLL 85 ASPLL 92 -1 N TYRLL 86 O THRLL 102 SHEET 4 AA9 4 ASNLL 95B PHELL 98 -1 O VALLL 97 N THRLL 90 SHEET 1 AB1 3 VALLL 19 SERLL 24 0 SHEET 2 AB1 3 SERLL 70 ILELL 75 -1 O ILELL 75 N VALLL 19 SHEET 3 AB1 3 PHELL 62 SERLL 67 -1 N SERLL 63 O GLYLL 74 SHEET 1 AB2 4 SERLL 115 PHELL 119 0 SHEET 2 AB2 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB2 4 TYRLL 173 LEULL 181 -1 O TYRLL 173 N PHELL 140 SHEET 4 AB2 4 VALLL 160 THRLL 162 -1 N GLULL 161 O TYRLL 178 SHEET 1 AB3 4 SERLL 115 PHELL 119 0 SHEET 2 AB3 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB3 4 TYRLL 173 LEULL 181 -1 O TYRLL 173 N PHELL 140 SHEET 4 AB3 4 SERLL 166 LYSLL 167 -1 N SERLL 166 O ALALL 174 SHEET 1 AB4 4 SERLL 154 VALLL 156 0 SHEET 2 AB4 4 THRLL 146 ALALL 151 -1 N ALALL 151 O SERLL 154 SHEET 3 AB4 4 TYRLL 192 HISLL 198 -1 O THRLL 197 N THRLL 146 SHEET 4 AB4 4 SERLL 201 VALLL 207 -1 O LYSLL 205 N CYSLL 194 SSBOND 1 CYSHH 22 CYSHH 92 1555 1555 2.05 SSBOND 2 CYSHH 140 CYSHH 196 1555 1555 2.04 SSBOND 3 CYSLL 23 CYSLL 88 1555 1555 2.03 SSBOND 4 CYSLL 135 CYSLL 194 1555 1555 2.04 LINK C HISAA 133 N CSOAA 134 1555 1555 1.34 LINK C CSOAA 134 N PROAA 135 1555 1555 1.36 LINK ND1 HISAA 120 MN MNAA 414 1555 1555 2.00 LINK OD2 ASPAA 143 MN MNAA 414 1555 1555 1.97 LINK OD1 ASPAA 143 MN MNAA 415 1555 1555 1.98 LINK ND1 HISAA 145 MN MNAA 415 1555 1555 2.06 LINK OD2 ASPAA 147 MN MNAA 414 1555 1555 2.00 LINK OD1 ASPAA 251 MN MNAA 414 1555 1555 2.04 LINK OD1 ASPAA 251 MN MNAA 415 1555 1555 2.03 LINK OD1 ASPAA 253 MN MNAA 415 1555 1555 2.06 LINK OD2 ASPAA 253 MN MNAA 415 1555 1555 2.00 LINK MN MNAA 414 O4 SO4AA 422 1555 1555 1.97 LINK MN MNAA 415 O4 SO4AA 422 1555 1555 1.97 CISPEP 1 VALAA 76 PROAA 77 0 8.98 CISPEP 2 GLYAA 117 GLYAA 118 0 3.11 CISPEP 3 ILEHH 54 PROHH 55 0 -6.77 CISPEP 4 PHEHH 146 PROHH 147 0 -17.12 CISPEP 5 GLUHH 148 PROHH 149 0 -2.79 CISPEP 6 TYRLL 141 PROLL 142 0 -0.94 CRYST1 149.061 149.061 123.287 90.00 90.00 120.00 H 3 9 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 0.006709 0.003873 0.000000 0.00000 SCALE2 0.000000 0.007746 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008111 0.00000