HEADER PROTEIN BINDING 06-SEP-19 6SRV TITLE STRUCTURE OF THE ARGINASE-2-INHIBITORY HUMAN ANTIGEN-BINDING FRAGMENT TITLE 2 FAB C0021144 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB C0021144 HEAVY CHAIN (IGG1); COMPND 3 CHAIN: HHH, III; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 6 NUMBERING SCHEME.; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB C0021144 LIGHT CHAIN (IGG1); COMPND 9 CHAIN: LLL, MMM; COMPND 10 ENGINEERED: YES; COMPND 11 OTHER_DETAILS: AMINO ACIDS ARE NUMBERED ACCORDING TO THE KABAT COMPND 12 NUMBERING SCHEME. RESIDUE 10 WOULD NOT BE PRESENT IN THE KABAT COMPND 13 SCHEME, BUT DUE TO PROBLEMS WITH NON-CONTINUOUS NUMBERING IN L- COMPND 14 PEPTIDES, WE INCLUDED IT. THEREFORE, RESIDUES 2-10 SHOULD BE READ AS COMPND 15 1-9, PER KABAT. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 15 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 16 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) : 49.90 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 47369 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) : 0.205 REMARK 3 FREE R VALUE : 0.241 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.999 REMARK 3 FREE R VALUE TEST SET COUNT : 2368 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) : 3263 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.4080 REMARK 3 BIN FREE R VALUE SET COUNT : 190 REMARK 3 BIN FREE R VALUE : 0.4390 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6489 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 126 REMARK 3 SOLVENT ATOMS : 78 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.97 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -1.01100 REMARK 3 B22 (A**2) : -1.01100 REMARK 3 B33 (A**2) : 3.28100 REMARK 3 B12 (A**2) : -0.50600 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): 0.304 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.227 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.257 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.953 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6749 ; 0.010 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 6127 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9166 ; 1.769 ; 1.645 REMARK 3 BOND ANGLES OTHERS (DEGREES): 14290 ; 1.232 ; 1.569 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 870 ; 8.762 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 256 ;31.574 ;22.812 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1021 ;18.870 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;22.303 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 888 ; 0.069 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7454 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1314 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1026 ; 0.187 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 71 ; 0.181 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3090 ; 0.165 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 149 ; 0.143 ; 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): 3496 ; 2.278 ; 3.845 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3491 ; 2.262 ; 3.837 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4358 ; 3.692 ; 5.745 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4359 ; 3.692 ; 5.746 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3253 ; 2.369 ; 4.181 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3254 ; 2.369 ; 4.183 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4808 ; 3.812 ; 6.098 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4809 ; 3.812 ; 6.100 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 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 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 : HH 1 HH 217 REMARK 3 ORIGIN FOR THE GROUP (A): 26.3719 -13.1697 49.2213 REMARK 3 T TENSOR REMARK 3 T11: 0.0774 T22: 0.0251 REMARK 3 T33: 0.4333 T12: 0.0080 REMARK 3 T13: 0.0292 T23: 0.0144 REMARK 3 L TENSOR REMARK 3 L11: 3.1129 L22: 1.3237 REMARK 3 L33: 0.8540 L12: 0.3410 REMARK 3 L13: 0.6506 L23: 0.0580 REMARK 3 S TENSOR REMARK 3 S11: -0.0158 S12: 0.1266 S13: 0.0254 REMARK 3 S21: -0.0601 S22: 0.0068 S23: -0.0389 REMARK 3 S31: 0.1669 S32: -0.0342 S33: 0.0090 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 : II 1 II 216 REMARK 3 ORIGIN FOR THE GROUP (A): 2.3031 -29.6119 56.8670 REMARK 3 T TENSOR REMARK 3 T11: 0.0260 T22: 0.0468 REMARK 3 T33: 0.4061 T12: 0.0336 REMARK 3 T13: 0.0089 T23: 0.0371 REMARK 3 L TENSOR REMARK 3 L11: 2.2169 L22: 3.3709 REMARK 3 L33: 0.9729 L12: 1.4733 REMARK 3 L13: 0.3657 L23: 0.6343 REMARK 3 S TENSOR REMARK 3 S11: -0.0394 S12: 0.0093 S13: 0.1021 REMARK 3 S21: -0.0186 S22: -0.0021 S23: 0.0238 REMARK 3 S31: 0.0930 S32: 0.1216 S33: 0.0415 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 211 REMARK 3 ORIGIN FOR THE GROUP (A): 28.6605 -27.0021 38.2021 REMARK 3 T TENSOR REMARK 3 T11: 0.2257 T22: 0.1003 REMARK 3 T33: 0.4934 T12: 0.0103 REMARK 3 T13: 0.0151 T23: -0.0399 REMARK 3 L TENSOR REMARK 3 L11: 3.5287 L22: 2.1693 REMARK 3 L33: 3.0190 L12: -1.6044 REMARK 3 L13: 2.6387 L23: -1.2725 REMARK 3 S TENSOR REMARK 3 S11: 0.1610 S12: 0.2898 S13: -0.1717 REMARK 3 S21: -0.3780 S22: 0.0069 S23: 0.0300 REMARK 3 S31: 0.3416 S32: 0.0389 S33: -0.1679 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : MM 2 MM 210 REMARK 3 ORIGIN FOR THE GROUP (A): 13.9815 -37.5937 67.9019 REMARK 3 T TENSOR REMARK 3 T11: 0.0406 T22: 0.1368 REMARK 3 T33: 0.5573 T12: 0.0586 REMARK 3 T13: -0.0133 T23: 0.0592 REMARK 3 L TENSOR REMARK 3 L11: 1.1219 L22: 3.5770 REMARK 3 L33: 2.7268 L12: 0.4100 REMARK 3 L13: 0.5569 L23: 2.1477 REMARK 3 S TENSOR REMARK 3 S11: 0.0460 S12: -0.1524 S13: -0.0954 REMARK 3 S21: 0.0480 S22: -0.0146 S23: -0.2289 REMARK 3 S31: 0.1441 S32: 0.1118 S33: -0.0314 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 6SRV 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_1292104038. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-OCT-18 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 : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979500 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 : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47369 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 49.901 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 29.50 REMARK 200 R MERGE (I) : 0.36000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.6000 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) : 2.48 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 20.90 REMARK 200 R MERGE FOR SHELL (I) : 9.90000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.400 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: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.54 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM NH4CL 20% PEG3350, VAPOR REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 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 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+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 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 86.34500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.85131 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 70.42000 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 86.34500 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 49.85131 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 70.42000 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 86.34500 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 49.85131 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 70.42000 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 86.34500 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 49.85131 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 70.42000 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 86.34500 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 49.85131 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 70.42000 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 86.34500 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 49.85131 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 70.42000 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 99.70262 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 140.84000 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 99.70262 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 140.84000 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 99.70262 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 140.84000 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 99.70262 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 140.84000 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 99.70262 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 140.84000 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 99.70262 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 140.84000 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: 5090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20490 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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: 5540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20380 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: III, MMM 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 CL CL H 301 LIES ON A SPECIAL POSITION. REMARK 375 CL CL I 301 LIES ON A SPECIAL POSITION. 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 GLY H -3 REMARK 465 ALA H -2 REMARK 465 HIS H -1 REMARK 465 SER H 0 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 I -3 REMARK 465 ALA I -2 REMARK 465 HIS I -1 REMARK 465 SER I 0 REMARK 465 ASP I 217 REMARK 465 LYS I 218 REMARK 465 THR I 219 REMARK 465 HIS I 220 REMARK 465 ALA I 221 REMARK 465 ALA I 222 REMARK 465 GLY L -2 REMARK 465 VAL L -1 REMARK 465 HIS L 0 REMARK 465 SER L 1 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 465 GLY M -2 REMARK 465 VAL M -1 REMARK 465 HIS M 0 REMARK 465 SER M 1 REMARK 465 GLU M 211 REMARK 465 CYS M 212 REMARK 465 SER M 213 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 CYSHH 22 CB - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 CYSII 22 CB - CA - C ANGL. DEV. = 8.3 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 CYSHH 22 104.51 -161.21 REMARK 500 VALHH 48 -45.76 -134.67 REMARK 500 ASNHH 76 45.17 38.36 REMARK 500 ASPHH 98 -63.53 -120.37 REMARK 500 SERHH 130 -3.09 -57.15 REMARK 500 THRHH 131 -62.26 -99.53 REMARK 500 SERHH 132 79.29 -49.71 REMARK 500 ASPHH 144 66.25 63.13 REMARK 500 CYSHH 216 129.18 -39.70 REMARK 500 VALII 48 -44.18 -134.91 REMARK 500 ASNII 76 47.93 32.26 REMARK 500 SERII 130 -1.69 -58.52 REMARK 500 THRII 131 -70.78 -93.38 REMARK 500 SERII 132 -53.96 -26.96 REMARK 500 ASPII 144 65.25 62.89 REMARK 500 ASNLL 27B -97.02 -102.84 REMARK 500 ASPLL 50 40.10 38.98 REMARK 500 THRLL 51 -35.10 74.21 REMARK 500 SERLL 56 125.68 -29.26 REMARK 500 ASPLL 60 -15.91 -48.13 REMARK 500 ALALL 84 171.15 168.82 REMARK 500 ALALL 158 115.54 -39.41 REMARK 500 ASNLL 171 -4.38 66.06 REMARK 500 ASNMM 27B -98.22 -100.91 REMARK 500 ASPMM 50 40.81 38.26 REMARK 500 THRMM 51 -36.50 72.89 REMARK 500 SERMM 56 128.77 -35.60 REMARK 500 ASPMM 60 -8.43 -57.65 REMARK 500 ALAMM 84 169.50 167.68 REMARK 500 ASPMM 152 -114.20 58.79 REMARK 500 ASNMM 171 -4.70 65.82 REMARK 500 PROMM 183 -37.69 -34.37 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 SERHH 7 GLYHH 8 149.32 REMARK 500 GLYII 133 GLYII 134 145.58 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6SRX RELATED DB: PDB REMARK 900 RELATED ID: 6SS0 RELATED DB: PDB REMARK 900 RELATED ID: 6SS2 RELATED DB: PDB REMARK 900 RELATED ID: 6SS3 RELATED DB: PDB REMARK 900 RELATED ID: 6SS4 RELATED DB: PDB REMARK 900 RELATED ID: 6SS6 RELATED DB: PDB REMARK 900 RELATED ID: 6TUL RELATED DB: PDB DBREF 6SRVHH -3 222 PDB 6SRV 6SRV -3 222 DBREF 6SRVII -3 222 PDB 6SRV 6SRV -3 222 DBREF 6SRVLL -2 213 PDB 6SRV 6SRV -2 213 DBREF 6SRVMM -2 213 PDB 6SRV 6SRV -2 213 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 ASP TYR HIS VAL SEQRES 4HH 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5HH 233 SER ALA ILE SER GLY SER GLY GLY SER THR 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 1II 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2II 233 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3II 233 ALA ALA SER GLY PHE THR PHE ARG TYR ASP TYR HIS VAL SEQRES 4II 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5II 233 SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA SEQRES 6II 233 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7II 233 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG SEQRES 8II 233 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LEU ARG SEQRES 9II 233 ALA ASP LEU GLY LEU TYR MET ASP LEU TRP GLY ARG GLY SEQRES 10II 233 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11II 233 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12II 233 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13II 233 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14II 233 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15II 233 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16II 233 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17II 233 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18II 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 VAL SER CYS SEQRES 3LL 220 SER GLY SER SER SER ASN ILE GLY ASN HIS HIS VAL SER SEQRES 4LL 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5LL 220 ILE TYR ASP THR THR VAL LEU SER SER 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 SEQRES 1MM 220 GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO PRO SER SEQRES 2MM 220 VAL SER ALA ALA PRO GLY GLN LYS VAL THR VAL SER CYS SEQRES 3MM 220 SER GLY SER SER SER ASN ILE GLY ASN HIS HIS VAL SER SEQRES 4MM 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5MM 220 ILE TYR ASP THR THR VAL LEU SER SER GLY VAL PRO ASP SEQRES 6MM 220 ARG PHE SER GLY SER LYS SER GLY THR SER ALA THR LEU SEQRES 7MM 220 GLY ILE THR GLY LEU GLN THR GLY ASP GLU ALA ASP TYR SEQRES 8MM 220 TYR CYS GLY THR TRP ASP GLU LEU THR SER ASN LEU VAL SEQRES 9MM 220 PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO SEQRES 10MM 220 LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11MM 220 GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU SEQRES 12MM 220 ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP SEQRES 13MM 220 LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR SEQRES 14MM 220 THR THR PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SEQRES 15MM 220 SER SER TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER SEQRES 16MM 220 HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU GLY SER SEQRES 17MM 220 THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SER HET CL HH 301 1 HET EDO HH 302 10 HET EDO HH 303 10 HET EDO HH 304 10 HET EDO HH 305 10 HET EDO HH 306 10 HET EDO HH 307 10 HET EDO HH 308 10 HET EDO HH 309 10 HET EDO HH 310 10 HET PEG HH 311 17 HET PEG HH 312 17 HET TRS HH 313 20 HET TRS HH 314 20 HET CL II 301 1 HET CL II 302 1 HET EDO II 303 10 HET PEG II 304 17 HET PEG II 305 17 HET PEG II 306 17 HET TRS LL 301 20 HET EDO MM 301 10 HET EDO MM 302 10 HET EDO MM 303 10 HET EDO MM 304 10 HET TRS MM 305 20 HETNAM CL CHLORIDE ION HETNAM EDO 1,2-ETHANEDIOL HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETSYN EDO ETHYLENE GLYCOL HETSYN TRS TRIS BUFFER FORMUL 5 CL 3(CL 1-) FORMUL 6 EDO 14(C2 H6 O2) FORMUL 15 PEG 5(C4 H10 O3) FORMUL 17 TRS 4(C4 H12 N O3 1+) FORMUL 31 HOH *78(H2 O) HELIX 1 AA1 THRHH 28 ASPHH 32 5 5 HELIX 2 AA2 ASPHH 61 LYSHH 64 5 4 HELIX 3 AA3 ASNHH 73 LYSHH 75 5 3 HELIX 4 AA4 ARGHH 83 THRHH 87 5 5 HELIX 5 AA5 SERHH 156 ALAHH 158 5 3 HELIX 6 AA6 SERHH 187 LEUHH 189 5 3 HELIX 7 AA7 LYSHH 201 ASNHH 204 5 4 HELIX 8 AA8 GLYII 26 ASPII 32 5 7 HELIX 9 AA9 ASPII 61 LYSII 64 5 4 HELIX 10 AB1 ASNII 73 LYSII 75 5 3 HELIX 11 AB2 ARGII 83 THRII 87 5 5 HELIX 12 AB3 SERII 128 GLYII 133 1 6 HELIX 13 AB4 SERII 156 ALAII 158 5 3 HELIX 14 AB5 SERII 187 LEUII 189 5 3 HELIX 15 AB6 LYSII 201 ASNII 204 5 4 HELIX 16 AB7 ASNLL 27B HISLL 31 5 5 HELIX 17 AB8 GLNLL 79 GLULL 83 5 5 HELIX 18 AB9 SERLL 122 ALALL 128 1 7 HELIX 19 AC1 THRLL 182 HISLL 189 1 8 HELIX 20 AC2 ASNMM 27B HISMM 31 5 5 HELIX 21 AC3 GLNMM 79 GLUMM 83 5 5 HELIX 22 AC4 SERMM 122 ALAMM 128 1 7 HELIX 23 AC5 THRMM 182 HISMM 189 1 8 SHEET 1 AA1 4 GLNHH 3 SERHH 7 0 SHEET 2 AA1 4 LEUHH 18 SERHH 25 -1 O ALAHH 23 N LEUHH 5 SHEET 3 AA1 4 THRHH 77 METHH 82 -1 O METHH 82 N LEUHH 18 SHEET 4 AA1 4 PHEHH 67 ASPHH 72 -1 N THRHH 68 O GLNHH 81 SHEET 1 AA2 6 GLYHH 10 VALHH 12 0 SHEET 2 AA2 6 THRHH 107 VALHH 111 1 O THRHH 110 N GLYHH 10 SHEET 3 AA2 6 ALAHH 88 ALAHH 97 -1 N TYRHH 90 O THRHH 107 SHEET 4 AA2 6 TYRHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 91 SHEET 5 AA2 6 GLUHH 46 ILEHH 51 -1 O GLUHH 46 N ARGHH 38 SHEET 6 AA2 6 THRHH 57 TYRHH 59 -1 O TYRHH 58 N ALAHH 50 SHEET 1 AA3 4 GLYHH 10 VALHH 12 0 SHEET 2 AA3 4 THRHH 107 VALHH 111 1 O THRHH 110 N GLYHH 10 SHEET 3 AA3 4 ALAHH 88 ALAHH 97 -1 N TYRHH 90 O THRHH 107 SHEET 4 AA3 4 LEUHH 100A TRPHH 103 -1 O TYRHH 100B N ARGHH 96 SHEET 1 AA4 4 SERHH 120 LEUHH 124 0 SHEET 2 AA4 4 THRHH 135 TYRHH 145 -1 O GLYHH 139 N LEUHH 124 SHEET 3 AA4 4 TYRHH 176 PROHH 185 -1 O TYRHH 176 N TYRHH 145 SHEET 4 AA4 4 VALHH 163 THRHH 165 -1 N HISHH 164 O VALHH 181 SHEET 1 AA5 4 SERHH 120 LEUHH 124 0 SHEET 2 AA5 4 THRHH 135 TYRHH 145 -1 O GLYHH 139 N LEUHH 124 SHEET 3 AA5 4 TYRHH 176 PROHH 185 -1 O TYRHH 176 N TYRHH 145 SHEET 4 AA5 4 VALHH 169 LEUHH 170 -1 N VALHH 169 O SERHH 177 SHEET 1 AA6 3 THRHH 151 TRPHH 154 0 SHEET 2 AA6 3 TYRHH 194 HISHH 200 -1 O ASNHH 197 N SERHH 153 SHEET 3 AA6 3 THRHH 205 VALHH 211 -1 O VALHH 211 N TYRHH 194 SHEET 1 AA7 4 LEUII 4 SERII 7 0 SHEET 2 AA7 4 LEUII 18 ALAII 24 -1 O SERII 21 N SERII 7 SHEET 3 AA7 4 THRII 77 METII 82 -1 O METII 82 N LEUII 18 SHEET 4 AA7 4 PHEII 67 ASPII 72 -1 N THRII 68 O GLNII 81 SHEET 1 AA8 6 GLYII 10 VALII 12 0 SHEET 2 AA8 6 THRII 107 VALII 111 1 O THRII 110 N GLYII 10 SHEET 3 AA8 6 ALAII 88 ALAII 97 -1 N TYRII 90 O THRII 107 SHEET 4 AA8 6 TYRII 33 GLNII 39 -1 N VALII 37 O TYRII 91 SHEET 5 AA8 6 GLUII 46 ILEII 51 -1 O GLUII 46 N ARGII 38 SHEET 6 AA8 6 THRII 57 TYRII 59 -1 O TYRII 58 N ALAII 50 SHEET 1 AA9 4 GLYII 10 VALII 12 0 SHEET 2 AA9 4 THRII 107 VALII 111 1 O THRII 110 N GLYII 10 SHEET 3 AA9 4 ALAII 88 ALAII 97 -1 N TYRII 90 O THRII 107 SHEET 4 AA9 4 LEUII 100A TRPII 103 -1 O LEUII 102 N ARGII 94 SHEET 1 AB1 4 SERII 120 LEUII 124 0 SHEET 2 AB1 4 THRII 135 TYRII 145 -1 O GLYII 139 N LEUII 124 SHEET 3 AB1 4 TYRII 176 PROII 185 -1 O TYRII 176 N TYRII 145 SHEET 4 AB1 4 VALII 163 THRII 165 -1 N HISII 164 O VALII 181 SHEET 1 AB2 4 SERII 120 LEUII 124 0 SHEET 2 AB2 4 THRII 135 TYRII 145 -1 O GLYII 139 N LEUII 124 SHEET 3 AB2 4 TYRII 176 PROII 185 -1 O TYRII 176 N TYRII 145 SHEET 4 AB2 4 VALII 169 LEUII 170 -1 N VALII 169 O SERII 177 SHEET 1 AB3 3 THRII 151 TRPII 154 0 SHEET 2 AB3 3 TYRII 194 HISII 200 -1 O ASNII 197 N SERII 153 SHEET 3 AB3 3 THRII 205 VALII 211 -1 O VALII 211 N TYRII 194 SHEET 1 AB4 6 SERLL 10 ALALL 13 0 SHEET 2 AB4 6 THRLL 102 VALLL 106 1 O THRLL 105 N VALLL 11 SHEET 3 AB4 6 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 SHEET 4 AB4 6 SERLL 34 GLNLL 38 -1 N GLNLL 38 O ASPLL 85 SHEET 5 AB4 6 LYSLL 45 TYRLL 49 -1 O LYSLL 45 N GLNLL 37 SHEET 6 AB4 6 VALLL 53 LEULL 54 -1 O VALLL 53 N TYRLL 49 SHEET 1 AB5 4 SERLL 10 ALALL 13 0 SHEET 2 AB5 4 THRLL 102 VALLL 106 1 O THRLL 105 N VALLL 11 SHEET 3 AB5 4 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 SHEET 4 AB5 4 ASNLL 95B PHELL 98 -1 O VALLL 97 N THRLL 90 SHEET 1 AB6 3 VALLL 19 SERLL 24 0 SHEET 2 AB6 3 SERLL 70 ILELL 75 -1 O LEULL 73 N VALLL 21 SHEET 3 AB6 3 PHELL 62 SERLL 67 -1 N SERLL 65 O THRLL 72 SHEET 1 AB7 4 SERLL 115 PHELL 119 0 SHEET 2 AB7 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB7 4 TYRLL 173 LEULL 181 -1 O TYRLL 173 N PHELL 140 SHEET 4 AB7 4 VALLL 160 THRLL 162 -1 N GLULL 161 O TYRLL 178 SHEET 1 AB8 4 SERLL 115 PHELL 119 0 SHEET 2 AB8 4 ALALL 131 PHELL 140 -1 O LEULL 136 N THRLL 117 SHEET 3 AB8 4 TYRLL 173 LEULL 181 -1 O TYRLL 173 N PHELL 140 SHEET 4 AB8 4 SERLL 166 LYSLL 167 -1 N SERLL 166 O ALALL 174 SHEET 1 AB9 4 SERLL 154 PROLL 155 0 SHEET 2 AB9 4 THRLL 146 ALALL 151 -1 N ALALL 151 O SERLL 154 SHEET 3 AB9 4 TYRLL 192 HISLL 198 -1 O THRLL 197 N THRLL 146 SHEET 4 AB9 4 SERLL 201 VALLL 207 -1 O VALLL 203 N VALLL 196 SHEET 1 AC1 6 SERMM 10 ALAMM 13 0 SHEET 2 AC1 6 THRMM 102 VALMM 106 1 O THRMM 105 N VALMM 11 SHEET 3 AC1 6 ALAMM 84 ASPMM 92 -1 N ALAMM 84 O LEUMM 104 SHEET 4 AC1 6 SERMM 34 GLNMM 38 -1 N GLNMM 38 O ASPMM 85 SHEET 5 AC1 6 LYSMM 45 TYRMM 49 -1 O LYSMM 45 N GLNMM 37 SHEET 6 AC1 6 VALMM 53 LEUMM 54 -1 O VALMM 53 N TYRMM 49 SHEET 1 AC2 4 SERMM 10 ALAMM 13 0 SHEET 2 AC2 4 THRMM 102 VALMM 106 1 O THRMM 105 N VALMM 11 SHEET 3 AC2 4 ALAMM 84 ASPMM 92 -1 N ALAMM 84 O LEUMM 104 SHEET 4 AC2 4 ASNMM 95B PHEMM 98 -1 O VALMM 97 N THRMM 90 SHEET 1 AC3 3 VALMM 19 SERMM 24 0 SHEET 2 AC3 3 SERMM 70 ILEMM 75 -1 O ILEMM 75 N VALMM 19 SHEET 3 AC3 3 PHEMM 62 SERMM 67 -1 N SERMM 63 O GLYMM 74 SHEET 1 AC4 4 SERMM 115 PHEMM 119 0 SHEET 2 AC4 4 ALAMM 131 PHEMM 140 -1 O LEUMM 136 N THRMM 117 SHEET 3 AC4 4 TYRMM 173 LEUMM 181 -1 O TYRMM 173 N PHEMM 140 SHEET 4 AC4 4 VALMM 160 THRMM 162 -1 N GLUMM 161 O TYRMM 178 SHEET 1 AC5 4 SERMM 115 PHEMM 119 0 SHEET 2 AC5 4 ALAMM 131 PHEMM 140 -1 O LEUMM 136 N THRMM 117 SHEET 3 AC5 4 TYRMM 173 LEUMM 181 -1 O TYRMM 173 N PHEMM 140 SHEET 4 AC5 4 SERMM 166 LYSMM 167 -1 N SERMM 166 O ALAMM 174 SHEET 1 AC6 4 SERMM 154 PROMM 155 0 SHEET 2 AC6 4 THRMM 146 ALAMM 151 -1 N ALAMM 151 O SERMM 154 SHEET 3 AC6 4 TYRMM 192 HISMM 198 -1 O THRMM 197 N THRMM 146 SHEET 4 AC6 4 SERMM 201 VALMM 207 -1 O SERMM 201 N HISMM 198 SSBOND 1 CYSHH 22 CYSHH 92 1555 1555 2.05 SSBOND 2 CYSHH 140 CYSHH 196 1555 1555 2.02 SSBOND 3 CYSII 22 CYSII 92 1555 1555 2.09 SSBOND 4 CYSII 140 CYSII 196 1555 1555 2.03 SSBOND 5 CYSLL 23 CYSLL 88 1555 1555 2.08 SSBOND 6 CYSLL 135 CYSLL 194 1555 1555 2.05 SSBOND 7 CYSMM 23 CYSMM 88 1555 1555 2.06 SSBOND 8 CYSMM 135 CYSMM 194 1555 1555 2.04 CISPEP 1 PHEHH 146 PROHH 147 0 -5.88 CISPEP 2 GLUHH 148 PROHH 149 0 -7.55 CISPEP 3 PHEII 146 PROII 147 0 -8.38 CISPEP 4 GLUII 148 PROII 149 0 -4.53 CISPEP 5 TYRLL 141 PROLL 142 0 -10.01 CISPEP 6 TYRMM 141 PROMM 142 0 -9.99 CRYST1 172.690 172.690 211.260 90.00 90.00 120.00 H 3 2 36 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 0.005791 0.003343 0.000000 0.00000 SCALE2 0.000000 0.006687 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004734 0.00000