HEADER PROTEIN BINDING 06-SEP-19 6SS4 TITLE STRUCTURE OF ARGINASE-2 IN COMPLEX WITH THE INHIBITORY HUMAN ANTIGEN- TITLE 2 BINDING FRAGMENT FAB C0021181 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 C0021181 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 C0021181 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_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 EXPRESSION_SYSTEM_VARIANT: EXPICHO; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PEU1.3 FAB; SOURCE 18 MOL_ID: 3; SOURCE 19 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 20 ORGANISM_COMMON: HUMAN; SOURCE 21 ORGANISM_TAXID: 9606; SOURCE 22 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 23 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 25 EXPRESSION_SYSTEM_VARIANT: EXPICHO; SOURCE 26 EXPRESSION_SYSTEM_CELL_LINE: CHO; SOURCE 27 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. 2.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 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) : 2.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.98 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 32381 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) : 0.266 REMARK 3 FREE R VALUE : 0.318 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.947 REMARK 3 FREE R VALUE TEST SET COUNT : 1602 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) : 2.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2229 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79 REMARK 3 BIN R VALUE (WORKING SET) : 1.2300 REMARK 3 BIN FREE R VALUE SET COUNT : 118 REMARK 3 BIN FREE R VALUE : 1.0510 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5619 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 7 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 79.62 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -14.10900 REMARK 3 B22 (A**2) : -14.10900 REMARK 3 B33 (A**2) : 28.21900 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): 0.137 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.779 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.923 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.892 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5773 ; 0.013 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 5246 ; 0.002 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7853 ; 2.012 ; 1.639 REMARK 3 BOND ANGLES OTHERS (DEGREES): 12210 ; 1.379 ; 1.570 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 743 ; 8.237 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 255 ;35.323 ;22.275 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 906 ;22.781 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;23.645 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 763 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6476 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1164 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1310 ; 0.223 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 47 ; 0.270 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2716 ; 0.185 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 181 ; 0.218 ; 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): 2981 ; 2.386 ; 3.808 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2980 ; 2.384 ; 3.808 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3721 ; 3.846 ; 5.706 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3722 ; 3.845 ; 5.707 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2792 ; 2.396 ; 3.897 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2788 ; 2.341 ; 3.890 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4132 ; 3.347 ; 5.820 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4127 ; 3.267 ; 5.811 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 : 0.5053 REMARK 3 TWIN DOMAIN : 2 REMARK 3 TWIN OPERATOR : -H,-K,L REMARK 3 TWIN FRACTION : 0.4947 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 0 AA 999 REMARK 3 ORIGIN FOR THE GROUP (A): 73.3003 -19.5498 32.4800 REMARK 3 T TENSOR REMARK 3 T11: 0.4937 T22: 0.4756 REMARK 3 T33: 0.0198 T12: -0.0262 REMARK 3 T13: -0.0083 T23: 0.0274 REMARK 3 L TENSOR REMARK 3 L11: 0.2375 L22: 1.9311 REMARK 3 L33: 1.2460 L12: -0.6675 REMARK 3 L13: -0.2464 L23: 0.4862 REMARK 3 S TENSOR REMARK 3 S11: 0.0414 S12: 0.0098 S13: 0.0575 REMARK 3 S21: -0.0250 S22: -0.0470 S23: -0.1780 REMARK 3 S31: -0.1105 S32: -0.0092 S33: 0.0056 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 0 HH 999 REMARK 3 ORIGIN FOR THE GROUP (A): 68.3672 -21.5597 86.9014 REMARK 3 T TENSOR REMARK 3 T11: 1.0907 T22: 0.8073 REMARK 3 T33: 0.0895 T12: -0.0235 REMARK 3 T13: 0.0139 T23: 0.0957 REMARK 3 L TENSOR REMARK 3 L11: 0.3435 L22: 0.4949 REMARK 3 L33: 0.5535 L12: -0.1077 REMARK 3 L13: 0.0900 L23: -0.4411 REMARK 3 S TENSOR REMARK 3 S11: 0.0248 S12: -0.3241 S13: -0.1631 REMARK 3 S21: 0.3041 S22: -0.0159 S23: 0.0314 REMARK 3 S31: 0.1016 S32: 0.0788 S33: -0.0088 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 0 LL 999 REMARK 3 ORIGIN FOR THE GROUP (A): 50.2571 -22.1170 86.5367 REMARK 3 T TENSOR REMARK 3 T11: 1.1030 T22: 1.0233 REMARK 3 T33: 0.3439 T12: -0.0768 REMARK 3 T13: 0.0042 T23: -0.0151 REMARK 3 L TENSOR REMARK 3 L11: 0.1432 L22: 0.3250 REMARK 3 L33: 0.0908 L12: 0.1405 REMARK 3 L13: -0.0358 L23: -0.1202 REMARK 3 S TENSOR REMARK 3 S11: 0.0199 S12: -0.2555 S13: 0.0113 REMARK 3 S21: 0.2692 S22: 0.0113 S23: 0.0117 REMARK 3 S31: 0.0595 S32: -0.1461 S33: -0.0312 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT 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 6SS4 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_1292104119. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-MAY-18 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.0 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 : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32384 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900 REMARK 200 RESOLUTION RANGE LOW (A) : 44.980 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 20.20 REMARK 200 R MERGE (I) : 0.35000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 20.80 REMARK 200 R MERGE FOR SHELL (I) : 5.19000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.700 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: 4HZE,6SS0 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 71.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MMT PH 5.0 (MALIC ACID, MES, REMARK 280 TRIS) 20% GLYCEROL 10% PEG4000 15 MM NANO3 15 MM NA2HPO4 15 MM REMARK 280 (NH4)2SO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1 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 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 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 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 APPLY THE FOLLOWING TO CHAINS: AAA, HHH, LLL REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 75.19000 REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 -130.23290 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, HHH, LLL REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 150.38000 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 PRO A 338 REMARK 465 THR A 339 REMARK 465 PRO A 340 REMARK 465 SER A 341 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 GLU H 1 REMARK 465 VAL H 2 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 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 GLN L 2 REMARK 465 SER L 3 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 OG SERHH 179 HH TYRLL 178 1.09 REMARK 500 HD1 HISAA 120 MN MNAA 401 1.12 REMARK 500 HD1 HISAA 145 MN MNAA 402 1.25 REMARK 500 HH TYRHH 59 H ILEHH 69 1.33 REMARK 500 HG1 THRAA 326 O GLYAA 329 1.42 REMARK 500 H CYSLL 23 O ALALL 71 1.55 REMARK 500 H GLNLL 168 O LYSLL 172 1.58 REMARK 500 OD2 ASPHH 32 HH21 ARGHH 96 1.59 REMARK 500 HH11 ARGHH 94 OD2 ASPHH 101 1.60 REMARK 500 OG SERHH 179 OH TYRLL 178 1.92 REMARK 500 OG SERLL 193 OG1 THRLL 206 1.93 REMARK 500 O SERLL 27 OG SERLL 30 2.15 REMARK 500 OE1 GLNLL 109 ND2 ASNLL 171 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 HE22 GLNAA 97 O LYSHH 64 5556 1.48 REMARK 500 NE2 GLNAA 97 O LYSHH 64 5556 1.88 REMARK 500 REMARK 500 REMARK: NULL 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),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLUAA 98 CD GLUAA 98 OE2 0.097 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 ARGAA 105 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 THRAA 311 CA - CB - OG1 ANGL. DEV. = -14.5 DEGREES REMARK 500 ASPHH 61 CB - CG - OD1 ANGL. DEV. = -6.8 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 VALAA 23 62.95 39.59 REMARK 500 GLNAA 37 -147.11 51.51 REMARK 500 ASPAA 79 41.53 -84.38 REMARK 500 HISAA 120 10.90 -61.02 REMARK 500 ASPAA 143 149.20 175.57 REMARK 500 GLNAA 162 4.68 -163.64 REMARK 500 ARGAA 199 -6.32 -149.39 REMARK 500 HISAA 331 -148.13 61.76 REMARK 500 VALAA 333 148.25 -172.83 REMARK 500 SERHH 65 -22.48 74.88 REMARK 500 ASPHH 98 -133.31 -161.37 REMARK 500 ASPHH 144 68.77 60.37 REMARK 500 PROHH 147 -153.87 -91.15 REMARK 500 THRHH 160 -54.37 -123.94 REMARK 500 HISHH 200 67.65 -114.99 REMARK 500 PROHH 213 46.44 -67.18 REMARK 500 ASNLL 27B -97.58 -127.81 REMARK 500 SERLL 30 -14.68 -142.40 REMARK 500 ASNLL 51 -53.79 71.49 REMARK 500 ALALL 84 -172.84 -175.25 REMARK 500 ASPLL 152 -113.04 53.68 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 GLYAA 117 GLYAA 118 139.96 REMARK 500 TYRAA 334 ASPAA 335 -145.24 REMARK 500 GLULL 211 CYSLL 212 141.84 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 401 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 120 ND1 REMARK 620 2 ASP A 143 OD2 106.6 REMARK 620 3 ASP A 147 OD2 84.2 81.1 REMARK 620 4 ASP A 251 OD2 117.2 86.7 157.9 REMARK 620 5 PO4 A 403 O1 158.3 93.3 90.5 71.7 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN A 402 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 143 OD1 REMARK 620 2 HIS A 145 ND1 94.4 REMARK 620 3 ASP A 251 OD2 73.6 159.7 REMARK 620 4 ASP A 253 OD1 86.6 117.4 78.9 REMARK 620 5 ASP A 253 OD2 144.6 87.4 112.0 61.8 REMARK 620 6 PO4 A 403 O1 93.4 93.2 71.7 149.3 121.8 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: 6SS2 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 6SS4AA 23 354 UNP P78540 ARGI2_HUMAN 23 354 DBREF 6SS4HH -3 222 PDB 6SS4 6SS4 -3 222 DBREF 6SS4LL -2 213 PDB 6SS4 6SS4 -2 213 SEQADV 6SS4 METAA 22 UNP P78540 INITIATING METHIONINE SEQADV 6SS4 HISAA 355 UNP P78540 EXPRESSION TAG SEQADV 6SS4 HISAA 356 UNP P78540 EXPRESSION TAG SEQADV 6SS4 HISAA 357 UNP P78540 EXPRESSION TAG SEQADV 6SS4 HISAA 358 UNP P78540 EXPRESSION TAG SEQADV 6SS4 HISAA 359 UNP P78540 EXPRESSION TAG SEQADV 6SS4 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 CYS 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 ARG PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3HH 233 ALA ALA SER GLU 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 SER 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 ALA VAL SER CYS SEQRES 3LL 220 SER GLY SER SER SER ASN ILE GLY SER 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 SER GLY ILE 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 ARG 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 HET MN AA 401 1 HET MN AA 402 1 HET PO4 AA 403 5 HETNAM MN MANGANESE (II) ION HETNAM PO4 PHOSPHATE ION FORMUL 4 MN 2(MN 2+) FORMUL 6 PO4 O4 P 3- HELIX 1 AA1 LYSAA 40 GLUAA 43 5 4 HELIX 2 AA2 HISAA 44 GLUAA 51 1 8 HELIX 3 AA3 GLYAA 53 SERAA 60 1 8 HELIX 4 AA4 ASPAA 80 ILEAA 86 1 7 HELIX 5 AA5 ASNAA 88 ASPAA 109 1 22 HELIX 6 AA6 LEUAA 122 CYSAA 134 1 13 HELIX 7 AA7 GLNAA 162 PHEAA 166 5 5 HELIX 8 AA8 LEUAA 171 VALAA 175 5 5 HELIX 9 AA9 ASPAA 202 TYRAA 212 1 11 HELIX 10 AB1 METAA 219 GLYAA 226 1 8 HELIX 11 AB2 GLYAA 226 GLYAA 240 1 15 HELIX 12 AB3 ASPAA 253 PHEAA 255 5 3 HELIX 13 AB4 THRAA 272 THRAA 286 1 15 HELIX 14 AB5 ASNAA 298 ALAAA 302 5 5 HELIX 15 AB6 SERAA 304 PHEAA 323 1 20 HELIX 16 AB7 GLUHH 26 ASPHH 32 5 7 HELIX 17 AB8 ASNHH 73 LYSHH 75 5 3 HELIX 18 AB9 ARGHH 83 THRHH 87 5 5 HELIX 19 AC1 PROHH 185 GLYHH 190 5 6 HELIX 20 AC2 LYSHH 201 ASNHH 204 5 4 HELIX 21 AC3 SERLL 122 ALALL 128 1 7 HELIX 22 AC4 THRLL 182 HISLL 189 1 8 SHEET 1 AA1 8 LEUAA 65 ASPAA 70 0 SHEET 2 AA1 8 VALAA 26 ALAAA 31 1 N GLYAA 30 O GLYAA 69 SHEET 3 AA1 8 SERAA 112 GLYAA 117 1 O SERAA 112 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 ILEAA 246 O SERAA 290 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 VALAA 194 N TRPAA 141 SHEET 8 AA1 8 TYRAA 216 SERAA 218 1 O PHEAA 217 N GLYAA 197 SHEET 1 AA2 4 LEUHH 4 SERHH 7 0 SHEET 2 AA2 4 LEUHH 18 ALAHH 24 -1 O ALAHH 23 N LEUHH 5 SHEET 3 AA2 4 THRHH 77 METHH 82 -1 O METHH 82 N LEUHH 18 SHEET 4 AA2 4 PHEHH 67 ASPHH 72 -1 N SERHH 70 O TYRHH 79 SHEET 1 AA3 6 GLYHH 10 VALHH 12 0 SHEET 2 AA3 6 THRHH 107 VALHH 111 1 O THRHH 110 N VALHH 12 SHEET 3 AA3 6 ALAHH 88 ALAHH 97 -1 N TYRHH 90 O THRHH 107 SHEET 4 AA3 6 TYRHH 33 GLNHH 39 -1 N TYRHH 33 O LEUHH 95 SHEET 5 AA3 6 LEUHH 45 ILEHH 51 -1 O VALHH 48 N TRPHH 36 SHEET 6 AA3 6 THRHH 57 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 VALHH 12 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 LEUHH 102 N ARGHH 94 SHEET 1 AA5 4 SERHH 120 LEUHH 124 0 SHEET 2 AA5 4 ALAHH 136 TYRHH 145 -1 O GLYHH 139 N LEUHH 124 SHEET 3 AA5 4 TYRHH 176 VALHH 184 -1 O VALHH 184 N ALAHH 136 SHEET 4 AA5 4 VALHH 163 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 GLYHH 139 N LEUHH 124 SHEET 3 AA6 4 TYRHH 176 VALHH 184 -1 O VALHH 184 N ALAHH 136 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 ILEHH 195 HISHH 200 -1 O ASNHH 197 N SERHH 153 SHEET 3 AA7 3 THRHH 205 ARGHH 210 -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 THRLL 105 N VALLL 11 SHEET 3 AA8 6 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 SHEET 4 AA8 6 SERLL 34 GLNLL 38 -1 N GLNLL 38 O ASPLL 85 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 THRLL 105 N VALLL 11 SHEET 3 AA9 4 ALALL 84 ASPLL 92 -1 N ALALL 84 O LEULL 104 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 ALALL 71 N CYSLL 23 SHEET 3 AB1 3 PHELL 62 SERLL 67 -1 N SERLL 67 O SERLL 70 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 ALALL 175 N ILELL 137 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 ALALL 175 N ILELL 137 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 VALLL 203 N VALLL 196 SSBOND 1 CYSHH 22 CYSHH 92 1555 1555 2.07 SSBOND 2 CYSHH 140 CYSHH 196 1555 1555 2.03 SSBOND 3 CYSHH 216 CYSLL 212 1555 1555 2.05 SSBOND 4 CYSLL 23 CYSLL 88 1555 1555 2.09 SSBOND 5 CYSLL 135 CYSLL 194 1555 1555 2.10 LINK ND1 HISAA 120 MN MNAA 401 1555 1555 1.96 LINK OD2 ASPAA 143 MN MNAA 401 1555 1555 1.97 LINK OD1 ASPAA 143 MN MNAA 402 1555 1555 2.06 LINK ND1 HISAA 145 MN MNAA 402 1555 1555 2.09 LINK OD2 ASPAA 147 MN MNAA 401 1555 1555 2.00 LINK OD2 ASPAA 251 MN MNAA 401 1555 1555 1.99 LINK OD2 ASPAA 251 MN MNAA 402 1555 1555 2.02 LINK OD1 ASPAA 253 MN MNAA 402 1555 1555 2.06 LINK OD2 ASPAA 253 MN MNAA 402 1555 1555 2.03 LINK MN MNAA 401 O1 PO4AA 403 1555 1555 2.00 LINK MN MNAA 402 O1 PO4AA 403 1555 1555 1.97 CISPEP 1 VALAA 76 PROAA 77 0 5.73 CISPEP 2 PHEHH 146 PROHH 147 0 -8.92 CISPEP 3 GLUHH 148 PROHH 149 0 -10.73 CISPEP 4 TYRLL 141 PROLL 142 0 -15.17 CRYST1 150.380 150.380 110.740 90.00 90.00 120.00 P 3 2 1 6 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 0.006650 0.003839 0.000000 0.00000 SCALE2 0.000000 0.007679 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009030 0.00000