HEADER PROTEIN BINDING 06-SEP-19 6SS6 TITLE STRUCTURE OF ARGINASE-2 IN COMPLEX WITH THE INHIBITORY HUMAN ANTIGEN- TITLE 2 BINDING FRAGMENT FAB C0020187 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ARGINASE-2, MITOCHONDRIAL; COMPND 3 CHAIN: AAA, BBB, CCC; 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 C0020187 HEAVY CHAIN (IGG1); COMPND 10 CHAIN: HHH, III, JJJ; 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 C0020187 LIGHT CHAIN (IGG1); COMPND 16 CHAIN: LLL, MMM, NNN; 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 D.T.Y.CHAN,L.JENKINSON,S.W.HAYNES,M.AUSTIN,A.DIAMANDAKIS, JRNL AUTH 2 D.BURSCHOWSKY,C.SEEWOORUTHUN,A.ADDYMAN,S.FIEDLER,S.RYMAN, JRNL AUTH 3 J.WHITEHOUSE,L.H.SLATER,E.GOWANS,Y.SHIBATA,M.BARNARD, JRNL AUTH 4 R.W.WILKINSON,T.J.VAUGHAN,S.V.HOLT,V.CERUNDOLO,M.D.CARR, JRNL AUTH 5 M.A.T.GROVES JRNL TITL EXTENSIVE SEQUENCE AND STRUCTURAL EVOLUTION OF ARGINASE 2 JRNL TITL 2 INHIBITORY ANTIBODIES ENABLED BY AN UNBIASED APPROACH TO JRNL TITL 3 AFFINITY MATURATION. JRNL REF PROC.NATL.ACAD.SCI.USA V. 117 16949 2020 JRNL REFN ESSN 1091-6490 JRNL PMID 32616569 JRNL DOI 10.1073/PNAS.1919565117 REMARK 2 REMARK 2 RESOLUTION. 3.25 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) : 3.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.76 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 50320 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) : 0.300 REMARK 3 FREE R VALUE : 0.361 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.066 REMARK 3 FREE R VALUE TEST SET COUNT : 2549 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.25 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.33 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3463 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94 REMARK 3 BIN R VALUE (WORKING SET) : 0.4530 REMARK 3 BIN FREE R VALUE SET COUNT : 164 REMARK 3 BIN FREE R VALUE : 0.4620 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 16814 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 141 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) : 99.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -4.89700 REMARK 3 B22 (A**2) : -4.89700 REMARK 3 B33 (A**2) : 15.88600 REMARK 3 B12 (A**2) : -2.44800 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): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.711 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.949 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 66.427 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.888 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.825 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17342 ; 0.005 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 15678 ; 0.002 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23611 ; 1.463 ; 1.637 REMARK 3 BOND ANGLES OTHERS (DEGREES): 36533 ; 1.170 ; 1.569 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2234 ; 6.723 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 735 ;35.811 ;22.544 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2706 ;22.106 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 81 ;18.707 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2291 ; 0.060 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19344 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 3425 ; 0.002 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4076 ; 0.223 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 258 ; 0.315 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8271 ; 0.163 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 526 ; 0.204 ; 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): 8963 ; 4.602 ;10.787 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8962 ; 4.601 ;10.787 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11188 ; 7.820 ;16.170 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 11189 ; 7.820 ;16.170 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8376 ; 3.675 ;10.899 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8269 ; 3.673 ;10.842 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12423 ; 6.507 ;16.309 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 12262 ; 6.519 ;16.224 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 : 9 REMARK 3 REMARK 3 NCS GROUP NUMBER : 1 REMARK 3 CHAIN NAMES : Chains A B REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 2 REMARK 3 CHAIN NAMES : Chains A C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 3 REMARK 3 CHAIN NAMES : Chains B C REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 4 REMARK 3 CHAIN NAMES : Chains H I REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 5 REMARK 3 CHAIN NAMES : Chains H J REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 6 REMARK 3 CHAIN NAMES : Chains I J REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 7 REMARK 3 CHAIN NAMES : Chains L M REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 8 REMARK 3 CHAIN NAMES : Chains L N REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 NCS GROUP NUMBER : 9 REMARK 3 CHAIN NAMES : Chains M N REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0 REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE REMARK 3 GROUP CHAIN COUNT RMS WEIGHT REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 6SS6 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_1292104168. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-SEP-17 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 : I04-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587 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 : 50453 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.250 REMARK 200 RESOLUTION RANGE LOW (A) : 48.780 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 10.40 REMARK 200 R MERGE (I) : 0.78000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.36 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 9.90 REMARK 200 R MERGE FOR SHELL (I) : 8.48000 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: 4HZE,6SS5 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.51 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M (NH4)2SO4, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+2/3 REMARK 290 3555 -X+Y,-X,Z+1/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+1/6 REMARK 290 6555 X-Y,X,Z+5/6 REMARK 290 7555 Y,X,-Z+2/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+1/3 REMARK 290 10555 -Y,-X,-Z+1/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+5/6 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 367.53800 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 183.76900 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 275.65350 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 91.88450 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 459.42250 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 367.53800 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 183.76900 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 91.88450 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 275.65350 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 459.42250 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: 24740 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 92300 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -424.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB, CCC, HHH, III, JJJ, REMARK 350 AND CHAINS: LLL, MMM, NNN REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 22 REMARK 465 VAL A 23 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 GLY A 355 REMARK 465 GLY A 356 REMARK 465 GLY A 357 REMARK 465 HIS A 358 REMARK 465 HIS A 359 REMARK 465 HIS A 360 REMARK 465 HIS A 361 REMARK 465 HIS A 362 REMARK 465 HIS A 363 REMARK 465 HIS A 364 REMARK 465 HIS A 365 REMARK 465 HIS A 366 REMARK 465 HIS A 367 REMARK 465 MET B 22 REMARK 465 VAL B 23 REMARK 465 ILE B 332 REMARK 465 VAL B 333 REMARK 465 TYR B 334 REMARK 465 ASP B 335 REMARK 465 GLN B 336 REMARK 465 LEU B 337 REMARK 465 PRO B 338 REMARK 465 THR B 339 REMARK 465 PRO B 340 REMARK 465 SER B 341 REMARK 465 SER B 342 REMARK 465 PRO B 343 REMARK 465 ASP B 344 REMARK 465 GLU B 345 REMARK 465 SER B 346 REMARK 465 GLU B 347 REMARK 465 ASN B 348 REMARK 465 GLN B 349 REMARK 465 ALA B 350 REMARK 465 ARG B 351 REMARK 465 VAL B 352 REMARK 465 ARG B 353 REMARK 465 ILE B 354 REMARK 465 GLY B 355 REMARK 465 GLY B 356 REMARK 465 GLY B 357 REMARK 465 HIS B 358 REMARK 465 HIS B 359 REMARK 465 HIS B 360 REMARK 465 HIS B 361 REMARK 465 HIS B 362 REMARK 465 HIS B 363 REMARK 465 HIS B 364 REMARK 465 HIS B 365 REMARK 465 HIS B 366 REMARK 465 HIS B 367 REMARK 465 MET C 22 REMARK 465 VAL C 23 REMARK 465 SER C 341 REMARK 465 SER C 342 REMARK 465 PRO C 343 REMARK 465 ASP C 344 REMARK 465 GLU C 345 REMARK 465 SER C 346 REMARK 465 GLU C 347 REMARK 465 ASN C 348 REMARK 465 GLN C 349 REMARK 465 ALA C 350 REMARK 465 ARG C 351 REMARK 465 VAL C 352 REMARK 465 ARG C 353 REMARK 465 ILE C 354 REMARK 465 GLY C 355 REMARK 465 GLY C 356 REMARK 465 GLY C 357 REMARK 465 HIS C 358 REMARK 465 HIS C 359 REMARK 465 HIS C 360 REMARK 465 HIS C 361 REMARK 465 HIS C 362 REMARK 465 HIS C 363 REMARK 465 HIS C 364 REMARK 465 HIS C 365 REMARK 465 HIS C 366 REMARK 465 HIS C 367 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 I -3 REMARK 465 ALA I -2 REMARK 465 HIS I -1 REMARK 465 SER I 0 REMARK 465 CYS I 216 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 J -3 REMARK 465 ALA J -2 REMARK 465 HIS J -1 REMARK 465 SER J 0 REMARK 465 GLU J 1 REMARK 465 PRO J 213 REMARK 465 LYS J 214 REMARK 465 SER J 215 REMARK 465 CYS J 216 REMARK 465 ASP J 217 REMARK 465 LYS J 218 REMARK 465 THR J 219 REMARK 465 HIS J 220 REMARK 465 ALA J 221 REMARK 465 ALA J 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 465 GLY N -2 REMARK 465 VAL N -1 REMARK 465 HIS N 0 REMARK 465 SER N 1 REMARK 465 PRO N 209 REMARK 465 THR N 210 REMARK 465 GLU N 211 REMARK 465 CYS N 212 REMARK 465 SER N 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 HG1 THRCC 154 ND2 ASNCC 158 0.70 REMARK 500 HH11 ARGCC 39 HD1 HISCC 160 0.87 REMARK 500 OG1 THRCC 154 HD22 ASNCC 158 0.95 REMARK 500 HB3 CYSNN 135 HH2 TRPNN 149 1.01 REMARK 500 HE22 GLNBB 35 HG2 ARGBB 39 1.03 REMARK 500 HZ3 TRPNN 149 HB2 CYSNN 194 1.13 REMARK 500 HD1 HISBB 120 MN MNBB 401 1.15 REMARK 500 HD1 HISCC 120 MN MNCC 401 1.18 REMARK 500 HB3 ASNBB 149 HG21 THRBB 154 1.19 REMARK 500 HZ3 LYSMM 167 HH TYRMM 173 1.21 REMARK 500 NH1 ARGCC 39 HD1 HISCC 160 1.21 REMARK 500 HB3 LEUNN 39 HD2 PRONN 40 1.26 REMARK 500 HD3 LYSNN 167 HH TYRNN 173 1.31 REMARK 500 HE ARGCC 199 HG13 VALCC 267 1.33 REMARK 500 HG SERHH 127 H SERHH 130 1.33 REMARK 500 HH11 ARGJJ 94 OD2 ASPJJ 101 1.34 REMARK 500 HD3 PROJJ 119 HD1 HISJJ 200 1.34 REMARK 500 HE2 LYSHH 143 HG1 THRLL 132 1.34 REMARK 500 OD1 ASPAA 143 HD1 HISAA 145 1.36 REMARK 500 OD1 ASNCC 298 H LEUCC 301 1.36 REMARK 500 O ASNLL 27B HD1 HISLL 31 1.37 REMARK 500 H THRNN 182 OE1 GLNNN 185 1.37 REMARK 500 O ALALL 13 H LEULL 107 1.38 REMARK 500 HD1 HISAA 120 MN MNAA 401 1.40 REMARK 500 OD1 ASNCC 88 HD3 PROCC 89 1.41 REMARK 500 O LEUBB 159 H GLNBB 162 1.44 REMARK 500 OG1 THRCC 154 ND2 ASNCC 158 1.47 REMARK 500 OG SERHH 127 H SERHH 130 1.51 REMARK 500 HE ARGJJ 94 OD1 ASPJJ 101 1.52 REMARK 500 O GLYJJ 52A HD21 ASNJJ 73 1.54 REMARK 500 OD1 ASPBB 143 HD1 HISBB 145 1.56 REMARK 500 OG1 THRHH 87 HG23 VALHH 111 1.56 REMARK 500 O THRCC 74 H VALCC 76 1.58 REMARK 500 O VALAA 102 HG3 ARGAA 105 1.58 REMARK 500 O VALCC 42 H GLYCC 45 1.59 REMARK 500 H VALJJ 2 O SERJJ 25 1.60 REMARK 500 OD1 ASPCC 119 OG SERCC 121 1.70 REMARK 500 OD2 ASPBB 251 OE1 GLUBB 296 1.96 REMARK 500 O THRBB 150 NE2 GLNBB 162 2.03 REMARK 500 OG1 THRCC 150 OG1 THRCC 153 2.06 REMARK 500 OD1 ASNCC 149 OE2 GLUCC 205 2.07 REMARK 500 OG SERNN 193 O LYSNN 205 2.10 REMARK 500 CZ3 TRPNN 149 CB CYSNN 194 2.11 REMARK 500 OG1 THRJJ 165 OG SERJJ 180 2.13 REMARK 500 NH1 ARGCC 39 ND1 HISCC 160 2.14 REMARK 500 OG SERHH 203 OG1 THRHH 205 2.16 REMARK 500 NH1 ARGJJ 94 OD2 ASPJJ 101 2.17 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 HG12 VALBB 76 HG SERNN 95A 8555 0.79 REMARK 500 HZ3 LYSAA 40 HZ3 LYSAA 40 8555 1.17 REMARK 500 HZ2 LYSAA 40 HZ2 LYSAA 40 8555 1.20 REMARK 500 HG SERLL 188 OG SERNN 26 8545 1.35 REMARK 500 CG1 VALBB 76 HG SERNN 95A 8555 1.39 REMARK 500 OG SERLL 188 HG SERNN 26 8545 1.43 REMARK 500 OE1 GLNAA 300 OE1 GLNAA 300 8555 1.48 REMARK 500 HG12 VALBB 76 OG SERNN 95A 8555 1.51 REMARK 500 ND2 ASNHH 204 O ARGII 105 8555 2.10 REMARK 500 CG1 VALBB 76 OG SERNN 95A 8555 2.14 REMARK 500 OG SERLL 188 OG SERNN 26 8545 2.15 REMARK 500 NZ LYSAA 40 NZ LYSAA 40 8555 2.16 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 TYRBB 82 CB - CA - C ANGL. DEV. = 18.9 DEGREES REMARK 500 PROCC 77 N - CA - CB ANGL. DEV. = -9.6 DEGREES REMARK 500 PROII 213 C - N - CA ANGL. DEV. = 12.8 DEGREES REMARK 500 PROII 213 CA - N - CD ANGL. DEV. = -8.4 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 PROAA 77 -81.58 -96.12 REMARK 500 ASPAA 79 166.69 79.99 REMARK 500 ASPAA 80 -121.60 58.85 REMARK 500 LEUAA 81 -136.69 54.61 REMARK 500 LEUAA 85 -9.50 87.15 REMARK 500 ILEAA 86 -82.71 -129.12 REMARK 500 CYSAA 134 72.56 -117.00 REMARK 500 ASPAA 143 143.37 -170.45 REMARK 500 ARGAA 199 -32.14 -141.15 REMARK 500 ASPAA 213 31.07 74.77 REMARK 500 ALAAA 260 62.73 -118.54 REMARK 500 ALAAA 262 62.50 -108.41 REMARK 500 VALAA 297 32.24 -97.87 REMARK 500 HISAA 331 -134.12 59.07 REMARK 500 LEUAA 337 45.44 -152.90 REMARK 500 GLNBB 37 -50.86 62.91 REMARK 500 VALBB 76 166.52 82.56 REMARK 500 LEUBB 81 119.61 -172.14 REMARK 500 TYRBB 82 -124.91 55.81 REMARK 500 ASNBB 83 -62.88 67.26 REMARK 500 ILEBB 86 -80.87 -129.76 REMARK 500 CYSBB 134 72.61 -117.18 REMARK 500 ASPBB 143 143.87 -171.25 REMARK 500 SERBB 155 -158.74 64.25 REMARK 500 PROBB 163 -72.69 -76.63 REMARK 500 VALBB 164 -36.12 -33.59 REMARK 500 ASPBB 213 33.44 73.51 REMARK 500 ALABB 260 62.10 -118.10 REMARK 500 ALABB 262 59.01 -107.49 REMARK 500 LYSCC 38 -12.00 76.39 REMARK 500 LEUCC 71 -155.68 -90.56 REMARK 500 THRCC 74 108.03 -55.79 REMARK 500 PROCC 75 41.94 -51.14 REMARK 500 PROCC 77 -120.08 12.65 REMARK 500 ASPCC 80 -149.96 -165.79 REMARK 500 LEUCC 81 -142.82 63.19 REMARK 500 ILECC 86 -43.23 -133.54 REMARK 500 CYSCC 134 73.00 -117.29 REMARK 500 ASPCC 143 144.11 -171.59 REMARK 500 SERCC 156 -56.41 70.54 REMARK 500 ASNCC 158 -97.59 -90.49 REMARK 500 GLNCC 162 18.93 -163.36 REMARK 500 PROCC 186 105.72 -44.41 REMARK 500 ARGCC 199 -33.94 -135.51 REMARK 500 ASPCC 213 33.06 74.03 REMARK 500 ALACC 260 64.13 -119.30 REMARK 500 ALACC 262 68.73 -108.84 REMARK 500 ARGCC 327 -45.28 72.05 REMARK 500 ILECC 332 119.78 -38.84 REMARK 500 LEUHH 18 144.23 -173.13 REMARK 500 REMARK 500 THIS ENTRY HAS 92 RAMACHANDRAN OUTLIERS. 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 GLYCC 157 ASNCC 158 -148.58 REMARK 500 ASNCC 158 LEUCC 159 -147.26 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 108.8 REMARK 620 3 ASP A 147 OD2 98.5 89.9 REMARK 620 4 ASP A 251 OD2 101.5 93.8 157.3 REMARK 620 N 1 2 3 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 66.7 REMARK 620 3 ASP A 251 OD2 96.4 146.7 REMARK 620 4 ASP A 253 OD1 85.3 116.4 89.0 REMARK 620 5 ASP A 253 OD2 150.2 121.9 87.3 65.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN B 401 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS B 120 ND1 REMARK 620 2 ASP B 143 OD2 113.8 REMARK 620 3 ASP B 147 OD2 97.6 91.6 REMARK 620 4 ASP B 251 OD2 106.0 94.6 150.6 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN B 402 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 143 OD1 REMARK 620 2 HIS B 145 ND1 74.2 REMARK 620 3 ASP B 251 OD2 94.7 150.8 REMARK 620 4 ASP B 253 OD1 96.8 103.8 104.4 REMARK 620 5 GLU B 296 OE1 143.8 132.7 49.5 98.2 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN C 401 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS C 120 ND1 REMARK 620 2 ASP C 143 OD2 115.7 REMARK 620 3 ASP C 147 OD2 71.1 88.7 REMARK 620 4 ASP C 251 OD2 114.0 95.9 170.4 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN C 402 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 143 OD1 REMARK 620 2 HIS C 145 ND1 83.9 REMARK 620 3 ASP C 251 OD2 90.2 131.4 REMARK 620 4 ASP C 253 OD1 86.7 146.5 80.6 REMARK 620 5 ASP C 253 OD2 151.4 120.9 83.4 64.8 REMARK 620 N 1 2 3 4 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: 6SS4 RELATED DB: PDB REMARK 900 RELATED ID: 6SS5 RELATED DB: PDB REMARK 900 RELATED ID: 6TUL RELATED DB: PDB DBREF 6SS6AA 23 354 UNP P78540 ARGI2_HUMAN 23 354 DBREF 6SS6BB 23 354 UNP P78540 ARGI2_HUMAN 23 354 DBREF 6SS6CC 23 354 UNP P78540 ARGI2_HUMAN 23 354 DBREF 6SS6HH -3 222 PDB 6SS6 6SS6 -3 222 DBREF 6SS6II -3 222 PDB 6SS6 6SS6 -3 222 DBREF 6SS6JJ -3 222 PDB 6SS6 6SS6 -3 222 DBREF 6SS6LL -2 213 PDB 6SS6 6SS6 -2 213 DBREF 6SS6MM -2 213 PDB 6SS6 6SS6 -2 213 DBREF 6SS6NN -2 213 PDB 6SS6 6SS6 -2 213 SEQADV 6SS6 METAA 22 UNP P78540 INITIATING METHIONINE SEQADV 6SS6 GLYAA 355 UNP P78540 EXPRESSION TAG SEQADV 6SS6 GLYAA 356 UNP P78540 EXPRESSION TAG SEQADV 6SS6 GLYAA 357 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 358 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 359 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 360 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 361 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 362 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 363 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 364 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 365 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 366 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISAA 367 UNP P78540 EXPRESSION TAG SEQADV 6SS6 METBB 22 UNP P78540 INITIATING METHIONINE SEQADV 6SS6 GLYBB 355 UNP P78540 EXPRESSION TAG SEQADV 6SS6 GLYBB 356 UNP P78540 EXPRESSION TAG SEQADV 6SS6 GLYBB 357 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 358 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 359 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 360 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 361 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 362 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 363 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 364 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 365 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 366 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISBB 367 UNP P78540 EXPRESSION TAG SEQADV 6SS6 METCC 22 UNP P78540 INITIATING METHIONINE SEQADV 6SS6 GLYCC 355 UNP P78540 EXPRESSION TAG SEQADV 6SS6 GLYCC 356 UNP P78540 EXPRESSION TAG SEQADV 6SS6 GLYCC 357 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 358 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 359 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 360 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 361 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 362 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 363 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 364 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 365 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 366 UNP P78540 EXPRESSION TAG SEQADV 6SS6 HISCC 367 UNP P78540 EXPRESSION TAG SEQRES 1AA 346 MET VAL HIS SER VAL ALA VAL ILE GLY ALA PRO PHE SER SEQRES 2AA 346 GLN GLY GLN LYS ARG LYS GLY VAL GLU HIS GLY PRO ALA SEQRES 3AA 346 ALA ILE ARG GLU ALA GLY LEU MET LYS ARG LEU SER SER SEQRES 4AA 346 LEU GLY CYS HIS LEU LYS ASP PHE GLY ASP LEU SER PHE SEQRES 5AA 346 THR PRO VAL PRO LYS ASP ASP LEU TYR ASN ASN LEU ILE SEQRES 6AA 346 VAL ASN PRO ARG SER VAL GLY LEU ALA ASN GLN GLU LEU SEQRES 7AA 346 ALA GLU VAL VAL SER ARG ALA VAL SER ASP GLY TYR SER SEQRES 8AA 346 CYS VAL THR LEU GLY GLY ASP HIS SER LEU ALA ILE GLY SEQRES 9AA 346 THR ILE SER GLY HIS ALA ARG HIS CYS PRO ASP LEU CYS SEQRES 10AA 346 VAL VAL TRP VAL ASP ALA HIS ALA ASP ILE ASN THR PRO SEQRES 11AA 346 LEU THR THR SER SER GLY ASN LEU HIS GLY GLN PRO VAL SEQRES 12AA 346 SER PHE LEU LEU ARG GLU LEU GLN ASP LYS VAL PRO GLN SEQRES 13AA 346 LEU PRO GLY PHE SER TRP ILE LYS PRO CYS ILE SER SER SEQRES 14AA 346 ALA SER ILE VAL TYR ILE GLY LEU ARG ASP VAL ASP PRO SEQRES 15AA 346 PRO GLU HIS PHE ILE LEU LYS ASN TYR ASP ILE GLN TYR SEQRES 16AA 346 PHE SER MET ARG ASP ILE ASP ARG LEU GLY ILE GLN LYS SEQRES 17AA 346 VAL MET GLU ARG THR PHE ASP LEU LEU ILE GLY LYS ARG SEQRES 18AA 346 GLN ARG PRO ILE HIS LEU SER PHE ASP ILE ASP ALA PHE SEQRES 19AA 346 ASP PRO THR LEU ALA PRO ALA THR GLY THR PRO VAL VAL SEQRES 20AA 346 GLY GLY LEU THR TYR ARG GLU GLY MET TYR ILE ALA GLU SEQRES 21AA 346 GLU ILE HIS ASN THR GLY LEU LEU SER ALA LEU ASP LEU SEQRES 22AA 346 VAL GLU VAL ASN PRO GLN LEU ALA THR SER GLU GLU GLU SEQRES 23AA 346 ALA LYS THR THR ALA ASN LEU ALA VAL ASP VAL ILE ALA SEQRES 24AA 346 SER SER PHE GLY GLN THR ARG GLU GLY GLY HIS ILE VAL SEQRES 25AA 346 TYR ASP GLN LEU PRO THR PRO SER SER PRO ASP GLU SER SEQRES 26AA 346 GLU ASN GLN ALA ARG VAL ARG ILE GLY GLY GLY HIS HIS SEQRES 27AA 346 HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1BB 346 MET VAL HIS SER VAL ALA VAL ILE GLY ALA PRO PHE SER SEQRES 2BB 346 GLN GLY GLN LYS ARG LYS GLY VAL GLU HIS GLY PRO ALA SEQRES 3BB 346 ALA ILE ARG GLU ALA GLY LEU MET LYS ARG LEU SER SER SEQRES 4BB 346 LEU GLY CYS HIS LEU LYS ASP PHE GLY ASP LEU SER PHE SEQRES 5BB 346 THR PRO VAL PRO LYS ASP ASP LEU TYR ASN ASN LEU ILE SEQRES 6BB 346 VAL ASN PRO ARG SER VAL GLY LEU ALA ASN GLN GLU LEU SEQRES 7BB 346 ALA GLU VAL VAL SER ARG ALA VAL SER ASP GLY TYR SER SEQRES 8BB 346 CYS VAL THR LEU GLY GLY ASP HIS SER LEU ALA ILE GLY SEQRES 9BB 346 THR ILE SER GLY HIS ALA ARG HIS CYS PRO ASP LEU CYS SEQRES 10BB 346 VAL VAL TRP VAL ASP ALA HIS ALA ASP ILE ASN THR PRO SEQRES 11BB 346 LEU THR THR SER SER GLY ASN LEU HIS GLY GLN PRO VAL SEQRES 12BB 346 SER PHE LEU LEU ARG GLU LEU GLN ASP LYS VAL PRO GLN SEQRES 13BB 346 LEU PRO GLY PHE SER TRP ILE LYS PRO CYS ILE SER SER SEQRES 14BB 346 ALA SER ILE VAL TYR ILE GLY LEU ARG ASP VAL ASP PRO SEQRES 15BB 346 PRO GLU HIS PHE ILE LEU LYS ASN TYR ASP ILE GLN TYR SEQRES 16BB 346 PHE SER MET ARG ASP ILE ASP ARG LEU GLY ILE GLN LYS SEQRES 17BB 346 VAL MET GLU ARG THR PHE ASP LEU LEU ILE GLY LYS ARG SEQRES 18BB 346 GLN ARG PRO ILE HIS LEU SER PHE ASP ILE ASP ALA PHE SEQRES 19BB 346 ASP PRO THR LEU ALA PRO ALA THR GLY THR PRO VAL VAL SEQRES 20BB 346 GLY GLY LEU THR TYR ARG GLU GLY MET TYR ILE ALA GLU SEQRES 21BB 346 GLU ILE HIS ASN THR GLY LEU LEU SER ALA LEU ASP LEU SEQRES 22BB 346 VAL GLU VAL ASN PRO GLN LEU ALA THR SER GLU GLU GLU SEQRES 23BB 346 ALA LYS THR THR ALA ASN LEU ALA VAL ASP VAL ILE ALA SEQRES 24BB 346 SER SER PHE GLY GLN THR ARG GLU GLY GLY HIS ILE VAL SEQRES 25BB 346 TYR ASP GLN LEU PRO THR PRO SER SER PRO ASP GLU SER SEQRES 26BB 346 GLU ASN GLN ALA ARG VAL ARG ILE GLY GLY GLY HIS HIS SEQRES 27BB 346 HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1CC 346 MET VAL HIS SER VAL ALA VAL ILE GLY ALA PRO PHE SER SEQRES 2CC 346 GLN GLY GLN LYS ARG LYS GLY VAL GLU HIS GLY PRO ALA SEQRES 3CC 346 ALA ILE ARG GLU ALA GLY LEU MET LYS ARG LEU SER SER SEQRES 4CC 346 LEU GLY CYS HIS LEU LYS ASP PHE GLY ASP LEU SER PHE SEQRES 5CC 346 THR PRO VAL PRO LYS ASP ASP LEU TYR ASN ASN LEU ILE SEQRES 6CC 346 VAL ASN PRO ARG SER VAL GLY LEU ALA ASN GLN GLU LEU SEQRES 7CC 346 ALA GLU VAL VAL SER ARG ALA VAL SER ASP GLY TYR SER SEQRES 8CC 346 CYS VAL THR LEU GLY GLY ASP HIS SER LEU ALA ILE GLY SEQRES 9CC 346 THR ILE SER GLY HIS ALA ARG HIS CYS PRO ASP LEU CYS SEQRES 10CC 346 VAL VAL TRP VAL ASP ALA HIS ALA ASP ILE ASN THR PRO SEQRES 11CC 346 LEU THR THR SER SER GLY ASN LEU HIS GLY GLN PRO VAL SEQRES 12CC 346 SER PHE LEU LEU ARG GLU LEU GLN ASP LYS VAL PRO GLN SEQRES 13CC 346 LEU PRO GLY PHE SER TRP ILE LYS PRO CYS ILE SER SER SEQRES 14CC 346 ALA SER ILE VAL TYR ILE GLY LEU ARG ASP VAL ASP PRO SEQRES 15CC 346 PRO GLU HIS PHE ILE LEU LYS ASN TYR ASP ILE GLN TYR SEQRES 16CC 346 PHE SER MET ARG ASP ILE ASP ARG LEU GLY ILE GLN LYS SEQRES 17CC 346 VAL MET GLU ARG THR PHE ASP LEU LEU ILE GLY LYS ARG SEQRES 18CC 346 GLN ARG PRO ILE HIS LEU SER PHE ASP ILE ASP ALA PHE SEQRES 19CC 346 ASP PRO THR LEU ALA PRO ALA THR GLY THR PRO VAL VAL SEQRES 20CC 346 GLY GLY LEU THR TYR ARG GLU GLY MET TYR ILE ALA GLU SEQRES 21CC 346 GLU ILE HIS ASN THR GLY LEU LEU SER ALA LEU ASP LEU SEQRES 22CC 346 VAL GLU VAL ASN PRO GLN LEU ALA THR SER GLU GLU GLU SEQRES 23CC 346 ALA LYS THR THR ALA ASN LEU ALA VAL ASP VAL ILE ALA SEQRES 24CC 346 SER SER PHE GLY GLN THR ARG GLU GLY GLY HIS ILE VAL SEQRES 25CC 346 TYR ASP GLN LEU PRO THR PRO SER SER PRO ASP GLU SER SEQRES 26CC 346 GLU ASN GLN ALA ARG VAL ARG ILE GLY GLY GLY HIS HIS SEQRES 27CC 346 HIS HIS HIS HIS HIS HIS HIS 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 SER SER TYR ALA MET SER 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 SER SER TYR ALA MET SER 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 1JJ 233 GLY ALA HIS SER GLU VAL GLN LEU LEU GLU SER GLY GLY SEQRES 2JJ 233 GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS SEQRES 3JJ 233 ALA ALA SER GLY PHE THR PHE SER SER TYR ALA MET SER SEQRES 4JJ 233 TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL SEQRES 5JJ 233 SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA SEQRES 6JJ 233 ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN SEQRES 7JJ 233 SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG SEQRES 8JJ 233 ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG LEU ARG SEQRES 9JJ 233 ALA ASP LEU GLY LEU TYR MET ASP LEU TRP GLY ARG GLY SEQRES 10JJ 233 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11JJ 233 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12JJ 233 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13JJ 233 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14JJ 233 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15JJ 233 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16JJ 233 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17JJ 233 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG SEQRES 18JJ 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 PRO 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 SER SER LEU SER ALA 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 ILE SER CYS SEQRES 3MM 220 SER GLY SER SER SER ASN ILE GLY ASN HIS TYR VAL SER SEQRES 4MM 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5MM 220 ILE TYR ASP ASN SER GLU ARG PRO SER GLY ILE 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 SER SER LEU SER ALA 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 SEQRES 1NN 220 GLY VAL HIS SER GLN SER VAL LEU THR GLN PRO PRO SER SEQRES 2NN 220 VAL SER ALA ALA PRO GLY GLN LYS VAL THR ILE SER CYS SEQRES 3NN 220 SER GLY SER SER SER ASN ILE GLY ASN HIS TYR VAL SER SEQRES 4NN 220 TRP TYR GLN GLN LEU PRO GLY THR ALA PRO LYS LEU LEU SEQRES 5NN 220 ILE TYR ASP ASN SER GLU ARG PRO SER GLY ILE PRO ASP SEQRES 6NN 220 ARG PHE SER GLY SER LYS SER GLY THR SER ALA THR LEU SEQRES 7NN 220 GLY ILE THR GLY LEU GLN THR GLY ASP GLU ALA ASP TYR SEQRES 8NN 220 TYR CYS GLY THR TRP ASP SER SER LEU SER ALA LEU VAL SEQRES 9NN 220 PHE GLY GLY GLY THR LYS LEU THR VAL LEU GLY GLN PRO SEQRES 10NN 220 LYS ALA ALA PRO SER VAL THR LEU PHE PRO PRO SER SER SEQRES 11NN 220 GLU GLU LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU SEQRES 12NN 220 ILE SER ASP PHE TYR PRO GLY ALA VAL THR VAL ALA TRP SEQRES 13NN 220 LYS ALA ASP SER SER PRO VAL LYS ALA GLY VAL GLU THR SEQRES 14NN 220 THR THR PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SEQRES 15NN 220 SER SER TYR LEU SER LEU THR PRO GLU GLN TRP LYS SER SEQRES 16NN 220 HIS ARG SER TYR SER CYS GLN VAL THR HIS GLU GLY SER SEQRES 17NN 220 THR VAL GLU LYS THR VAL ALA PRO THR GLU CYS SER HET MN AA 401 1 HET MN AA 402 1 HET SO4 AA 403 5 HET SO4 AA 404 5 HET SO4 AA 405 5 HET MN BB 401 1 HET MN BB 402 1 HET SO4 BB 403 5 HET SO4 BB 404 5 HET SO4 BB 405 5 HET MN CC 401 1 HET MN CC 402 1 HET SO4 CC 403 5 HET SO4 CC 404 5 HET SO4 CC 405 5 HET SO4 CC 406 5 HET SO4 CC 407 5 HET SO4 CC 408 5 HET SO4 HH 301 5 HET SO4 HH 302 5 HET SO4 HH 303 5 HET SO4 HH 304 5 HET SO4 HH 305 5 HET SO4 II 301 5 HET SO4 II 302 5 HET SO4 II 303 5 HET SO4 II 304 5 HET SO4 JJ 301 5 HET SO4 LL 301 5 HET SO4 LL 302 5 HET SO4 MM 301 5 HET SO4 MM 302 5 HET SO4 MM 303 5 HETNAM MN MANGANESE (II) ION HETNAM SO4 SULFATE ION FORMUL 10 MN 6(MN 2+) FORMUL 12 SO4 27(O4 S 2-) HELIX 1 AA1 GLUAA 43 ALAAA 52 1 10 HELIX 2 AA2 GLYAA 53 LEUAA 61 1 9 HELIX 3 AA3 ILEAA 86 ASPAA 109 1 24 HELIX 4 AA4 ASPAA 119 SERAA 121 5 3 HELIX 5 AA5 LEUAA 122 ARGAA 132 1 11 HELIX 6 AA6 VALAA 164 VALAA 175 5 12 HELIX 7 AA7 SERAA 189 ALAAA 191 5 3 HELIX 8 AA8 ASPAA 202 TYRAA 212 1 11 HELIX 9 AA9 METAA 219 GLYAA 226 1 8 HELIX 10 AB1 GLYAA 226 ILEAA 239 1 14 HELIX 11 AB2 ASPAA 253 PHEAA 255 5 3 HELIX 12 AB3 THRAA 272 GLYAA 287 1 16 HELIX 13 AB4 ASNAA 298 ALAAA 302 5 5 HELIX 14 AB5 SERAA 304 PHEAA 323 1 20 HELIX 15 AB6 ARGBB 39 GLUBB 43 5 5 HELIX 16 AB7 HISBB 44 ALABB 52 1 9 HELIX 17 AB8 GLYBB 53 LEUBB 61 1 9 HELIX 18 AB9 ILEBB 86 ASPBB 109 1 24 HELIX 19 AC1 ASPBB 119 SERBB 121 5 3 HELIX 20 AC2 LEUBB 122 ARGBB 132 1 11 HELIX 21 AC3 PROBB 163 VALBB 175 5 13 HELIX 22 AC4 SERBB 189 ALABB 191 5 3 HELIX 23 AC5 ASPBB 202 TYRBB 212 1 11 HELIX 24 AC6 METBB 219 GLYBB 226 1 8 HELIX 25 AC7 GLYBB 226 ILEBB 239 1 14 HELIX 26 AC8 ASPBB 253 PHEBB 255 5 3 HELIX 27 AC9 THRBB 272 GLYBB 287 1 16 HELIX 28 AD1 ASNBB 298 ALABB 302 5 5 HELIX 29 AD2 SERBB 304 PHEBB 323 1 20 HELIX 30 AD3 GLUCC 43 ALACC 52 1 10 HELIX 31 AD4 GLYCC 53 LEUCC 61 1 9 HELIX 32 AD5 ILECC 86 ASPCC 109 1 24 HELIX 33 AD6 ASPCC 119 SERCC 121 5 3 HELIX 34 AD7 LEUCC 122 ARGCC 132 1 11 HELIX 35 AD8 THRCC 150 THRCC 154 5 5 HELIX 36 AD9 ASNCC 158 LEUCC 168 5 11 HELIX 37 AE1 LEUCC 171 VALCC 175 5 5 HELIX 38 AE2 SERCC 189 ALACC 191 5 3 HELIX 39 AE3 ASPCC 202 TYRCC 212 1 11 HELIX 40 AE4 METCC 219 GLYCC 226 1 8 HELIX 41 AE5 GLYCC 226 ILECC 239 1 14 HELIX 42 AE6 ASPCC 253 PHECC 255 5 3 HELIX 43 AE7 THRCC 272 GLYCC 287 1 16 HELIX 44 AE8 SERCC 304 PHECC 323 1 20 HELIX 45 AE9 THRHH 28 TYRHH 32 5 5 HELIX 46 AF1 ASNHH 73 LYSHH 75 5 3 HELIX 47 AF2 ARGHH 83 THRHH 87 5 5 HELIX 48 AF3 SERHH 156 ALAHH 158 5 3 HELIX 49 AF4 SERHH 186 GLYHH 190 1 5 HELIX 50 AF5 PROHH 202 ASNHH 204 5 3 HELIX 51 AF6 THRII 28 TYRII 32 5 5 HELIX 52 AF7 ARGII 83 THRII 87 5 5 HELIX 53 AF8 SERII 156 ALAII 158 5 3 HELIX 54 AF9 SERII 187 GLNII 192 5 6 HELIX 55 AG1 PROII 202 ASNII 204 5 3 HELIX 56 AG2 THRJJ 28 TYRJJ 32 5 5 HELIX 57 AG3 ASNJJ 73 LYSJJ 75 5 3 HELIX 58 AG4 ARGJJ 83 THRJJ 87 5 5 HELIX 59 AG5 SERJJ 156 ALAJJ 158 5 3 HELIX 60 AG6 SERJJ 186 GLYJJ 190 1 5 HELIX 61 AG7 LYSJJ 201 ASNJJ 204 5 4 HELIX 62 AG8 GLNLL 79 GLULL 83 5 5 HELIX 63 AG9 SERLL 122 ALALL 128 1 7 HELIX 64 AH1 THRLL 182 SERLL 188 1 7 HELIX 65 AH2 GLNMM 79 GLUMM 83 5 5 HELIX 66 AH3 SERMM 122 ALAMM 128 1 7 HELIX 67 AH4 THRMM 182 SERMM 188 1 7 HELIX 68 AH5 GLNNN 79 GLUNN 83 5 5 HELIX 69 AH6 SERNN 122 ASNNN 129 1 8 HELIX 70 AH7 THRNN 182 SERNN 188 1 7 SHEET 1 AA1 8 HISAA 64 ASPAA 70 0 SHEET 2 AA1 8 SERAA 25 ALAAA 31 1 N VALAA 26 O HISAA 64 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 PHEAA 250 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 8 HISBB 64 ASPBB 70 0 SHEET 2 AA2 8 SERBB 25 ALABB 31 1 N VALBB 26 O HISBB 64 SHEET 3 AA2 8 SERBB 112 GLYBB 117 1 O VALBB 114 N ALABB 27 SHEET 4 AA2 8 LEUBB 289 VALBB 295 1 O LEUBB 292 N CYSBB 113 SHEET 5 AA2 8 ILEBB 246 ASPBB 251 1 N PHEBB 250 O ASPBB 293 SHEET 6 AA2 8 CYSBB 138 VALBB 142 1 N VALBB 142 O ASPBB 251 SHEET 7 AA2 8 ILEBB 193 LEUBB 198 1 O ILEBB 196 N TRPBB 141 SHEET 8 AA2 8 GLNBB 215 SERBB 218 1 O PHEBB 217 N TYRBB 195 SHEET 1 AA3 8 HISCC 64 ASPCC 70 0 SHEET 2 AA3 8 SERCC 25 ALACC 31 1 N VALCC 26 O HISCC 64 SHEET 3 AA3 8 SERCC 112 GLYCC 117 1 O VALCC 114 N ALACC 27 SHEET 4 AA3 8 LEUCC 289 VALCC 295 1 O LEUCC 292 N CYSCC 113 SHEET 5 AA3 8 ILECC 246 ASPCC 251 1 N PHECC 250 O ASPCC 293 SHEET 6 AA3 8 CYSCC 138 VALCC 142 1 N VALCC 142 O ASPCC 251 SHEET 7 AA3 8 ILECC 193 LEUCC 198 1 O ILECC 196 N TRPCC 141 SHEET 8 AA3 8 GLNCC 215 SERCC 218 1 O PHECC 217 N GLYCC 197 SHEET 1 AA4 4 GLNHH 3 SERHH 7 0 SHEET 2 AA4 4 LEUHH 18 SERHH 25 -1 O ALAHH 23 N LEUHH 5 SHEET 3 AA4 4 THRHH 77 METHH 82 -1 O METHH 82 N LEUHH 18 SHEET 4 AA4 4 PHEHH 67 ASPHH 72 -1 N SERHH 70 O TYRHH 79 SHEET 1 AA5 5 THRHH 57 TYRHH 59 0 SHEET 2 AA5 5 LEUHH 45 ILEHH 51 -1 N ALAHH 50 O TYRHH 58 SHEET 3 AA5 5 ALAHH 33 GLNHH 39 -1 N TRPHH 36 O SERHH 49 SHEET 4 AA5 5 ALAHH 88 ARGHH 96 -1 O TYRHH 91 N VALHH 37 SHEET 5 AA5 5 TYRHH 100B TRPHH 103 -1 O TYRHH 100B N ARGHH 96 SHEET 1 AA6 5 THRHH 57 TYRHH 59 0 SHEET 2 AA6 5 LEUHH 45 ILEHH 51 -1 N ALAHH 50 O TYRHH 58 SHEET 3 AA6 5 ALAHH 33 GLNHH 39 -1 N TRPHH 36 O SERHH 49 SHEET 4 AA6 5 ALAHH 88 ARGHH 96 -1 O TYRHH 91 N VALHH 37 SHEET 5 AA6 5 LEUHH 108 VALHH 109 -1 O VALHH 109 N ALAHH 88 SHEET 1 AA7 4 SERHH 120 LEUHH 124 0 SHEET 2 AA7 4 THRHH 135 TYRHH 145 -1 O LYSHH 143 N SERHH 120 SHEET 3 AA7 4 TYRHH 176 PROHH 185 -1 O VALHH 182 N LEUHH 138 SHEET 4 AA7 4 VALHH 163 THRHH 165 -1 N HISHH 164 O VALHH 181 SHEET 1 AA8 4 SERHH 120 LEUHH 124 0 SHEET 2 AA8 4 THRHH 135 TYRHH 145 -1 O LYSHH 143 N SERHH 120 SHEET 3 AA8 4 TYRHH 176 PROHH 185 -1 O VALHH 182 N LEUHH 138 SHEET 4 AA8 4 VALHH 169 LEUHH 170 -1 N VALHH 169 O SERHH 177 SHEET 1 AA9 3 VALHH 150 TRPHH 154 0 SHEET 2 AA9 3 ILEHH 195 HISHH 200 -1 O ASNHH 197 N SERHH 153 SHEET 3 AA9 3 THRHH 205 ARGHH 210 -1 O THRHH 205 N HISHH 200 SHEET 1 AB1 4 GLNII 3 SERII 7 0 SHEET 2 AB1 4 LEUII 18 SERII 25 -1 O ALAII 23 N LEUII 5 SHEET 3 AB1 4 THRII 77 METII 82 -1 O METII 82 N LEUII 18 SHEET 4 AB1 4 PHEII 67 ASPII 72 -1 N ASPII 72 O THRII 77 SHEET 1 AB2 6 LEUII 11 VALII 12 0 SHEET 2 AB2 6 LEUII 108 VALII 111 1 O THRII 110 N VALII 12 SHEET 3 AB2 6 ALAII 88 ARGII 96 -1 N ALAII 88 O VALII 109 SHEET 4 AB2 6 ALAII 33 GLNII 39 -1 N VALII 37 O TYRII 91 SHEET 5 AB2 6 LEUII 45 ILEII 51 -1 O SERII 49 N TRPII 36 SHEET 6 AB2 6 THRII 57 TYRII 59 -1 O TYRII 58 N ALAII 50 SHEET 1 AB3 4 LEUII 11 VALII 12 0 SHEET 2 AB3 4 LEUII 108 VALII 111 1 O THRII 110 N VALII 12 SHEET 3 AB3 4 ALAII 88 ARGII 96 -1 N ALAII 88 O VALII 109 SHEET 4 AB3 4 TYRII 100B TRPII 103 -1 O LEUII 102 N ARGII 94 SHEET 1 AB4 4 SERII 120 PROII 123 0 SHEET 2 AB4 4 THRII 135 TYRII 145 -1 O LYSII 143 N SERII 120 SHEET 3 AB4 4 TYRII 176 PROII 185 -1 O VALII 182 N LEUII 138 SHEET 4 AB4 4 VALII 163 THRII 165 -1 N HISII 164 O VALII 181 SHEET 1 AB5 4 SERII 120 PROII 123 0 SHEET 2 AB5 4 THRII 135 TYRII 145 -1 O LYSII 143 N SERII 120 SHEET 3 AB5 4 TYRII 176 PROII 185 -1 O VALII 182 N LEUII 138 SHEET 4 AB5 4 VALII 169 LEUII 170 -1 N VALII 169 O SERII 177 SHEET 1 AB6 3 VALII 150 TRPII 154 0 SHEET 2 AB6 3 ILEII 195 HISII 200 -1 O ASNII 197 N SERII 153 SHEET 3 AB6 3 THRII 205 ARGII 210 -1 O THRII 205 N HISII 200 SHEET 1 AB7 4 GLNJJ 3 SERJJ 7 0 SHEET 2 AB7 4 LEUJJ 18 SERJJ 25 -1 O ALAJJ 23 N LEUJJ 5 SHEET 3 AB7 4 THRJJ 77 METJJ 82 -1 O METJJ 82 N LEUJJ 18 SHEET 4 AB7 4 PHEJJ 67 ASPJJ 72 -1 N SERJJ 70 O TYRJJ 79 SHEET 1 AB8 6 LEUJJ 11 VALJJ 12 0 SHEET 2 AB8 6 LEUJJ 108 VALJJ 111 1 O THRJJ 110 N VALJJ 12 SHEET 3 AB8 6 ALAJJ 88 ARGJJ 96 -1 N ALAJJ 88 O VALJJ 109 SHEET 4 AB8 6 ALAJJ 33 GLNJJ 39 -1 N VALJJ 37 O TYRJJ 91 SHEET 5 AB8 6 LEUJJ 45 ILEJJ 51 -1 O ILEJJ 51 N METJJ 34 SHEET 6 AB8 6 THRJJ 57 TYRJJ 59 -1 O TYRJJ 58 N ALAJJ 50 SHEET 1 AB9 4 LEUJJ 11 VALJJ 12 0 SHEET 2 AB9 4 LEUJJ 108 VALJJ 111 1 O THRJJ 110 N VALJJ 12 SHEET 3 AB9 4 ALAJJ 88 ARGJJ 96 -1 N ALAJJ 88 O VALJJ 109 SHEET 4 AB9 4 TYRJJ 100B TRPJJ 103 -1 O LEUJJ 102 N ARGJJ 94 SHEET 1 AC1 4 SERJJ 120 LEUJJ 124 0 SHEET 2 AC1 4 THRJJ 135 TYRJJ 145 -1 O GLYJJ 139 N LEUJJ 124 SHEET 3 AC1 4 TYRJJ 176 PROJJ 185 -1 O VALJJ 182 N LEUJJ 138 SHEET 4 AC1 4 VALJJ 163 THRJJ 165 -1 N HISJJ 164 O VALJJ 181 SHEET 1 AC2 4 SERJJ 120 LEUJJ 124 0 SHEET 2 AC2 4 THRJJ 135 TYRJJ 145 -1 O GLYJJ 139 N LEUJJ 124 SHEET 3 AC2 4 TYRJJ 176 PROJJ 185 -1 O VALJJ 182 N LEUJJ 138 SHEET 4 AC2 4 VALJJ 169 LEUJJ 170 -1 N VALJJ 169 O SERJJ 177 SHEET 1 AC3 3 THRJJ 151 TRPJJ 154 0 SHEET 2 AC3 3 ILEJJ 195 HISJJ 200 -1 O ASNJJ 197 N SERJJ 153 SHEET 3 AC3 3 THRJJ 205 ARGJJ 210 -1 O THRJJ 205 N HISJJ 200 SHEET 1 AC4 5 SERLL 10 ALALL 13 0 SHEET 2 AC4 5 THRLL 102 VALLL 106 1 O LYSLL 103 N VALLL 11 SHEET 3 AC4 5 ASPLL 85 ASPLL 92 -1 N TYRLL 86 O THRLL 102 SHEET 4 AC4 5 SERLL 34 GLNLL 38 -1 N GLNLL 38 O ASPLL 85 SHEET 5 AC4 5 LYSLL 45 ILELL 48 -1 O ILELL 48 N TRPLL 35 SHEET 1 AC5 4 SERLL 10 ALALL 13 0 SHEET 2 AC5 4 THRLL 102 VALLL 106 1 O LYSLL 103 N VALLL 11 SHEET 3 AC5 4 ASPLL 85 ASPLL 92 -1 N TYRLL 86 O THRLL 102 SHEET 4 AC5 4 ALALL 95B PHELL 98 -1 O VALLL 97 N THRLL 90 SHEET 1 AC6 3 VALLL 19 SERLL 24 0 SHEET 2 AC6 3 SERLL 70 ILELL 75 -1 O LEULL 73 N ILELL 21 SHEET 3 AC6 3 PHELL 62 SERLL 67 -1 N SERLL 63 O GLYLL 74 SHEET 1 AC7 4 THRLL 117 PHELL 119 0 SHEET 2 AC7 4 ALALL 131 PHELL 140 -1 O VALLL 134 N PHELL 119 SHEET 3 AC7 4 TYRLL 173 LEULL 181 -1 O LEULL 181 N ALALL 131 SHEET 4 AC7 4 VALLL 160 THRLL 162 -1 N GLULL 161 O TYRLL 178 SHEET 1 AC8 4 THRLL 117 PHELL 119 0 SHEET 2 AC8 4 ALALL 131 PHELL 140 -1 O VALLL 134 N PHELL 119 SHEET 3 AC8 4 TYRLL 173 LEULL 181 -1 O LEULL 181 N ALALL 131 SHEET 4 AC8 4 SERLL 166 LYSLL 167 -1 N SERLL 166 O ALALL 174 SHEET 1 AC9 4 SERLL 154 VALLL 156 0 SHEET 2 AC9 4 THRLL 146 ALALL 151 -1 N ALALL 151 O SERLL 154 SHEET 3 AC9 4 TYRLL 192 HISLL 198 -1 O GLNLL 195 N ALALL 148 SHEET 4 AC9 4 SERLL 201 VALLL 207 -1 O VALLL 203 N VALLL 196 SHEET 1 AD1 5 SERMM 10 ALAMM 13 0 SHEET 2 AD1 5 THRMM 102 VALMM 106 1 O LYSMM 103 N VALMM 11 SHEET 3 AD1 5 ASPMM 85 ASPMM 92 -1 N TYRMM 86 O THRMM 102 SHEET 4 AD1 5 SERMM 34 GLNMM 38 -1 N GLNMM 38 O ASPMM 85 SHEET 5 AD1 5 LYSMM 45 ILEMM 48 -1 O ILEMM 48 N TRPMM 35 SHEET 1 AD2 4 SERMM 10 ALAMM 13 0 SHEET 2 AD2 4 THRMM 102 VALMM 106 1 O LYSMM 103 N VALMM 11 SHEET 3 AD2 4 ASPMM 85 ASPMM 92 -1 N TYRMM 86 O THRMM 102 SHEET 4 AD2 4 ALAMM 95B PHEMM 98 -1 O VALMM 97 N THRMM 90 SHEET 1 AD3 3 VALMM 19 SERMM 24 0 SHEET 2 AD3 3 SERMM 70 ILEMM 75 -1 O LEUMM 73 N ILEMM 21 SHEET 3 AD3 3 PHEMM 62 SERMM 67 -1 N SERMM 63 O GLYMM 74 SHEET 1 AD4 4 SERMM 115 PHEMM 119 0 SHEET 2 AD4 4 ALAMM 131 PHEMM 140 -1 O SERMM 138 N SERMM 115 SHEET 3 AD4 4 TYRMM 173 LEUMM 181 -1 O LEUMM 181 N ALAMM 131 SHEET 4 AD4 4 VALMM 160 THRMM 162 -1 N GLUMM 161 O TYRMM 178 SHEET 1 AD5 4 SERMM 115 PHEMM 119 0 SHEET 2 AD5 4 ALAMM 131 PHEMM 140 -1 O SERMM 138 N SERMM 115 SHEET 3 AD5 4 TYRMM 173 LEUMM 181 -1 O LEUMM 181 N ALAMM 131 SHEET 4 AD5 4 SERMM 166 LYSMM 167 -1 N SERMM 166 O ALAMM 174 SHEET 1 AD6 4 SERMM 154 VALMM 156 0 SHEET 2 AD6 4 THRMM 146 ALAMM 151 -1 N ALAMM 151 O SERMM 154 SHEET 3 AD6 4 TYRMM 192 HISMM 198 -1 O GLNMM 195 N ALAMM 148 SHEET 4 AD6 4 SERMM 201 VALMM 207 -1 O VALMM 203 N VALMM 196 SHEET 1 AD7 5 SERNN 10 VALNN 11 0 SHEET 2 AD7 5 THRNN 102 LEUNN 104 1 O LYSNN 103 N VALNN 11 SHEET 3 AD7 5 ASPNN 85 ASPNN 92 -1 N TYRNN 86 O THRNN 102 SHEET 4 AD7 5 VALNN 33 GLNNN 38 -1 N GLNNN 38 O ASPNN 85 SHEET 5 AD7 5 LYSNN 45 ILENN 48 -1 O ILENN 48 N TRPNN 35 SHEET 1 AD8 4 SERNN 10 VALNN 11 0 SHEET 2 AD8 4 THRNN 102 LEUNN 104 1 O LYSNN 103 N VALNN 11 SHEET 3 AD8 4 ASPNN 85 ASPNN 92 -1 N TYRNN 86 O THRNN 102 SHEET 4 AD8 4 ALANN 95B PHENN 98 -1 O VALNN 97 N THRNN 90 SHEET 1 AD9 3 VALNN 19 SERNN 24 0 SHEET 2 AD9 3 SERNN 70 ILENN 75 -1 O LEUNN 73 N ILENN 21 SHEET 3 AD9 3 PHENN 62 SERNN 67 -1 N SERNN 63 O GLYNN 74 SHEET 1 AE1 4 THRNN 117 PHENN 119 0 SHEET 2 AE1 4 ALANN 131 PHENN 140 -1 O VALNN 134 N PHENN 119 SHEET 3 AE1 4 TYRNN 173 LEUNN 181 -1 O LEUNN 179 N LEUNN 133 SHEET 4 AE1 4 VALNN 160 THRNN 162 -1 N GLUNN 161 O TYRNN 178 SHEET 1 AE2 4 THRNN 117 PHENN 119 0 SHEET 2 AE2 4 ALANN 131 PHENN 140 -1 O VALNN 134 N PHENN 119 SHEET 3 AE2 4 TYRNN 173 LEUNN 181 -1 O LEUNN 179 N LEUNN 133 SHEET 4 AE2 4 SERNN 166 LYSNN 167 -1 N SERNN 166 O ALANN 174 SHEET 1 AE3 3 THRNN 146 ALANN 151 0 SHEET 2 AE3 3 TYRNN 192 THRNN 197 -1 O THRNN 197 N THRNN 146 SHEET 3 AE3 3 THRNN 202 GLUNN 204 -1 O VALNN 203 N VALNN 196 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 2.06 SSBOND 4 CYSII 140 CYSII 196 1555 1555 2.03 SSBOND 5 CYSJJ 22 CYSJJ 92 1555 1555 2.05 SSBOND 6 CYSJJ 140 CYSJJ 196 1555 1555 2.03 SSBOND 7 CYSLL 23 CYSLL 88 1555 1555 2.03 SSBOND 8 CYSLL 135 CYSLL 194 1555 1555 2.03 SSBOND 9 CYSMM 23 CYSMM 88 1555 1555 2.03 SSBOND 10 CYSMM 135 CYSMM 194 1555 1555 2.04 SSBOND 11 CYSNN 23 CYSNN 88 1555 1555 2.02 SSBOND 12 CYSNN 135 CYSNN 194 1555 1555 2.02 LINK ND1 HISAA 120 MN MNAA 401 1555 1555 2.00 LINK OD2 ASPAA 143 MN MNAA 401 1555 1555 1.98 LINK OD1 ASPAA 143 MN MNAA 402 1555 1555 2.02 LINK ND1 HISAA 145 MN MNAA 402 1555 1555 2.00 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 1.98 LINK OD1 ASPAA 253 MN MNAA 402 1555 1555 1.98 LINK OD2 ASPAA 253 MN MNAA 402 1555 1555 2.02 LINK ND1 HISBB 120 MN MNBB 401 1555 1555 1.97 LINK OD2 ASPBB 143 MN MNBB 401 1555 1555 1.96 LINK OD1 ASPBB 143 MN MNBB 402 1555 1555 1.97 LINK ND1 HISBB 145 MN MNBB 402 1555 1555 1.99 LINK OD2 ASPBB 147 MN MNBB 401 1555 1555 1.98 LINK OD2 ASPBB 251 MN MNBB 401 1555 1555 1.99 LINK OD2 ASPBB 251 MN MNBB 402 1555 1555 2.00 LINK OD1 ASPBB 253 MN MNBB 402 1555 1555 1.97 LINK OE1 GLUBB 296 MN MNBB 402 1555 1555 2.54 LINK ND1 HISCC 120 MN MNCC 401 1555 1555 1.96 LINK OD2 ASPCC 143 MN MNCC 401 1555 1555 1.97 LINK OD1 ASPCC 143 MN MNCC 402 1555 1555 2.05 LINK ND1 HISCC 145 MN MNCC 402 1555 1555 2.05 LINK OD2 ASPCC 147 MN MNCC 401 1555 1555 1.98 LINK OD2 ASPCC 251 MN MNCC 401 1555 1555 1.98 LINK OD2 ASPCC 251 MN MNCC 402 1555 1555 2.00 LINK OD1 ASPCC 253 MN MNCC 402 1555 1555 1.99 LINK OD2 ASPCC 253 MN MNCC 402 1555 1555 2.05 CISPEP 1 GLYAA 117 GLYAA 118 0 8.46 CISPEP 2 GLYBB 117 GLYBB 118 0 3.50 CISPEP 3 GLYCC 117 GLYCC 118 0 7.95 CISPEP 4 PHEHH 146 PROHH 147 0 -17.57 CISPEP 5 GLUHH 148 PROHH 149 0 -12.10 CISPEP 6 PHEII 146 PROII 147 0 -14.19 CISPEP 7 GLUII 148 PROII 149 0 -12.69 CISPEP 8 GLUJJ 148 PROJJ 149 0 13.30 CISPEP 9 TYRLL 141 PROLL 142 0 9.68 CISPEP 10 TYRMM 141 PROMM 142 0 2.47 CISPEP 11 TYRNN 141 PRONN 142 0 -20.68 CRYST1 138.126 138.126 551.307 90.00 90.00 120.00 P 65 2 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 0.007240 0.004180 0.000000 0.00000 SCALE2 0.000000 0.008360 0.000000 0.00000 SCALE3 0.000000 0.000000 0.001814 0.00000