HEADER OXIDOREDUCTASE 06-MAY-04 1T6I
TITLE NICKEL SUPEROXIDE DISMUTASE (NISOD) APO STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [NI];
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: NISOD, NICKEL- CONTAINING SUPEROXIDE DISMUTASE;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;
SOURCE 3 ORGANISM_TAXID: 1902;
SOURCE 4 GENE: SODN, SOD1, SCO5254, 2SC7G11.16C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS NICKEL, 4-HELIX BUNDLE, HEXAMER, SUPEROXIDE DISMUTASE, NISOD, SOD,
KEYWDS 2 APO, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.P.BARONDEAU,C.J.KASSMANN,C.K.BRUNS,J.A.TAINER,E.D.GETZOFF
REVDAT 3 13-JUL-11 1T6I 1 VERSN
REVDAT 2 24-FEB-09 1T6I 1 VERSN
REVDAT 1 13-JUL-04 1T6I 0
JRNL AUTH D.P.BARONDEAU,C.J.KASSMANN,C.K.BRUNS,J.A.TAINER,E.D.GETZOFF
JRNL TITL NICKEL SUPEROXIDE DISMUTASE STRUCTURE AND MECHANISM.
JRNL REF BIOCHEMISTRY V. 43 8038 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15209499
JRNL DOI 10.1021/BI0496081
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 309608.650
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 8940
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.400
REMARK 3 FREE R VALUE TEST SET COUNT : 927
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1177
REMARK 3 BIN R VALUE (WORKING SET) : 0.3470
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 8.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 113
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.038
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2647
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 22
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -22.36000
REMARK 3 B22 (A**2) : -5.57000
REMARK 3 B33 (A**2) : 27.93000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 ESD FROM SIGMAA (A) : 0.41
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.130
REMARK 3 BOND ANGLES (DEGREES) : 1.38
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.55
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.650 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.520 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.29
REMARK 3 BSOL : 10.00
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WAT.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T6I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-04.
REMARK 100 THE RCSB ID CODE IS RCSB022373.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.911656, 0.97912, 0.979311
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPEG 2000, HEPES, METHANOL, CALCIUM
REMARK 280 CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.32950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.32950
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 30.21500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.12050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 30.21500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.12050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.32950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 30.21500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 55.12050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 55.32950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 30.21500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 55.12050
REMARK 290 SMTRY3 8 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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HEXAMER GENERATED FROM THE
REMARK 300 TRIMER IN THE ASYMMETRIC UNIT BY THE OPERATION -X,Y,-Z+1/2
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 55.32950
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 MSE A 0
REMARK 465 HIS A 1
REMARK 465 CYS A 2
REMARK 465 ASP A 3
REMARK 465 LEU A 4
REMARK 465 PRO A 5
REMARK 465 CYS A 6
REMARK 465 MSE B 0
REMARK 465 HIS B 1
REMARK 465 CYS B 2
REMARK 465 ASP B 3
REMARK 465 LEU B 4
REMARK 465 PRO B 5
REMARK 465 CYS B 6
REMARK 465 GLY B 7
REMARK 465 MSE C 0
REMARK 465 HIS C 1
REMARK 465 CYS C 2
REMARK 465 ASP C 3
REMARK 465 LEU C 4
REMARK 465 PRO C 5
REMARK 465 CYS C 6
REMARK 465 GLY C 7
REMARK 465 ALA C 117
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 ASP A 10 134.15 -170.04
REMARK 500 ASP A 32 -9.96 -145.50
REMARK 500 ASP B 10 126.56 -172.00
REMARK 500 PRO B 11 2.60 -68.88
REMARK 500 TYR B 62 -60.76 -90.84
REMARK 500 TYR C 62 -68.33 -93.69
REMARK 500 PHE C 63 104.07 -57.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 62 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1T6I A 1 117 UNP P80735 SODN_STRCO 15 131
DBREF 1T6I B 1 117 UNP P80735 SODN_STRCO 15 131
DBREF 1T6I C 1 117 UNP P80735 SODN_STRCO 15 131
SEQADV 1T6I MSE A 0 UNP P80735 INITIATING METHIONINE
SEQADV 1T6I MSE A 28 UNP P80735 MET 42 MODIFIED RESIDUE
SEQADV 1T6I MSE A 85 UNP P80735 LEU 99 ENGINEERED
SEQADV 1T6I MSE B 0 UNP P80735 INITIATING METHIONINE
SEQADV 1T6I MSE B 28 UNP P80735 MET 42 MODIFIED RESIDUE
SEQADV 1T6I MSE B 85 UNP P80735 LEU 99 ENGINEERED
SEQADV 1T6I MSE C 0 UNP P80735 INITIATING METHIONINE
SEQADV 1T6I MSE C 28 UNP P80735 MET 42 MODIFIED RESIDUE
SEQADV 1T6I MSE C 85 UNP P80735 LEU 99 ENGINEERED
SEQRES 1 A 118 MSE HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA
SEQRES 2 A 118 GLN ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN
SEQRES 3 A 118 GLU LYS MSE ALA GLY ASN ASP ASP PRO HIS PHE GLN THR
SEQRES 4 A 118 ARG ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA
SEQRES 5 A 118 LYS HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS
SEQRES 6 A 118 PRO PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU
SEQRES 7 A 118 VAL ASN ASP THR LEU LYS ALA MSE SER ALA ALA LYS GLY
SEQRES 8 A 118 SER LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR
SEQRES 9 A 118 ILE ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS
SEQRES 10 A 118 ALA
SEQRES 1 B 118 MSE HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA
SEQRES 2 B 118 GLN ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN
SEQRES 3 B 118 GLU LYS MSE ALA GLY ASN ASP ASP PRO HIS PHE GLN THR
SEQRES 4 B 118 ARG ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA
SEQRES 5 B 118 LYS HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS
SEQRES 6 B 118 PRO PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU
SEQRES 7 B 118 VAL ASN ASP THR LEU LYS ALA MSE SER ALA ALA LYS GLY
SEQRES 8 B 118 SER LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR
SEQRES 9 B 118 ILE ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS
SEQRES 10 B 118 ALA
SEQRES 1 C 118 MSE HIS CYS ASP LEU PRO CYS GLY VAL TYR ASP PRO ALA
SEQRES 2 C 118 GLN ALA ARG ILE GLU ALA GLU SER VAL LYS ALA VAL GLN
SEQRES 3 C 118 GLU LYS MSE ALA GLY ASN ASP ASP PRO HIS PHE GLN THR
SEQRES 4 C 118 ARG ALA THR VAL ILE LYS GLU GLN ARG ALA GLU LEU ALA
SEQRES 5 C 118 LYS HIS HIS VAL SER VAL LEU TRP SER ASP TYR PHE LYS
SEQRES 6 C 118 PRO PRO HIS PHE GLU LYS TYR PRO GLU LEU HIS GLN LEU
SEQRES 7 C 118 VAL ASN ASP THR LEU LYS ALA MSE SER ALA ALA LYS GLY
SEQRES 8 C 118 SER LYS ASP PRO ALA THR GLY GLN LYS ALA LEU ASP TYR
SEQRES 9 C 118 ILE ALA GLN ILE ASP LYS ILE PHE TRP GLU THR LYS LYS
SEQRES 10 C 118 ALA
MODRES 1T6I MSE A 28 MET SELENOMETHIONINE
MODRES 1T6I MSE A 85 MET SELENOMETHIONINE
MODRES 1T6I MSE B 28 MET SELENOMETHIONINE
MODRES 1T6I MSE B 85 MET SELENOMETHIONINE
MODRES 1T6I MSE C 28 MET SELENOMETHIONINE
MODRES 1T6I MSE C 85 MET SELENOMETHIONINE
HET MSE A 28 8
HET MSE A 85 8
HET MSE B 28 8
HET MSE B 85 8
HET MSE C 28 8
HET MSE C 85 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 4 HOH *22(H2 O)
HELIX 1 1 PRO A 11 ASN A 31 1 21
HELIX 2 2 ASP A 33 ASP A 61 1 29
HELIX 3 3 LYS A 64 TYR A 71 1 8
HELIX 4 4 GLU A 73 SER A 91 1 19
HELIX 5 5 ASP A 93 LYS A 115 1 23
HELIX 6 6 PRO B 11 MSE B 28 1 18
HELIX 7 7 ASP B 33 TYR B 62 1 30
HELIX 8 8 LYS B 64 TYR B 71 1 8
HELIX 9 9 GLU B 73 GLY B 90 1 18
HELIX 10 10 ASP B 93 ALA B 117 1 25
HELIX 11 11 PRO C 11 GLY C 30 1 20
HELIX 12 12 ASP C 33 TYR C 62 1 30
HELIX 13 13 LYS C 64 TYR C 71 1 8
HELIX 14 14 GLU C 73 GLY C 90 1 18
HELIX 15 15 ASP C 93 GLU C 113 1 21
LINK C LYS A 27 N MSE A 28 1555 1555 1.34
LINK C MSE A 28 N ALA A 29 1555 1555 1.34
LINK C ALA A 84 N MSE A 85 1555 1555 1.34
LINK C MSE A 85 N SER A 86 1555 1555 1.34
LINK C LYS B 27 N MSE B 28 1555 1555 1.34
LINK C MSE B 28 N ALA B 29 1555 1555 1.33
LINK C ALA B 84 N MSE B 85 1555 1555 1.34
LINK C MSE B 85 N SER B 86 1555 1555 1.34
LINK C LYS C 27 N MSE C 28 1555 1555 1.34
LINK C MSE C 28 N ALA C 29 1555 1555 1.33
LINK C ALA C 84 N MSE C 85 1555 1555 1.34
LINK C MSE C 85 N SER C 86 1555 1555 1.34
CRYST1 60.430 110.241 110.659 90.00 90.00 90.00 C 2 2 21 24
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 0.016548 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009037 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
