HEADER OXIDOREDUCTASE 14-OCT-02 1N0N
TITLE CATALYTIC AND STRUCTURAL EFFECTS OF AMINO-ACID SUBSTITUTION AT HIS30
TITLE 2 IN HUMAN MANGANESE SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [MN];
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SODAB;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHMNSOD4
KEYWDS 4-HELIX BUNDLE METALLOENZYME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.E.O.BORGSTAHL,H.E.PARGE,M.J.HICKEY,W.F.BEYER JR.,R.A.HALLEWELL,
AUTHOR 2 J.A.TAINER
REVDAT 6 14-FEB-24 1N0N 1 REMARK
REVDAT 5 27-OCT-21 1N0N 1 REMARK SEQADV LINK
REVDAT 4 11-OCT-17 1N0N 1 REMARK
REVDAT 3 13-JUL-11 1N0N 1 VERSN
REVDAT 2 24-FEB-09 1N0N 1 VERSN
REVDAT 1 06-NOV-02 1N0N 0
SPRSDE 06-NOV-02 1N0N 1LUS
JRNL AUTH G.E.O.BORGSTAHL,H.E.PARGE,M.J.HICKEY,W.F.BEYER JR.,
JRNL AUTH 2 R.A.HALLEWELL,J.A.TAINER
JRNL TITL CATALYTIC AND STRUCTURAL EFFECTS OF AMINO-ACID SUBSTITUTION
JRNL TITL 2 AT HIS30 IN HUMAN MANGANESE SUPEROXIDE DISMUTASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 41507
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) : 0.224
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4191
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6063
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 694
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 337
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.51000
REMARK 3 B22 (A**2) : 1.51000
REMARK 3 B33 (A**2) : -3.02000
REMARK 3 B12 (A**2) : 1.89000
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.950
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 44.52
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 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017371.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-99
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41609
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, IMIDAZOLE/MALATE, PH
REMARK 280 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 80.29400
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 160.58800
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 120.44100
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 200.73500
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 40.14700
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 80.29400
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 160.58800
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 200.73500
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 120.44100
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 40.14700
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: TETRAMER GENERATED BY CRYSTALLOGRAPHIC SYMMETRY
REMARK 300 -Y,-X,5/6-Z
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 9880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.500000 -0.866025 0.000000 39.90750
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 69.12182
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 200.73500
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 776 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 MET B 0
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 O HOH A 619 O HOH A 766 2.12
REMARK 500 O HOH A 699 O HOH A 767 2.18
REMARK 500 OG SER B 82 OD1 ASN B 84 2.19
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 CYS A 196 CA - CB - SG ANGL. DEV. = 7.0 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 ASN A 142 -123.46 47.38
REMARK 500 TYR A 165 -21.85 -149.64
REMARK 500 LYS A 170 -142.83 52.30
REMARK 500 ASN B 142 -122.59 47.83
REMARK 500 TYR B 165 -13.03 -149.64
REMARK 500 LYS B 170 -138.69 54.00
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 199 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 26 NE2
REMARK 620 2 HIS A 74 NE2 90.3
REMARK 620 3 ASP A 159 OD1 81.8 110.7
REMARK 620 4 HIS A 163 NE2 85.9 129.3 118.6
REMARK 620 5 HOH A 769 O 172.9 93.2 91.1 96.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 199 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 26 NE2
REMARK 620 2 HIS B 74 NE2 92.5
REMARK 620 3 ASP B 159 OD1 86.9 111.8
REMARK 620 4 HIS B 163 NE2 86.3 130.8 117.2
REMARK 620 5 HOH B 872 O 170.0 96.1 85.1 92.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LUV RELATED DB: PDB
REMARK 900 1LUV IS WILD-TYPE HMNSOD
DBREF 1N0N A 1 198 UNP P04179 SODM_HUMAN 25 222
DBREF 1N0N B 1 198 UNP P04179 SODM_HUMAN 25 222
SEQADV 1N0N MET A 0 UNP P04179 CLONING ARTIFACT
SEQADV 1N0N VAL A 30 UNP P04179 HIS 54 ENGINEERED MUTATION
SEQADV 1N0N MET B 0 UNP P04179 CLONING ARTIFACT
SEQADV 1N0N VAL B 30 UNP P04179 HIS 54 ENGINEERED MUTATION
SEQRES 1 A 199 MET LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY
SEQRES 2 A 199 ALA LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU
SEQRES 3 A 199 HIS HIS SER LYS VAL HIS ALA ALA TYR VAL ASN ASN LEU
SEQRES 4 A 199 ASN VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS
SEQRES 5 A 199 GLY ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU
SEQRES 6 A 199 LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE
SEQRES 7 A 199 TRP THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS
SEQRES 8 A 199 GLY GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER
SEQRES 9 A 199 PHE ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL
SEQRES 10 A 199 GLY VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN
SEQRES 11 A 199 LYS GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN
SEQRES 12 A 199 GLN ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU
SEQRES 13 A 199 LEU GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN
SEQRES 14 A 199 TYR LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP
SEQRES 15 A 199 ASN VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET
SEQRES 16 A 199 ALA CYS LYS LYS
SEQRES 1 B 199 MET LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY
SEQRES 2 B 199 ALA LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU
SEQRES 3 B 199 HIS HIS SER LYS VAL HIS ALA ALA TYR VAL ASN ASN LEU
SEQRES 4 B 199 ASN VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS
SEQRES 5 B 199 GLY ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU
SEQRES 6 B 199 LYS PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE
SEQRES 7 B 199 TRP THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS
SEQRES 8 B 199 GLY GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER
SEQRES 9 B 199 PHE ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL
SEQRES 10 B 199 GLY VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN
SEQRES 11 B 199 LYS GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN
SEQRES 12 B 199 GLN ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU
SEQRES 13 B 199 LEU GLY ILE ASP VAL TRP GLU HIS ALA TYR TYR LEU GLN
SEQRES 14 B 199 TYR LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP
SEQRES 15 B 199 ASN VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET
SEQRES 16 B 199 ALA CYS LYS LYS
HET MN A 199 1
HET SO4 A 601 5
HET SO4 A 602 5
HET MN B 199 1
HET SO4 B 701 5
HET SO4 B 702 5
HETNAM MN MANGANESE (II) ION
HETNAM SO4 SULFATE ION
FORMUL 3 MN 2(MN 2+)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 9 HOH *337(H2 O)
HELIX 1 1 ASN A 19 LYS A 29 1 11
HELIX 2 2 LYS A 29 GLY A 52 1 24
HELIX 3 3 ASP A 53 LEU A 60 1 8
HELIX 4 4 LEU A 60 ASN A 80 1 21
HELIX 5 5 LYS A 90 GLY A 102 1 13
HELIX 6 6 SER A 103 GLY A 117 1 15
HELIX 7 7 PRO A 145 GLY A 151 1 7
HELIX 8 8 TRP A 161 ALA A 164 5 4
HELIX 9 9 TYR A 165 LYS A 170 1 6
HELIX 10 10 VAL A 172 TRP A 181 1 10
HELIX 11 11 ASN A 182 ILE A 184 5 3
HELIX 12 12 ASN A 185 CYS A 196 1 12
HELIX 13 13 ASN B 19 LYS B 29 1 11
HELIX 14 14 LYS B 29 GLY B 52 1 24
HELIX 15 15 ASP B 53 LEU B 60 1 8
HELIX 16 16 LEU B 60 ASN B 80 1 21
HELIX 17 17 LYS B 90 GLY B 102 1 13
HELIX 18 18 SER B 103 GLY B 117 1 15
HELIX 19 19 PRO B 145 GLY B 151 1 7
HELIX 20 20 TRP B 161 ALA B 164 5 4
HELIX 21 21 TYR B 165 LYS B 170 1 6
HELIX 22 22 VAL B 172 TRP B 181 1 10
HELIX 23 23 ASN B 182 ILE B 184 5 3
HELIX 24 24 ASN B 185 LYS B 197 1 13
SHEET 1 A 3 HIS A 134 PRO A 141 0
SHEET 2 A 3 GLY A 122 ASN A 129 -1 N GLY A 127 O GLN A 136
SHEET 3 A 3 ILE A 153 ASP A 159 -1 O ILE A 158 N GLY A 124
SHEET 1 B 3 HIS B 134 PRO B 141 0
SHEET 2 B 3 GLY B 122 ASN B 129 -1 N GLY B 127 O GLN B 136
SHEET 3 B 3 ILE B 153 ASP B 159 -1 O ILE B 158 N GLY B 124
LINK NE2 HIS A 26 MN MN A 199 1555 1555 2.23
LINK NE2 HIS A 74 MN MN A 199 1555 1555 2.23
LINK OD1 ASP A 159 MN MN A 199 1555 1555 2.05
LINK NE2 HIS A 163 MN MN A 199 1555 1555 2.12
LINK MN MN A 199 O HOH A 769 1555 1555 2.11
LINK NE2 HIS B 26 MN MN B 199 1555 1555 2.16
LINK NE2 HIS B 74 MN MN B 199 1555 1555 2.15
LINK OD1 ASP B 159 MN MN B 199 1555 1555 2.03
LINK NE2 HIS B 163 MN MN B 199 1555 1555 2.13
LINK MN MN B 199 O HOH B 872 1555 1555 2.22
CISPEP 1 GLU A 15 PRO A 16 0 0.58
CISPEP 2 GLU B 15 PRO B 16 0 0.33
SITE 1 AC1 5 HIS A 26 HIS A 74 ASP A 159 HIS A 163
SITE 2 AC1 5 HOH A 769
SITE 1 AC2 5 HIS A 2 SER A 3 HIS A 71 HOH A 726
SITE 2 AC2 5 HOH A 762
SITE 1 AC3 6 ALA A 63 ASN A 67 GLN A 119 HOH A 628
SITE 2 AC3 6 HOH A 724 HOH A 767
SITE 1 AC4 5 HIS B 26 HIS B 74 ASP B 159 HIS B 163
SITE 2 AC4 5 HOH B 872
SITE 1 AC5 5 LYS A 178 HIS B 2 SER B 3 HIS B 71
SITE 2 AC5 5 HOH B 862
SITE 1 AC6 8 ASN B 37 ALA B 63 ASN B 67 GLN B 119
SITE 2 AC6 8 HOH B 717 HOH B 720 HOH B 762 HOH B 858
CRYST1 79.815 79.815 240.882 90.00 90.00 120.00 P 61 2 2 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 0.012529 0.007234 0.000000 0.00000
SCALE2 0.000000 0.014467 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
