HEADER OXIDOREDUCTASE 28-JAN-08 3C3S
TITLE ROLE OF A GLUTAMATE BRIDGE SPANNING THE DIMERIC INTERFACE OF HUMAN
TITLE 2 MANGANESE SUPEROXIDE DISMUTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUPEROXIDE DISMUTASE [MN];
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 25-222;
COMPND 5 EC: 1.15.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SOD2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: QC774;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS METALLOENZYME, ACETYLATION, MANGANESE, METAL-BINDING, MITOCHONDRION,
KEYWDS 2 OXIDOREDUCTASE, POLYMORPHISM, TRANSIT PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.S.QUINT,J.F.DOMSIC,D.E.CABELLI,R.MCKENNA,D.N.SILVERMAN
REVDAT 4 30-AUG-23 3C3S 1 REMARK
REVDAT 3 20-OCT-21 3C3S 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 3C3S 1 VERSN
REVDAT 1 22-APR-08 3C3S 0
JRNL AUTH P.S.QUINT,J.F.DOMSIC,D.E.CABELLI,R.MCKENNA,D.N.SILVERMAN
JRNL TITL ROLE OF A GLUTAMATE BRIDGE SPANNING THE DIMERIC INTERFACE OF
JRNL TITL 2 HUMAN MANGANESE SUPEROXIDE DISMUTASE.
JRNL REF BIOCHEMISTRY V. 47 4621 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18373354
JRNL DOI 10.1021/BI7024518
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 491477.910
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 88.6
REMARK 3 NUMBER OF REFLECTIONS : 15267
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) : 0.179
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 747
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2347
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE : 0.2530
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 134
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3100
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 103
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -0.91000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.17
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 2.460
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) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.830 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 45.65
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 : SULFO.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : SULFO.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3C3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046304.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 300
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15609
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21000
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: PDB ENTRY 1LUV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM IMIDZOLE, 100MM MALIC ACID, 3.0M
REMARK 280 AMMONIUM SULFATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 300K
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 80.83367
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 161.66733
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 121.25050
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 202.08417
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 40.41683
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 80.83367
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 161.66733
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 202.08417
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 121.25050
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 40.41683
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9180 ANGSTROM**2
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 40.63500
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 70.38188
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 202.08417
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2220 ANGSTROM**2
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2150 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 40.63500
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 70.38188
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 202.08417
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2110 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 40.63500
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 70.38188
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 202.08417
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 A 322 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 315 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 LYS A 197
REMARK 465 LYS A 198
REMARK 465 LYS B 197
REMARK 465 LYS B 198
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 O2 SO4 B 401 O HOH B 333 1.43
REMARK 500 O4 SO4 B 401 O HOH B 332 1.84
REMARK 500 O4 SO4 A 402 O HOH A 334 1.89
REMARK 500 O3 SO4 B 401 O HOH B 331 2.13
REMARK 500 ND2 ASN A 67 O HOH A 245 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 44 N LYS A 44 CA -0.141
REMARK 500 LYS A 44 C LYS A 44 O -0.149
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 PRO A 8 7.61 -69.32
REMARK 500 ASN A 142 -135.22 48.09
REMARK 500 TYR A 165 -16.71 -157.12
REMARK 500 LYS A 170 -139.70 49.15
REMARK 500 TYR B 9 -168.37 -126.37
REMARK 500 ASN B 142 -132.98 48.22
REMARK 500 TYR B 165 -22.04 -153.74
REMARK 500 LYS B 170 -138.79 52.73
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 TRP A 125 LEU A 126 146.40
REMARK 500 LEU B 60 GLN B 61 -144.11
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 ASP A 159 OD1
REMARK 620 2 HOH A 338 O 88.0
REMARK 620 N 1
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 ASP B 159 OD1
REMARK 620 2 HOH B 337 O 94.9
REMARK 620 N 1
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 MN B 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3C3T RELATED DB: PDB
REMARK 900 SAME PROTEIN WITH MUTATION E162D
DBREF 3C3S A 1 198 UNP P04179 SODM_HUMAN 25 222
DBREF 3C3S B 1 198 UNP P04179 SODM_HUMAN 25 222
SEQADV 3C3S ALA A 162 UNP P04179 GLU 186 ENGINEERED MUTATION
SEQADV 3C3S ALA B 162 UNP P04179 GLU 186 ENGINEERED MUTATION
SEQRES 1 A 198 LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA
SEQRES 2 A 198 LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS
SEQRES 3 A 198 HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN
SEQRES 4 A 198 VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY
SEQRES 5 A 198 ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS
SEQRES 6 A 198 PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP
SEQRES 7 A 198 THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY
SEQRES 8 A 198 GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE
SEQRES 9 A 198 ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY
SEQRES 10 A 198 VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS
SEQRES 11 A 198 GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN
SEQRES 12 A 198 ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU
SEQRES 13 A 198 GLY ILE ASP VAL TRP ALA HIS ALA TYR TYR LEU GLN TYR
SEQRES 14 A 198 LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN
SEQRES 15 A 198 VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA
SEQRES 16 A 198 CYS LYS LYS
SEQRES 1 B 198 LYS HIS SER LEU PRO ASP LEU PRO TYR ASP TYR GLY ALA
SEQRES 2 B 198 LEU GLU PRO HIS ILE ASN ALA GLN ILE MET GLN LEU HIS
SEQRES 3 B 198 HIS SER LYS HIS HIS ALA ALA TYR VAL ASN ASN LEU ASN
SEQRES 4 B 198 VAL THR GLU GLU LYS TYR GLN GLU ALA LEU ALA LYS GLY
SEQRES 5 B 198 ASP VAL THR ALA GLN ILE ALA LEU GLN PRO ALA LEU LYS
SEQRES 6 B 198 PHE ASN GLY GLY GLY HIS ILE ASN HIS SER ILE PHE TRP
SEQRES 7 B 198 THR ASN LEU SER PRO ASN GLY GLY GLY GLU PRO LYS GLY
SEQRES 8 B 198 GLU LEU LEU GLU ALA ILE LYS ARG ASP PHE GLY SER PHE
SEQRES 9 B 198 ASP LYS PHE LYS GLU LYS LEU THR ALA ALA SER VAL GLY
SEQRES 10 B 198 VAL GLN GLY SER GLY TRP GLY TRP LEU GLY PHE ASN LYS
SEQRES 11 B 198 GLU ARG GLY HIS LEU GLN ILE ALA ALA CYS PRO ASN GLN
SEQRES 12 B 198 ASP PRO LEU GLN GLY THR THR GLY LEU ILE PRO LEU LEU
SEQRES 13 B 198 GLY ILE ASP VAL TRP ALA HIS ALA TYR TYR LEU GLN TYR
SEQRES 14 B 198 LYS ASN VAL ARG PRO ASP TYR LEU LYS ALA ILE TRP ASN
SEQRES 15 B 198 VAL ILE ASN TRP GLU ASN VAL THR GLU ARG TYR MET ALA
SEQRES 16 B 198 CYS LYS LYS
HET MN A 199 1
HET SO4 A 402 5
HET MN B 199 1
HET SO4 B 401 5
HETNAM MN MANGANESE (II) ION
HETNAM SO4 SULFATE ION
FORMUL 3 MN 2(MN 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *103(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 LYS B 51 1 23
HELIX 15 15 ASP B 53 LEU B 60 1 8
HELIX 16 16 PRO B 62 LEU B 81 1 20
HELIX 17 17 GLY B 91 GLY B 102 1 12
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 ALA B 195 1 11
SHEET 1 A 3 HIS A 134 PRO A 141 0
SHEET 2 A 3 GLY A 122 ASN A 129 -1 N TRP A 125 O ALA A 138
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 153 N PHE B 128
LINK OD1 ASP A 159 MN MN A 199 1555 1555 2.00
LINK MN MN A 199 O HOH A 338 1555 1555 2.01
LINK OD1 ASP B 159 MN MN B 199 1555 1555 1.92
LINK MN MN B 199 O HOH B 337 1555 1555 1.98
CISPEP 1 GLU A 15 PRO A 16 0 0.07
CISPEP 2 GLU B 15 PRO B 16 0 -0.06
SITE 1 AC1 4 HIS A 26 HIS A 74 ASP A 159 HIS A 163
SITE 1 AC2 4 HIS B 26 HIS B 74 ASP B 159 HIS B 163
SITE 1 AC3 5 HIS B 30 TRP B 161 HIS B 163 TYR B 165
SITE 2 AC3 5 ARG B 173
SITE 1 AC4 5 HIS A 30 TRP A 161 HIS A 163 TYR A 165
SITE 2 AC4 5 TYR A 166
CRYST1 81.270 81.270 242.501 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 0.012305 0.007104 0.000000 0.00000
SCALE2 0.000000 0.014208 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004124 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
