HEADER METAL BINDING PROTEIN 07-MAY-12 4F28
TITLE THE CRYSTAL STRUCTURE OF A HUMAN MITONEET MUTANT WITH MET 62 REPLACED
TITLE 2 BY A GLY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CDGSH IRON-SULFUR DOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: WATER-SOLUBLE DOMAIN, UNP RESIDUES 33-108;
COMPND 5 SYNONYM: MITONEET;
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: C10ORF70, CISD1, MDS029, ZCD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B21-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET28-A(+)
KEYWDS 2FE-2S PROTEINS, MEMBRANE, SIGNAL-ANCHOR, TRANSMEMBRANE METAL BINDING
KEYWDS 2 PROTEIN, PROTEIN FRUSTRATION, MITOCHONDRIAL OUTER MEMBRANE, METAL
KEYWDS 3 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.L.BAXTER,J.A.ZURIS,C.WANG,H.L.AXELROD,A.E.COHEN,M.L.PADDOCK,
AUTHOR 2 R.NECHUSHTAI,J.N.ONUCHIC,P.A.JENNINGS
REVDAT 3 28-FEB-24 4F28 1 REMARK SEQADV LINK
REVDAT 2 30-JAN-13 4F28 1 JRNL
REVDAT 1 26-DEC-12 4F28 0
JRNL AUTH E.L.BAXTER,J.A.ZURIS,C.WANG,P.L.VO,H.L.AXELROD,A.E.COHEN,
JRNL AUTH 2 M.L.PADDOCK,R.NECHUSHTAI,J.N.ONUCHIC,P.A.JENNINGS
JRNL TITL ALLOSTERIC CONTROL IN A METALLOPROTEIN DRAMATICALLY ALTERS
JRNL TITL 2 FUNCTION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 948 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23271805
JRNL DOI 10.1073/PNAS.1208286110
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 20401
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 + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1044
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2690
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2328
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2554
REMARK 3 BIN R VALUE (WORKING SET) : 0.2321
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.06
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 136
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 978
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.71820
REMARK 3 B22 (A**2) : -7.36910
REMARK 3 B33 (A**2) : 8.08730
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) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1040 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 1405 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 487 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 24 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 157 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1040 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 134 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1193 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.07
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.74
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.32
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|42 - 104}
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2837 -3.0094 9.1700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2070 T22: -0.1055
REMARK 3 T33: -0.2376 T12: -0.0489
REMARK 3 T13: 0.0186 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 1.9830 L22: 1.8392
REMARK 3 L33: 8.3155 L12: -0.5969
REMARK 3 L13: 1.6755 L23: -1.1825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0843 S12: -0.0929 S13: -0.1100
REMARK 3 S21: -0.1189 S22: 0.0348 S23: 0.0336
REMARK 3 S31: 0.5442 S32: -0.5442 S33: 0.0495
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {B|43 - 106}
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1212 5.2430 5.9129
REMARK 3 T TENSOR
REMARK 3 T11: 0.1680 T22: -0.1326
REMARK 3 T33: -0.1616 T12: 0.0305
REMARK 3 T13: -0.0348 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.1692 L22: 2.2263
REMARK 3 L33: 8.3155 L12: -1.4972
REMARK 3 L13: 1.9082 L23: -2.0125
REMARK 3 S TENSOR
REMARK 3 S11: -0.1537 S12: 0.1378 S13: 0.2341
REMARK 3 S21: 0.1457 S22: -0.2368 S23: -0.1968
REMARK 3 S31: -0.4960 S32: 0.2091 S33: 0.3905
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. ATOM RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND
REMARK 3 RESIDUAL U FACTORS. 2. NCS RESTRAINTS WERE APPLIED USING BUSTER'
REMARK 3 S LSSR RESTRAINT REPRESENTATION (-AUTONCS). DIFFERENCE ELECTRON
REMARK 3 DENSITY, MOST LIKELY CORRESPONDING TO PROTEIN RESIDUES AT THE N-
REMARK 3 TERMINAL END OF CHAINS A OR B COULD NOT BE DEFINITIVELY ASSIGNED
REMARK 3 AND WERE NOT MODELED
REMARK 4
REMARK 4 4F28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072362.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-09
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 : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : RH COATED FLAT MIRROR, TOROIDAL
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20457
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 33.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.2600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.99100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.560
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 20.66500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.55500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.55500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.66500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.30000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 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 ARG A 33
REMARK 465 PHE A 34
REMARK 465 TYR A 35
REMARK 465 VAL A 36
REMARK 465 LYS A 37
REMARK 465 ASP A 38
REMARK 465 HIS A 39
REMARK 465 ARG A 40
REMARK 465 ASN A 41
REMARK 465 LYS A 105
REMARK 465 LYS A 106
REMARK 465 GLU A 107
REMARK 465 THR A 108
REMARK 465 ARG B 33
REMARK 465 PHE B 34
REMARK 465 TYR B 35
REMARK 465 VAL B 36
REMARK 465 LYS B 37
REMARK 465 ASP B 38
REMARK 465 HIS B 39
REMARK 465 ARG B 40
REMARK 465 ASN B 41
REMARK 465 LYS B 42
REMARK 465 GLU B 107
REMARK 465 THR B 108
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 42 CB CG CD CE NZ
REMARK 470 GLU A 63 CG CD OE1 OE2
REMARK 470 ASP A 67 CG OD1 OD2
REMARK 470 LYS A 89 CE NZ
REMARK 470 GLU A 92 CG CD OE1 OE2
REMARK 470 GLU B 63 CG CD OE1 OE2
REMARK 470 ASP B 64 CG OD1 OD2
REMARK 470 ASP B 67 CG OD1 OD2
REMARK 470 LYS B 105 CE NZ
REMARK 470 LYS B 106 CD CE NZ
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 GLN A 50 57.91 33.68
REMARK 500 GLN B 50 57.33 36.21
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 FES A 201 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 72 SG
REMARK 620 2 FES A 201 S1 110.0
REMARK 620 3 FES A 201 S2 113.8 104.4
REMARK 620 4 CYS A 74 SG 102.1 112.4 114.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 201 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 83 SG
REMARK 620 2 FES A 201 S1 108.7
REMARK 620 3 FES A 201 S2 126.4 103.6
REMARK 620 4 HIS A 87 ND1 99.3 116.1 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 201 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 72 SG
REMARK 620 2 FES B 201 S1 111.0
REMARK 620 3 FES B 201 S2 115.9 105.9
REMARK 620 4 CYS B 74 SG 100.7 106.4 116.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 201 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 83 SG
REMARK 620 2 FES B 201 S1 110.7
REMARK 620 3 FES B 201 S2 123.9 103.4
REMARK 620 4 HIS B 87 ND1 96.3 117.6 105.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LPQ RELATED DB: PDB
REMARK 900 HUMAN MITONEET WITH 2FE-2S COORDINATING LIGAND HIS 87 REPLACE WITH
REMARK 900 CYS
REMARK 900 RELATED ID: 3EW0 RELATED DB: PDB
REMARK 900 THE NOVEL 2FE-2S OUTER MITOCHONDRIAL PROTEIN MITONEET DISPLAYS
REMARK 900 CONFORMATIONAL FLEXIBILITY IN ITS N-TERMINAL CYTOPLASMIC TETHERING
REMARK 900 DOMAIN
REMARK 900 RELATED ID: 2QH7 RELATED DB: PDB
REMARK 900 MITONEET IS A UNIQUELY FOLDED 2FE-2S OUTER MITOCHONDRIAL MEMBRANE
REMARK 900 PROTEIN STABILIZED BY PIOGLITAZONE
REMARK 900 RELATED ID: 4F1E RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH D67G MUTATION
REMARK 900 RELATED ID: 4F2C RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH G66A, D67A MUTATIONS
REMARK 900 RELATED ID: 4EZF RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH D67A, K68A MUTATIONS
DBREF 4F28 A 33 108 UNP Q9NZ45 CISD1_HUMAN 33 108
DBREF 4F28 B 33 108 UNP Q9NZ45 CISD1_HUMAN 33 108
SEQADV 4F28 GLY A 62 UNP Q9NZ45 MET 62 ENGINEERED MUTATION
SEQADV 4F28 GLY B 62 UNP Q9NZ45 MET 62 ENGINEERED MUTATION
SEQRES 1 A 76 ARG PHE TYR VAL LYS ASP HIS ARG ASN LYS ALA MET ILE
SEQRES 2 A 76 ASN LEU HIS ILE GLN LYS ASP ASN PRO LYS ILE VAL HIS
SEQRES 3 A 76 ALA PHE ASP GLY GLU ASP LEU GLY ASP LYS ALA VAL TYR
SEQRES 4 A 76 CYS ARG CYS TRP ARG SER LYS LYS PHE PRO PHE CYS ASP
SEQRES 5 A 76 GLY ALA HIS THR LYS HIS ASN GLU GLU THR GLY ASP ASN
SEQRES 6 A 76 VAL GLY PRO LEU ILE ILE LYS LYS LYS GLU THR
SEQRES 1 B 76 ARG PHE TYR VAL LYS ASP HIS ARG ASN LYS ALA MET ILE
SEQRES 2 B 76 ASN LEU HIS ILE GLN LYS ASP ASN PRO LYS ILE VAL HIS
SEQRES 3 B 76 ALA PHE ASP GLY GLU ASP LEU GLY ASP LYS ALA VAL TYR
SEQRES 4 B 76 CYS ARG CYS TRP ARG SER LYS LYS PHE PRO PHE CYS ASP
SEQRES 5 B 76 GLY ALA HIS THR LYS HIS ASN GLU GLU THR GLY ASP ASN
SEQRES 6 B 76 VAL GLY PRO LEU ILE ILE LYS LYS LYS GLU THR
HET FES A 201 4
HET FES B 201 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 3 FES 2(FE2 S2)
FORMUL 5 HOH *84(H2 O)
HELIX 1 1 GLU A 63 LEU A 65 5 3
HELIX 2 2 GLY A 85 GLY A 95 1 11
HELIX 3 3 GLU B 63 LEU B 65 5 3
HELIX 4 4 GLY B 85 GLY B 95 1 11
SHEET 1 A 3 ILE A 56 ASP A 61 0
SHEET 2 A 3 VAL B 98 LYS B 104 1 O ILE B 102 N HIS A 58
SHEET 3 A 3 LYS B 68 TYR B 71 -1 N TYR B 71 O LEU B 101
SHEET 1 B 3 ALA A 69 TYR A 71 0
SHEET 2 B 3 VAL A 98 LYS A 104 -1 O LEU A 101 N TYR A 71
SHEET 3 B 3 ILE B 56 ASP B 61 1 O HIS B 58 N ILE A 102
LINK SG CYS A 72 FE1 FES A 201 1555 1555 2.36
LINK SG CYS A 74 FE1 FES A 201 1555 1555 2.24
LINK SG CYS A 83 FE2 FES A 201 1555 1555 2.20
LINK ND1 HIS A 87 FE2 FES A 201 1555 1555 2.13
LINK SG CYS B 72 FE1 FES B 201 1555 1555 2.33
LINK SG CYS B 74 FE1 FES B 201 1555 1555 2.25
LINK SG CYS B 83 FE2 FES B 201 1555 1555 2.31
LINK ND1 HIS B 87 FE2 FES B 201 1555 1555 2.12
CISPEP 1 PHE A 80 PRO A 81 0 12.75
CISPEP 2 PHE B 80 PRO B 81 0 12.01
SITE 1 AC1 9 CYS A 72 ARG A 73 CYS A 74 SER A 77
SITE 2 AC1 9 CYS A 83 ASP A 84 GLY A 85 ALA A 86
SITE 3 AC1 9 HIS A 87
SITE 1 AC2 8 CYS B 72 ARG B 73 CYS B 74 SER B 77
SITE 2 AC2 8 CYS B 83 ASP B 84 ALA B 86 HIS B 87
CRYST1 41.330 56.600 59.110 90.00 90.00 90.00 P 21 21 21 8
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 0.024195 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017668 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016918 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
