HEADER METAL BINDING PROTEIN 01-AUG-19 6SF5
TITLE MN-CONTAINING FORM OF THE RIBONUCLEOTIDE REDUCTASE NRDB PROTEIN FROM
TITLE 2 LEEUWENHOEKIELLA BLANDENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE, BETA SUBUNIT 1;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.17.4.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEEUWENHOEKIELLA BLANDENSIS;
SOURCE 3 ORGANISM_TAXID: 360293;
SOURCE 4 GENE: MED217_17135;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: /PET28A(+)
KEYWDS RIBONUCLEOTIDE REDUCTASE APOPROTEIN MANGANESE BINDING REDOX PROTEIN
KEYWDS 2 DEOXYRIBONUCLEOTIDE SYNTHESIS, METAL BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HASAN,I.ROZMAN GRINBERG,B.M.SJOBERG,D.T.LOGAN
REVDAT 4 24-JAN-24 6SF5 1 LINK
REVDAT 3 20-NOV-19 6SF5 1 LINK
REVDAT 2 02-OCT-19 6SF5 1 JRNL
REVDAT 1 28-AUG-19 6SF5 0
JRNL AUTH I.ROZMAN GRINBERG,S.BERGLUND,M.HASAN,D.LUNDIN,F.M.HO,
JRNL AUTH 2 A.MAGNUSON,D.T.LOGAN,B.M.SJOBERG,G.BERGGREN
JRNL TITL CLASS ID RIBONUCLEOTIDE REDUCTASE UTILIZES A MN2(IV,III)
JRNL TITL 2 COFACTOR AND UNDERGOES LARGE CONFORMATIONAL CHANGES ON METAL
JRNL TITL 3 LOADING.
JRNL REF J.BIOL.INORG.CHEM. V. 24 863 2019
JRNL REFN ESSN 1432-1327
JRNL PMID 31414238
JRNL DOI 10.1007/S00775-019-01697-8
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 58284
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2895
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.37
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1166
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2257
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1115
REMARK 3 BIN R VALUE (WORKING SET) : 0.2221
REMARK 3 BIN FREE R VALUE : 0.3088
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 51
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 : 4892
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 387
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.56960
REMARK 3 B22 (A**2) : 7.56200
REMARK 3 B33 (A**2) : 6.00760
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) : 0.230
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.130
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.113
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.126
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.112
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 : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5042 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6818 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1816 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 866 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5042 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 659 ; 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 : 6364 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.94
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.82
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.95
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3507 -1.922 155.943
REMARK 3 T TENSOR
REMARK 3 T11: -0.1329 T22: -0.1074
REMARK 3 T33: -0.0788 T12: -0.0288
REMARK 3 T13: 0.0345 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.0701 L22: 2.0431
REMARK 3 L33: 1.7906 L12: -0.7146
REMARK 3 L13: 0.5072 L23: 0.15
REMARK 3 S TENSOR
REMARK 3 S11: 0.0246 S12: -0.1438 S13: -0.116
REMARK 3 S21: -0.1438 S22: 0.0073 S23: 0.0343
REMARK 3 S31: -0.116 S32: 0.0343 S33: -0.0319
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0991 8.4655 189.872
REMARK 3 T TENSOR
REMARK 3 T11: -0.0008 T22: -0.0872
REMARK 3 T33: -0.1959 T12: 0.0244
REMARK 3 T13: 0.0742 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 1.4117 L22: 2.0736
REMARK 3 L33: 2.3058 L12: 0.8849
REMARK 3 L13: 0.5923 L23: 0.854
REMARK 3 S TENSOR
REMARK 3 S11: 0.1714 S12: 0.5249 S13: 0.0716
REMARK 3 S21: 0.5249 S22: -0.176 S23: -0.4239
REMARK 3 S31: 0.0716 S32: -0.4239 S33: 0.0046
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6SF5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1292103616.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 80.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.13700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: 6SF4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 7.5 MG/ML IN 50 MM TRIS-HCL
REMARK 280 PH 7.8, 300 MM NACL, 10% GLYCEROL, 20 MM MGCL2, 2 MM TRIS(2-
REMARK 280 CARBOXYETHYL)PHOSPHINE (TCEP) AND 10 MM MNCL2. 200+200 NL
REMARK 280 SITTING DROPS. PRECIPITANT 0.1 M BIS-TRIS PH 5.5, 25% W/V
REMARK 280 POLYETHYLENE GLYCOL 3350., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 28.53000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.11400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.30100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.11400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.53000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.30100
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: 2600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 MET A 80
REMARK 465 GLY A 81
REMARK 465 SER A 82
REMARK 465 SER A 83
REMARK 465 HIS A 84
REMARK 465 HIS A 85
REMARK 465 HIS A 86
REMARK 465 HIS A 87
REMARK 465 HIS A 88
REMARK 465 HIS A 89
REMARK 465 SER A 90
REMARK 465 SER A 91
REMARK 465 GLY A 92
REMARK 465 LEU A 93
REMARK 465 VAL A 94
REMARK 465 PRO A 95
REMARK 465 ARG A 96
REMARK 465 GLY A 97
REMARK 465 SER A 98
REMARK 465 HIS A 99
REMARK 465 LEU A 100
REMARK 465 GLU A 101
REMARK 465 ARG A 102
REMARK 465 LYS A 103
REMARK 465 GLY A 400
REMARK 465 THR A 401
REMARK 465 LYS A 402
REMARK 465 HIS A 403
REMARK 465 GLY A 404
REMARK 465 ASP A 405
REMARK 465 PHE A 406
REMARK 465 PHE A 407
REMARK 465 VAL A 408
REMARK 465 LYS A 409
REMARK 465 ARG A 410
REMARK 465 SER A 411
REMARK 465 ILE A 412
REMARK 465 ASN A 413
REMARK 465 TYR A 414
REMARK 465 SER A 415
REMARK 465 LYS A 416
REMARK 465 ARG A 417
REMARK 465 THR A 418
REMARK 465 GLN A 419
REMARK 465 SER A 420
REMARK 465 ILE A 421
REMARK 465 THR A 422
REMARK 465 SER A 423
REMARK 465 ASP A 424
REMARK 465 ASP A 425
REMARK 465 LEU A 426
REMARK 465 PHE A 427
REMARK 465 MET B 80
REMARK 465 GLY B 81
REMARK 465 SER B 82
REMARK 465 SER B 83
REMARK 465 HIS B 84
REMARK 465 HIS B 85
REMARK 465 HIS B 86
REMARK 465 HIS B 87
REMARK 465 HIS B 88
REMARK 465 HIS B 89
REMARK 465 SER B 90
REMARK 465 SER B 91
REMARK 465 GLY B 92
REMARK 465 LEU B 93
REMARK 465 VAL B 94
REMARK 465 PRO B 95
REMARK 465 ARG B 96
REMARK 465 GLY B 97
REMARK 465 SER B 98
REMARK 465 HIS B 99
REMARK 465 LEU B 100
REMARK 465 GLU B 101
REMARK 465 ARG B 102
REMARK 465 LYS B 103
REMARK 465 GLY B 400
REMARK 465 THR B 401
REMARK 465 LYS B 402
REMARK 465 HIS B 403
REMARK 465 GLY B 404
REMARK 465 ASP B 405
REMARK 465 PHE B 406
REMARK 465 PHE B 407
REMARK 465 VAL B 408
REMARK 465 LYS B 409
REMARK 465 ARG B 410
REMARK 465 SER B 411
REMARK 465 ILE B 412
REMARK 465 ASN B 413
REMARK 465 TYR B 414
REMARK 465 SER B 415
REMARK 465 LYS B 416
REMARK 465 ARG B 417
REMARK 465 THR B 418
REMARK 465 GLN B 419
REMARK 465 SER B 420
REMARK 465 ILE B 421
REMARK 465 THR B 422
REMARK 465 SER B 423
REMARK 465 ASP B 424
REMARK 465 ASP B 425
REMARK 465 LEU B 426
REMARK 465 PHE B 427
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 VAL A 265 -38.32 -137.00
REMARK 500 VAL B 265 -39.66 -136.34
REMARK 500 PHE B 320 66.23 -100.68
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 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 170 OE1
REMARK 620 2 GLU A 170 OE2 57.8
REMARK 620 3 GLU A 200 OE1 84.2 142.0
REMARK 620 4 HIS A 203 ND1 103.7 99.7 91.1
REMARK 620 5 GLU A 298 OE2 146.6 89.2 128.3 85.2
REMARK 620 6 HOH A 768 O 80.6 81.4 90.7 175.4 90.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 502 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 200 OE2
REMARK 620 2 GLU A 263 OE2 146.8
REMARK 620 3 GLU A 298 OE1 111.4 100.1
REMARK 620 4 HIS A 301 ND1 89.8 93.8 101.8
REMARK 620 5 HOH A 601 O 73.3 74.0 152.3 105.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 501 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 170 OE1
REMARK 620 2 GLU B 170 OE2 57.3
REMARK 620 3 GLU B 200 OE1 83.3 140.6
REMARK 620 4 HIS B 203 ND1 102.1 98.5 90.4
REMARK 620 5 GLU B 298 OE2 147.0 89.9 129.2 84.8
REMARK 620 6 HOH B 682 O 83.7 84.1 90.8 174.2 90.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 502 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 200 OE2
REMARK 620 2 GLU B 263 OE1 143.4
REMARK 620 3 GLU B 298 OE1 109.5 104.2
REMARK 620 4 HIS B 301 ND1 89.4 96.5 103.4
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 MN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6SF4 RELATED DB: PDB
REMARK 900 APO FORM OF SAME PROTEIN
DBREF 6SF5 A 100 427 UNP A3XHF9 A3XHF9_LEEBM 100 427
DBREF 6SF5 B 100 427 UNP A3XHF9 A3XHF9_LEEBM 100 427
SEQADV 6SF5 MET A 80 UNP A3XHF9 INITIATING METHIONINE
SEQADV 6SF5 GLY A 81 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER A 82 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER A 83 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS A 84 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS A 85 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS A 86 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS A 87 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS A 88 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS A 89 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER A 90 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER A 91 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 GLY A 92 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 LEU A 93 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 VAL A 94 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 PRO A 95 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 ARG A 96 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 GLY A 97 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER A 98 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS A 99 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 MET B 80 UNP A3XHF9 INITIATING METHIONINE
SEQADV 6SF5 GLY B 81 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER B 82 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER B 83 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS B 84 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS B 85 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS B 86 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS B 87 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS B 88 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS B 89 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER B 90 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER B 91 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 GLY B 92 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 LEU B 93 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 VAL B 94 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 PRO B 95 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 ARG B 96 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 GLY B 97 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 SER B 98 UNP A3XHF9 EXPRESSION TAG
SEQADV 6SF5 HIS B 99 UNP A3XHF9 EXPRESSION TAG
SEQRES 1 A 348 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 348 LEU VAL PRO ARG GLY SER HIS LEU GLU ARG LYS THR ASN
SEQRES 3 A 348 ILE PHE GLU LYS ARG ILE ASN LEU LYS PRO TYR GLU TYR
SEQRES 4 A 348 PRO GLU LEU ASN GLU TYR VAL ALA ALA ILE ARG HIS SER
SEQRES 5 A 348 TYR TRP ILE HIS THR GLU PHE ASN PHE THR SER ASP ILE
SEQRES 6 A 348 GLN ASP PHE LYS THR GLY LEU SER GLU VAL GLU ARG SER
SEQRES 7 A 348 ALA ILE LYS ASN THR MET LEU ALA ILE SER GLN ILE GLU
SEQRES 8 A 348 VAL ALA VAL LYS THR PHE TRP GLY ASP VAL HIS HIS ARG
SEQRES 9 A 348 LEU PRO LYS PRO GLU ILE ALA ALA VAL GLY ALA THR PHE
SEQRES 10 A 348 ALA GLU SER GLU VAL ARG HIS HIS ASP ALA TYR SER HIS
SEQRES 11 A 348 LEU LEU GLU ILE LEU GLY LEU ASN GLU GLU PHE LYS GLU
SEQRES 12 A 348 LEU LYS LYS LYS PRO VAL ILE MET LYS ARG VAL HIS TYR
SEQRES 13 A 348 LEU GLU THR SER LEU LYS HIS ALA LYS SER ASP ASP ASP
SEQRES 14 A 348 ARG GLU TYR THR GLU SER ILE LEU LEU PHE ALA LEU PHE
SEQRES 15 A 348 ILE GLU HIS VAL SER LEU PHE SER GLN PHE LEU ILE ILE
SEQRES 16 A 348 MET ALA PHE ASN LYS HIS LYS ASN MET LEU LYS GLY ILE
SEQRES 17 A 348 SER ASN ALA VAL GLU ALA THR SER LYS GLU GLU GLN ILE
SEQRES 18 A 348 HIS GLY ASP PHE GLY VAL ASP ILE ILE ASN ILE ILE LYS
SEQRES 19 A 348 LYS GLU ASN PRO GLU TRP PHE ASP GLU GLU HIS ASN ASN
SEQRES 20 A 348 LEU ILE LYS GLU MET CYS LEU ASN SER PHE GLU ALA GLU
SEQRES 21 A 348 SER LYS VAL VAL ASP TRP ILE PHE GLU LYS GLY GLU LEU
SEQRES 22 A 348 ASP PHE LEU PRO LYS ALA VAL ILE ASN GLU PHE LEU LYS
SEQRES 23 A 348 ASN ARG PHE ASN LYS SER LEU GLU ALA ILE GLY LEU GLU
SEQRES 24 A 348 LYS LEU PHE ASP ILE ASP GLU ALA LEU LEU GLN GLU THR
SEQRES 25 A 348 GLU TRP PHE ASP ASP GLU ILE ILE GLY THR LYS HIS GLY
SEQRES 26 A 348 ASP PHE PHE VAL LYS ARG SER ILE ASN TYR SER LYS ARG
SEQRES 27 A 348 THR GLN SER ILE THR SER ASP ASP LEU PHE
SEQRES 1 B 348 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 348 LEU VAL PRO ARG GLY SER HIS LEU GLU ARG LYS THR ASN
SEQRES 3 B 348 ILE PHE GLU LYS ARG ILE ASN LEU LYS PRO TYR GLU TYR
SEQRES 4 B 348 PRO GLU LEU ASN GLU TYR VAL ALA ALA ILE ARG HIS SER
SEQRES 5 B 348 TYR TRP ILE HIS THR GLU PHE ASN PHE THR SER ASP ILE
SEQRES 6 B 348 GLN ASP PHE LYS THR GLY LEU SER GLU VAL GLU ARG SER
SEQRES 7 B 348 ALA ILE LYS ASN THR MET LEU ALA ILE SER GLN ILE GLU
SEQRES 8 B 348 VAL ALA VAL LYS THR PHE TRP GLY ASP VAL HIS HIS ARG
SEQRES 9 B 348 LEU PRO LYS PRO GLU ILE ALA ALA VAL GLY ALA THR PHE
SEQRES 10 B 348 ALA GLU SER GLU VAL ARG HIS HIS ASP ALA TYR SER HIS
SEQRES 11 B 348 LEU LEU GLU ILE LEU GLY LEU ASN GLU GLU PHE LYS GLU
SEQRES 12 B 348 LEU LYS LYS LYS PRO VAL ILE MET LYS ARG VAL HIS TYR
SEQRES 13 B 348 LEU GLU THR SER LEU LYS HIS ALA LYS SER ASP ASP ASP
SEQRES 14 B 348 ARG GLU TYR THR GLU SER ILE LEU LEU PHE ALA LEU PHE
SEQRES 15 B 348 ILE GLU HIS VAL SER LEU PHE SER GLN PHE LEU ILE ILE
SEQRES 16 B 348 MET ALA PHE ASN LYS HIS LYS ASN MET LEU LYS GLY ILE
SEQRES 17 B 348 SER ASN ALA VAL GLU ALA THR SER LYS GLU GLU GLN ILE
SEQRES 18 B 348 HIS GLY ASP PHE GLY VAL ASP ILE ILE ASN ILE ILE LYS
SEQRES 19 B 348 LYS GLU ASN PRO GLU TRP PHE ASP GLU GLU HIS ASN ASN
SEQRES 20 B 348 LEU ILE LYS GLU MET CYS LEU ASN SER PHE GLU ALA GLU
SEQRES 21 B 348 SER LYS VAL VAL ASP TRP ILE PHE GLU LYS GLY GLU LEU
SEQRES 22 B 348 ASP PHE LEU PRO LYS ALA VAL ILE ASN GLU PHE LEU LYS
SEQRES 23 B 348 ASN ARG PHE ASN LYS SER LEU GLU ALA ILE GLY LEU GLU
SEQRES 24 B 348 LYS LEU PHE ASP ILE ASP GLU ALA LEU LEU GLN GLU THR
SEQRES 25 B 348 GLU TRP PHE ASP ASP GLU ILE ILE GLY THR LYS HIS GLY
SEQRES 26 B 348 ASP PHE PHE VAL LYS ARG SER ILE ASN TYR SER LYS ARG
SEQRES 27 B 348 THR GLN SER ILE THR SER ASP ASP LEU PHE
HET MN A 501 1
HET MN A 502 1
HET MN B 501 1
HET MN B 502 1
HETNAM MN MANGANESE (II) ION
FORMUL 3 MN 4(MN 2+)
FORMUL 7 HOH *387(H2 O)
HELIX 1 AA1 TYR A 118 LEU A 121 5 4
HELIX 2 AA2 ASN A 122 TYR A 132 1 11
HELIX 3 AA3 ILE A 134 PHE A 138 5 5
HELIX 4 AA4 PHE A 140 GLY A 150 1 11
HELIX 5 AA5 SER A 152 VAL A 171 1 20
HELIX 6 AA6 THR A 175 LEU A 184 1 10
HELIX 7 AA7 LYS A 186 LEU A 214 1 29
HELIX 8 AA8 LEU A 216 LEU A 223 1 8
HELIX 9 AA9 LYS A 226 LEU A 240 1 15
HELIX 10 AB1 ASP A 247 PHE A 261 1 15
HELIX 11 AB2 PHE A 261 SER A 266 1 6
HELIX 12 AB3 LEU A 267 ASN A 282 1 16
HELIX 13 AB4 LEU A 284 ASN A 316 1 33
HELIX 14 AB5 PRO A 317 PHE A 320 5 4
HELIX 15 AB6 ASP A 321 PHE A 347 1 27
HELIX 16 AB7 PRO A 356 ILE A 375 1 20
HELIX 17 AB8 ASP A 384 GLU A 390 1 7
HELIX 18 AB9 THR A 391 ILE A 399 1 9
HELIX 19 AC1 TYR B 118 LEU B 121 5 4
HELIX 20 AC2 ASN B 122 TYR B 132 1 11
HELIX 21 AC3 ILE B 134 PHE B 138 5 5
HELIX 22 AC4 PHE B 140 GLY B 150 1 11
HELIX 23 AC5 SER B 152 VAL B 171 1 20
HELIX 24 AC6 THR B 175 LEU B 184 1 10
HELIX 25 AC7 LYS B 186 LEU B 214 1 29
HELIX 26 AC8 LEU B 216 LEU B 223 1 8
HELIX 27 AC9 LYS B 226 LEU B 240 1 15
HELIX 28 AD1 ASP B 247 PHE B 261 1 15
HELIX 29 AD2 PHE B 261 SER B 266 1 6
HELIX 30 AD3 LEU B 267 ASN B 282 1 16
HELIX 31 AD4 LEU B 284 ASN B 316 1 33
HELIX 32 AD5 PRO B 317 PHE B 320 5 4
HELIX 33 AD6 ASP B 321 PHE B 347 1 27
HELIX 34 AD7 PRO B 356 ILE B 375 1 20
HELIX 35 AD8 ASP B 384 GLU B 390 1 7
HELIX 36 AD9 THR B 391 ILE B 399 1 9
LINK OE1 GLU A 170 MN MN A 501 1555 1555 2.29
LINK OE2 GLU A 170 MN MN A 501 1555 1555 2.24
LINK OE1 GLU A 200 MN MN A 501 1555 1555 2.17
LINK OE2 GLU A 200 MN MN A 502 1555 1555 2.08
LINK ND1 HIS A 203 MN MN A 501 1555 1555 2.22
LINK OE2 GLU A 263 MN MN A 502 1555 1555 2.16
LINK OE2 GLU A 298 MN MN A 501 1555 1555 2.07
LINK OE1 GLU A 298 MN MN A 502 1555 1555 2.05
LINK ND1 HIS A 301 MN MN A 502 1555 1555 2.12
LINK MN MN A 501 O HOH A 768 1555 1555 2.31
LINK MN MN A 502 O HOH A 601 1555 1555 2.21
LINK OE1 GLU B 170 MN MN B 501 1555 1555 2.30
LINK OE2 GLU B 170 MN MN B 501 1555 1555 2.26
LINK OE1 GLU B 200 MN MN B 501 1555 1555 2.21
LINK OE2 GLU B 200 MN MN B 502 1555 1555 2.13
LINK ND1 HIS B 203 MN MN B 501 1555 1555 2.26
LINK OE1 GLU B 263 MN MN B 502 1555 1555 2.09
LINK OE2 GLU B 298 MN MN B 501 1555 1555 2.02
LINK OE1 GLU B 298 MN MN B 502 1555 1555 2.05
LINK ND1 HIS B 301 MN MN B 502 1555 1555 2.10
LINK MN MN B 501 O HOH B 682 1555 1555 2.22
CISPEP 1 LYS A 114 PRO A 115 0 -0.70
CISPEP 2 LYS B 114 PRO B 115 0 0.81
SITE 1 AC1 5 GLU A 170 GLU A 200 HIS A 203 GLU A 298
SITE 2 AC1 5 HOH A 768
SITE 1 AC2 5 GLU A 200 GLU A 263 GLU A 298 HIS A 301
SITE 2 AC2 5 HOH A 601
SITE 1 AC3 5 GLU B 170 GLU B 200 HIS B 203 GLU B 298
SITE 2 AC3 5 HOH B 682
SITE 1 AC4 4 GLU B 200 GLU B 263 GLU B 298 HIS B 301
CRYST1 57.060 80.602 158.228 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 0.017525 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012407 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
