HEADER METAL BINDING PROTEIN 12-FEB-16 5I4K
TITLE METAL ABC TRANSPORTER FROM LISTERIA MONOCYTOGENES WITH MANGANESE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANGANESE-BINDING LIPOPROTEIN MNTA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES EGD-E;
SOURCE 3 ORGANISM_TAXID: 169963;
SOURCE 4 STRAIN: ATCC BAA-679 / EGD-E;
SOURCE 5 GENE: MNTA, LMO1847;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG53
KEYWDS STRUCTURAL GENOMICS, IDP02508, METAL ABC TRANSPORTER, MANGANESE,
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, METAL
KEYWDS 3 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 3 11-DEC-19 5I4K 1 REMARK
REVDAT 2 20-SEP-17 5I4K 1 REMARK
REVDAT 1 24-FEB-16 5I4K 0
JRNL AUTH J.OSIPIUK,M.ZHOU,S.GRIMSHAW,W.F.ANDERSON,A.JOACHIMIAK,
JRNL AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 3 (CSGID)
JRNL TITL METAL ABC TRANSPORTER FROM LISTERIA MONOCYTOGENES WITH
JRNL TITL 2 MANGANESE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.79 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.79
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 24530
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1225
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.79
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1344
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.2750
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2204
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 222
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.58
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.81000
REMARK 3 B22 (A**2) : -0.52000
REMARK 3 B33 (A**2) : -0.29000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.110
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.078
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.973
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.956
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2308 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2209 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3136 ; 1.424 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5134 ; 0.778 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 6.171 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;33.875 ;26.091
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 410 ;13.920 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;10.090 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 347 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2630 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 483 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1137 ; 1.529 ; 2.008
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1136 ; 1.510 ; 2.005
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1424 ; 2.351 ; 3.002
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 31 A 503
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4838 27.4851 46.5028
REMARK 3 T TENSOR
REMARK 3 T11: 0.0355 T22: 0.0157
REMARK 3 T33: 0.0152 T12: -0.0179
REMARK 3 T13: -0.0208 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.2625 L22: 0.8827
REMARK 3 L33: 0.1352 L12: 0.0887
REMARK 3 L13: 0.0426 L23: -0.0192
REMARK 3 S TENSOR
REMARK 3 S11: -0.0380 S12: -0.0157 S13: 0.0277
REMARK 3 S21: -0.1338 S22: 0.0628 S23: 0.0606
REMARK 3 S31: 0.0149 S32: -0.0095 S33: -0.0248
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5I4K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218235.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25812
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 32.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.900
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.87200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 8000, 0.2 M MANGANESE
REMARK 280 CHLORIDE, 0.1 M TRIS, PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
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 28.95300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.74600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.15550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.74600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.95300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.15550
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 SER A 21
REMARK 465 ASN A 22
REMARK 465 ALA A 23
REMARK 465 SER A 24
REMARK 465 ASP A 25
REMARK 465 SER A 26
REMARK 465 LYS A 27
REMARK 465 LYS A 28
REMARK 465 THR A 29
REMARK 465 ASP A 30
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 OE1 GLU A 153 O HOH A 601 2.17
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 ILE A 59 -63.89 -96.55
REMARK 500 HIS A 140 48.43 -84.52
REMARK 500 THR A 280 -73.21 -120.13
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 HIS A 67 NE2
REMARK 620 2 HIS A 140 NE2 103.1
REMARK 620 3 GLU A 206 OE1 136.5 94.7
REMARK 620 4 GLU A 206 OE2 85.7 88.8 55.0
REMARK 620 5 ASP A 281 OD1 111.8 86.5 108.6 162.4
REMARK 620 6 ASP A 281 OD2 92.7 142.3 96.9 126.8 55.9
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 ASP A 291 OD1
REMARK 620 2 GLU A 295 OE1 82.5
REMARK 620 3 GLU A 295 OE2 101.6 50.8
REMARK 620 4 HOH A 623 O 95.1 114.5 66.2
REMARK 620 5 HOH A 724 O 91.0 78.7 124.7 166.1
REMARK 620 6 HOH A 637 O 91.6 158.8 150.2 86.2 81.1
REMARK 620 7 HOH A 779 O 171.0 103.4 87.5 88.7 83.6 80.5
REMARK 620 N 1 2 3 4 5 6
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 CL A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP02508 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 5HX7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, APO-FORM
DBREF 5I4K A 24 310 UNP Q8Y653 MNTA_LISMO 24 310
SEQADV 5I4K SER A 21 UNP Q8Y653 EXPRESSION TAG
SEQADV 5I4K ASN A 22 UNP Q8Y653 EXPRESSION TAG
SEQADV 5I4K ALA A 23 UNP Q8Y653 EXPRESSION TAG
SEQRES 1 A 290 SER ASN ALA SER ASP SER LYS LYS THR ASP GLY LYS LEU
SEQRES 2 A 290 ASN VAL VAL ALA THR TYR SER ILE LEU ALA ASP ILE VAL
SEQRES 3 A 290 LYS ASN VAL GLY GLY ASN LYS ILE GLU LEU HIS SER ILE
SEQRES 4 A 290 VAL PRO VAL GLY VAL ASP PRO HIS GLU TYR ASP PRO LEU
SEQRES 5 A 290 PRO ALA ASN ILE GLN SER ALA ALA ASP ALA ASP LEU ILE
SEQRES 6 A 290 PHE TYR ASN GLY LEU ASN LEU GLU THR GLY ASN GLY TRP
SEQRES 7 A 290 PHE ASP ARG MSE LEU GLU THR ALA ASP LYS SER ARG GLU
SEQRES 8 A 290 ASP LYS ASN GLN VAL VAL GLU LEU SER LYS GLY VAL LYS
SEQRES 9 A 290 PRO LYS TYR LEU THR GLU LYS GLY LYS THR SER GLU THR
SEQRES 10 A 290 ASP PRO HIS ALA TRP LEU ASP LEU HIS ASN GLY ILE ILE
SEQRES 11 A 290 TYR THR GLU ASN VAL ARG ASP ALA LEU VAL LYS ALA ASP
SEQRES 12 A 290 PRO ASP ASN ALA ASP PHE TYR LYS GLU ASN ALA LYS LYS
SEQRES 13 A 290 TYR ILE ASP LYS LEU ALA THR LEU ASP LYS GLU ALA LYS
SEQRES 14 A 290 GLN LYS PHE ALA ASP LEU PRO GLU ASN GLN LYS THR LEU
SEQRES 15 A 290 VAL THR SER GLU GLY ALA PHE LYS TYR PHE ALA ALA ARG
SEQRES 16 A 290 TYR GLY LEU LYS ALA ALA TYR ILE TRP GLU ILE ASN THR
SEQRES 17 A 290 GLU SER GLN GLY THR PRO ASP GLN MSE LYS GLN ILE VAL
SEQRES 18 A 290 GLY ILE VAL GLU LYS GLU LYS VAL PRO ASN LEU PHE VAL
SEQRES 19 A 290 GLU THR SER VAL ASP PRO ARG SER MSE GLU SER VAL SER
SEQRES 20 A 290 LYS GLU THR GLY VAL PRO ILE PHE ALA LYS ILE PHE THR
SEQRES 21 A 290 ASP SER THR ALA LYS LYS GLY GLU VAL GLY ASP THR TYR
SEQRES 22 A 290 LEU GLU MSE MSE ARG TYR ASN LEU ASP LYS ILE HIS ASP
SEQRES 23 A 290 GLY LEU ALA LYS
MODRES 5I4K MSE A 102 MET MODIFIED RESIDUE
MODRES 5I4K MSE A 237 MET MODIFIED RESIDUE
MODRES 5I4K MSE A 263 MET MODIFIED RESIDUE
MODRES 5I4K MSE A 296 MET MODIFIED RESIDUE
MODRES 5I4K MSE A 297 MET MODIFIED RESIDUE
HET MSE A 102 8
HET MSE A 237 8
HET MSE A 263 8
HET MSE A 296 8
HET MSE A 297 8
HET MN A 501 1
HET MN A 502 1
HET CL A 503 1
HETNAM MSE SELENOMETHIONINE
HETNAM MN MANGANESE (II) ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 MN 2(MN 2+)
FORMUL 4 CL CL 1-
FORMUL 5 HOH *222(H2 O)
HELIX 1 AA1 TYR A 39 GLY A 51 1 13
HELIX 2 AA2 LEU A 72 ALA A 82 1 11
HELIX 3 AA3 THR A 94 ASN A 96 5 3
HELIX 4 AA4 GLY A 97 ALA A 106 1 10
HELIX 5 AA5 HIS A 140 LEU A 143 5 4
HELIX 6 AA6 ASP A 144 ASP A 163 1 20
HELIX 7 AA7 ASN A 166 PHE A 192 1 27
HELIX 8 AA8 PHE A 209 GLY A 217 1 9
HELIX 9 AA9 THR A 233 GLU A 247 1 15
HELIX 10 AB1 PRO A 260 GLY A 271 1 12
HELIX 11 AB2 THR A 292 ALA A 309 1 18
SHEET 1 AA1 4 ILE A 54 SER A 58 0
SHEET 2 AA1 4 LEU A 33 ALA A 37 1 N LEU A 33 O GLU A 55
SHEET 3 AA1 4 LEU A 84 TYR A 87 1 O PHE A 86 N VAL A 36
SHEET 4 AA1 4 VAL A 116 GLU A 118 1 O VAL A 117 N ILE A 85
SHEET 1 AA2 2 THR A 201 GLU A 206 0
SHEET 2 AA2 2 LYS A 219 TRP A 224 1 O LYS A 219 N LEU A 202
SHEET 1 AA3 2 LEU A 252 GLU A 255 0
SHEET 2 AA3 2 ILE A 274 ILE A 278 1 O PHE A 275 N LEU A 252
LINK NE2 HIS A 67 MN MN A 501 1555 1555 2.25
LINK C ARG A 101 N MSE A 102 1555 1555 1.33
LINK C MSE A 102 N LEU A 103 1555 1555 1.33
LINK NE2 HIS A 140 MN MN A 501 1555 1555 2.15
LINK OE1 GLU A 206 MN MN A 501 1555 1555 2.18
LINK OE2 GLU A 206 MN MN A 501 1555 1555 2.54
LINK C GLN A 236 N MSE A 237 1555 1555 1.33
LINK C MSE A 237 N LYS A 238 1555 1555 1.33
LINK C SER A 262 N MSE A 263 1555 1555 1.33
LINK C MSE A 263 N GLU A 264 1555 1555 1.34
LINK OD1 ASP A 281 MN MN A 501 1555 1555 2.47
LINK OD2 ASP A 281 MN MN A 501 1555 1555 2.14
LINK OD1 ASP A 291 MN MN A 502 1555 1555 2.25
LINK C GLU A 295 N MSE A 296 1555 1555 1.33
LINK OE1 GLU A 295 MN MN A 502 1555 1555 2.42
LINK OE2 GLU A 295 MN MN A 502 1555 1555 2.72
LINK C MSE A 296 N MSE A 297 1555 1555 1.34
LINK C MSE A 297 N ARG A 298 1555 1555 1.33
LINK MN MN A 502 O HOH A 623 1555 1555 1.90
LINK MN MN A 502 O HOH A 724 1555 1555 2.05
LINK MN MN A 502 O HOH A 637 1555 1555 2.33
LINK MN MN A 502 O HOH A 779 1555 1555 1.99
SITE 1 AC1 4 HIS A 67 HIS A 140 GLU A 206 ASP A 281
SITE 1 AC2 6 ASP A 291 GLU A 295 HOH A 623 HOH A 637
SITE 2 AC2 6 HOH A 724 HOH A 779
SITE 1 AC3 3 LYS A 126 TYR A 127 HOH A 664
CRYST1 57.906 62.311 75.492 90.00 90.00 90.00 P 21 21 21 4
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 0.017269 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013246 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
