HEADER HYDROLASE 22-JUL-13 4LS9
TITLE STRUCTURE OF MYCOBACTERIAL NRNA HOMOLOG REVEALS MULTIFUNCTIONAL
TITLE 2 NUCLEASE ACTIVITIES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DHH FAMILY PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;
SOURCE 3 ORGANISM_TAXID: 246196;
SOURCE 4 STRAIN: MC(2)155;
SOURCE 5 GENE: MSMEG_2630;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS DHH-FAMILY, NANORNASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KUMAR,R.SRIVASTAV,A.GROVER,B.A.MANJASETTY,R.SHARMA,B.TANEJA
REVDAT 1 16-JUL-14 4LS9 0
JRNL AUTH R.SRIVASTAV,D.KUMAR,A.GROVER,A.SINGH,B.A.MANJASETTY,
JRNL AUTH 2 R.SHARMA,B.TANEJA
JRNL TITL UNIQUE SUBUNIT PACKING IN MYCOBACTERIAL NANORNASE LEADS TO
JRNL TITL 2 ALTERNATE SUBSTRATE RECOGNITIONS IN DHH PHOSPHODIESTERASES
JRNL REF NUCLEIC ACIDS RES. V. 42 7894 2014
JRNL REFN ISSN 0305-1048
JRNL PMID 24878921
JRNL DOI 10.1093/NAR/GKU425
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 32831
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1666
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 : 16
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.27
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2988
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1867
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2825
REMARK 3 BIN R VALUE (WORKING SET) : 0.1834
REMARK 3 BIN FREE R VALUE : 0.2434
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.46
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 163
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 : 4708
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 268
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.92220
REMARK 3 B22 (A**2) : 6.77210
REMARK 3 B33 (A**2) : 2.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 5.03700
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.286
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.247
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.191
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.245
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.194
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 : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4893 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6696 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1629 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 98 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 755 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4893 ; 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 : 652 ; 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 : 5885 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.13
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.64
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.81
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|22 - 189}
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8405 7.7300 49.2651
REMARK 3 T TENSOR
REMARK 3 T11: -0.1007 T22: -0.0951
REMARK 3 T33: -0.0007 T12: 0.0174
REMARK 3 T13: -0.0495 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.4481 L22: 3.1334
REMARK 3 L33: 1.2343 L12: 1.0585
REMARK 3 L13: 0.3340 L23: 0.1948
REMARK 3 S TENSOR
REMARK 3 S11: -0.0662 S12: -0.0357 S13: 0.2272
REMARK 3 S21: -0.0919 S22: -0.0479 S23: 0.0938
REMARK 3 S31: -0.1001 S32: 0.0235 S33: 0.1142
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|190 - 240}
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1652 -13.0269 52.1721
REMARK 3 T TENSOR
REMARK 3 T11: -0.0630 T22: -0.0506
REMARK 3 T33: 0.0404 T12: 0.0003
REMARK 3 T13: 0.0018 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 1.2824 L22: 1.8835
REMARK 3 L33: 0.7751 L12: -0.0147
REMARK 3 L13: -0.0581 L23: -0.7911
REMARK 3 S TENSOR
REMARK 3 S11: 0.0214 S12: -0.1703 S13: 0.0274
REMARK 3 S21: 0.1058 S22: 0.0647 S23: 0.2508
REMARK 3 S31: 0.0182 S32: -0.1365 S33: -0.0861
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|241 - 340}
REMARK 3 ORIGIN FOR THE GROUP (A): -37.9815 -10.1303 44.8430
REMARK 3 T TENSOR
REMARK 3 T11: -0.1066 T22: 0.0827
REMARK 3 T33: 0.2471 T12: 0.0128
REMARK 3 T13: 0.0261 T23: 0.0452
REMARK 3 L TENSOR
REMARK 3 L11: 5.0920 L22: 5.0880
REMARK 3 L33: 5.0062 L12: -2.5953
REMARK 3 L13: 2.5271 L23: -2.2696
REMARK 3 S TENSOR
REMARK 3 S11: 0.1485 S12: 0.2022 S13: 0.2812
REMARK 3 S21: -0.4079 S22: -0.0867 S23: 0.5319
REMARK 3 S31: 0.1145 S32: -0.1663 S33: -0.0618
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {B|22 - 189}
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9922 -37.2821 38.8591
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: -0.1325
REMARK 3 T33: 0.0128 T12: 0.0466
REMARK 3 T13: -0.1417 T23: -0.0167
REMARK 3 L TENSOR
REMARK 3 L11: 1.3895 L22: 3.5562
REMARK 3 L33: 2.4149 L12: 0.4371
REMARK 3 L13: 0.7619 L23: 1.2286
REMARK 3 S TENSOR
REMARK 3 S11: 0.2378 S12: 0.1158 S13: -0.1955
REMARK 3 S21: 0.1616 S22: 0.0305 S23: -0.1998
REMARK 3 S31: 0.5964 S32: 0.1380 S33: -0.2682
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {B|190 - 240}
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0923 -20.2060 48.6572
REMARK 3 T TENSOR
REMARK 3 T11: -0.1035 T22: -0.0660
REMARK 3 T33: 0.0736 T12: 0.0038
REMARK 3 T13: -0.0743 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 1.2214 L22: 2.0069
REMARK 3 L33: 2.0391 L12: -0.5864
REMARK 3 L13: -0.2341 L23: 0.3707
REMARK 3 S TENSOR
REMARK 3 S11: -0.0753 S12: -0.1647 S13: -0.1484
REMARK 3 S21: -0.0439 S22: 0.1127 S23: 0.1995
REMARK 3 S31: 0.1618 S32: -0.1561 S33: -0.0374
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {B|241 - 340}
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7147 -26.4660 68.3758
REMARK 3 T TENSOR
REMARK 3 T11: -0.0908 T22: 0.1838
REMARK 3 T33: 0.0922 T12: 0.0387
REMARK 3 T13: 0.1077 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 1.6735 L22: 5.0664
REMARK 3 L33: 1.7190 L12: -1.1140
REMARK 3 L13: 1.0588 L23: -0.8043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1734 S12: -0.3642 S13: -0.1842
REMARK 3 S21: 0.4229 S22: 0.2589 S23: 0.0695
REMARK 3 S31: -0.1006 S32: -0.1453 S33: -0.0855
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4LS9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-AUG-13.
REMARK 100 THE RCSB ID CODE IS RCSB081021.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9788
REMARK 200 MONOCHROMATOR : SILICON MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33001
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 58.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: AUTORICKSHAW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, PH 7.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 43.04500
REMARK 290 SMTRY3 2 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: 4430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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 SER A 0
REMARK 465 MSE A 1
REMARK 465 PRO A 2
REMARK 465 VAL A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 THR A 6
REMARK 465 ASP A 7
REMARK 465 PRO A 8
REMARK 465 LYS A 9
REMARK 465 THR A 10
REMARK 465 GLY A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 THR A 14
REMARK 465 GLY A 15
REMARK 465 PRO A 16
REMARK 465 ASP A 17
REMARK 465 ALA A 18
REMARK 465 GLN A 19
REMARK 465 ILE A 20
REMARK 465 ALA A 21
REMARK 465 SER B 0
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 VAL B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 THR B 6
REMARK 465 ASP B 7
REMARK 465 PRO B 8
REMARK 465 LYS B 9
REMARK 465 THR B 10
REMARK 465 GLY B 11
REMARK 465 LEU B 12
REMARK 465 LEU B 13
REMARK 465 THR B 14
REMARK 465 GLY B 15
REMARK 465 PRO B 16
REMARK 465 ASP B 17
REMARK 465 ALA B 18
REMARK 465 GLN B 19
REMARK 465 ILE B 20
REMARK 465 ALA B 21
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 ALA A 119 1.79 -66.76
REMARK 500 ASP A 219 57.94 -118.83
REMARK 500 PRO A 263 -37.64 -37.88
REMARK 500 ASP B 219 17.24 51.64
REMARK 500 MSE B 291 -19.48 80.51
REMARK 500 SER B 301 -18.82 -140.95
REMARK 500 ALA B 319 78.66 -156.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 302 24.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1173 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH A1194 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B1156 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B1162 DISTANCE = 7.58 ANGSTROMS
REMARK 525 HOH B1177 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH B1208 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B1231 DISTANCE = 6.66 ANGSTROMS
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 B1001 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 51 OD2
REMARK 620 2 ASP B 185 OD2 81.4
REMARK 620 3 HIS B 135 NE2 99.2 83.2
REMARK 620 4 ASP B 110 OD2 85.5 145.1 130.9
REMARK 620 5 ASP B 110 OD1 88.4 160.3 81.9 49.2
REMARK 620 6 HOH B1191 O 111.1 77.5 140.8 77.4 122.0
REMARK 620 7 HOH B1109 O 174.1 102.4 76.9 93.7 86.7 74.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1001 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 51 OD2
REMARK 620 2 ASP A 110 OD1 82.6
REMARK 620 3 ASP A 185 OD2 80.2 157.1
REMARK 620 4 HIS A 135 NE2 101.0 83.9 84.5
REMARK 620 5 ASP A 110 OD2 87.5 52.6 140.9 134.5
REMARK 620 6 HOH A1228 O 174.9 96.2 99.5 73.9 95.8
REMARK 620 7 HOH A1229 O 105.6 126.7 73.1 141.2 74.9 79.0
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1002
DBREF 4LS9 A 1 340 UNP A0QVM9 A0QVM9_MYCS2 1 340
DBREF 4LS9 B 1 340 UNP A0QVM9 A0QVM9_MYCS2 1 340
SEQADV 4LS9 SER A 0 UNP A0QVM9 EXPRESSION TAG
SEQADV 4LS9 SER B 0 UNP A0QVM9 EXPRESSION TAG
SEQRES 1 A 341 SER MSE PRO VAL THR THR THR ASP PRO LYS THR GLY LEU
SEQRES 2 A 341 LEU THR GLY PRO ASP ALA GLN ILE ALA GLY ALA ARG VAL
SEQRES 3 A 341 ASP ALA ARG GLY ALA ALA ASP LEU LEU THR ALA ALA SER
SEQRES 4 A 341 SER VAL SER VAL ILE CYS HIS VAL TYR PRO ASP ALA ASP
SEQRES 5 A 341 THR ILE GLY ALA GLY LEU ALA LEU ALA GLN VAL LEU ALA
SEQRES 6 A 341 ALA SER GLY LYS HIS VAL GLU VAL SER PHE ALA THR PRO
SEQRES 7 A 341 ALA GLN LEU PRO GLU SER LEU GLN SER LEU PRO GLY GLY
SEQRES 8 A 341 HIS LEU LEU VAL ALA PRO GLU ALA MSE ARG ARG ASP ALA
SEQRES 9 A 341 ASP LEU VAL VAL THR VAL ASP ILE PRO SER ILE ASN ARG
SEQRES 10 A 341 LEU GLY ALA LEU SER GLY LEU ALA GLY PRO GLY ARG GLU
SEQRES 11 A 341 VAL LEU VAL ILE ASP HIS HIS ALA SER ASN GLN LEU PHE
SEQRES 12 A 341 GLY THR ALA ASN TYR ILE ASP PRO SER ALA ASP SER THR
SEQRES 13 A 341 THR MSE LEU VAL ALA GLU LEU LEU ASP ALA TRP GLY LYS
SEQRES 14 A 341 PRO ILE ASP GLU LYS VAL ALA HIS CYS LEU TYR ALA GLY
SEQRES 15 A 341 LEU THR THR ASP THR GLY SER PHE ARG TRP ALA THR ALA
SEQRES 16 A 341 ARG ALA HIS ARG LEU ALA ALA ARG LEU VAL GLU LEU GLY
SEQRES 17 A 341 VAL ASP ASN ALA SER ILE SER ARG THR LEU LEU ASP THR
SEQRES 18 A 341 HIS PRO PHE ALA TRP LEU PRO MSE LEU SER ARG VAL LEU
SEQRES 19 A 341 ALA THR ALA ARG LEU LEU PRO ASP ALA LEU ASP GLY ARG
SEQRES 20 A 341 GLY PHE VAL TYR ALA VAL VAL PRO HIS ASP GLU TRP SER
SEQRES 21 A 341 GLU ALA ARG PRO GLU GLU VAL GLU SER ILE VAL ASP ILE
SEQRES 22 A 341 VAL ARG THR THR GLN GLN ALA GLU VAL ALA ALA VAL PHE
SEQRES 23 A 341 LYS GLU ILE GLU PRO MSE HIS TRP SER VAL SER MSE ARG
SEQRES 24 A 341 ALA LYS SER VAL ASN LEU ALA SER VAL ALA SER ALA PHE
SEQRES 25 A 341 GLY GLY GLY GLY HIS PRO HIS ALA ALA GLY TYR SER ALA
SEQRES 26 A 341 THR GLY SER ALA ASP ASP VAL VAL GLN ALA LEU ALA ARG
SEQRES 27 A 341 ALA LEU GLY
SEQRES 1 B 341 SER MSE PRO VAL THR THR THR ASP PRO LYS THR GLY LEU
SEQRES 2 B 341 LEU THR GLY PRO ASP ALA GLN ILE ALA GLY ALA ARG VAL
SEQRES 3 B 341 ASP ALA ARG GLY ALA ALA ASP LEU LEU THR ALA ALA SER
SEQRES 4 B 341 SER VAL SER VAL ILE CYS HIS VAL TYR PRO ASP ALA ASP
SEQRES 5 B 341 THR ILE GLY ALA GLY LEU ALA LEU ALA GLN VAL LEU ALA
SEQRES 6 B 341 ALA SER GLY LYS HIS VAL GLU VAL SER PHE ALA THR PRO
SEQRES 7 B 341 ALA GLN LEU PRO GLU SER LEU GLN SER LEU PRO GLY GLY
SEQRES 8 B 341 HIS LEU LEU VAL ALA PRO GLU ALA MSE ARG ARG ASP ALA
SEQRES 9 B 341 ASP LEU VAL VAL THR VAL ASP ILE PRO SER ILE ASN ARG
SEQRES 10 B 341 LEU GLY ALA LEU SER GLY LEU ALA GLY PRO GLY ARG GLU
SEQRES 11 B 341 VAL LEU VAL ILE ASP HIS HIS ALA SER ASN GLN LEU PHE
SEQRES 12 B 341 GLY THR ALA ASN TYR ILE ASP PRO SER ALA ASP SER THR
SEQRES 13 B 341 THR MSE LEU VAL ALA GLU LEU LEU ASP ALA TRP GLY LYS
SEQRES 14 B 341 PRO ILE ASP GLU LYS VAL ALA HIS CYS LEU TYR ALA GLY
SEQRES 15 B 341 LEU THR THR ASP THR GLY SER PHE ARG TRP ALA THR ALA
SEQRES 16 B 341 ARG ALA HIS ARG LEU ALA ALA ARG LEU VAL GLU LEU GLY
SEQRES 17 B 341 VAL ASP ASN ALA SER ILE SER ARG THR LEU LEU ASP THR
SEQRES 18 B 341 HIS PRO PHE ALA TRP LEU PRO MSE LEU SER ARG VAL LEU
SEQRES 19 B 341 ALA THR ALA ARG LEU LEU PRO ASP ALA LEU ASP GLY ARG
SEQRES 20 B 341 GLY PHE VAL TYR ALA VAL VAL PRO HIS ASP GLU TRP SER
SEQRES 21 B 341 GLU ALA ARG PRO GLU GLU VAL GLU SER ILE VAL ASP ILE
SEQRES 22 B 341 VAL ARG THR THR GLN GLN ALA GLU VAL ALA ALA VAL PHE
SEQRES 23 B 341 LYS GLU ILE GLU PRO MSE HIS TRP SER VAL SER MSE ARG
SEQRES 24 B 341 ALA LYS SER VAL ASN LEU ALA SER VAL ALA SER ALA PHE
SEQRES 25 B 341 GLY GLY GLY GLY HIS PRO HIS ALA ALA GLY TYR SER ALA
SEQRES 26 B 341 THR GLY SER ALA ASP ASP VAL VAL GLN ALA LEU ALA ARG
SEQRES 27 B 341 ALA LEU GLY
MODRES 4LS9 MSE A 99 MET SELENOMETHIONINE
MODRES 4LS9 MSE A 157 MET SELENOMETHIONINE
MODRES 4LS9 MSE A 228 MET SELENOMETHIONINE
MODRES 4LS9 MSE A 291 MET SELENOMETHIONINE
MODRES 4LS9 MSE A 297 MET SELENOMETHIONINE
MODRES 4LS9 MSE B 99 MET SELENOMETHIONINE
MODRES 4LS9 MSE B 157 MET SELENOMETHIONINE
MODRES 4LS9 MSE B 228 MET SELENOMETHIONINE
MODRES 4LS9 MSE B 291 MET SELENOMETHIONINE
MODRES 4LS9 MSE B 297 MET SELENOMETHIONINE
HET MSE A 99 8
HET MSE A 157 8
HET MSE A 228 8
HET MSE A 291 8
HET MSE A 297 8
HET MSE B 99 8
HET MSE B 157 8
HET MSE B 228 8
HET MSE B 291 8
HET MSE B 297 8
HET MN A1001 1
HET MN B1001 1
HET GOL B1002 6
HETNAM MSE SELENOMETHIONINE
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 3 MN 2(MN 2+)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *268(H2 O)
HELIX 1 1 ASP A 26 ALA A 37 1 12
HELIX 2 2 ASP A 49 SER A 66 1 18
HELIX 3 3 PRO A 81 SER A 86 1 6
HELIX 4 4 GLY A 89 LEU A 93 5 5
HELIX 5 5 SER A 113 GLY A 125 5 13
HELIX 6 6 SER A 154 GLY A 167 1 14
HELIX 7 7 ASP A 171 THR A 186 1 16
HELIX 8 8 THR A 193 LEU A 206 1 14
HELIX 9 9 ASP A 209 ASP A 219 1 11
HELIX 10 10 ALA A 224 ALA A 234 1 11
HELIX 11 11 PRO A 254 ALA A 261 1 8
HELIX 12 12 ARG A 262 SER A 268 1 7
HELIX 13 13 SER A 268 ARG A 274 1 7
HELIX 14 14 LEU A 304 PHE A 311 1 8
HELIX 15 15 SER A 327 GLY A 340 1 14
HELIX 16 16 ASP B 26 ALA B 37 1 12
HELIX 17 17 ASP B 49 SER B 66 1 18
HELIX 18 18 PRO B 81 LEU B 87 5 7
HELIX 19 19 GLY B 89 LEU B 93 5 5
HELIX 20 20 SER B 113 GLY B 125 5 13
HELIX 21 21 SER B 154 TRP B 166 1 13
HELIX 22 22 ASP B 171 THR B 186 1 16
HELIX 23 23 THR B 193 LEU B 206 1 14
HELIX 24 24 ASP B 209 LEU B 218 1 10
HELIX 25 25 ALA B 224 ALA B 234 1 11
HELIX 26 26 ASP B 241 ARG B 246 1 6
HELIX 27 27 PRO B 254 ALA B 261 1 8
HELIX 28 28 ARG B 262 SER B 268 1 7
HELIX 29 29 SER B 268 ARG B 274 1 7
HELIX 30 30 LEU B 304 PHE B 311 1 8
HELIX 31 31 SER B 327 GLY B 340 1 14
SHEET 1 A 5 HIS A 69 SER A 73 0
SHEET 2 A 5 SER A 39 CYS A 44 1 N VAL A 42 O GLU A 71
SHEET 3 A 5 LEU A 105 VAL A 109 1 O VAL A 107 N ILE A 43
SHEET 4 A 5 GLU A 129 ASP A 134 1 O LEU A 131 N VAL A 106
SHEET 5 A 5 ALA A 145 ILE A 148 1 O TYR A 147 N VAL A 132
SHEET 1 B 6 ARG A 237 LEU A 239 0
SHEET 2 B 6 PHE A 248 VAL A 253 -1 O PHE A 248 N LEU A 239
SHEET 3 B 6 VAL A 281 GLU A 289 1 O PHE A 285 N VAL A 253
SHEET 4 B 6 HIS A 292 ALA A 299 -1 O SER A 294 N LYS A 286
SHEET 5 B 6 ALA A 319 THR A 325 -1 O ALA A 324 N TRP A 293
SHEET 6 B 6 GLY A 314 GLY A 315 -1 N GLY A 314 O GLY A 321
SHEET 1 C 5 HIS B 69 SER B 73 0
SHEET 2 C 5 SER B 39 ILE B 43 1 N VAL B 40 O HIS B 69
SHEET 3 C 5 LEU B 105 VAL B 109 1 O VAL B 107 N SER B 41
SHEET 4 C 5 GLU B 129 ASP B 134 1 O LEU B 131 N THR B 108
SHEET 5 C 5 ALA B 145 ILE B 148 1 O TYR B 147 N VAL B 132
SHEET 1 D 6 ARG B 237 LEU B 239 0
SHEET 2 D 6 PHE B 248 VAL B 253 -1 O PHE B 248 N LEU B 239
SHEET 3 D 6 VAL B 281 GLU B 289 1 O PHE B 285 N VAL B 253
SHEET 4 D 6 HIS B 292 ALA B 299 -1 O SER B 294 N LYS B 286
SHEET 5 D 6 ALA B 319 THR B 325 -1 O ALA B 324 N TRP B 293
SHEET 6 D 6 GLY B 314 HIS B 316 -1 N GLY B 314 O GLY B 321
LINK C ALA A 98 N MSE A 99 1555 1555 1.35
LINK C MSE A 99 N ARG A 100 1555 1555 1.36
LINK C THR A 156 N MSE A 157 1555 1555 1.38
LINK C MSE A 157 N LEU A 158 1555 1555 1.35
LINK C PRO A 227 N MSE A 228 1555 1555 1.36
LINK C MSE A 228 N LEU A 229 1555 1555 1.37
LINK C PRO A 290 N MSE A 291 1555 1555 1.36
LINK C MSE A 291 N HIS A 292 1555 1555 1.34
LINK C SER A 296 N MSE A 297 1555 1555 1.33
LINK C MSE A 297 N ARG A 298 1555 1555 1.33
LINK C ALA B 98 N MSE B 99 1555 1555 1.36
LINK C MSE B 99 N ARG B 100 1555 1555 1.34
LINK C THR B 156 N MSE B 157 1555 1555 1.36
LINK C MSE B 157 N LEU B 158 1555 1555 1.35
LINK C PRO B 227 N MSE B 228 1555 1555 1.36
LINK C MSE B 228 N LEU B 229 1555 1555 1.35
LINK C PRO B 290 N MSE B 291 1555 1555 1.35
LINK C MSE B 291 N HIS B 292 1555 1555 1.35
LINK C SER B 296 N MSE B 297 1555 1555 1.32
LINK C MSE B 297 N ARG B 298 1555 1555 1.33
LINK OD2 ASP B 51 MN MN B1001 1555 1555 2.07
LINK OD2 ASP A 51 MN MN A1001 1555 1555 2.17
LINK OD1 ASP A 110 MN MN A1001 1555 1555 2.29
LINK OD2 ASP B 185 MN MN B1001 1555 1555 2.32
LINK OD2 ASP A 185 MN MN A1001 1555 1555 2.37
LINK NE2 HIS A 135 MN MN A1001 1555 1555 2.41
LINK NE2 HIS B 135 MN MN B1001 1555 1555 2.42
LINK OD2 ASP B 110 MN MN B1001 1555 1555 2.61
LINK OD2 ASP A 110 MN MN A1001 1555 1555 2.62
LINK OD1 ASP B 110 MN MN B1001 1555 1555 2.68
LINK MN MN A1001 O HOH A1228 1555 1555 2.39
LINK MN MN B1001 O HOH B1191 1555 1555 2.60
LINK MN MN A1001 O HOH A1229 1555 1555 2.70
LINK MN MN B1001 O HOH B1109 1555 1555 2.77
CISPEP 1 THR A 76 PRO A 77 0 -2.41
CISPEP 2 THR B 76 PRO B 77 0 -3.03
SITE 1 AC1 6 ASP A 51 ASP A 110 HIS A 135 ASP A 185
SITE 2 AC1 6 HOH A1228 HOH A1229
SITE 1 AC2 6 ASP B 51 ASP B 110 HIS B 135 ASP B 185
SITE 2 AC2 6 HOH B1109 HOH B1191
SITE 1 AC3 1 PRO B 150
CRYST1 65.870 86.090 66.030 90.00 118.37 90.00 P 1 21 1 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 0.015181 0.000000 0.008198 0.00000
SCALE2 0.000000 0.011616 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017212 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
