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HEADER HYDROLASE 18-JUN-13 4L9A
TITLE CRYSTAL STRUCTURE OF SMU.1393C FROM CARIOGENIC PATHOGEN STREPTOCOCCUS
TITLE 2 MUTANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN SMU.1393C;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS;
SOURCE 3 ORGANISM_TAXID: 210007;
SOURCE 4 STRAIN: ATCC 700610 / UA159;
SOURCE 5 GENE: SMU_1393C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS ALPHA/BETA HYDROLASE, CARBOXYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WANG,L.LI,X.-D.SU
REVDAT 1 17-JUL-13 4L9A 0
SPRSDE 17-JUL-13 4L9A 3L80
JRNL AUTH Z.WANG,L.LI,X.-D.SU
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A NOVEL
JRNL TITL 2 HYDROLASE FROM CARIOGENIC PATHOGEN STREPTOCOCCUS MUTANS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 40226
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2025
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 41.4074 - 4.8116 0.99 2776 142 0.1587 0.1725
REMARK 3 2 4.8116 - 3.8200 1.00 2761 147 0.1293 0.1607
REMARK 3 3 3.8200 - 3.3374 1.00 2719 163 0.1530 0.1932
REMARK 3 4 3.3374 - 3.0323 1.00 2754 141 0.1700 0.1899
REMARK 3 5 3.0323 - 2.8150 1.00 2766 161 0.1829 0.2256
REMARK 3 6 2.8150 - 2.6491 1.00 2700 144 0.1846 0.2510
REMARK 3 7 2.6491 - 2.5165 1.00 2741 156 0.1863 0.2509
REMARK 3 8 2.5165 - 2.4069 1.00 2759 132 0.1789 0.2189
REMARK 3 9 2.4069 - 2.3143 1.00 2719 150 0.1703 0.2255
REMARK 3 10 2.3143 - 2.2344 1.00 2735 142 0.1758 0.2359
REMARK 3 11 2.2344 - 2.1646 1.00 2719 123 0.1784 0.2487
REMARK 3 12 2.1646 - 2.1027 1.00 2730 174 0.1791 0.2721
REMARK 3 13 2.1027 - 2.0473 1.00 2740 135 0.2022 0.2747
REMARK 3 14 2.0473 - 1.9974 0.94 2582 115 0.2181 0.2731
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 42.47
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.470
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.84640
REMARK 3 B22 (A**2) : -12.69910
REMARK 3 B33 (A**2) : 4.85270
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 3.20800
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4413
REMARK 3 ANGLE : 0.996 5962
REMARK 3 CHIRALITY : 0.071 648
REMARK 3 PLANARITY : 0.004 766
REMARK 3 DIHEDRAL : 14.313 1608
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (chain A and resid 3:129)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0871 28.6473 1.2054
REMARK 3 T TENSOR
REMARK 3 T11: 0.2875 T22: 0.2131
REMARK 3 T33: 0.1520 T12: 0.0077
REMARK 3 T13: 0.0137 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.4674 L22: 4.2087
REMARK 3 L33: 1.6084 L12: -0.5542
REMARK 3 L13: -0.0774 L23: -0.9770
REMARK 3 S TENSOR
REMARK 3 S11: 0.1536 S12: 0.2040 S13: -0.0390
REMARK 3 S21: -0.7545 S22: -0.1238 S23: -0.1245
REMARK 3 S31: 0.1721 S32: 0.0331 S33: -0.0295
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (chain A and resid 130:141)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1254 48.8861 14.8923
REMARK 3 T TENSOR
REMARK 3 T11: 0.5681 T22: 0.6103
REMARK 3 T33: 0.6513 T12: -0.1190
REMARK 3 T13: 0.0477 T23: -0.3110
REMARK 3 L TENSOR
REMARK 3 L11: 6.0538 L22: 5.1297
REMARK 3 L33: 1.6664 L12: -4.2406
REMARK 3 L13: 0.8678 L23: 1.1207
REMARK 3 S TENSOR
REMARK 3 S11: -0.5319 S12: -0.6881 S13: 0.8571
REMARK 3 S21: 0.7244 S22: 0.5425 S23: 0.0778
REMARK 3 S31: -0.5871 S32: 0.6871 S33: -0.1012
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (chain A and resid 142:175)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.2059 38.4975 18.5528
REMARK 3 T TENSOR
REMARK 3 T11: 0.4472 T22: 0.3376
REMARK 3 T33: 0.4046 T12: 0.0614
REMARK 3 T13: 0.1660 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 1.8409 L22: 6.2199
REMARK 3 L33: 2.5185 L12: 2.2670
REMARK 3 L13: 1.0918 L23: 0.4132
REMARK 3 S TENSOR
REMARK 3 S11: -0.0046 S12: -0.2329 S13: 0.0227
REMARK 3 S21: 1.3457 S22: 0.1428 S23: 0.8562
REMARK 3 S31: -0.2701 S32: -0.1533 S33: -0.0805
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (chain A and resid 176:275)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8138 39.3076 4.3925
REMARK 3 T TENSOR
REMARK 3 T11: 0.2151 T22: 0.2086
REMARK 3 T33: 0.1776 T12: -0.0246
REMARK 3 T13: 0.0280 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.4062 L22: 4.0588
REMARK 3 L33: 2.1865 L12: -0.5269
REMARK 3 L13: 0.0988 L23: -0.8984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0858 S12: 0.0833 S13: 0.1521
REMARK 3 S21: -0.3172 S22: -0.0216 S23: -0.0050
REMARK 3 S31: -0.0833 S32: 0.0035 S33: -0.0442
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (chain B and resid 2:124)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9931 4.0746 22.2499
REMARK 3 T TENSOR
REMARK 3 T11: 0.1865 T22: 0.2433
REMARK 3 T33: 0.2342 T12: -0.0154
REMARK 3 T13: -0.0154 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 1.3650 L22: 4.4578
REMARK 3 L33: 2.7096 L12: -0.4706
REMARK 3 L13: -0.1761 L23: -1.4512
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: -0.1140 S13: -0.0350
REMARK 3 S21: 0.3330 S22: -0.0640 S23: -0.0053
REMARK 3 S31: -0.1142 S32: -0.0523 S33: 0.0874
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (chain B and resid 125:160)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2438 3.4345 10.9651
REMARK 3 T TENSOR
REMARK 3 T11: 0.2844 T22: 0.3774
REMARK 3 T33: 0.5828 T12: -0.0157
REMARK 3 T13: -0.0019 T23: 0.0362
REMARK 3 L TENSOR
REMARK 3 L11: 1.9636 L22: 1.3240
REMARK 3 L33: 0.2593 L12: 1.5286
REMARK 3 L13: -0.6198 L23: -0.6018
REMARK 3 S TENSOR
REMARK 3 S11: -0.1514 S12: -0.1287 S13: -0.2289
REMARK 3 S21: -0.1893 S22: -0.0700 S23: -0.3506
REMARK 3 S31: 0.1151 S32: 0.0064 S33: 0.1744
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (chain B and resid 161:204)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6309 1.3439 5.4213
REMARK 3 T TENSOR
REMARK 3 T11: 0.3183 T22: 0.2455
REMARK 3 T33: 0.2289 T12: 0.0254
REMARK 3 T13: 0.0687 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 1.4529 L22: 5.0309
REMARK 3 L33: 2.3056 L12: 0.0623
REMARK 3 L13: -0.0778 L23: -0.4533
REMARK 3 S TENSOR
REMARK 3 S11: -0.0671 S12: 0.2956 S13: -0.0321
REMARK 3 S21: -0.8020 S22: 0.0720 S23: -0.3968
REMARK 3 S31: 0.2362 S32: 0.0745 S33: 0.0090
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (chain B and resid 205:272)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7228 -5.8671 26.9077
REMARK 3 T TENSOR
REMARK 3 T11: 0.2778 T22: 0.3359
REMARK 3 T33: 0.5183 T12: -0.0254
REMARK 3 T13: -0.1179 T23: 0.1676
REMARK 3 L TENSOR
REMARK 3 L11: 1.5091 L22: 1.9676
REMARK 3 L33: 2.1524 L12: 0.6558
REMARK 3 L13: 0.6801 L23: 0.5280
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: -0.3199 S13: -0.3279
REMARK 3 S21: 0.2956 S22: -0.2738 S23: -1.0779
REMARK 3 S31: 0.1367 S32: 0.4368 S33: 0.1259
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SF FILE CONTAINS FRIEDEL PAIRS UNDER I_
REMARK 3 PLUS/MINUS AND F_PLUS/MINUS COLUMN.
REMARK 4
REMARK 4 4L9A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUL-13.
REMARK 100 THE RCSB ID CODE IS RCSB080342.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97898, 0.97926, 0.96403
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79331
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.AUTOSOL)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M BIS-TRIS
REMARK 280 PH6.5, 25% W/V PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
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 67.97900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 GLY A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 MSE A -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MSE A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MSE A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MSE A 1
REMARK 465 ALA A 2
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 MSE B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MSE B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLN B -6
REMARK 465 GLN B -5
REMARK 465 MSE B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MSE B 1
REMARK 465 LEU B 146
REMARK 465 ARG B 147
REMARK 465 ARG B 148
REMARK 465 GLN B 149
REMARK 465 LYS B 150
REMARK 465 LEU B 151
REMARK 465 LYS B 152
REMARK 465 GLU B 273
REMARK 465 LYS B 274
REMARK 465 LEU B 275
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 SER A 101 -123.70 55.11
REMARK 500 GLU A 125 54.51 38.06
REMARK 500 SER A 137 34.53 77.30
REMARK 500 ASP A 139 -17.92 95.88
REMARK 500 SER B 101 -128.20 54.60
REMARK 500 GLU B 125 60.85 36.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301
DBREF 4L9A A 1 275 UNP Q8DTF4 Q8DTF4_STRMU 1 275
DBREF 4L9A B 1 275 UNP Q8DTF4 Q8DTF4_STRMU 1 275
SEQADV 4L9A GLY A -16 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A SER A -15 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A HIS A -14 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A MSE A -13 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A ALA A -12 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A SER A -11 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A MSE A -10 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A THR A -9 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY A -8 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY A -7 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLN A -6 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLN A -5 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A MSE A -4 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY A -3 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A ARG A -2 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY A -1 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A SER A 0 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY B -16 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A SER B -15 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A HIS B -14 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A MSE B -13 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A ALA B -12 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A SER B -11 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A MSE B -10 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A THR B -9 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY B -8 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY B -7 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLN B -6 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLN B -5 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A MSE B -4 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY B -3 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A ARG B -2 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A GLY B -1 UNP Q8DTF4 EXPRESSION TAG
SEQADV 4L9A SER B 0 UNP Q8DTF4 EXPRESSION TAG
SEQRES 1 A 292 GLY SER HIS MSE ALA SER MSE THR GLY GLY GLN GLN MSE
SEQRES 2 A 292 GLY ARG GLY SER MSE ALA ALA LEU ASN LYS GLU MSE VAL
SEQRES 3 A 292 ASN THR LEU LEU GLY PRO ILE TYR THR CYS HIS ARG GLU
SEQRES 4 A 292 GLY ASN PRO CYS PHE VAL PHE LEU SER GLY ALA GLY PHE
SEQRES 5 A 292 PHE SER THR ALA ASP ASN PHE ALA ASN ILE ILE ASP LYS
SEQRES 6 A 292 LEU PRO ASP SER ILE GLY ILE LEU THR ILE ASP ALA PRO
SEQRES 7 A 292 ASN SER GLY TYR SER PRO VAL SER ASN GLN ALA ASN VAL
SEQRES 8 A 292 GLY LEU ARG ASP TRP VAL ASN ALA ILE LEU MSE ILE PHE
SEQRES 9 A 292 GLU HIS PHE LYS PHE GLN SER TYR LEU LEU CYS VAL HIS
SEQRES 10 A 292 SER ILE GLY GLY PHE ALA ALA LEU GLN ILE MSE ASN GLN
SEQRES 11 A 292 SER SER LYS ALA CYS LEU GLY PHE ILE GLY LEU GLU PRO
SEQRES 12 A 292 THR THR VAL MSE ILE TYR ARG ALA GLY PHE SER SER ASP
SEQRES 13 A 292 LEU TYR PRO GLN LEU ALA LEU ARG ARG GLN LYS LEU LYS
SEQRES 14 A 292 THR ALA ALA ASP ARG LEU ASN TYR LEU LYS ASP LEU SER
SEQRES 15 A 292 ARG SER HIS PHE SER SER GLN GLN PHE LYS GLN LEU TRP
SEQRES 16 A 292 ARG GLY TYR ASP TYR CYS GLN ARG GLN LEU ASN ASP VAL
SEQRES 17 A 292 GLN SER LEU PRO ASP PHE LYS ILE ARG LEU ALA LEU GLY
SEQRES 18 A 292 GLU GLU ASP PHE LYS THR GLY ILE SER GLU LYS ILE PRO
SEQRES 19 A 292 SER ILE VAL PHE SER GLU SER PHE ARG GLU LYS GLU TYR
SEQRES 20 A 292 LEU GLU SER GLU TYR LEU ASN LYS HIS THR GLN THR LYS
SEQRES 21 A 292 LEU ILE LEU CYS GLY GLN HIS HIS TYR LEU HIS TRP SER
SEQRES 22 A 292 GLU THR ASN SER ILE LEU GLU LYS VAL GLU GLN LEU LEU
SEQRES 23 A 292 SER ASN HIS GLU LYS LEU
SEQRES 1 B 292 GLY SER HIS MSE ALA SER MSE THR GLY GLY GLN GLN MSE
SEQRES 2 B 292 GLY ARG GLY SER MSE ALA ALA LEU ASN LYS GLU MSE VAL
SEQRES 3 B 292 ASN THR LEU LEU GLY PRO ILE TYR THR CYS HIS ARG GLU
SEQRES 4 B 292 GLY ASN PRO CYS PHE VAL PHE LEU SER GLY ALA GLY PHE
SEQRES 5 B 292 PHE SER THR ALA ASP ASN PHE ALA ASN ILE ILE ASP LYS
SEQRES 6 B 292 LEU PRO ASP SER ILE GLY ILE LEU THR ILE ASP ALA PRO
SEQRES 7 B 292 ASN SER GLY TYR SER PRO VAL SER ASN GLN ALA ASN VAL
SEQRES 8 B 292 GLY LEU ARG ASP TRP VAL ASN ALA ILE LEU MSE ILE PHE
SEQRES 9 B 292 GLU HIS PHE LYS PHE GLN SER TYR LEU LEU CYS VAL HIS
SEQRES 10 B 292 SER ILE GLY GLY PHE ALA ALA LEU GLN ILE MSE ASN GLN
SEQRES 11 B 292 SER SER LYS ALA CYS LEU GLY PHE ILE GLY LEU GLU PRO
SEQRES 12 B 292 THR THR VAL MSE ILE TYR ARG ALA GLY PHE SER SER ASP
SEQRES 13 B 292 LEU TYR PRO GLN LEU ALA LEU ARG ARG GLN LYS LEU LYS
SEQRES 14 B 292 THR ALA ALA ASP ARG LEU ASN TYR LEU LYS ASP LEU SER
SEQRES 15 B 292 ARG SER HIS PHE SER SER GLN GLN PHE LYS GLN LEU TRP
SEQRES 16 B 292 ARG GLY TYR ASP TYR CYS GLN ARG GLN LEU ASN ASP VAL
SEQRES 17 B 292 GLN SER LEU PRO ASP PHE LYS ILE ARG LEU ALA LEU GLY
SEQRES 18 B 292 GLU GLU ASP PHE LYS THR GLY ILE SER GLU LYS ILE PRO
SEQRES 19 B 292 SER ILE VAL PHE SER GLU SER PHE ARG GLU LYS GLU TYR
SEQRES 20 B 292 LEU GLU SER GLU TYR LEU ASN LYS HIS THR GLN THR LYS
SEQRES 21 B 292 LEU ILE LEU CYS GLY GLN HIS HIS TYR LEU HIS TRP SER
SEQRES 22 B 292 GLU THR ASN SER ILE LEU GLU LYS VAL GLU GLN LEU LEU
SEQRES 23 B 292 SER ASN HIS GLU LYS LEU
MODRES 4L9A MSE A 8 MET SELENOMETHIONINE
MODRES 4L9A MSE A 85 MET SELENOMETHIONINE
MODRES 4L9A MSE A 111 MET SELENOMETHIONINE
MODRES 4L9A MSE A 130 MET SELENOMETHIONINE
MODRES 4L9A MSE B 8 MET SELENOMETHIONINE
MODRES 4L9A MSE B 85 MET SELENOMETHIONINE
MODRES 4L9A MSE B 111 MET SELENOMETHIONINE
MODRES 4L9A MSE B 130 MET SELENOMETHIONINE
HET MSE A 8 8
HET MSE A 85 8
HET MSE A 111 8
HET MSE A 130 8
HET MSE B 8 8
HET MSE B 85 8
HET MSE B 111 8
HET MSE B 130 8
HET GOL A 301 6
HET GOL B 301 6
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *286(H2 O)
HELIX 1 1 SER A 37 PHE A 42 1 6
HELIX 2 2 PHE A 42 ASP A 47 1 6
HELIX 3 3 GLY A 75 PHE A 90 1 16
HELIX 4 4 ILE A 102 SER A 114 1 13
HELIX 5 5 THR A 128 GLY A 135 1 8
HELIX 6 6 TYR A 141 LEU A 151 1 11
HELIX 7 7 THR A 153 PHE A 169 1 17
HELIX 8 8 SER A 170 ASP A 190 1 21
HELIX 9 9 GLY A 204 LYS A 209 5 6
HELIX 10 10 GLU A 223 PHE A 225 5 3
HELIX 11 11 ARG A 226 GLU A 232 1 7
HELIX 12 12 TYR A 252 GLU A 257 1 6
HELIX 13 13 GLU A 257 ASN A 271 1 15
HELIX 14 14 SER B 37 PHE B 42 1 6
HELIX 15 15 PHE B 42 ASP B 47 1 6
HELIX 16 16 GLY B 75 PHE B 90 1 16
HELIX 17 17 GLY B 103 SER B 114 1 12
HELIX 18 18 THR B 128 TYR B 141 1 14
HELIX 19 19 PRO B 142 ALA B 145 5 4
HELIX 20 20 ALA B 154 PHE B 169 1 16
HELIX 21 21 SER B 170 ASN B 189 1 20
HELIX 22 22 GLY B 204 PHE B 208 5 5
HELIX 23 23 GLU B 223 PHE B 225 5 3
HELIX 24 24 ARG B 226 GLU B 232 1 7
HELIX 25 25 TYR B 252 GLU B 257 1 6
HELIX 26 26 GLU B 257 ASN B 271 1 15
SHEET 1 A 8 ASN A 5 VAL A 9 0
SHEET 2 A 8 ILE A 16 ARG A 21 -1 O ILE A 16 N VAL A 9
SHEET 3 A 8 GLY A 54 ILE A 58 -1 O THR A 57 N CYS A 19
SHEET 4 A 8 CYS A 26 LEU A 30 1 N PHE A 27 O GLY A 54
SHEET 5 A 8 SER A 94 HIS A 100 1 O CYS A 98 N VAL A 28
SHEET 6 A 8 ALA A 117 LEU A 124 1 O LEU A 119 N TYR A 95
SHEET 7 A 8 SER A 218 SER A 222 1 O ILE A 219 N PHE A 121
SHEET 8 A 8 LYS A 243 LEU A 246 1 O ILE A 245 N VAL A 220
SHEET 1 B 8 ASN B 5 VAL B 9 0
SHEET 2 B 8 ILE B 16 ARG B 21 -1 O ILE B 16 N VAL B 9
SHEET 3 B 8 GLY B 54 ILE B 58 -1 O THR B 57 N CYS B 19
SHEET 4 B 8 CYS B 26 LEU B 30 1 N PHE B 27 O GLY B 54
SHEET 5 B 8 SER B 94 HIS B 100 1 O CYS B 98 N VAL B 28
SHEET 6 B 8 ALA B 117 LEU B 124 1 O LEU B 119 N TYR B 95
SHEET 7 B 8 SER B 218 SER B 222 1 O ILE B 219 N PHE B 121
SHEET 8 B 8 LYS B 243 LEU B 246 1 O ILE B 245 N VAL B 220
LINK C GLU A 7 N MSE A 8 1555 1555 1.33
LINK C MSE A 8 N VAL A 9 1555 1555 1.33
LINK C LEU A 84 N MSE A 85 1555 1555 1.33
LINK C MSE A 85 N ILE A 86 1555 1555 1.33
LINK C ILE A 110 N MSE A 111 1555 1555 1.33
LINK C MSE A 111 N ASN A 112 1555 1555 1.33
LINK C VAL A 129 N MSE A 130 1555 1555 1.33
LINK C MSE A 130 N ILE A 131 1555 1555 1.33
LINK C GLU B 7 N MSE B 8 1555 1555 1.33
LINK C MSE B 8 N VAL B 9 1555 1555 1.33
LINK C LEU B 84 N MSE B 85 1555 1555 1.33
LINK C MSE B 85 N ILE B 86 1555 1555 1.33
LINK C ILE B 110 N MSE B 111 1555 1555 1.32
LINK C MSE B 111 N ASN B 112 1555 1555 1.33
LINK C VAL B 129 N MSE B 130 1555 1555 1.33
LINK C MSE B 130 N ILE B 131 1555 1555 1.33
CISPEP 1 ASN A 24 PRO A 25 0 0.76
CISPEP 2 ASN B 24 PRO B 25 0 -0.45
SITE 1 AC1 8 ASN A 70 ASN A 73 HOH A 432 HOH A 469
SITE 2 AC1 8 HOH A 478 LEU B 12 ASN B 73 HOH B 440
SITE 1 AC2 7 LEU A 12 ASN A 73 HOH A 470 ASN B 70
SITE 2 AC2 7 ASN B 73 HOH B 422 HOH B 438
CRYST1 43.504 135.958 51.568 90.00 92.51 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 0.022986 0.000000 0.001006 0.00000
SCALE2 0.000000 0.007355 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019410 0.00000 END |