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HEADER HYDROLASE 17-AUG-15 5D8M
TITLE CRYSTAL STRUCTURE OF THE METAGENOMIC CARBOXYL ESTERASE MGS0156
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METAGENOMIC CARBOXYL ESTERASE MGS0156;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 75-421;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED ORGANISM;
SOURCE 3 ORGANISM_TAXID: 155900;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.CUI,B.NOCEK,A.TCHIGVINTSEV,A.POPOVIC,A.SAVCHENKO,A.JOACHIMIAK,
AUTHOR 2 A.YAKUNIN
REVDAT 1 05-OCT-16 5D8M 0
JRNL AUTH B.NOCEK,H.CUI,A.TCHIGVINTSEV,A.POPOVIC,A.SAVCHENKO,
JRNL AUTH 2 A.JOACHIMIAK,A.YAKUNIN
JRNL TITL CRYSTAL STRUCTURE OF ESTERASE (MGS0156)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1888
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 26361
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2268
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 36.0617 - 4.9088 0.85 2784 143 0.1551 0.1768
REMARK 3 2 4.9088 - 3.8978 0.90 2961 155 0.1314 0.1452
REMARK 3 3 3.8978 - 3.4055 0.92 2992 147 0.1323 0.1738
REMARK 3 4 3.4055 - 3.0943 0.93 3047 161 0.1458 0.2155
REMARK 3 5 3.0943 - 2.8726 0.94 3072 165 0.1601 0.1956
REMARK 3 6 2.8726 - 2.7033 0.94 3031 182 0.1620 0.2043
REMARK 3 7 2.7033 - 2.5680 0.94 3093 159 0.1612 0.1885
REMARK 3 8 2.5680 - 2.4562 0.93 3040 138 0.1485 0.1961
REMARK 3 9 2.4562 - 2.3617 0.91 2956 183 0.1507 0.1807
REMARK 3 10 2.3617 - 2.2802 0.88 2812 157 0.1484 0.2226
REMARK 3 11 2.2802 - 2.2089 0.83 2724 121 0.1602 0.2303
REMARK 3 12 2.2089 - 2.1458 0.78 2526 129 0.1657 0.2108
REMARK 3 13 2.1458 - 2.0893 0.70 2298 141 0.1715 0.2127
REMARK 3 14 2.0893 - 2.0383 0.63 2058 113 0.1744 0.2020
REMARK 3 15 2.0383 - 1.9920 0.55 1775 110 0.1764 0.2157
REMARK 3 16 1.9920 - 1.9496 0.45 1485 66 0.1861 0.2178
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.570
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.010 2538
REMARK 3 ANGLE : 1.160 3473
REMARK 3 CHIRALITY : 0.054 406
REMARK 3 PLANARITY : 0.006 456
REMARK 3 DIHEDRAL : 10.924 924
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 121)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1586 20.7920 60.5719
REMARK 3 T TENSOR
REMARK 3 T11: 0.1063 T22: 0.1739
REMARK 3 T33: 0.1074 T12: 0.0256
REMARK 3 T13: -0.0066 T23: 0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 2.3519 L22: 0.5148
REMARK 3 L33: 2.3422 L12: -0.0477
REMARK 3 L13: -1.4619 L23: 0.3155
REMARK 3 S TENSOR
REMARK 3 S11: -0.0186 S12: 0.0467 S13: -0.0123
REMARK 3 S21: -0.0078 S22: 0.0139 S23: -0.0533
REMARK 3 S31: 0.2343 S32: -0.0598 S33: -0.0021
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 122 THROUGH 205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3645 23.2807 44.0745
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.1163
REMARK 3 T33: 0.1147 T12: 0.0192
REMARK 3 T13: 0.0290 T23: 0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.2705 L22: 0.8492
REMARK 3 L33: 1.5463 L12: -0.0842
REMARK 3 L13: -0.4463 L23: 0.2805
REMARK 3 S TENSOR
REMARK 3 S11: -0.0589 S12: -0.0318 S13: 0.0010
REMARK 3 S21: -0.1185 S22: 0.0156 S23: -0.1032
REMARK 3 S31: 0.1229 S32: 0.3051 S33: 0.0329
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 206 THROUGH 272 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4599 19.0991 45.9462
REMARK 3 T TENSOR
REMARK 3 T11: 0.0958 T22: 0.0842
REMARK 3 T33: 0.1158 T12: -0.0302
REMARK 3 T13: -0.0075 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 2.4333 L22: 1.4056
REMARK 3 L33: 2.4706 L12: 0.0432
REMARK 3 L13: 0.0587 L23: -0.5247
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: 0.0838 S13: -0.1341
REMARK 3 S21: -0.1036 S22: -0.0032 S23: 0.1579
REMARK 3 S31: 0.2232 S32: -0.2260 S33: 0.0318
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 310 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4887 31.9156 50.4709
REMARK 3 T TENSOR
REMARK 3 T11: 0.1776 T22: 0.2702
REMARK 3 T33: 0.2440 T12: 0.0183
REMARK 3 T13: 0.0063 T23: -0.0277
REMARK 3 L TENSOR
REMARK 3 L11: 1.2988 L22: 3.8941
REMARK 3 L33: 7.7982 L12: -0.1173
REMARK 3 L13: 0.7514 L23: -4.3170
REMARK 3 S TENSOR
REMARK 3 S11: -0.1417 S12: -0.1399 S13: 0.2759
REMARK 3 S21: 0.2891 S22: 0.3948 S23: 0.5014
REMARK 3 S31: -0.6808 S32: -0.8104 S33: -0.2693
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 311 THROUGH 372 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9315 27.6314 57.5418
REMARK 3 T TENSOR
REMARK 3 T11: 0.0611 T22: 0.1257
REMARK 3 T33: 0.0648 T12: 0.0090
REMARK 3 T13: 0.0142 T23: 0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.5763 L22: 1.8758
REMARK 3 L33: 2.3454 L12: -0.1188
REMARK 3 L13: -0.5402 L23: -0.2467
REMARK 3 S TENSOR
REMARK 3 S11: -0.0524 S12: -0.1732 S13: 0.0538
REMARK 3 S21: 0.1098 S22: 0.1251 S23: -0.0172
REMARK 3 S31: -0.0484 S32: 0.1123 S33: -0.0634
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 373 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2330 28.7999 45.4786
REMARK 3 T TENSOR
REMARK 3 T11: 0.0968 T22: 0.1275
REMARK 3 T33: 0.0771 T12: -0.0053
REMARK 3 T13: 0.0213 T23: -0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 2.1057 L22: 4.8236
REMARK 3 L33: 1.9576 L12: -0.9785
REMARK 3 L13: -0.2895 L23: 0.7880
REMARK 3 S TENSOR
REMARK 3 S11: 0.1339 S12: -0.0078 S13: 0.2014
REMARK 3 S21: -0.4735 S22: -0.1229 S23: -0.1622
REMARK 3 S31: -0.1508 S32: 0.2353 S33: 0.0189
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5D8M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212847.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27606
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 36.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE PH5.6, 0.2M
REMARK 280 AMMONIUM ACETATE, 30%PEG4K, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.88200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.95350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 67.80200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.88200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.95350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 67.80200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.88200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.95350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 67.80200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.88200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.95350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 67.80200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 135.60400
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 LEU A 75
REMARK 465 PHE A 76
REMARK 465 PRO A 77
REMARK 465 GLY A 78
REMARK 465 CYS A 79
REMARK 465 ALA A 80
REMARK 465 ARG A 81
REMARK 465 GLY A 414
REMARK 465 PRO A 415
REMARK 465 GLU A 416
REMARK 465 LYS A 417
REMARK 465 GLY A 418
REMARK 465 ARG A 419
REMARK 465 GLU A 420
REMARK 465 ASN A 421
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 82 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 312 CD NE CZ NH1 NH2
REMARK 470 LYS A 382 CG CD CE NZ
REMARK 470 LYS A 383 CG CD CE NZ
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 OG SER A 232 O HOH A 501 2.01
REMARK 500 O HOH A 729 O HOH A 749 2.03
REMARK 500 O HOH A 789 O HOH A 796 2.15
REMARK 500 O HOH A 668 O HOH A 704 2.17
REMARK 500 NH1 ARG A 208 O HOH A 502 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 734 O HOH A 734 3556 2.11
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 HIS A 122 32.61 -152.06
REMARK 500 SER A 232 -120.10 48.16
REMARK 500 SER A 232 -125.71 57.14
REMARK 500 ALA A 377 -23.45 -151.73
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 A 818 DISTANCE = 5.84 ANGSTROMS
DBREF1 5D8M A 75 421 UNP A0A0G3FEJ8_9ZZZZ
DBREF2 5D8M A A0A0G3FEJ8 75 421
SEQRES 1 A 347 LEU PHE PRO GLY CYS ALA ARG ARG PRO VAL ALA PRO LEU
SEQRES 2 A 347 ALA HIS ALA MSE SER PRO SER VAL LEU VAL PRO ALA GLY
SEQRES 3 A 347 LEU ALA GLY ILE GLN ASP GLY ARG GLY ARG PHE ARG GLU
SEQRES 4 A 347 ILE MSE THR ALA ILE MSE ALA ASP HIS GLY ALA PHE LEU
SEQRES 5 A 347 PRO GLY ASP ARG SER SER ASP GLY ASP GLY ILE LEU TRP
SEQRES 6 A 347 ARG LEU ALA GLY GLU PRO GLY PRO THR GLY ARG PRO VAL
SEQRES 7 A 347 PRO LEU GLY VAL SER THR ALA GLY ILE ARG LEU VAL LEU
SEQRES 8 A 347 VAL PRO GLY LEU LEU ALA GLU CYS VAL SER GLU SER SER
SEQRES 9 A 347 LEU LEU PHE ASP ASP ALA ARG PRO ASP VAL GLU ARG TYR
SEQRES 10 A 347 GLY TYR ALA THR THR LEU VAL ARG THR GLY GLY ARG TRP
SEQRES 11 A 347 GLY SER ALA ARG ASN ALA ALA ILE ILE HIS GLU VAL VAL
SEQRES 12 A 347 ALA LYS LEU PRO GLU ASN ASP THR ILE VAL PHE VAL THR
SEQRES 13 A 347 HIS SER LYS GLY ALA VAL ASP VAL LEU GLU ALA LEU VAL
SEQRES 14 A 347 SER TYR PRO ASP LEU ALA ALA ARG THR ALA ALA VAL VAL
SEQRES 15 A 347 SER VAL ALA GLY ALA ILE ASP GLY SER PRO LEU ALA GLU
SEQRES 16 A 347 THR PHE SER ASP GLY LEU LEU ARG PHE ALA GLU SER MSE
SEQRES 17 A 347 PRO LEU SER SER CYS PRO PRO GLY GLU GLY THR GLU ALA
SEQRES 18 A 347 LEU ASP SER LEU LYS ARG ALA TYR ARG LEU ARG PHE LEU
SEQRES 19 A 347 ALA GLU HIS ARG LEU PRO ALA ARG VAL ARG TYR TYR SER
SEQRES 20 A 347 LEU ALA ALA PHE ALA SER ARG GLU GLU THR SER ALA ILE
SEQRES 21 A 347 LEU ARG PRO PHE TYR ASP ILE LEU ALA LYS THR ASP ALA
SEQRES 22 A 347 LEU ASN ASP GLY LEU VAL ILE ALA ALA ASP ALA ILE ILE
SEQRES 23 A 347 PRO GLY GLY THR LEU LEU GLY TYR PRO ASN ALA ASP HIS
SEQRES 24 A 347 LEU ALA VAL ALA MSE PRO PHE SER LYS LYS PRO SER LEU
SEQRES 25 A 347 LEU THR SER VAL ILE SER LYS ASN SER TYR PRO ARG PRO
SEQRES 26 A 347 ALA LEU LEU GLU ALA ILE ALA ARG TYR VAL GLU GLU ASP
SEQRES 27 A 347 LEU GLY PRO GLU LYS GLY ARG GLU ASN
MODRES 5D8M MSE A 91 MET MODIFIED RESIDUE
MODRES 5D8M MSE A 115 MET MODIFIED RESIDUE
MODRES 5D8M MSE A 119 MET MODIFIED RESIDUE
MODRES 5D8M MSE A 282 MET MODIFIED RESIDUE
MODRES 5D8M MSE A 378 MET MODIFIED RESIDUE
HET MSE A 91 8
HET MSE A 115 8
HET MSE A 119 8
HET MSE A 282 8
HET MSE A 378 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 HOH *318(H2 O)
HELIX 1 AA1 PRO A 83 MSE A 91 1 9
HELIX 2 AA2 PRO A 98 GLY A 103 5 6
HELIX 3 AA3 GLY A 107 GLY A 123 1 17
HELIX 4 AA4 ALA A 171 SER A 175 5 5
HELIX 5 AA5 PHE A 181 ASP A 183 5 3
HELIX 6 AA6 ALA A 184 TYR A 191 1 8
HELIX 7 AA7 GLY A 205 ALA A 218 1 14
HELIX 8 AA8 LYS A 233 TYR A 245 1 13
HELIX 9 AA9 TYR A 245 ARG A 251 1 7
HELIX 10 AB1 PRO A 266 PHE A 271 1 6
HELIX 11 AB2 SER A 272 MSE A 282 1 11
HELIX 12 AB3 THR A 293 SER A 298 1 6
HELIX 13 AB4 LYS A 300 HIS A 311 1 12
HELIX 14 AB5 SER A 327 THR A 331 5 5
HELIX 15 AB6 SER A 332 ILE A 334 5 3
HELIX 16 AB7 LEU A 335 LYS A 344 1 10
HELIX 17 AB8 ILE A 354 ALA A 358 5 5
HELIX 18 AB9 SER A 385 ILE A 391 1 7
HELIX 19 AC1 PRO A 397 LEU A 413 1 17
SHEET 1 AA1 7 GLN A 105 ASP A 106 0
SHEET 2 AA1 7 THR A 364 GLY A 367 1 O LEU A 365 N GLN A 105
SHEET 3 AA1 7 ARG A 318 LEU A 322 1 N SER A 321 O LEU A 366
SHEET 4 AA1 7 THR A 252 VAL A 258 1 N SER A 257 O TYR A 320
SHEET 5 AA1 7 THR A 225 HIS A 231 1 N THR A 230 O VAL A 256
SHEET 6 AA1 7 ILE A 161 VAL A 166 1 N ARG A 162 O THR A 225
SHEET 7 AA1 7 ALA A 194 LEU A 197 1 O ALA A 194 N LEU A 163
SSBOND 1 CYS A 173 CYS A 287 1555 1555 2.09
LINK C ALA A 90 N MSE A 91 1555 1555 1.33
LINK C MSE A 91 N SER A 92 1555 1555 1.33
LINK C ILE A 114 N MSE A 115 1555 1555 1.33
LINK C MSE A 115 N THR A 116 1555 1555 1.32
LINK C ILE A 118 N MSE A 119 1555 1555 1.33
LINK C MSE A 119 N ALA A 120 1555 1555 1.33
LINK C SER A 281 N MSE A 282 1555 1555 1.33
LINK C MSE A 282 N PRO A 283 1555 1555 1.34
LINK C ALA A 377 N MSE A 378 1555 1555 1.34
LINK C MSE A 378 N PRO A 379 1555 1555 1.35
CISPEP 1 LYS A 383 PRO A 384 0 -0.86
CRYST1 59.764 95.907 135.604 90.00 90.00 90.00 I 2 2 2 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 0.016732 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010427 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007374 0.00000
TER 2475 LEU A 413
MASTER 422 0 5 19 7 0 0 6 2779 1 52 27
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