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HEADER HYDROLASE 10-AUG-23 8TRU
TITLE CRYSTAL STRUCTURE OF A CE15 FROM FIBROBACTER SUCCINOGENES SUBSP.
TITLE 2 SUCCINOGENES S85
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCURONYL ESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 153-536;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: C-TERMINAL HIS-TAGGED CONSTRUCT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FIBROBACTER SUCCINOGENES SUBSP. SUCCINOGENES;
SOURCE 3 ORGANISM_TAXID: 59374;
SOURCE 4 STRAIN: ATCC 19169 / S85;
SOURCE 5 GENE: FSU_2898;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS CARBOHYDRATE, ESTERASE, GLUCURONYL ESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.GRUNINGER,D.R.JONES
REVDAT 1 28-AUG-24 8TRU 0
JRNL AUTH R.J.GRUNINGER,M.KEVORKOVA,K.E.LOW,D.R.JONES,L.WORRALL,
JRNL AUTH 2 T.A.MCALLISTER,D.W.ABBOTT
JRNL TITL STRUCTURAL, BIOCHEMICAL, AND PHYLOGENETIC ANALYSIS OF
JRNL TITL 2 BACTERIAL AND FUNGAL CARBOHYDRATE ESTERASE FAMILY 15
JRNL TITL 3 GLUCURONOYL ESTERASES IN THE RUMEN.
JRNL REF PROTEIN J. 2024
JRNL REFN ISSN 1572-3887
JRNL PMID 39153129
JRNL DOI 10.1007/S10930-024-10221-0
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 30274
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1512
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 19.9370 - 4.2135 1.00 2855 151 0.1588 0.1826
REMARK 3 2 4.2135 - 3.3495 1.00 2684 141 0.1653 0.2162
REMARK 3 3 3.3495 - 2.9276 1.00 2638 139 0.2077 0.2844
REMARK 3 4 2.9276 - 2.6606 1.00 2614 137 0.2284 0.2590
REMARK 3 5 2.6606 - 2.4703 1.00 2588 136 0.2337 0.2829
REMARK 3 6 2.4703 - 2.3249 1.00 2593 136 0.2269 0.2889
REMARK 3 7 2.3249 - 2.2086 1.00 2546 134 0.2359 0.3230
REMARK 3 8 2.2086 - 2.1126 1.00 2580 136 0.2490 0.3179
REMARK 3 9 2.1126 - 2.0313 1.00 2553 134 0.2761 0.3115
REMARK 3 10 2.0313 - 1.9613 1.00 2574 136 0.3069 0.3612
REMARK 3 11 1.9613 - 1.9000 1.00 2537 132 0.3441 0.3661
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.14
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 : 0.006 2919
REMARK 3 ANGLE : 0.766 3942
REMARK 3 CHIRALITY : 0.049 413
REMARK 3 PLANARITY : 0.005 520
REMARK 3 DIHEDRAL : 4.438 2378
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 155 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9885 24.6632 19.7542
REMARK 3 T TENSOR
REMARK 3 T11: 0.2754 T22: 0.2643
REMARK 3 T33: 0.4407 T12: -0.0113
REMARK 3 T13: 0.0256 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.8547 L22: 1.3366
REMARK 3 L33: 0.3484 L12: 0.1622
REMARK 3 L13: 0.2214 L23: 0.0534
REMARK 3 S TENSOR
REMARK 3 S11: -0.1117 S12: 0.0900 S13: 0.2724
REMARK 3 S21: -0.0593 S22: 0.0722 S23: 0.0169
REMARK 3 S31: -0.1633 S32: 0.0176 S33: 0.0454
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 192 THROUGH 238 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1727 18.1653 16.0936
REMARK 3 T TENSOR
REMARK 3 T11: 0.2513 T22: 0.3083
REMARK 3 T33: 0.4702 T12: -0.0686
REMARK 3 T13: 0.0920 T23: -0.0922
REMARK 3 L TENSOR
REMARK 3 L11: 1.3361 L22: 0.4293
REMARK 3 L33: 0.5007 L12: 0.4461
REMARK 3 L13: 0.3517 L23: -0.1149
REMARK 3 S TENSOR
REMARK 3 S11: -0.2317 S12: 0.3186 S13: -0.0053
REMARK 3 S21: -0.1443 S22: 0.1938 S23: -0.1863
REMARK 3 S31: 0.0277 S32: 0.0357 S33: 0.0121
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 239 THROUGH 274 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5435 3.6106 7.8839
REMARK 3 T TENSOR
REMARK 3 T11: 0.3830 T22: 0.5020
REMARK 3 T33: 0.6983 T12: -0.1458
REMARK 3 T13: 0.1995 T23: -0.2092
REMARK 3 L TENSOR
REMARK 3 L11: 0.1675 L22: 0.4476
REMARK 3 L33: 0.0580 L12: 0.2524
REMARK 3 L13: -0.0717 L23: -0.1579
REMARK 3 S TENSOR
REMARK 3 S11: -0.3196 S12: 0.4020 S13: -0.2868
REMARK 3 S21: -0.1137 S22: 0.1586 S23: -0.2199
REMARK 3 S31: 0.1617 S32: -0.0483 S33: 0.0482
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 275 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.6809 6.5445 18.6242
REMARK 3 T TENSOR
REMARK 3 T11: 0.2434 T22: 0.3044
REMARK 3 T33: 0.4295 T12: -0.0260
REMARK 3 T13: 0.0706 T23: -0.0695
REMARK 3 L TENSOR
REMARK 3 L11: 0.9762 L22: 1.0260
REMARK 3 L33: 0.3027 L12: 0.4091
REMARK 3 L13: 0.0760 L23: 0.0445
REMARK 3 S TENSOR
REMARK 3 S11: -0.1229 S12: 0.1435 S13: -0.1967
REMARK 3 S21: -0.1025 S22: 0.1283 S23: -0.1028
REMARK 3 S31: 0.0027 S32: 0.0586 S33: 0.0058
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 514 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.4503 0.8293 2.1076
REMARK 3 T TENSOR
REMARK 3 T11: 0.4174 T22: 0.4626
REMARK 3 T33: 0.4063 T12: -0.1233
REMARK 3 T13: 0.0984 T23: -0.1688
REMARK 3 L TENSOR
REMARK 3 L11: 0.8331 L22: 0.1665
REMARK 3 L33: 0.0986 L12: -0.3393
REMARK 3 L13: -0.1957 L23: 0.1116
REMARK 3 S TENSOR
REMARK 3 S11: -0.1904 S12: 0.2749 S13: -0.3712
REMARK 3 S21: -0.2806 S22: 0.1887 S23: 0.0701
REMARK 3 S31: 0.0839 S32: -0.1008 S33: -0.0046
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 515 THROUGH 538 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.8786 11.0316 17.1893
REMARK 3 T TENSOR
REMARK 3 T11: 0.2288 T22: 0.3329
REMARK 3 T33: 0.4352 T12: -0.0206
REMARK 3 T13: 0.0433 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 1.0548 L22: 2.4147
REMARK 3 L33: 0.4563 L12: -0.3149
REMARK 3 L13: 0.2880 L23: 0.2350
REMARK 3 S TENSOR
REMARK 3 S11: -0.2247 S12: 0.2474 S13: 0.1280
REMARK 3 S21: 0.1423 S22: 0.1710 S23: 0.4339
REMARK 3 S31: -0.0006 S32: -0.1328 S33: 0.0816
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 8TRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1000276536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-FEB-19
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0334
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30281
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 19.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.50
REMARK 200 R MERGE (I) : 0.17200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
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) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.90
REMARK 200 R MERGE FOR SHELL (I) : 1.13400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000, 100 MM SODIUM ACETATE, PH
REMARK 280 5.0, 10 MM ZINC CHLORIDE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 111.08000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 28.64000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 28.64000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 55.54000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 28.64000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 28.64000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 166.62000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 28.64000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 28.64000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 55.54000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 28.64000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 28.64000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 166.62000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 111.08000
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 904 LIES ON A SPECIAL POSITION.
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 152
REMARK 465 ASN A 153
REMARK 465 GLU A 154
REMARK 465 THR A 252
REMARK 465 LYS A 253
REMARK 465 GLY A 266
REMARK 465 MET A 267
REMARK 465 MET A 268
REMARK 465 GLY A 269
REMARK 465 ALA A 539
REMARK 465 PHE A 540
REMARK 465 LEU A 541
REMARK 465 TYR A 542
REMARK 465 LYS A 543
REMARK 465 PRO A 544
REMARK 465 ALA A 545
REMARK 465 PHE A 546
REMARK 465 LEU A 547
REMARK 465 TYR A 548
REMARK 465 LYS A 549
REMARK 465 VAL A 550
REMARK 465 VAL A 551
REMARK 465 ILE A 552
REMARK 465 MET A 553
REMARK 465 HIS A 554
REMARK 465 HIS A 555
REMARK 465 HIS A 556
REMARK 465 HIS A 557
REMARK 465 HIS A 558
REMARK 465 HIS A 559
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 LYS A 187 CG CD CE NZ
REMARK 470 LYS A 246 CG CD CE NZ
REMARK 470 ASP A 254 CG OD1 OD2
REMARK 470 LYS A 255 CG CD CE NZ
REMARK 470 LYS A 338 CG CD CE NZ
REMARK 470 GLU A 470 CG CD OE1 OE2
REMARK 470 LYS A 523 CD CE NZ
REMARK 470 SER A 534 OG
REMARK 470 LYS A 536 CG CD CE NZ
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 MET A 210 -54.19 -124.12
REMARK 500 ASP A 236 147.07 -172.79
REMARK 500 ASN A 249 173.17 67.98
REMARK 500 ALA A 250 -149.73 -163.29
REMARK 500 ALA A 294 90.84 -160.40
REMARK 500 ASN A 307 39.42 -153.37
REMARK 500 SER A 346 -124.48 62.74
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 945 DISTANCE = 6.44 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 ZN A 602 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 159 ND1
REMARK 620 2 GLU A 360 OE1 97.0
REMARK 620 3 GLU A 360 OE2 103.0 56.4
REMARK 620 4 HOH A 718 O 111.3 132.0 79.4
REMARK 620 5 HOH A 864 O 118.4 81.7 124.1 114.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 488 O
REMARK 620 2 ASP A 491 OD1 86.5
REMARK 620 3 ASP A 491 OD2 143.1 58.6
REMARK 620 4 GLU A 492 OE2 112.6 109.1 91.6
REMARK 620 5 HOH A 778 O 71.6 158.1 142.3 81.4
REMARK 620 N 1 2 3 4
DBREF 8TRU A 153 536 UNP C9RKY6 C9RKY6_FIBSS 153 536
SEQADV 8TRU MET A 152 UNP C9RKY6 INITIATING METHIONINE
SEQADV 8TRU ASP A 537 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU PRO A 538 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU ALA A 539 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU PHE A 540 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU LEU A 541 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU TYR A 542 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU LYS A 543 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU PRO A 544 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU ALA A 545 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU PHE A 546 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU LEU A 547 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU TYR A 548 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU LYS A 549 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU VAL A 550 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU VAL A 551 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU ILE A 552 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU MET A 553 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU HIS A 554 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU HIS A 555 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU HIS A 556 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU HIS A 557 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU HIS A 558 UNP C9RKY6 EXPRESSION TAG
SEQADV 8TRU HIS A 559 UNP C9RKY6 EXPRESSION TAG
SEQRES 1 A 408 MET ASN GLU PHE VAL GLU ASP HIS ARG SER GLU CYS GLN
SEQRES 2 A 408 ILE GLY ASN ILE PRO SER SER VAL ASN ASN ALA LYS LEU
SEQRES 3 A 408 PRO ASP PRO PHE MET GLY LEU ASP GLY LYS ARG ILE SER
SEQRES 4 A 408 SER LYS ALA ASP TRP LYS CYS ARG ARG GLU GLU ILE GLY
SEQRES 5 A 408 ALA MET TYR GLU LYS LEU MET PHE GLY THR LYS PRO ARG
SEQRES 6 A 408 ASN PRO GLU LYS VAL GLU GLY SER TYR SER GLY GLY LYS
SEQRES 7 A 408 LEU THR ILE LYS VAL THR ASP LYS GLY LYS SER GLY SER
SEQRES 8 A 408 PHE SER VAL LYS ILE SER ASN ALA GLY THR LYS ASP LYS
SEQRES 9 A 408 PRO LYS PRO ALA MET ILE GLY PHE GLY GLY GLY MET MET
SEQRES 10 A 408 GLY GLY CYS GLY SER LEU GLY ASN ALA THR ASN GLY LEU
SEQRES 11 A 408 ASP ILE ALA GLN ILE THR PHE ASN PRO ASP ASP VAL ALA
SEQRES 12 A 408 PRO GLU SER GLY GLY GLY MET PHE PHE GLN LEU TYR ASN
SEQRES 13 A 408 GLN GLY GLN GLY THR ILE ILE ALA TRP ALA TRP GLY VAL
SEQRES 14 A 408 SER ARG ILE ILE ASP ALA LEU GLU LYS THR PRO GLU ALA
SEQRES 15 A 408 GLY ILE ASP VAL LYS HIS LEU ALA MET THR GLY CYS SER
SEQRES 16 A 408 ARG TRP GLY LYS GLY THR LEU ALA VAL GLY ALA PHE ASP
SEQRES 17 A 408 GLU ARG ILE ALA LEU THR ILE PRO GLN GLU SER GLY SER
SEQRES 18 A 408 GLY GLY ALA SER LEU TRP ARG VAL GLY ALA GLN VAL ASN
SEQRES 19 A 408 LYS GLN LYS GLY LYS GLN PHE VAL GLN GLY LEU SER SER
SEQRES 20 A 408 ALA GLY THR GLU GLY LYS TRP MET ILE SER SER PHE LYS
SEQRES 21 A 408 ASN TYR ASP GLY LYS GLU ASN THR LEU PRO PHE ASP GLN
SEQRES 22 A 408 HIS MET LEU VAL ALA MET VAL ALA PRO ARG ALA LEU LEU
SEQRES 23 A 408 ILE LEU ASP ASN ALA GLY GLN GLU TRP LEU GLY GLU VAL
SEQRES 24 A 408 PRO SER ASN TYR CYS GLY GLN ALA SER LYS GLU VAL TYR
SEQRES 25 A 408 ASP ALA LEU GLY ALA THR GLU ASN TYR THR TYR SER GLN
SEQRES 26 A 408 GLU GLY GLY HIS GLY HIS CYS GLN LEU PRO ASN GLY GLN
SEQRES 27 A 408 PHE ASP GLU VAL LYS ASP PHE MET ASN LYS PHE LEU LEU
SEQRES 28 A 408 GLY LYS ASP ALA LYS THR GLY LYS ILE ASP TYR THR LYS
SEQRES 29 A 408 ASN THR GLN THR ILE ASN PHE LYS LYS SER GLU TRP ILE
SEQRES 30 A 408 ASP TRP GLU THR PRO SER LEU LYS ASP PRO ALA PHE LEU
SEQRES 31 A 408 TYR LYS PRO ALA PHE LEU TYR LYS VAL VAL ILE MET HIS
SEQRES 32 A 408 HIS HIS HIS HIS HIS
HET ZN A 601 1
HET ZN A 602 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 HOH *245(H2 O)
HELIX 1 AA1 HIS A 159 CYS A 163 5 5
HELIX 2 AA2 SER A 191 ALA A 193 5 3
HELIX 3 AA3 ASP A 194 MET A 210 1 17
HELIX 4 AA4 LEU A 274 ASN A 279 5 6
HELIX 5 AA5 ASN A 289 VAL A 293 5 5
HELIX 6 AA6 MET A 301 TYR A 306 1 6
HELIX 7 AA7 GLY A 311 LYS A 329 1 19
HELIX 8 AA8 THR A 330 ALA A 333 5 4
HELIX 9 AA9 SER A 346 ASP A 359 1 14
HELIX 10 AB1 LEU A 377 GLY A 389 1 13
HELIX 11 AB2 GLY A 395 GLY A 400 1 6
HELIX 12 AB3 THR A 401 TRP A 405 5 5
HELIX 13 AB4 SER A 409 LEU A 420 5 12
HELIX 14 AB5 GLN A 424 ALA A 432 1 9
HELIX 15 AB6 GLY A 448 LEU A 466 1 19
HELIX 16 AB7 ALA A 468 GLU A 470 5 3
HELIX 17 AB8 PRO A 486 GLY A 488 5 3
HELIX 18 AB9 GLN A 489 LEU A 501 1 13
HELIX 19 AC1 LYS A 523 ILE A 528 1 6
SHEET 1 AA110 LYS A 220 SER A 226 0
SHEET 2 AA110 LYS A 229 ASP A 236 -1 O LYS A 233 N GLU A 222
SHEET 3 AA110 LYS A 239 SER A 248 -1 O PHE A 243 N ILE A 232
SHEET 4 AA110 ALA A 284 PHE A 288 -1 O GLN A 285 N SER A 248
SHEET 5 AA110 LYS A 257 PHE A 263 1 N PRO A 258 O ALA A 284
SHEET 6 AA110 ILE A 335 CYS A 345 1 O ALA A 341 N ILE A 261
SHEET 7 AA110 LEU A 364 GLN A 368 1 O ILE A 366 N MET A 342
SHEET 8 AA110 ALA A 435 ASP A 440 1 O LEU A 437 N THR A 365
SHEET 9 AA110 TYR A 472 GLU A 477 1 O SER A 475 N ILE A 438
SHEET 10 AA110 LYS A 510 THR A 514 1 O ASP A 512 N GLN A 476
SSBOND 1 CYS A 163 CYS A 197 1555 1555 2.02
SSBOND 2 CYS A 345 CYS A 483 1555 1555 2.04
LINK ND1 HIS A 159 ZN ZN A 602 1555 1555 2.05
LINK OE1 GLU A 360 ZN ZN A 602 1555 1555 2.52
LINK OE2 GLU A 360 ZN ZN A 602 1555 1555 1.99
LINK O GLY A 488 ZN ZN A 601 1555 1555 2.03
LINK OD1 ASP A 491 ZN ZN A 601 1555 1555 2.06
LINK OD2 ASP A 491 ZN ZN A 601 1555 1555 2.39
LINK OE2 GLU A 492 ZN ZN A 601 1555 1555 2.14
LINK ZN ZN A 601 O HOH A 778 1555 1555 2.62
LINK ZN ZN A 602 O HOH A 718 1555 1555 1.88
LINK ZN ZN A 602 O HOH A 864 1555 1555 2.21
CISPEP 1 ALA A 432 PRO A 433 0 2.41
CRYST1 57.280 57.280 222.160 90.00 90.00 90.00 P 41 21 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 0.017458 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017458 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004501 0.00000
TER 2857 PRO A 538
MASTER 425 0 2 19 10 0 0 6 3098 1 18 32
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