| content |
HEADER HYDROLASE 01-OCT-14 4RGY
TITLE STRUCTURAL AND FUNCTIONAL ANALYSIS OF A LOW-TEMPERATURE-ACTIVE
TITLE 2 ALKALINE ESTERASE FROM SOUTH CHINA SEA MARINE SEDIMENT MICROBIAL
TITLE 3 METAGENOMIC LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM FLS12;
SOURCE 3 ORGANISM_TAXID: 651659;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU
REVDAT 1 16-SEP-15 4RGY 0
JRNL AUTH Y.LIU
JRNL TITL STRUCTURAL AND FUNCTIONAL ANALYSIS OF A
JRNL TITL 2 LOW-TEMPERATURE-ACTIVE ALKALINE ESTERASE FROM SOUTH CHINA
JRNL TITL 3 SEA MARINE SEDIMENT MICROBIAL METAGENOMIC LIBRARY.
JRNL REF J. IND. MICROBIOL. 2015
JRNL REF 2 BIOTECHNOL.
JRNL REFN ISSN 1476-5535
JRNL DOI 10.1007/S10295-015-1653-2
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT 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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.3
REMARK 3 NUMBER OF REFLECTIONS : 95656
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5070
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 35.0780 - 4.3403 0.97 3711 209 0.1834 0.1858
REMARK 3 2 4.3403 - 3.4460 1.00 3771 188 0.1513 0.1492
REMARK 3 3 3.4460 - 3.0107 0.99 3724 199 0.1719 0.1624
REMARK 3 4 3.0107 - 2.7355 1.00 3696 205 0.1837 0.1958
REMARK 3 5 2.7355 - 2.5395 1.00 3719 196 0.1796 0.1728
REMARK 3 6 2.5395 - 2.3898 1.00 3731 196 0.1793 0.1820
REMARK 3 7 2.3898 - 2.2702 1.00 3740 200 0.1789 0.1778
REMARK 3 8 2.2702 - 2.1714 1.00 3709 194 0.1726 0.2016
REMARK 3 9 2.1714 - 2.0878 1.00 3737 201 0.1738 0.1799
REMARK 3 10 2.0878 - 2.0158 1.00 3677 208 0.1698 0.1727
REMARK 3 11 2.0158 - 1.9527 1.00 3726 197 0.1741 0.1765
REMARK 3 12 1.9527 - 1.8969 1.00 3705 202 0.1785 0.2050
REMARK 3 13 1.8969 - 1.8470 1.00 3678 200 0.1825 0.1929
REMARK 3 14 1.8470 - 1.8019 1.00 3721 185 0.1830 0.2052
REMARK 3 15 1.8019 - 1.7610 1.00 3650 213 0.1825 0.1868
REMARK 3 16 1.7610 - 1.7235 0.98 3637 196 0.1847 0.2058
REMARK 3 17 1.7235 - 1.6890 0.96 3546 199 0.1911 0.1964
REMARK 3 18 1.6890 - 1.6571 0.91 3390 190 0.1834 0.1940
REMARK 3 19 1.6571 - 1.6275 0.86 3154 189 0.1853 0.2057
REMARK 3 20 1.6275 - 1.6000 0.82 3044 149 0.1814 0.1847
REMARK 3 21 1.6000 - 1.5741 0.79 2911 159 0.1810 0.2059
REMARK 3 22 1.5741 - 1.5499 0.75 2820 123 0.1815 0.1922
REMARK 3 23 1.5499 - 1.5271 0.73 2720 135 0.1782 0.2108
REMARK 3 24 1.5271 - 1.5056 0.69 2576 112 0.1863 0.2020
REMARK 3 25 1.5056 - 1.4853 0.67 2455 127 0.1884 0.1739
REMARK 3 26 1.4853 - 1.4660 0.64 2390 114 0.1772 0.1759
REMARK 3 27 1.4660 - 1.4477 0.60 2203 114 0.1793 0.1813
REMARK 3 28 1.4477 - 1.4302 0.57 2120 87 0.1797 0.2150
REMARK 3 29 1.4302 - 1.4136 0.54 2017 93 0.1784 0.2314
REMARK 3 30 1.4136 - 1.4000 0.41 1503 90 0.1872 0.2384
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) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.670
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 : 0.007 3863
REMARK 3 ANGLE : 1.191 5243
REMARK 3 CHIRALITY : 0.079 558
REMARK 3 PLANARITY : 0.005 679
REMARK 3 DIHEDRAL : 14.189 1360
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4RGY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-14.
REMARK 100 THE RCSB ID CODE IS RCSB087333.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0001
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101251
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 35.067
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
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) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.72
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1 M TRIS HYDROCHLORIDE, PH 8.5, 24% W/V PEG4000, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 66.72950
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.88350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 66.72950
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.88350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 159.89869
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 141.45357
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 319 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 330 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 303 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 312 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 335 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 352 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 581 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 THR A 27
REMARK 465 THR A 28
REMARK 465 GLY A 29
REMARK 465 GLN A 30
REMARK 465 ILE A 31
REMARK 465 GLY A 32
REMARK 465 MET A 33
REMARK 465 ALA A 34
REMARK 465 GLY A 35
REMARK 465 GLY A 36
REMARK 465 SER A 37
REMARK 465 GLU A 38
REMARK 465 ARG A 39
REMARK 465 ARG A 40
REMARK 465 PHE A 156
REMARK 465 ASP A 157
REMARK 465 PRO A 158
REMARK 465 ALA A 159
REMARK 465 GLU A 160
REMARK 465 HIS A 161
REMARK 465 ILE A 162
REMARK 465 ALA A 163
REMARK 465 MET A 164
REMARK 465 GLU A 165
REMARK 465 ASP A 166
REMARK 465 ASP A 167
REMARK 465 ARG A 263
REMARK 465 PRO A 264
REMARK 465 PRO A 265
REMARK 465 GLY A 266
REMARK 465 THR A 267
REMARK 465 ALA A 268
REMARK 465 PRO A 269
REMARK 465 ALA A 270
REMARK 465 THR B 27
REMARK 465 THR B 28
REMARK 465 GLY B 29
REMARK 465 GLN B 30
REMARK 465 ILE B 31
REMARK 465 GLY B 32
REMARK 465 MET B 33
REMARK 465 ALA B 34
REMARK 465 GLY B 35
REMARK 465 GLY B 36
REMARK 465 SER B 37
REMARK 465 GLU B 38
REMARK 465 ARG B 39
REMARK 465 ARG B 40
REMARK 465 ASP B 157
REMARK 465 PRO B 158
REMARK 465 ALA B 159
REMARK 465 GLU B 160
REMARK 465 HIS B 161
REMARK 465 ILE B 162
REMARK 465 ALA B 163
REMARK 465 MET B 164
REMARK 465 GLU B 165
REMARK 465 ASP B 166
REMARK 465 ASP B 167
REMARK 465 VAL B 168
REMARK 465 TRP B 169
REMARK 465 ARG B 263
REMARK 465 PRO B 264
REMARK 465 PRO B 265
REMARK 465 GLY B 266
REMARK 465 THR B 267
REMARK 465 ALA B 268
REMARK 465 PRO B 269
REMARK 465 ALA B 270
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 O HOH A 544 O HOH B 373 1.82
REMARK 500 O HOH B 397 O HOH B 557 1.83
REMARK 500 O HOH B 574 O HOH B 577 1.84
REMARK 500 O HOH B 400 O HOH B 561 1.84
REMARK 500 O HOH A 395 O HOH A 439 1.85
REMARK 500 O HOH B 541 O HOH B 614 1.86
REMARK 500 O HOH A 447 O HOH A 558 1.91
REMARK 500 O HOH A 459 O HOH A 569 1.91
REMARK 500 OE2 GLU A 117 O HOH A 571 1.92
REMARK 500 O HOH A 371 O HOH A 496 1.93
REMARK 500 O HOH A 479 O HOH A 489 1.93
REMARK 500 O HOH A 609 O HOH B 565 1.94
REMARK 500 O HOH A 371 O HOH A 537 1.95
REMARK 500 NH2 ARG A 229 O HOH A 372 1.95
REMARK 500 NE ARG A 229 O HOH A 524 1.96
REMARK 500 O HOH B 465 O HOH B 612 1.98
REMARK 500 O HOH B 381 O HOH B 507 1.99
REMARK 500 O HOH B 450 O HOH B 466 1.99
REMARK 500 O HOH A 371 O HOH A 532 2.00
REMARK 500 O HOH B 466 O HOH B 511 2.00
REMARK 500 NH2 ARG B 61 O HOH B 486 2.03
REMARK 500 N GLU B 41 O HOH B 477 2.03
REMARK 500 O HOH B 528 O HOH B 608 2.05
REMARK 500 O HOH A 371 O HOH A 553 2.05
REMARK 500 O HOH A 465 O HOH A 568 2.06
REMARK 500 O HOH B 302 O HOH B 317 2.07
REMARK 500 O HOH B 302 O HOH B 329 2.08
REMARK 500 O HOH B 302 O HOH B 328 2.08
REMARK 500 OG SER A 125 O HOH A 315 2.09
REMARK 500 O HOH B 556 O HOH B 603 2.09
REMARK 500 O HOH B 381 O HOH B 563 2.09
REMARK 500 O HOH A 302 O HOH A 343 2.09
REMARK 500 O HOH A 302 O HOH A 327 2.09
REMARK 500 N GLU A 41 O HOH A 428 2.10
REMARK 500 O HOH B 535 O HOH B 609 2.10
REMARK 500 O HOH B 582 O HOH B 590 2.10
REMARK 500 O HOH A 549 O HOH A 611 2.10
REMARK 500 O HOH B 381 O HOH B 449 2.10
REMARK 500 O HOH A 302 O HOH A 329 2.11
REMARK 500 O HOH B 381 O HOH B 543 2.12
REMARK 500 O HOH A 371 O HOH A 451 2.13
REMARK 500 O HOH B 381 O HOH B 505 2.14
REMARK 500 O HOH A 434 O HOH A 446 2.15
REMARK 500 O HOH B 381 O HOH B 484 2.15
REMARK 500 O HOH A 371 O HOH A 528 2.16
REMARK 500 O HOH B 302 O HOH B 339 2.16
REMARK 500 O HOH B 311 O HOH B 380 2.17
REMARK 500 O HOH A 302 O HOH A 345 2.17
REMARK 500 O HOH A 464 O HOH A 533 2.17
REMARK 500 O HOH A 483 O HOH A 562 2.17
REMARK 500
REMARK 500 THIS ENTRY HAS 53 CLOSE CONTACTS
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 583 O HOH B 564 4748 1.84
REMARK 500 O HOH B 537 O HOH B 566 2758 1.85
REMARK 500 O HOH B 311 O HOH B 387 2758 2.13
REMARK 500 O HOH A 317 O HOH B 311 4748 2.15
REMARK 500 O HOH B 311 O HOH B 364 2758 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 102 CB - CG - CD1 ANGL. DEV. = -10.9 DEGREES
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 SER A 52 -6.27 88.76
REMARK 500 ASP A 54 -165.93 -124.58
REMARK 500 HIS A 81 -144.61 54.97
REMARK 500 ARG A 82 52.54 -102.33
REMARK 500 GLU A 100 -64.90 -124.35
REMARK 500 SER A 125 -117.58 47.88
REMARK 500 SER B 52 -4.88 91.56
REMARK 500 ASP B 54 -166.94 -124.33
REMARK 500 HIS B 81 -142.64 54.81
REMARK 500 ARG B 82 57.22 -105.34
REMARK 500 GLU B 100 -61.55 -124.34
REMARK 500 SER B 125 -117.25 49.01
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 446 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH A 548 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH A 560 DISTANCE = 5.26 ANGSTROMS
REMARK 525 HOH A 561 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH B 580 DISTANCE = 5.49 ANGSTROMS
REMARK 525 HOH B 582 DISTANCE = 5.01 ANGSTROMS
DBREF 4RGY A 1 270 UNP B8Y562 B8Y562_9BACT 1 270
DBREF 4RGY B 1 270 UNP B8Y562 B8Y562_9BACT 1 270
SEQADV 4RGY HIS A 0 UNP B8Y562 EXPRESSION TAG
SEQADV 4RGY HIS B 0 UNP B8Y562 EXPRESSION TAG
SEQRES 1 A 271 HIS MET ALA LEU PHE GLN CYS ASP PHE PHE SER ASP VAL
SEQRES 2 A 271 LEU GLY LEU SER THR SER MET THR VAL ILE LEU PRO GLN
SEQRES 3 A 271 GLU THR THR GLY GLN ILE GLY MET ALA GLY GLY SER GLU
SEQRES 4 A 271 ARG ARG GLU HIS PRO THR LEU PHE LEU LEU HIS GLY LEU
SEQRES 5 A 271 SER ASP ASP HIS THR ILE TRP LEU ARG ARG THR SER ILE
SEQRES 6 A 271 GLU ARG TYR VAL ALA GLU MET GLY LEU ALA VAL VAL MET
SEQRES 7 A 271 PRO ALA VAL HIS ARG SER PHE TYR THR ASP MET ALA HIS
SEQRES 8 A 271 GLY LEU GLN TYR TRP THR PHE ILE SER GLU GLU LEU PRO
SEQRES 9 A 271 ALA LEU ALA ARG SER PHE PHE PRO LEU ALA THR ALA ARG
SEQRES 10 A 271 GLU ASP THR PHE VAL ALA GLY LEU SER MET GLY GLY TYR
SEQRES 11 A 271 GLY ALA LEU LYS LEU GLY MET ARG HIS PRO GLU ARG PHE
SEQRES 12 A 271 ALA ALA ALA ALA SER LEU SER GLY ALA LEU ASP ILE THR
SEQRES 13 A 271 PHE ASP PRO ALA GLU HIS ILE ALA MET GLU ASP ASP VAL
SEQRES 14 A 271 TRP VAL ALA GLU GLN ARG ASN ILE PHE GLY ASP LEU ALA
SEQRES 15 A 271 ALA LEU PRO GLY SER ASP HIS ASP LEU PHE ALA LEU ALA
SEQRES 16 A 271 GLU ARG MET ALA GLN SER ASP GLY PRO VAL PRO LYS LEU
SEQRES 17 A 271 TYR GLN CYS CYS GLY THR GLU ASP PHE LEU TYR GLU ASP
SEQRES 18 A 271 ASN VAL ARG PHE ARG ASP HIS VAL ARG GLY LEU GLY LEU
SEQRES 19 A 271 ASP PHE MET TYR GLU GLU SER PRO GLY GLU HIS GLU TRP
SEQRES 20 A 271 GLY TYR TRP ASP ALA GLN ILE GLN ARG VAL LEU ALA TRP
SEQRES 21 A 271 LEU PRO LEU ARG PRO PRO GLY THR ALA PRO ALA
SEQRES 1 B 271 HIS MET ALA LEU PHE GLN CYS ASP PHE PHE SER ASP VAL
SEQRES 2 B 271 LEU GLY LEU SER THR SER MET THR VAL ILE LEU PRO GLN
SEQRES 3 B 271 GLU THR THR GLY GLN ILE GLY MET ALA GLY GLY SER GLU
SEQRES 4 B 271 ARG ARG GLU HIS PRO THR LEU PHE LEU LEU HIS GLY LEU
SEQRES 5 B 271 SER ASP ASP HIS THR ILE TRP LEU ARG ARG THR SER ILE
SEQRES 6 B 271 GLU ARG TYR VAL ALA GLU MET GLY LEU ALA VAL VAL MET
SEQRES 7 B 271 PRO ALA VAL HIS ARG SER PHE TYR THR ASP MET ALA HIS
SEQRES 8 B 271 GLY LEU GLN TYR TRP THR PHE ILE SER GLU GLU LEU PRO
SEQRES 9 B 271 ALA LEU ALA ARG SER PHE PHE PRO LEU ALA THR ALA ARG
SEQRES 10 B 271 GLU ASP THR PHE VAL ALA GLY LEU SER MET GLY GLY TYR
SEQRES 11 B 271 GLY ALA LEU LYS LEU GLY MET ARG HIS PRO GLU ARG PHE
SEQRES 12 B 271 ALA ALA ALA ALA SER LEU SER GLY ALA LEU ASP ILE THR
SEQRES 13 B 271 PHE ASP PRO ALA GLU HIS ILE ALA MET GLU ASP ASP VAL
SEQRES 14 B 271 TRP VAL ALA GLU GLN ARG ASN ILE PHE GLY ASP LEU ALA
SEQRES 15 B 271 ALA LEU PRO GLY SER ASP HIS ASP LEU PHE ALA LEU ALA
SEQRES 16 B 271 GLU ARG MET ALA GLN SER ASP GLY PRO VAL PRO LYS LEU
SEQRES 17 B 271 TYR GLN CYS CYS GLY THR GLU ASP PHE LEU TYR GLU ASP
SEQRES 18 B 271 ASN VAL ARG PHE ARG ASP HIS VAL ARG GLY LEU GLY LEU
SEQRES 19 B 271 ASP PHE MET TYR GLU GLU SER PRO GLY GLU HIS GLU TRP
SEQRES 20 B 271 GLY TYR TRP ASP ALA GLN ILE GLN ARG VAL LEU ALA TRP
SEQRES 21 B 271 LEU PRO LEU ARG PRO PRO GLY THR ALA PRO ALA
FORMUL 3 HOH *644(H2 O)
HELIX 1 1 THR A 56 THR A 62 1 7
HELIX 2 2 SER A 63 VAL A 68 1 6
HELIX 3 3 GLN A 93 GLU A 100 1 8
HELIX 4 4 GLU A 100 PHE A 110 1 11
HELIX 5 5 ALA A 115 GLU A 117 5 3
HELIX 6 6 SER A 125 HIS A 138 1 14
HELIX 7 7 TRP A 169 GLY A 178 1 10
HELIX 8 8 ASP A 179 LEU A 183 5 5
HELIX 9 9 ASP A 189 SER A 200 1 12
HELIX 10 10 LEU A 217 GLY A 232 1 16
HELIX 11 11 GLU A 245 LEU A 260 1 16
HELIX 12 12 THR B 56 THR B 62 1 7
HELIX 13 13 SER B 63 VAL B 68 1 6
HELIX 14 14 GLN B 93 GLU B 100 1 8
HELIX 15 15 GLU B 100 PHE B 110 1 11
HELIX 16 16 ALA B 115 GLU B 117 5 3
HELIX 17 17 SER B 125 HIS B 138 1 14
HELIX 18 18 PRO B 139 PHE B 142 5 4
HELIX 19 19 ALA B 171 GLY B 178 1 8
HELIX 20 20 ASP B 179 LEU B 183 5 5
HELIX 21 21 ASP B 189 GLN B 199 1 11
HELIX 22 22 LEU B 217 ARG B 229 1 13
HELIX 23 23 GLU B 245 LEU B 260 1 16
SHEET 1 A 8 MET A 1 SER A 10 0
SHEET 2 A 8 LEU A 15 PRO A 24 -1 O LEU A 23 N ALA A 2
SHEET 3 A 8 ALA A 74 PRO A 78 -1 O MET A 77 N THR A 20
SHEET 4 A 8 THR A 44 LEU A 48 1 N LEU A 45 O ALA A 74
SHEET 5 A 8 THR A 119 LEU A 124 1 O ALA A 122 N LEU A 48
SHEET 6 A 8 ALA A 144 LEU A 148 1 O LEU A 148 N GLY A 123
SHEET 7 A 8 LYS A 206 GLY A 212 1 O TYR A 208 N SER A 147
SHEET 8 A 8 PHE A 235 SER A 240 1 O MET A 236 N GLN A 209
SHEET 1 B 8 MET B 1 SER B 10 0
SHEET 2 B 8 LEU B 15 PRO B 24 -1 O LEU B 23 N ALA B 2
SHEET 3 B 8 ALA B 74 PRO B 78 -1 O MET B 77 N THR B 20
SHEET 4 B 8 THR B 44 LEU B 48 1 N LEU B 45 O ALA B 74
SHEET 5 B 8 THR B 119 LEU B 124 1 O ALA B 122 N LEU B 48
SHEET 6 B 8 ALA B 144 LEU B 148 1 O LEU B 148 N GLY B 123
SHEET 7 B 8 LYS B 206 GLY B 212 1 O TYR B 208 N SER B 147
SHEET 8 B 8 PHE B 235 SER B 240 1 O MET B 236 N GLN B 209
CRYST1 133.459 63.767 88.688 90.00 127.11 90.00 C 1 2 1 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 0.007493 0.000000 0.005668 0.00000
SCALE2 0.000000 0.015682 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014138 0.00000
TER 1885 LEU A 262
TER 3760 LEU B 262
MASTER 466 0 0 23 16 0 0 6 4402 2 0 42
END |