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HEADER HYDROLASE 31-AUG-19 6SP8
TITLE STRUCTURE OF HYPERSTABLE HALOALKANE DEHALOGENASE VARIANT DHAA115
TITLE 2 PREPARED BY THE 'SOAK-AND-FREEZE' METHOD UNDER 150 BAR OF KRYPTON
TITLE 3 PRESSURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.CHMELOVA,K.MARKOVA,J.DAMBORSKY,M.MAREK
REVDAT 1 18-NOV-20 6SP8 0
JRNL AUTH K.MARKOVA,K.CHMELOVA,S.M.MARQUES,P.CARPENTIER,D.BEDNAR,
JRNL AUTH 2 J.DAMBORSKY,M.MAREK
JRNL TITL DECODING THE INTRICATE NETWORK OF MOLECULAR INTERACTIONS OF
JRNL TITL 2 A HYPERSTABLE ENGINEERED BIOCATALYST
JRNL REF CHEM SCI 2020
JRNL REFN ESSN 2041-6539
JRNL DOI 10.1039/D0SC03367G
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 115973
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 5785
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 49.2030 - 4.8148 0.98 3957 184 0.1703 0.1934
REMARK 3 2 4.8148 - 3.8221 0.98 3755 206 0.1309 0.1407
REMARK 3 3 3.8221 - 3.3391 1.00 3784 222 0.1466 0.1563
REMARK 3 4 3.3391 - 3.0338 1.00 3755 195 0.1573 0.1743
REMARK 3 5 3.0338 - 2.8164 0.99 3728 202 0.1617 0.1906
REMARK 3 6 2.8164 - 2.6504 0.98 3642 200 0.1653 0.1996
REMARK 3 7 2.6504 - 2.5176 1.00 3710 211 0.1670 0.1691
REMARK 3 8 2.5176 - 2.4080 1.00 3704 197 0.1611 0.1864
REMARK 3 9 2.4080 - 2.3153 1.00 3726 200 0.1564 0.1689
REMARK 3 10 2.3153 - 2.2354 1.00 3698 203 0.1571 0.1623
REMARK 3 11 2.2354 - 2.1655 0.99 3679 177 0.1587 0.1764
REMARK 3 12 2.1655 - 2.1036 0.96 3589 178 0.1627 0.1963
REMARK 3 13 2.1036 - 2.0483 0.99 3670 196 0.1582 0.1923
REMARK 3 14 2.0483 - 1.9983 1.00 3689 184 0.1579 0.2043
REMARK 3 15 1.9983 - 1.9529 0.99 3676 185 0.1585 0.2001
REMARK 3 16 1.9529 - 1.9113 0.99 3666 205 0.1660 0.2008
REMARK 3 17 1.9113 - 1.8731 0.99 3657 186 0.1598 0.2055
REMARK 3 18 1.8731 - 1.8377 1.00 3692 187 0.1583 0.2021
REMARK 3 19 1.8377 - 1.8049 0.99 3619 196 0.1636 0.1826
REMARK 3 20 1.8049 - 1.7743 0.97 3561 186 0.1581 0.1920
REMARK 3 21 1.7743 - 1.7457 0.98 3617 178 0.1593 0.1922
REMARK 3 22 1.7457 - 1.7188 0.98 3652 187 0.1702 0.2024
REMARK 3 23 1.7188 - 1.6935 0.99 3638 194 0.1714 0.2043
REMARK 3 24 1.6935 - 1.6697 0.99 3650 202 0.1741 0.2117
REMARK 3 25 1.6697 - 1.6471 0.99 3643 184 0.1806 0.2001
REMARK 3 26 1.6471 - 1.6257 0.99 3628 196 0.1885 0.2442
REMARK 3 27 1.6257 - 1.6054 0.98 3608 204 0.2033 0.2223
REMARK 3 28 1.6054 - 1.5861 0.99 3595 187 0.2109 0.2365
REMARK 3 29 1.5861 - 1.5676 0.98 3615 185 0.2353 0.2770
REMARK 3 30 1.5676 - 1.5500 0.97 3585 168 0.2540 0.2790
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.05
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 5101
REMARK 3 ANGLE : 0.849 6969
REMARK 3 CHIRALITY : 0.057 713
REMARK 3 PLANARITY : 0.007 905
REMARK 3 DIHEDRAL : 8.465 4114
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 6SP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1292104091.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-18
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.860999
REMARK 200 MONOCHROMATOR : NULL
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 : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116195
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 49.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 13.50
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 13.50
REMARK 200 R MERGE FOR SHELL (I) : 0.88000
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: 6SP5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, BIS-TRIS PROPANE, POTASSIUM
REMARK 280 ISOTHIOCYANATE, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 33.98900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.08800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.02250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.08800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.98900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.02250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 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 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 PRO A 9 56.35 -90.99
REMARK 500 ASP A 31 -165.76 -119.66
REMARK 500 PRO A 42 47.12 -105.92
REMARK 500 THR A 43 -158.26 -101.96
REMARK 500 SER A 44 -168.71 -161.74
REMARK 500 GLU A 98 -87.86 -102.69
REMARK 500 GLU A 98 -88.56 -102.69
REMARK 500 ASP A 106 -131.18 51.96
REMARK 500 ASP A 156 -53.19 70.16
REMARK 500 VAL A 245 -71.14 -129.82
REMARK 500 LEU A 271 -97.05 -111.41
REMARK 500 PRO B 9 57.59 -90.29
REMARK 500 ASP B 31 -164.48 -118.69
REMARK 500 PRO B 42 48.60 -107.02
REMARK 500 THR B 43 -158.28 -103.78
REMARK 500 SER B 44 -169.80 -162.78
REMARK 500 GLU B 98 -89.00 -107.27
REMARK 500 ASP B 106 -131.64 54.43
REMARK 500 ASP B 156 -55.15 71.38
REMARK 500 VAL B 245 -70.70 -128.80
REMARK 500 LEU B 271 -93.92 -111.70
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 719 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B 698 DISTANCE = 6.45 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KR B 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue B3P B 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 319
DBREF 6SP8 A 3 293 UNP P0A3G2 DHAA_RHORH 3 293
DBREF 6SP8 B 3 293 UNP P0A3G2 DHAA_RHORH 3 293
SEQADV 6SP8 SER A 20 UNP P0A3G2 GLU 20 ENGINEERED MUTATION
SEQADV 6SP8 ARG A 80 UNP P0A3G2 PHE 80 ENGINEERED MUTATION
SEQADV 6SP8 PHE A 128 UNP P0A3G2 CYS 128 ENGINEERED MUTATION
SEQADV 6SP8 LEU A 148 UNP P0A3G2 THR 148 ENGINEERED MUTATION
SEQADV 6SP8 PRO A 155 UNP P0A3G2 ALA 155 ENGINEERED MUTATION
SEQADV 6SP8 ILE A 172 UNP P0A3G2 ALA 172 ENGINEERED MUTATION
SEQADV 6SP8 PHE A 176 UNP P0A3G2 CYS 176 ENGINEERED MUTATION
SEQADV 6SP8 TRP A 198 UNP P0A3G2 ASP 198 ENGINEERED MUTATION
SEQADV 6SP8 TRP A 219 UNP P0A3G2 VAL 219 ENGINEERED MUTATION
SEQADV 6SP8 LEU A 262 UNP P0A3G2 CYS 262 ENGINEERED MUTATION
SEQADV 6SP8 PHE A 266 UNP P0A3G2 ASP 266 ENGINEERED MUTATION
SEQADV 6SP8 SER B 20 UNP P0A3G2 GLU 20 ENGINEERED MUTATION
SEQADV 6SP8 ARG B 80 UNP P0A3G2 PHE 80 ENGINEERED MUTATION
SEQADV 6SP8 PHE B 128 UNP P0A3G2 CYS 128 ENGINEERED MUTATION
SEQADV 6SP8 LEU B 148 UNP P0A3G2 THR 148 ENGINEERED MUTATION
SEQADV 6SP8 PRO B 155 UNP P0A3G2 ALA 155 ENGINEERED MUTATION
SEQADV 6SP8 ILE B 172 UNP P0A3G2 ALA 172 ENGINEERED MUTATION
SEQADV 6SP8 PHE B 176 UNP P0A3G2 CYS 176 ENGINEERED MUTATION
SEQADV 6SP8 TRP B 198 UNP P0A3G2 ASP 198 ENGINEERED MUTATION
SEQADV 6SP8 TRP B 219 UNP P0A3G2 VAL 219 ENGINEERED MUTATION
SEQADV 6SP8 LEU B 262 UNP P0A3G2 CYS 262 ENGINEERED MUTATION
SEQADV 6SP8 PHE B 266 UNP P0A3G2 ASP 266 ENGINEERED MUTATION
SEQRES 1 A 291 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 A 291 GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 A 291 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 A 291 PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 A 291 VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 A 291 GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP TYR ARG
SEQRES 7 A 291 PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES 8 A 291 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 A 291 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 A 291 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 A 291 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 A 291 ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP VAL GLY
SEQRES 13 A 291 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES 14 A 291 ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 A 291 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 16 A 291 TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 A 291 ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU VAL GLU
SEQRES 18 A 291 ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 A 291 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 A 291 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN LEU
SEQRES 21 A 291 LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR LEU GLN
SEQRES 22 A 291 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 A 291 TRP LEU PRO ALA LEU
SEQRES 1 B 291 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 B 291 GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 B 291 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 B 291 PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 B 291 VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 B 291 GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP TYR ARG
SEQRES 7 B 291 PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES 8 B 291 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 B 291 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 B 291 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 B 291 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 B 291 ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP VAL GLY
SEQRES 13 B 291 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES 14 B 291 ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 B 291 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 16 B 291 TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 B 291 ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU VAL GLU
SEQRES 18 B 291 ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 B 291 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 B 291 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN LEU
SEQRES 21 B 291 LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR LEU GLN
SEQRES 22 B 291 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 B 291 TRP LEU PRO ALA LEU
HET KR A 301 1
HET KR A 302 1
HET KR A 303 1
HET KR A 304 1
HET KR A 305 1
HET KR A 306 1
HET KR A 307 1
HET KR A 308 1
HET KR A 309 1
HET KR A 310 1
HET KR A 311 1
HET KR A 312 1
HET SCN A 313 3
HET SCN A 314 3
HET SCN A 315 3
HET B3P A 316 19
HET GOL A 317 6
HET GOL A 318 6
HET KR B 301 1
HET KR B 302 1
HET KR B 303 1
HET KR B 304 1
HET KR B 305 1
HET KR B 306 1
HET KR B 307 1
HET KR B 308 1
HET KR B 309 1
HET SCN B 310 3
HET SCN B 311 3
HET SCN B 312 3
HET B3P B 313 19
HET GOL B 314 6
HET GOL B 315 6
HET GOL B 316 6
HET GOL B 317 6
HET GOL B 318 6
HET GOL B 319 6
HETNAM KR KRYPTON
HETNAM SCN THIOCYANATE ION
HETNAM B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-
HETNAM 2 B3P PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 KR 21(KR)
FORMUL 15 SCN 6(C N S 1-)
FORMUL 18 B3P 2(C11 H26 N2 O6)
FORMUL 19 GOL 8(C3 H8 O3)
FORMUL 40 HOH *617(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 ARG A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 ARG A 153 1 12
HELIX 7 AA7 ASP A 156 ILE A 163 1 8
HELIX 8 AA8 ASN A 166 GLY A 171 1 6
HELIX 9 AA9 GLY A 171 PHE A 176 1 6
HELIX 10 AB1 THR A 182 GLU A 191 1 10
HELIX 11 AB2 PRO A 192 LEU A 194 5 3
HELIX 12 AB3 LYS A 195 TRP A 198 5 4
HELIX 13 AB4 ARG A 199 LEU A 209 1 11
HELIX 14 AB5 PRO A 215 SER A 232 1 18
HELIX 15 AB6 PRO A 248 LEU A 259 1 12
HELIX 16 AB7 TYR A 273 ASP A 277 5 5
HELIX 17 AB8 ASN A 278 LEU A 290 1 13
HELIX 18 AB9 PRO A 291 LEU A 293 5 3
HELIX 19 AC1 SER B 44 ARG B 49 5 6
HELIX 20 AC2 ILE B 51 ALA B 56 1 6
HELIX 21 AC3 ARG B 80 LEU B 95 1 16
HELIX 22 AC4 ASP B 106 ASN B 119 1 14
HELIX 23 AC5 THR B 137 TRP B 141 5 5
HELIX 24 AC6 PRO B 142 ARG B 153 1 12
HELIX 25 AC7 ASP B 156 ILE B 163 1 8
HELIX 26 AC8 ASN B 166 GLY B 171 1 6
HELIX 27 AC9 GLY B 171 PHE B 176 1 6
HELIX 28 AD1 THR B 182 GLU B 191 1 10
HELIX 29 AD2 PRO B 192 LEU B 194 5 3
HELIX 30 AD3 LYS B 195 TRP B 198 5 4
HELIX 31 AD4 ARG B 199 LEU B 209 1 11
HELIX 32 AD5 PRO B 215 SER B 232 1 18
HELIX 33 AD6 PRO B 248 LEU B 259 1 12
HELIX 34 AD7 TYR B 273 ASN B 278 1 6
HELIX 35 AD8 ASN B 278 LEU B 290 1 13
HELIX 36 AD9 PRO B 291 LEU B 293 5 3
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 SER A 20 VAL A 27 -1 O SER A 20 N VAL A 17
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 LEU A 262 GLY A 270 1 O ILE A 267 N TRP A 240
SHEET 1 AA2 8 HIS B 13 VAL B 17 0
SHEET 2 AA2 8 SER B 20 VAL B 27 -1 O SER B 20 N VAL B 17
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N PHE B 37 O ILE B 62
SHEET 5 AA2 8 VAL B 100 HIS B 105 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 MET B 129 1 O ALA B 127 N LEU B 102
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 128
SHEET 8 AA2 8 LEU B 262 GLY B 270 1 O LYS B 263 N LEU B 238
CISPEP 1 ASN A 41 PRO A 42 0 -4.20
CISPEP 2 GLU A 214 PRO A 215 0 -4.37
CISPEP 3 THR A 242 PRO A 243 0 5.51
CISPEP 4 ASN B 41 PRO B 42 0 -3.97
CISPEP 5 GLU B 214 PRO B 215 0 -6.13
CISPEP 6 THR B 242 PRO B 243 0 5.71
SITE 1 AC1 2 MET A 22 LEU A 88
SITE 1 AC2 3 ILE A 92 LEU A 102 TRP A 115
SITE 1 AC3 2 KR A 304 SCN A 313
SITE 1 AC4 5 PHE A 168 HIS A 272 TYR A 273 KR A 303
SITE 2 AC4 5 SCN A 313
SITE 1 AC5 3 ARG A 133 ILE A 135 PRO A 210
SITE 1 AC6 4 ARG A 133 ILE A 135 GLU A 140 VAL A 245
SITE 1 AC7 5 TYR A 79 ARG A 80 PHE A 81 PHE A 205
SITE 2 AC7 5 GLU A 208
SITE 1 AC8 2 TRP A 240 ALA A 252
SITE 1 AC9 1 TRP B 240
SITE 1 AD1 2 PRO A 196 GLU A 200
SITE 1 AD2 3 ARG A 254 GLU A 257 HOH A 469
SITE 1 AD3 7 ASN A 41 ASP A 106 TRP A 107 PHE A 205
SITE 2 AD3 7 PRO A 206 KR A 303 KR A 304
SITE 1 AD4 2 ALA A 56 HOH A 489
SITE 1 AD5 2 GLY A 268 PRO B 269
SITE 1 AD6 13 ASP A 76 LEU A 77 ASP A 78 GLU A 200
SITE 2 AD6 13 ARG A 204 HOH A 405 HOH A 413 HOH A 451
SITE 3 AD6 13 HOH A 453 HOH A 460 HOH A 521 HIS B 13
SITE 4 AD6 13 HOH B 493
SITE 1 AD7 4 ARG A 153 ASN A 207 PRO A 215 HOH A 506
SITE 1 AD8 5 GLU A 3 ASP A 277 ASN A 278 PRO A 279
SITE 2 AD8 5 ASP A 280
SITE 1 AD9 3 ILE B 92 LEU B 102 TRP B 115
SITE 1 AE1 5 PHE B 168 HIS B 272 TYR B 273 KR B 303
SITE 2 AE1 5 SCN B 310
SITE 1 AE2 2 KR B 302 SCN B 310
SITE 1 AE3 2 ARG B 133 ILE B 135
SITE 1 AE4 2 MET B 22 LEU B 88
SITE 1 AE5 5 PHE B 81 TRP B 107 PHE B 205 GLU B 208
SITE 2 AE5 5 HOH B 411
SITE 1 AE6 3 PHE B 81 LEU B 221 TYR B 225
SITE 1 AE7 3 ILE B 135 GLU B 140 VAL B 245
SITE 1 AE8 3 PRO B 196 VAL B 197 GLU B 200
SITE 1 AE9 7 ASN B 41 ASP B 106 TRP B 107 PHE B 205
SITE 2 AE9 7 PRO B 206 KR B 302 KR B 303
SITE 1 AF1 3 PRO B 53 ALA B 56 HOH B 496
SITE 1 AF2 13 HIS A 13 ASP B 76 LEU B 77 ASP B 78
SITE 2 AF2 13 GLU B 200 ARG B 204 HOH B 405 HOH B 422
SITE 3 AF2 13 HOH B 431 HOH B 460 HOH B 474 HOH B 504
SITE 4 AF2 13 HOH B 560
SITE 1 AF3 5 GLU A 214 ASP B 82 HIS B 114 HOH B 410
SITE 2 AF3 5 HOH B 537
SITE 1 AF4 8 ASP B 89 TRP B 115 ARG B 118 ASN B 119
SITE 2 AF4 8 ARG B 122 HOH B 413 HOH B 438 HOH B 547
SITE 1 AF5 9 TRP A 198 ARG B 30 ASP B 31 GLY B 32
SITE 2 AF5 9 ARG B 60 GLY B 96 HOH B 515 HOH B 548
SITE 3 AF5 9 HOH B 587
SITE 1 AF6 8 ALA A 216 ALA A 220 ASP B 78 ARG B 80
SITE 2 AF6 8 ASP B 82 HOH B 402 HOH B 545 HOH B 602
SITE 1 AF7 4 ASP B 277 ASN B 278 PRO B 279 ASP B 280
SITE 1 AF8 9 PHE B 8 SER B 44 TYR B 46 HIS B 188
SITE 2 AF8 9 GLU B 191 HOH B 401 HOH B 442 HOH B 605
SITE 3 AF8 9 HOH B 606
CRYST1 67.978 82.045 144.176 90.00 90.00 90.00 P 21 21 21 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 0.014711 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006936 0.00000
TER 2417 LEU A 293
TER 4829 LEU B 293
MASTER 417 0 37 36 16 0 55 6 5480 2 104 46
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