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HEADER HYDROLASE 29-MAY-24 8ZP6
TITLE CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE MDEH (MYCOBACTERIUM
TITLE 2 DIOXANOTROPHICUS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EPOXIDE HYDROLASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM DIOXANOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 482462;
SOURCE 4 GENE: BTO20_37290;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EPOXIDE HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHOU,D.M.LAN,Y.H.WANG
REVDAT 1 04-JUN-25 8ZP6 0
JRNL AUTH Y.ZHOU,D.M.LAN,Y.H.WANG
JRNL TITL CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE MDEH (MYCOBACTERIUM
JRNL TITL 2 DIOXANOTROPHICUS)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692+SVN
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.336
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 54289
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.240
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.233
REMARK 3 FREE R VALUE TEST SET COUNT : 1755
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 4.9315 - 3.9169 1.00 4089 137 0.2086 0.2252
REMARK 3 2 3.9169 - 3.4226 1.00 4066 135 0.2152 0.2322
REMARK 3 3 3.4226 - 3.1100 1.00 4026 135 0.2312 0.2683
REMARK 3 4 3.1100 - 2.8872 1.00 4040 135 0.2488 0.2442
REMARK 3 5 2.8872 - 2.7171 1.00 4052 136 0.2612 0.3009
REMARK 3 6 2.7171 - 2.5811 1.00 4008 134 0.2727 0.2925
REMARK 3 7 2.5811 - 2.4688 1.00 4024 134 0.2685 0.2650
REMARK 3 8 2.4688 - 2.3738 1.00 4022 134 0.2665 0.2954
REMARK 3 9 2.3738 - 2.2919 1.00 4011 134 0.2729 0.2856
REMARK 3 10 2.2919 - 2.2203 1.00 4014 133 0.2758 0.2950
REMARK 3 11 2.2203 - 2.1568 1.00 4007 135 0.2653 0.3077
REMARK 3 12 2.1568 - 2.1001 1.00 3988 133 0.2724 0.2997
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) : 0.254
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.061
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.08
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 2459
REMARK 3 ANGLE : 1.008 3357
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 8ZP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 03-JUN-24.
REMARK 100 THE DEPOSITION ID IS D_1300048272.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JAN-24
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61853
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 31.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
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: 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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 3350, AMMONIUM
REMARK 280 SULFATE, BIS-TRIS, PH 8.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 89.64500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.75656
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 50.45000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 89.64500
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 51.75656
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 50.45000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 89.64500
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 51.75656
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 50.45000
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 89.64500
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 51.75656
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 50.45000
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 89.64500
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 51.75656
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 50.45000
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 89.64500
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 51.75656
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 50.45000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 103.51313
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 100.90000
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 103.51313
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 100.90000
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 103.51313
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 100.90000
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 103.51313
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 100.90000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 103.51313
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 100.90000
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 103.51313
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 100.90000
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 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 -0.500000 -0.866025 0.000000 89.64500
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 155.26969
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -89.64500
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 155.26969
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -0.500000 0.866025 0.000000 -89.64500
REMARK 350 BIOMT2 4 0.866025 0.500000 0.000000 51.75656
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 50.45000
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 -1.000000 0.000000 207.02626
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 50.45000
REMARK 350 BIOMT1 6 -0.500000 -0.866025 0.000000 89.64500
REMARK 350 BIOMT2 6 -0.866025 0.500000 0.000000 51.75656
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 50.45000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 -0.500000 0.866025 0.000000 -89.64500
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 51.75656
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 50.45000
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 429 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 582 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 652 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 1
REMARK 465 THR A 2
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 600 O HOH A 647 1.90
REMARK 500 O HOH A 313 O HOH A 447 1.92
REMARK 500 O HOH A 563 O HOH A 638 1.94
REMARK 500 O HOH A 574 O HOH A 597 1.94
REMARK 500 O HOH A 505 O HOH A 605 1.98
REMARK 500 O HOH A 539 O HOH A 545 1.98
REMARK 500 OE2 GLU A 170 O HOH A 301 2.02
REMARK 500 O HOH A 554 O HOH A 595 2.02
REMARK 500 O HOH A 305 O HOH A 578 2.08
REMARK 500 OD2 ASP A 122 O HOH A 302 2.09
REMARK 500 O HOH A 588 O HOH A 651 2.10
REMARK 500 O HOH A 550 O HOH A 639 2.13
REMARK 500 O HOH A 583 O HOH A 660 2.16
REMARK 500 O HOH A 409 O HOH A 459 2.16
REMARK 500 O HOH A 583 O HOH A 638 2.16
REMARK 500 O HOH A 367 O HOH A 640 2.16
REMARK 500 O HOH A 573 O HOH A 591 2.18
REMARK 500 O HOH A 456 O HOH A 608 2.18
REMARK 500 O HOH A 517 O HOH A 605 2.19
REMARK 500 O HOH A 304 O HOH A 394 2.19
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 657 O HOH A 662 10455 2.01
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 PHE A 41 -167.20 -169.41
REMARK 500 ASP A 73 106.76 -20.78
REMARK 500 ASP A 107 -133.49 58.69
REMARK 500 ASN A 206 -0.72 71.44
REMARK 500 ARG A 231 37.91 -89.22
REMARK 500 PHE A 275 73.17 -113.83
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 669 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 670 DISTANCE = 6.98 ANGSTROMS
DBREF1 8ZP6 A 1 293 UNP A0A1Y0CH10_9MYCO
DBREF2 8ZP6 A A0A1Y0CH10 1 293
SEQRES 1 A 293 MET THR ILE ARG ARG PRO GLU HIS PHE THR HIS HIS GLU
SEQRES 2 A 293 VAL GLN LEU SER ASP VAL LYS ILE HIS TYR VAL ARG GLU
SEQRES 3 A 293 GLY ALA GLY PRO THR LEU LEU LEU LEU HIS GLY TRP PRO
SEQRES 4 A 293 GLY PHE TRP TRP GLU TRP SER LYS VAL ILE GLY PRO LEU
SEQRES 5 A 293 SER GLU ARG PHE ASP VAL ILE VAL PRO ASP LEU ARG GLY
SEQRES 6 A 293 PHE GLY ASP SER GLU LYS PRO ASP LEU SER ASP LEU ALA
SEQRES 7 A 293 GLN TYR SER LEU GLU ARG VAL ALA ASP ASP GLN ALA GLU
SEQRES 8 A 293 LEU LEU ASN ALA LEU GLY ILE ASP GLN ALA TYR VAL VAL
SEQRES 9 A 293 GLY HIS ASP TYR SER ALA ILE VAL VAL HIS LYS PHE ILE
SEQRES 10 A 293 ARG LYS TYR PRO ASP ARG VAL VAL LYS ALA ALA ILE PHE
SEQRES 11 A 293 ASP PRO ILE THR PRO ASP PHE GLY PRO PHE TYR LEU GLY
SEQRES 12 A 293 PHE PRO HIS ILE ALA GLU SER TRP TYR SER GLN PHE HIS
SEQRES 13 A 293 GLN THR ASP MET SER VAL GLU LEU VAL THR SER SER ARG
SEQRES 14 A 293 GLU ALA CYS ARG ILE TYR PHE LYS HIS PHE PHE ASP HIS
SEQRES 15 A 293 TRP SER TYR HIS ALA PRO LEU LEU THR GLN ASP GLU LEU
SEQRES 16 A 293 ASP ILE TYR VAL ASP ASN CYS MET LYS PRO ASN ASN VAL
SEQRES 17 A 293 HIS GLY GLY PHE ASN TYR TYR ARG SER ASN LEU SER VAL
SEQRES 18 A 293 THR SER ASP PRO TRP THR ASP LEU ASP ARG THR VAL SER
SEQRES 19 A 293 ASP LEU PRO VAL THR MET LEU TRP GLY VAL GLY ASP PRO
SEQRES 20 A 293 VAL VAL PRO SER SER LEU VAL HIS GLN VAL PRO ASN TYR
SEQRES 21 A 293 TYR SER ASN TYR THR MET GLU LEU ILE GLN ASP ALA GLY
SEQRES 22 A 293 HIS PHE MET MET VAL GLU LYS PRO GLU VAL VAL ILE ASP
SEQRES 23 A 293 ARG LEU LYS ALA GLY PHE ARG
FORMUL 2 HOH *370(H2 O)
HELIX 1 AA1 ARG A 5 PHE A 9 5 5
HELIX 2 AA2 PHE A 41 GLU A 44 5 4
HELIX 3 AA3 TRP A 45 SER A 53 1 9
HELIX 4 AA4 ASP A 76 TYR A 80 5 5
HELIX 5 AA5 SER A 81 LEU A 96 1 16
HELIX 6 AA6 ASP A 107 TYR A 120 1 14
HELIX 7 AA7 ASP A 136 LEU A 142 1 7
HELIX 8 AA8 HIS A 146 HIS A 156 1 11
HELIX 9 AA9 THR A 158 THR A 166 1 9
HELIX 10 AB1 SER A 168 TRP A 183 1 16
HELIX 11 AB2 THR A 191 MET A 203 1 13
HELIX 12 AB3 ASN A 206 LEU A 219 1 14
HELIX 13 AB4 ASP A 228 THR A 232 5 5
HELIX 14 AB5 PRO A 250 VAL A 257 5 8
HELIX 15 AB6 PHE A 275 LYS A 280 1 6
HELIX 16 AB7 LYS A 280 PHE A 292 1 13
SHEET 1 AA1 8 HIS A 11 GLN A 15 0
SHEET 2 AA1 8 LYS A 20 GLU A 26 -1 O TYR A 23 N HIS A 12
SHEET 3 AA1 8 ASP A 57 PRO A 61 -1 O VAL A 60 N VAL A 24
SHEET 4 AA1 8 THR A 31 LEU A 35 1 N LEU A 32 O ILE A 59
SHEET 5 AA1 8 ALA A 101 HIS A 106 1 O TYR A 102 N LEU A 33
SHEET 6 AA1 8 VAL A 124 PHE A 130 1 O ALA A 128 N VAL A 103
SHEET 7 AA1 8 VAL A 238 GLY A 243 1 O THR A 239 N ALA A 127
SHEET 8 AA1 8 TYR A 264 ILE A 269 1 O ILE A 269 N TRP A 242
CISPEP 1 TRP A 38 PRO A 39 0 6.58
CISPEP 2 PHE A 144 PRO A 145 0 5.35
CISPEP 3 ALA A 187 PRO A 188 0 2.29
CRYST1 179.290 179.290 151.350 90.00 90.00 120.00 H 3 2 18
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 0.005578 0.003220 0.000000 0.00000
SCALE2 0.000000 0.006440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006607 0.00000
TER 2380 ARG A 293
MASTER 394 0 0 16 8 0 0 6 2749 1 0 23
END |