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HEADER HYDROLASE 28-MAY-20 6Z69
TITLE A NOVEL METAGENOMIC ALPHA/BETA-FOLD ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL ESTERASE/LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDONOCARDIA THERMOPHILA;
SOURCE 3 ORGANISM_TAXID: 1848;
SOURCE 4 GENE: SAMN05443637_118146;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-FOLD HYDROLASE; ESTERASE; METAGENOME; INHIBITOR-BOUND;
KEYWDS 2 SUBSTRATE PROMISCUITY, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BOLLINGER,S.THIES,A.HOEPPNER,S.KOBUS,K.-E.JAEGER,S.H.J.SMITS
REVDAT 1 30-DEC-20 6Z69 0
JRNL AUTH A.HOPPNER,A.BOLLINGER,S.KOBUS,S.THIES,C.COSCOLIN,M.FERRER,
JRNL AUTH 2 K.E.JAEGER,S.H.J.SMITS
JRNL TITL CRYSTAL STRUCTURES OF A NOVEL FAMILY IV ESTERASE IN FREE AND
JRNL TITL 2 SUBSTRATE-BOUND FORM.
JRNL REF FEBS J. 2020
JRNL REFN ISSN 1742-464X
JRNL PMID 33342083
JRNL DOI 10.1111/FEBS.15680
REMARK 2
REMARK 2 RESOLUTION. 1.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 59945
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.151
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3152
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4430
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 200
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5436
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 962
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -0.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.787
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5659 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5250 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7713 ; 1.648 ; 1.663
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12098 ; 1.442 ; 1.586
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 727 ; 6.094 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 313 ;27.424 ;19.968
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 819 ;13.541 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;18.474 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 709 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6513 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1249 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6Z69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-20.
REMARK 100 THE DEPOSITION ID IS D_1292108905.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63348
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 43.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55500
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: 6Z68
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M TRIS
REMARK 280 PH 8.5, 30 % (W/V) PEG 4000, 2 MM METHYL 4-METHYLUMBELLIFERYL
REMARK 280 HEXYLPHOSPHAT, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 285K
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 36.20500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.05500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.35000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.05500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.20500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.35000
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 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 465 THR A 3
REMARK 465 THR A 4
REMARK 465 SER A 5
REMARK 465 ASN A 6
REMARK 465 SER A 7
REMARK 465 THR A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 GLY A 11
REMARK 465 LEU A 369
REMARK 465 GLU A 370
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
REMARK 465 HIS A 376
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 THR B 3
REMARK 465 THR B 4
REMARK 465 LEU B 369
REMARK 465 GLU B 370
REMARK 465 HIS B 371
REMARK 465 HIS B 372
REMARK 465 HIS B 373
REMARK 465 HIS B 374
REMARK 465 HIS B 375
REMARK 465 HIS B 376
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 801 O HOH A 815 2.02
REMARK 500 O HOH A 806 O HOH A 821 2.02
REMARK 500 O HOH B 861 O HOH B 933 2.07
REMARK 500 O HOH B 869 O HOH B 902 2.08
REMARK 500 O HOH A 521 O HOH A 658 2.09
REMARK 500 O HOH B 862 O HOH B 960 2.10
REMARK 500 NH1 ARG A 214 O HOH A 501 2.11
REMARK 500 O HOH B 881 O HOH B 886 2.13
REMARK 500 O HOH B 889 O HOH B 923 2.15
REMARK 500 O HOH B 831 O HOH B 933 2.16
REMARK 500 O HOH B 536 O HOH B 805 2.16
REMARK 500 O HOH A 597 O HOH B 960 2.16
REMARK 500 O HOH B 614 O HOH B 904 2.17
REMARK 500 O HOH A 928 O HOH A 939 2.18
REMARK 500 O HOH A 514 O HOH A 624 2.19
REMARK 500 NH1 ARG B 319 O HOH B 501 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 B 517 O HOH B 837 2454 1.94
REMARK 500 O HOH A 849 O HOH B 946 3554 2.03
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 ARG A 329 CG - CD - NE ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG A 329 NE - CZ - NH2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASN B 6 CB - CA - C ANGL. DEV. = -15.6 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 ASP A 31 108.75 -56.76
REMARK 500 MET A 129 10.46 59.96
REMARK 500 LEU A 132 148.42 87.29
REMARK 500 SER A 194 -96.38 -86.47
REMARK 500 SER A 202 -118.73 60.82
REMARK 500 VAL A 231 54.86 38.47
REMARK 500 PHE A 259 -51.62 71.73
REMARK 500 ALA A 339 18.02 59.61
REMARK 500 PHE A 344 50.16 -99.71
REMARK 500 ASN B 6 -17.36 159.63
REMARK 500 LEU B 132 149.55 84.67
REMARK 500 SER B 194 -96.33 -93.24
REMARK 500 SER B 202 -119.50 59.52
REMARK 500 VAL B 231 55.71 35.97
REMARK 500 PHE B 259 -59.77 70.52
REMARK 500 THR B 276 45.05 38.56
REMARK 500 PHE B 344 49.88 -101.37
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 959 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A 960 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH A 961 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH B 997 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 998 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 999 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH B1000 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH B1001 DISTANCE = 6.60 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 HEE A 401
REMARK 610 HEE A 402
REMARK 610 HEE B 401
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 MG B 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 577 O
REMARK 620 2 HOH B 618 O 90.4
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4MU A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues HEE A 402 and 4MU A
REMARK 800 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEE B 401 and SER B
REMARK 800 202
DBREF1 6Z69 A 1 368 UNP A0A1M6Y2K1_PSETH
DBREF2 6Z69 A A0A1M6Y2K1 1 368
DBREF1 6Z69 B 1 368 UNP A0A1M6Y2K1_PSETH
DBREF2 6Z69 B A0A1M6Y2K1 1 368
SEQADV 6Z69 VAL A 271 UNP A0A1M6Y2K LEU 271 CONFLICT
SEQADV 6Z69 LEU A 369 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 GLU A 370 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS A 371 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS A 372 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS A 373 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS A 374 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS A 375 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS A 376 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 VAL B 271 UNP A0A1M6Y2K LEU 271 CONFLICT
SEQADV 6Z69 LEU B 369 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 GLU B 370 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS B 371 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS B 372 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS B 373 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS B 374 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS B 375 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z69 HIS B 376 UNP A0A1M6Y2K EXPRESSION TAG
SEQRES 1 A 376 MET THR THR THR SER ASN SER THR GLU THR GLY ARG ARG
SEQRES 2 A 376 PRO GLY ARG LEU GLY ASP PRO ASP ARG CYS LEU ARG THR
SEQRES 3 A 376 ASP PRO ARG THR ASP PRO ARG THR VAL GLU ALA LEU ALA
SEQRES 4 A 376 PRO PHE GLY LEU ASP VAL ASN ALA ALA PRO ALA PRO ILE
SEQRES 5 A 376 GLY PRO ASP ALA PRO ARG GLU GLN GLN LEU GLU TYR ALA
SEQRES 6 A 376 MET GLY ALA GLU ALA ALA PHE GLU GLY VAL PHE ALA ALA
SEQRES 7 A 376 LEU MET ASP GLY LEU ASP PRO VAL PRO GLY ILE GLU ARG
SEQRES 8 A 376 ARG THR GLU THR ILE SER GLY PRO ALA GLY ASN GLU ILE
SEQRES 9 A 376 LYS LEU TYR VAL HIS ARG PRO ALA GLY ALA VAL GLY PRO
SEQRES 10 A 376 LEU PRO GLY ILE PHE HIS ILE HIS GLY GLY GLY MET VAL
SEQRES 11 A 376 ILE LEU GLN ALA ALA GLY PRO VAL TYR VAL ARG PHE ARG
SEQRES 12 A 376 ASP GLU LEU ALA ALA THR GLY THR VAL VAL VAL GLY VAL
SEQRES 13 A 376 GLU TYR ARG ASN GLY ALA GLY VAL LEU GLY PRO HIS PRO
SEQRES 14 A 376 PHE PRO ALA GLY LEU HIS ASP CYS ALA VAL ALA LEU ASP
SEQRES 15 A 376 TRP VAL HIS ALA ARG ARG ALA GLU LEU GLY ILE SER THR
SEQRES 16 A 376 LEU THR VAL ALA GLY GLU SER GLY GLY GLY ASN LEU THR
SEQRES 17 A 376 LEU ALA THR ALA ILE ARG ALA LYS ARG GLU GLY ARG LEU
SEQRES 18 A 376 ASP ALA ILE ASP GLY VAL TYR ALA LEU VAL PRO TYR ILE
SEQRES 19 A 376 SER GLY MET TYR GLY ARG SER ARG GLU GLU ARG GLU ALA
SEQRES 20 A 376 GLU LEU PRO SER LEU VAL GLU CYS ASP GLY TYR PHE ILE
SEQRES 21 A 376 SER CYS ASP LEU CYS ALA VAL PHE VAL GLU VAL TYR ASP
SEQRES 22 A 376 PRO GLY THR ALA HIS LEU THR ASP PRO LEU ALA TRP PRO
SEQRES 23 A 376 TYR HIS ALA ALA ARG GLU ASP LEU VAL GLY LEU PRO PRO
SEQRES 24 A 376 HIS VAL ILE SER VAL ASN GLU VAL ASP PRO LEU ARG ASP
SEQRES 25 A 376 GLU GLY LEU ALA TYR TYR ARG LYS LEU VAL GLU ALA GLY
SEQRES 26 A 376 VAL GLU ALA ARG SER ARG VAL VAL PRO GLY ALA CYS HIS
SEQRES 27 A 376 ALA ALA ASP MET MET PHE ARG LYS ALA ALA PRO ASP MET
SEQRES 28 A 376 TYR GLU ALA THR VAL GLN ASP ILE HIS ASP PHE VAL THR
SEQRES 29 A 376 SER LEU HIS ARG LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 376 MET THR THR THR SER ASN SER THR GLU THR GLY ARG ARG
SEQRES 2 B 376 PRO GLY ARG LEU GLY ASP PRO ASP ARG CYS LEU ARG THR
SEQRES 3 B 376 ASP PRO ARG THR ASP PRO ARG THR VAL GLU ALA LEU ALA
SEQRES 4 B 376 PRO PHE GLY LEU ASP VAL ASN ALA ALA PRO ALA PRO ILE
SEQRES 5 B 376 GLY PRO ASP ALA PRO ARG GLU GLN GLN LEU GLU TYR ALA
SEQRES 6 B 376 MET GLY ALA GLU ALA ALA PHE GLU GLY VAL PHE ALA ALA
SEQRES 7 B 376 LEU MET ASP GLY LEU ASP PRO VAL PRO GLY ILE GLU ARG
SEQRES 8 B 376 ARG THR GLU THR ILE SER GLY PRO ALA GLY ASN GLU ILE
SEQRES 9 B 376 LYS LEU TYR VAL HIS ARG PRO ALA GLY ALA VAL GLY PRO
SEQRES 10 B 376 LEU PRO GLY ILE PHE HIS ILE HIS GLY GLY GLY MET VAL
SEQRES 11 B 376 ILE LEU GLN ALA ALA GLY PRO VAL TYR VAL ARG PHE ARG
SEQRES 12 B 376 ASP GLU LEU ALA ALA THR GLY THR VAL VAL VAL GLY VAL
SEQRES 13 B 376 GLU TYR ARG ASN GLY ALA GLY VAL LEU GLY PRO HIS PRO
SEQRES 14 B 376 PHE PRO ALA GLY LEU HIS ASP CYS ALA VAL ALA LEU ASP
SEQRES 15 B 376 TRP VAL HIS ALA ARG ARG ALA GLU LEU GLY ILE SER THR
SEQRES 16 B 376 LEU THR VAL ALA GLY GLU SER GLY GLY GLY ASN LEU THR
SEQRES 17 B 376 LEU ALA THR ALA ILE ARG ALA LYS ARG GLU GLY ARG LEU
SEQRES 18 B 376 ASP ALA ILE ASP GLY VAL TYR ALA LEU VAL PRO TYR ILE
SEQRES 19 B 376 SER GLY MET TYR GLY ARG SER ARG GLU GLU ARG GLU ALA
SEQRES 20 B 376 GLU LEU PRO SER LEU VAL GLU CYS ASP GLY TYR PHE ILE
SEQRES 21 B 376 SER CYS ASP LEU CYS ALA VAL PHE VAL GLU VAL TYR ASP
SEQRES 22 B 376 PRO GLY THR ALA HIS LEU THR ASP PRO LEU ALA TRP PRO
SEQRES 23 B 376 TYR HIS ALA ALA ARG GLU ASP LEU VAL GLY LEU PRO PRO
SEQRES 24 B 376 HIS VAL ILE SER VAL ASN GLU VAL ASP PRO LEU ARG ASP
SEQRES 25 B 376 GLU GLY LEU ALA TYR TYR ARG LYS LEU VAL GLU ALA GLY
SEQRES 26 B 376 VAL GLU ALA ARG SER ARG VAL VAL PRO GLY ALA CYS HIS
SEQRES 27 B 376 ALA ALA ASP MET MET PHE ARG LYS ALA ALA PRO ASP MET
SEQRES 28 B 376 TYR GLU ALA THR VAL GLN ASP ILE HIS ASP PHE VAL THR
SEQRES 29 B 376 SER LEU HIS ARG LEU GLU HIS HIS HIS HIS HIS HIS
HET HEE A 401 10
HET HEE A 402 10
HET 4MU A 403 13
HET 4MU A 404 13
HET HEE B 401 11
HET MG B 402 1
HETNAM HEE N-HEXYLPHOSPHONATE ETHYL ESTER
HETNAM 4MU 7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE
HETNAM MG MAGNESIUM ION
HETSYN 4MU 4-METHYLUMBELLIFERONE
FORMUL 3 HEE 3(C8 H19 O3 P)
FORMUL 5 4MU 2(C10 H8 O3)
FORMUL 8 MG MG 2+
FORMUL 9 HOH *962(H2 O)
HELIX 1 AA1 PRO A 14 ASP A 19 1 6
HELIX 2 AA2 ASP A 31 ALA A 39 1 9
HELIX 3 AA3 PRO A 40 GLY A 42 5 3
HELIX 4 AA4 PRO A 57 ASP A 81 1 25
HELIX 5 AA5 GLY A 136 THR A 149 1 14
HELIX 6 AA6 ALA A 162 GLY A 166 5 5
HELIX 7 AA7 PRO A 171 ARG A 187 1 17
HELIX 8 AA8 ARG A 187 GLY A 192 1 6
HELIX 9 AA9 SER A 202 GLU A 218 1 17
HELIX 10 AB1 ARG A 220 ILE A 224 5 5
HELIX 11 AB2 SER A 241 LEU A 249 1 9
HELIX 12 AB3 PRO A 250 CYS A 255 1 6
HELIX 13 AB4 SER A 261 ASP A 273 1 13
HELIX 14 AB5 TRP A 285 ALA A 289 5 5
HELIX 15 AB6 ALA A 290 VAL A 295 1 6
HELIX 16 AB7 LEU A 310 ALA A 324 1 15
HELIX 17 AB8 ALA A 339 PHE A 344 1 6
HELIX 18 AB9 ALA A 348 LEU A 366 1 19
HELIX 19 AC1 PRO B 14 ASP B 19 1 6
HELIX 20 AC2 ASP B 31 ALA B 39 1 9
HELIX 21 AC3 PRO B 40 GLY B 42 5 3
HELIX 22 AC4 PRO B 57 ASP B 81 1 25
HELIX 23 AC5 GLY B 136 THR B 149 1 14
HELIX 24 AC6 ALA B 162 GLY B 166 5 5
HELIX 25 AC7 PRO B 171 ARG B 187 1 17
HELIX 26 AC8 ARG B 187 GLY B 192 1 6
HELIX 27 AC9 SER B 202 GLU B 218 1 17
HELIX 28 AD1 ARG B 220 ILE B 224 5 5
HELIX 29 AD2 SER B 241 LEU B 249 1 9
HELIX 30 AD3 PRO B 250 CYS B 255 1 6
HELIX 31 AD4 SER B 261 ASP B 273 1 13
HELIX 32 AD5 TRP B 285 ALA B 289 5 5
HELIX 33 AD6 ALA B 290 VAL B 295 1 6
HELIX 34 AD7 LEU B 310 ALA B 324 1 15
HELIX 35 AD8 ALA B 339 PHE B 344 1 6
HELIX 36 AD9 ALA B 348 LEU B 366 1 19
SHEET 1 AA116 ILE A 89 SER A 97 0
SHEET 2 AA116 GLU A 103 PRO A 111 -1 O ILE A 104 N ILE A 96
SHEET 3 AA116 VAL A 152 GLU A 157 -1 O GLY A 155 N TYR A 107
SHEET 4 AA116 LEU A 118 ILE A 124 1 N ILE A 121 O VAL A 154
SHEET 5 AA116 ILE A 193 GLU A 201 1 O THR A 197 N PHE A 122
SHEET 6 AA116 GLY A 226 LEU A 230 1 O LEU A 230 N GLY A 200
SHEET 7 AA116 HIS A 300 ASN A 305 1 O VAL A 301 N ALA A 229
SHEET 8 AA116 ALA A 328 VAL A 333 1 O ARG A 331 N VAL A 304
SHEET 9 AA116 ALA B 328 VAL B 333 -1 O SER B 330 N SER A 330
SHEET 10 AA116 HIS B 300 ASN B 305 1 N VAL B 304 O VAL B 333
SHEET 11 AA116 GLY B 226 LEU B 230 1 N ALA B 229 O VAL B 301
SHEET 12 AA116 ILE B 193 GLU B 201 1 N VAL B 198 O TYR B 228
SHEET 13 AA116 LEU B 118 ILE B 124 1 N PHE B 122 O THR B 197
SHEET 14 AA116 VAL B 152 GLU B 157 1 O VAL B 154 N ILE B 121
SHEET 15 AA116 GLU B 103 PRO B 111 -1 N TYR B 107 O GLY B 155
SHEET 16 AA116 ILE B 89 SER B 97 -1 N ARG B 92 O VAL B 108
LINK OG SER A 202 P HEE A 401 1555 1555 1.51
LINK P HEE A 402 O1' 4MU A 404 1555 1555 1.48
LINK CB SER B 202 O3P HEE B 401 1555 1555 1.36
LINK MG MG B 402 O HOH B 577 1555 1555 2.98
LINK MG MG B 402 O HOH B 618 1555 1555 2.96
CISPEP 1 GLY A 166 PRO A 167 0 -7.37
CISPEP 2 PHE A 170 PRO A 171 0 1.14
CISPEP 3 GLY B 166 PRO B 167 0 -2.09
CISPEP 4 PHE B 170 PRO B 171 0 2.80
SITE 1 AC1 10 GLY A 127 GLY A 128 TYR A 139 GLU A 201
SITE 2 AC1 10 SER A 202 GLY A 203 TYR A 233 HIS A 338
SITE 3 AC1 10 ALA A 339 4MU A 403
SITE 1 AC2 10 PHE A 72 GLY A 127 GLY A 128 PHE A 259
SITE 2 AC2 10 ILE A 260 SER A 261 LEU A 264 PHE A 268
SITE 3 AC2 10 HEE A 401 HOH A 504
SITE 1 AC3 6 PHE B 76 GLY B 136 PRO B 137 VAL B 138
SITE 2 AC3 6 HOH B 577 HOH B 618
SITE 1 AC4 13 PHE A 41 TYR A 64 GLY A 67 ALA A 68
SITE 2 AC4 13 ALA A 71 PHE A 72 VAL A 75 HOH A 527
SITE 3 AC4 13 HOH A 680 TYR B 64 GLY B 67 ALA B 68
SITE 4 AC4 13 ALA B 71
SITE 1 AC5 11 GLY B 127 GLY B 128 GLU B 201 GLY B 203
SITE 2 AC5 11 GLY B 204 GLY B 205 ASN B 206 LEU B 230
SITE 3 AC5 11 VAL B 231 TYR B 233 HIS B 338
CRYST1 72.410 86.700 110.110 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 0.013810 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011534 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009082 0.00000
TER 2714 ARG A 368
TER 5464 ARG B 368
MASTER 443 0 6 36 16 0 15 6 6456 2 62 58
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