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HEADER HYDROLASE 28-MAY-20 6Z68
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 6Z68 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. 1.35 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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 153608
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) : 0.138
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1994
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6671
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 88
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5429
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 936
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.99000
REMARK 3 B22 (A**2) : 1.85000
REMARK 3 B33 (A**2) : 1.13000
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): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.052
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.051
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.086
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5702 ; 0.017 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5307 ; 0.005 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7776 ; 2.006 ; 1.649
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12254 ; 1.617 ; 1.571
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 746 ; 6.234 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 316 ;27.600 ;20.095
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 837 ;12.673 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;17.858 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 717 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6577 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1252 ; 0.002 ; 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): 11009 ; 7.916 ; 3.000
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 6Z68 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_1292108901.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-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 : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976246
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 155980
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 55.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.6400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.40
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
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: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: XXXX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25 M MAGNESIUM CHLORIDE, 0.1 M TRIS
REMARK 280 PH 8.5 AND 35 % (W/V) PEG 4000 WITH 0.01 M TCEP, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 29.35500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.25500
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 29.35500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 81.25500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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 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 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 SER B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 THR B 8
REMARK 465 GLU B 9
REMARK 465 THR B 10
REMARK 465 GLY B 11
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 12 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 310 CD2
REMARK 470 HIS A 374 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 12 CG CD NE CZ NH1 NH2
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 528 O HOH B 890 1.79
REMARK 500 O HOH A 929 O HOH B 890 1.82
REMARK 500 O HOH A 893 O HOH B 573 1.83
REMARK 500 O HOH A 893 O HOH B 945 1.92
REMARK 500 O HOH B 872 O HOH B 954 1.97
REMARK 500 O HOH A 538 O HOH A 893 1.99
REMARK 500 O HOH B 513 O HOH B 558 2.04
REMARK 500 O HOH A 559 O HOH A 694 2.05
REMARK 500 OD1 ASP B 312 O HOH B 501 2.06
REMARK 500 O HOH B 872 O HOH B 922 2.07
REMARK 500 O HOH A 884 O HOH A 918 2.08
REMARK 500 O HOH B 587 O HOH B 872 2.08
REMARK 500 O HOH B 558 O HOH B 890 2.09
REMARK 500 O HOH A 765 O HOH A 918 2.09
REMARK 500 OE1 GLU A 94 O HOH A 501 2.10
REMARK 500 O HOH B 752 O HOH B 755 2.11
REMARK 500 O HOH A 795 O HOH A 918 2.12
REMARK 500 O HOH A 918 O HOH B 925 2.14
REMARK 500 O HOH B 872 O HOH B 898 2.14
REMARK 500 O HOH A 776 O HOH A 918 2.15
REMARK 500 O HOH A 743 O HOH A 893 2.16
REMARK 500 O HOH A 513 O HOH A 646 2.17
REMARK 500 O HOH B 766 O HOH B 832 2.18
REMARK 500 O HOH A 745 O HOH A 844 2.18
REMARK 500 O HOH B 890 O HOH B 915 2.19
REMARK 500 NH2 ARG B 319 O HOH B 502 2.19
REMARK 500 O HOH B 836 O HOH B 872 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 13 C PRO A 14 N 0.125
REMARK 500 GLU A 243 CD GLU A 243 OE1 0.115
REMARK 500 GLU A 243 CD GLU A 243 OE2 0.206
REMARK 500 GLU A 270 CD GLU A 270 OE1 0.122
REMARK 500 PRO A 274 N PRO A 274 CA 0.192
REMARK 500 ARG A 329 CZ ARG A 329 NH2 0.089
REMARK 500 GLU B 63 CD GLU B 63 OE1 0.072
REMARK 500 GLU B 63 CD GLU B 63 OE2 0.104
REMARK 500 GLU B 73 CD GLU B 73 OE2 0.082
REMARK 500 GLU B 243 CD GLU B 243 OE1 0.083
REMARK 500 GLU B 243 CD GLU B 243 OE2 0.139
REMARK 500 PRO B 274 C GLY B 275 N 0.150
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 13 CG - CD - NE ANGL. DEV. = -17.8 DEGREES
REMARK 500 ARG A 13 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 TYR A 258 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 PRO A 274 C - N - CA ANGL. DEV. = 11.4 DEGREES
REMARK 500 ASP A 312 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG B 29 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 GLU B 73 CG - CD - OE1 ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG B 92 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP B 144 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 TYR B 258 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG B 311 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 329 CG - CD - NE ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG B 329 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 329 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 329 NE - CZ - NH2 ANGL. DEV. = 4.5 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 LEU A 132 152.40 81.08
REMARK 500 SER A 194 -93.62 -92.36
REMARK 500 SER A 202 -119.58 62.48
REMARK 500 VAL A 231 53.93 34.31
REMARK 500 PHE A 259 -52.90 76.29
REMARK 500 PHE A 344 52.68 -100.40
REMARK 500 HIS A 373 131.71 -38.98
REMARK 500 LEU B 132 152.94 84.23
REMARK 500 SER B 194 -87.04 -92.39
REMARK 500 SER B 202 -118.92 67.11
REMARK 500 VAL B 231 53.10 33.11
REMARK 500 PHE B 259 -55.40 76.99
REMARK 500 VAL B 307 41.00 -109.91
REMARK 500 PHE B 344 50.38 -97.30
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 971 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 972 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 973 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A 974 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 975 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 976 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH A 977 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH B 957 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B 958 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH B 959 DISTANCE = 6.70 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 403
DBREF1 6Z68 A 1 368 UNP A0A1M6Y2K1_PSETH
DBREF2 6Z68 A A0A1M6Y2K1 1 368
DBREF1 6Z68 B 1 368 UNP A0A1M6Y2K1_PSETH
DBREF2 6Z68 B A0A1M6Y2K1 1 368
SEQADV 6Z68 VAL A 271 UNP A0A1M6Y2K LEU 271 CONFLICT
SEQADV 6Z68 LEU A 369 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 GLU A 370 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS A 371 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS A 372 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS A 373 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS A 374 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS A 375 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS A 376 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 VAL B 271 UNP A0A1M6Y2K LEU 271 CONFLICT
SEQADV 6Z68 LEU B 369 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 GLU B 370 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS B 371 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS B 372 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS B 373 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS B 374 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 HIS B 375 UNP A0A1M6Y2K EXPRESSION TAG
SEQADV 6Z68 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 PEG A 401 7
HET PG4 A 402 13
HET PEG B 401 7
HET PG4 B 402 13
HET MG B 403 1
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM MG MAGNESIUM ION
FORMUL 3 PEG 2(C4 H10 O3)
FORMUL 4 PG4 2(C8 H18 O5)
FORMUL 7 MG MG 2+
FORMUL 8 HOH *936(H2 O)
HELIX 1 AA1 PRO A 14 ASP A 19 1 6
HELIX 2 AA2 CYS A 23 ASP A 27 5 5
HELIX 3 AA3 ASP A 31 ALA A 39 1 9
HELIX 4 AA4 PRO A 40 GLY A 42 5 3
HELIX 5 AA5 PRO A 57 ASP A 81 1 25
HELIX 6 AA6 GLY A 136 THR A 149 1 14
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 GLY A 219 1 18
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 ARG A 368 HIS A 372 5 5
HELIX 20 AC2 PRO B 14 ASP B 19 1 6
HELIX 21 AC3 ASP B 31 ALA B 39 1 9
HELIX 22 AC4 PRO B 40 GLY B 42 5 3
HELIX 23 AC5 PRO B 57 ASP B 81 1 25
HELIX 24 AC6 GLY B 136 THR B 149 1 14
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 GLY B 219 1 18
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 VAL A 108 N ARG A 92
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 195 N GLY A 120
SHEET 6 AA116 GLY A 226 LEU A 230 1 O TYR A 228 N VAL A 198
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 ARG B 331
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
CISPEP 1 GLY A 166 PRO A 167 0 1.57
CISPEP 2 PHE A 170 PRO A 171 0 5.08
CISPEP 3 GLY B 166 PRO B 167 0 -2.92
CISPEP 4 PHE B 170 PRO B 171 0 7.15
SITE 1 AC1 7 GLY A 126 GLY A 127 TYR A 139 GLU A 201
SITE 2 AC1 7 SER A 202 HOH A 515 HOH A 867
SITE 1 AC2 7 PHE A 41 ALA A 68 ALA A 71 PHE A 72
SITE 2 AC2 7 HOH A 692 HOH A 721 HOH A 778
SITE 1 AC3 4 PHE B 76 TYR B 139 ALA B 339 HOH B 674
SITE 1 AC4 5 PHE B 41 ALA B 68 PHE B 72 HOH B 593
SITE 2 AC4 5 HOH B 750
SITE 1 AC5 3 ARG A 58 HOH A 816 ARG B 58
CRYST1 58.710 77.190 162.510 90.00 90.00 90.00 P 21 2 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 0.017033 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012955 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006153 0.00000
TER 2774 HIS A 374
TER 5509 ARG B 368
MASTER 463 0 5 36 16 0 8 6 6406 2 40 58
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