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HEADER HYDROLASE 13-SEP-17 6EHN
TITLE STRUCTURAL INSIGHT INTO A PROMISCUOUS CE15 ESTERASE FROM THE MARINE
TITLE 2 BACTERIAL METAGENOME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE MZ0003;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNKNOWN PROKARYOTIC ORGANISM;
SOURCE 3 ORGANISM_TAXID: 2725;
SOURCE 4 GENE: MZ0003;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, PROTEIN STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.HELLAND,C.DE SANTI,O.GANI,A.K.WILLIAMSON
REVDAT 1 21-MAR-18 6EHN 0
JRNL AUTH C.DE SANTI,O.A.GANI,R.HELLAND,A.WILLIAMSON
JRNL TITL STRUCTURAL INSIGHT INTO A CE15 ESTERASE FROM THE MARINE
JRNL TITL 2 BACTERIAL METAGENOME.
JRNL REF SCI REP V. 7 17278 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 29222424
JRNL DOI 10.1038/S41598-017-17677-4
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0151
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 41585
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2077
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3024
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.3280
REMARK 3 BIN FREE R VALUE SET COUNT : 143
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3090
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : -0.21000
REMARK 3 B33 (A**2) : 0.69000
REMARK 3 B12 (A**2) : -0.11000
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): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.427
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3220 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2957 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4378 ; 2.004 ; 1.933
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6779 ; 1.149 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 403 ;14.626 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 150 ;37.543 ;23.400
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 500 ;15.067 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;20.476 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 461 ; 0.148 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3718 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 785 ; 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): 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 : NULL
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 6EHN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006632.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91840, 1.28202
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43689
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.59300
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: SAD
REMARK 200 SOFTWARE USED: PHASER, SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, 24% NACITRATE, PH 6, 0.1 M,
REMARK 280 PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 52.44400
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 26.22200
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 26.22200
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 52.44400
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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 ASP A 104
REMARK 465 ALA A 105
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 LYS A 33 CG CD CE NZ
REMARK 470 LYS A 38 CG CD CE NZ
REMARK 470 GLN A 45 CG CD OE1 NE2
REMARK 470 LYS A 54 CE NZ
REMARK 470 GLU A 88 CG CD OE1 OE2
REMARK 470 LYS A 89 CG CD CE NZ
REMARK 470 GLU A 90 CG CD OE1 OE2
REMARK 470 ASP A 91 CG OD1 OD2
REMARK 470 LYS A 106 CG CD CE NZ
REMARK 470 LYS A 127 CD CE NZ
REMARK 470 LYS A 140 CE NZ
REMARK 470 LYS A 148 CD CE NZ
REMARK 470 ASP A 200 CB CG OD1 OD2
REMARK 470 GLU A 205 CG CD OE1 OE2
REMARK 470 LYS A 206 NZ
REMARK 470 LYS A 235 CD CE NZ
REMARK 470 LYS A 307 CD CE NZ
REMARK 470 LYS A 362 CG CD CE NZ
REMARK 470 LYS A 363 CE NZ
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 681 O HOH A 705 1.52
REMARK 500 O HOH A 688 O HOH A 863 2.10
REMARK 500 O HOH A 602 O HOH A 863 2.11
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 784 O HOH A 811 4555 1.98
REMARK 500 O HOH A 822 O HOH A 822 4555 2.02
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 THR A 330 CB THR A 330 CG2 -0.248
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 261 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 297 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 322 CD - NE - CZ ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH2 ANGL. DEV. = -8.7 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 LYS A 38 -54.27 -125.41
REMARK 500 MET A 51 -62.34 -133.31
REMARK 500 GLU A 61 74.97 -119.20
REMARK 500 ASP A 66 -62.28 8.36
REMARK 500 ALA A 67 33.09 75.78
REMARK 500 LYS A 68 -96.17 -50.76
REMARK 500 ALA A 76 -64.00 32.99
REMARK 500 ALA A 92 91.30 33.16
REMARK 500 ARG A 108 128.75 -37.92
REMARK 500 ASP A 126 114.63 -28.06
REMARK 500 ASP A 126 114.63 -32.95
REMARK 500 ASN A 186 37.06 -93.13
REMARK 500 SER A 243 -129.64 56.95
REMARK 500 ASP A 303 15.61 56.17
REMARK 500 ASN A 368 35.89 77.82
REMARK 500 HIS A 384 107.02 -54.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 73 GLY A 74 -147.79
REMARK 500 GLY A 74 GLY A 75 -42.54
REMARK 500 GLY A 75 ALA A 76 82.51
REMARK 500 GLU A 90 ASP A 91 -59.06
REMARK 500 ASP A 91 ALA A 92 80.93
REMARK 500 TRP A 209 GLY A 210 46.66
REMARK 500 GLY A 210 THR A 211 138.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 210 -10.71
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 915 DISTANCE = 7.14 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
DBREF1 6EHN A 4 402 UNP CE15_UNKP
DBREF2 6EHN A A0A0K2VM55 29 427
SEQRES 1 A 399 GLY PHE ASN TYR ASP GLU ALA GLN VAL PRO LYS TYR THR
SEQRES 2 A 399 LEU PRO ASP PRO LEU VAL MET VAL ASP GLY THR LYS VAL
SEQRES 3 A 399 THR SER ALA LYS GLN TRP ASN ASP LYS ARG ARG ASP GLU
SEQRES 4 A 399 VAL GLN GLN LEU PHE GLU ALA TYR MET TYR GLY LYS VAL
SEQRES 5 A 399 PRO ASP GLY GLU THR GLU LEU ILE PHE THR ASP ALA LYS
SEQRES 6 A 399 GLY GLU ARG ALA LEU GLY GLY ALA ALA ILE ARG LYS GLN
SEQRES 7 A 399 VAL LYS ILE SER PHE GLY GLU LYS GLU ASP ALA PRO ALA
SEQRES 8 A 399 MET ASP LEU LEU ILE TYR LEU PRO ALA ASP ALA LYS VAL
SEQRES 9 A 399 ARG VAL PRO VAL PHE LEU GLY LEU ASN PHE HIS GLY ASN
SEQRES 10 A 399 HIS THR ILE HIS LYS ASP LYS GLU ILE TRP LEU THR GLU
SEQRES 11 A 399 SER TRP VAL ARG THR ASN LYS LYS PHE GLY ILE THR LYS
SEQRES 12 A 399 ASN LYS ALA ASN GLU LEU SER ARG GLY VAL ALA ALA GLY
SEQRES 13 A 399 ARG TRP GLN ILE GLU LYS ALA ILE ALA LYS GLY TYR GLY
SEQRES 14 A 399 VAL ALA THR ILE TYR CYS GLY ASP ILE ASP PRO ASP PHE
SEQRES 15 A 399 ASN PHE PRO SER ASN GLY ILE GLN ALA TYR TYR TYR LYS
SEQRES 16 A 399 LYS ASP GLN THR ILE PRO GLU LYS GLY GLN TRP GLY THR
SEQRES 17 A 399 ILE ALA ALA TRP ALA PHE GLY LEU SER CYS ALA MET ASP
SEQRES 18 A 399 TYR PHE GLU THR ASP THR ASP ILE ASP HIS LYS LYS VAL
SEQRES 19 A 399 ALA VAL LEU GLY HIS SER ARG LEU GLY LYS THR SER LEU
SEQRES 20 A 399 TRP ALA GLY ALA ILE ASP THR ARG PHE ALA LEU THR ILE
SEQRES 21 A 399 SER ASN CYS SER GLY CYS GLY GLY ALA ALA LEU SER ARG
SEQRES 22 A 399 ARG ARG PHE GLY GLU THR VAL ARG ARG ILE ASN THR SER
SEQRES 23 A 399 PHE PRO HIS TRP PHE CYS SER ARG PHE HIS GLN TYR ASN
SEQRES 24 A 399 ASP LYS GLU ASP LYS LEU PRO ILE ASP GLN HIS MET LEU
SEQRES 25 A 399 ILE ALA LEU CYS ALA PRO ARG PRO VAL LEU ILE ASN SER
SEQRES 26 A 399 ALA THR GLU ASP LYS TRP ALA ASP PRO HIS GLY GLU PHE
SEQRES 27 A 399 LEU ALA ALA GLN GLY ALA ASP ALA VAL TYR ARG MET LEU
SEQRES 28 A 399 GLY THR GLY GLY LEU ASP ALA LYS LYS TRP PRO GLU PRO
SEQRES 29 A 399 ASN LYS LEU VAL LYS SER THR ILE GLY TYR HIS LEU ARG
SEQRES 30 A 399 PRO GLY LYS HIS ASP VAL THR ALA ARG ASP TRP ASP VAL
SEQRES 31 A 399 TYR ILE GLU PHE ALA ASP HIS HIS MET
HET GOL A 501 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *315(H2 O)
HELIX 1 AA1 ASP A 8 VAL A 12 5 5
HELIX 2 AA2 SER A 31 LYS A 38 1 8
HELIX 3 AA3 LYS A 38 MET A 51 1 14
HELIX 4 AA4 LEU A 73 GLY A 75 5 3
HELIX 5 AA5 GLY A 119 ILE A 123 5 5
HELIX 6 AA6 ASN A 150 ARG A 154 5 5
HELIX 7 AA7 ALA A 157 TRP A 161 5 5
HELIX 8 AA8 GLN A 162 LYS A 169 1 8
HELIX 9 AA9 CYS A 178 ASP A 182 1 5
HELIX 10 AB1 GLY A 191 LYS A 198 1 8
HELIX 11 AB2 PRO A 204 GLN A 208 5 5
HELIX 12 AB3 GLY A 210 ASP A 229 1 20
HELIX 13 AB4 SER A 243 ASP A 256 1 14
HELIX 14 AB5 LEU A 274 ARG A 278 5 5
HELIX 15 AB6 THR A 282 PHE A 290 1 9
HELIX 16 AB7 CYS A 295 ASN A 302 5 8
HELIX 17 AB8 LYS A 304 LEU A 308 5 5
HELIX 18 AB9 ASP A 311 CYS A 319 1 9
HELIX 19 AC1 ASP A 332 ALA A 335 5 4
HELIX 20 AC2 ASP A 336 ALA A 347 1 12
HELIX 21 AC3 ALA A 347 LEU A 354 1 8
HELIX 22 AC4 THR A 387 MET A 402 1 16
SHEET 1 AA1 3 LEU A 62 PHE A 64 0
SHEET 2 AA1 3 ALA A 77 PHE A 86 -1 O SER A 85 N ILE A 63
SHEET 3 AA1 3 GLU A 70 ALA A 72 -1 N GLU A 70 O ARG A 79
SHEET 1 AA2 9 LEU A 62 PHE A 64 0
SHEET 2 AA2 9 ALA A 77 PHE A 86 -1 O SER A 85 N ILE A 63
SHEET 3 AA2 9 ALA A 94 PRO A 102 -1 O LEU A 97 N VAL A 82
SHEET 4 AA2 9 GLY A 172 TYR A 177 -1 O VAL A 173 N TYR A 100
SHEET 5 AA2 9 VAL A 109 ASN A 116 1 N ASN A 116 O ILE A 176
SHEET 6 AA2 9 ILE A 232 LEU A 240 1 O ALA A 238 N LEU A 113
SHEET 7 AA2 9 LEU A 261 ASN A 265 1 O ILE A 263 N VAL A 239
SHEET 8 AA2 9 VAL A 324 ALA A 329 1 O LEU A 325 N THR A 262
SHEET 9 AA2 9 ILE A 375 ARG A 380 1 O GLY A 376 N VAL A 324
CISPEP 1 ALA A 320 PRO A 321 0 8.68
SITE 1 AC1 8 SER A 243 ARG A 244 LYS A 247 GLU A 281
SITE 2 AC1 8 ILE A 286 TRP A 334 HOH A 622 HOH A 761
CRYST1 110.212 110.212 78.666 90.00 90.00 120.00 P 32 2 1 6
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 0.009073 0.005239 0.000000 0.00000
SCALE2 0.000000 0.010477 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012712 0.00000
TER 3128 MET A 402
MASTER 437 0 1 22 12 0 2 6 3411 1 6 31
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