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HEADER HYDROLASE 22-SEP-15 5DWD
TITLE CRYSTAL STRUCTURE OF ESTERASE PE8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-219;
COMPND 5 SYNONYM: PHOSPHOLIPASE/CARBOXYLESTERASE FAMILY PROTEIN;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PELAGIBACTERIUM HALOTOLERANS (STRAIN JCM 15775
SOURCE 3 / CGMCC 1.7692 / B2);
SOURCE 4 ORGANISM_TAXID: 1082931;
SOURCE 5 STRAIN: JCM 15775 / CGMCC 1.7692 / B2;
SOURCE 6 GENE: KKY_2995;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ESTERASE, PE8, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LI,J.HUANG
REVDAT 1 26-OCT-16 5DWD 0
JRNL AUTH J.LI,J.HUANG
JRNL TITL STRUCTURE OF ESTERASE PE8
JRNL REF TO BE PUBLISHED
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 43312
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) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2304
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) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2812
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.1940
REMARK 3 BIN FREE R VALUE SET COUNT : 149
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3230
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 325
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.61000
REMARK 3 B22 (A**2) : 0.48000
REMARK 3 B33 (A**2) : -0.59000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.093
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.098
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.946
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3331 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3253 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4546 ; 2.063 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7491 ; 1.161 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 435 ; 6.771 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;34.525 ;23.782
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 488 ;14.533 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;15.857 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 532 ; 0.168 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3735 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 689 ; 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): 1749 ; 2.418 ; 2.295
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1748 ; 2.401 ; 2.293
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2181 ; 3.449 ; 3.430
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2182 ; 3.456 ; 3.432
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1582 ; 3.547 ; 2.659
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1582 ; 3.544 ; 2.659
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2366 ; 5.231 ; 3.843
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3925 ; 7.393 ;20.334
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3926 ; 7.393 ;20.335
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
REMARK 4
REMARK 4 5DWD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213923.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9785
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45616
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 64.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.5400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M CALCIUM CHLORIDE DEHYDRATE;0.1M
REMARK 280 BIS-TRIS PH 6.5;30%(V/V) POLYETHYLENE GLYCOL MONOMETHYL ETHER
REMARK 280 550, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 36.69900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 GLU A 3
REMARK 465 PRO A 4
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 VAL A 5 CG1 CG2
REMARK 470 LYS A 6 CG CD CE NZ
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 ARG B -3 CG CD NE CZ NH1 NH2
REMARK 470 THR B 2 OG1 CG2
REMARK 470 LYS B 6 CG CD CE NZ
REMARK 470 GLU B 76 CG CD OE1 OE2
REMARK 470 GLU B 149 CG CD OE1 OE2
REMARK 470 GLN B 197 CG CD OE1 NE2
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 C LEU A 219 O HOH A 302 1.80
REMARK 500 O HOH A 315 O HOH A 317 2.03
REMARK 500 O HOH A 387 O HOH A 415 2.13
REMARK 500 O GLY B 17 O HOH B 401 2.17
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 ASP B 32 CB - CG - OD1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG B 192 NE - CZ - NH2 ANGL. DEV. = -3.3 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 SER A 118 -121.00 62.02
REMARK 500 LEU B -6 -179.02 102.65
REMARK 500 VAL B -5 103.98 173.85
REMARK 500 SER B 31 -160.42 -105.19
REMARK 500 SER B 118 -120.31 59.95
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 B -6 VAL B -5 -142.48
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 450 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH B 574 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B 575 DISTANCE = 5.97 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
DBREF 5DWD A 1 219 UNP G4RFI7 G4RFI7_PELHB 1 219
DBREF 5DWD B 1 219 UNP G4RFI7 G4RFI7_PELHB 1 219
SEQADV 5DWD MET A -20 UNP G4RFI7 INITIATING METHIONINE
SEQADV 5DWD GLY A -19 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER A -18 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER A -17 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A -16 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A -15 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A -14 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A -13 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A -12 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A -11 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A -10 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER A -9 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER A -8 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD GLY A -7 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD LEU A -6 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD VAL A -5 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD PRO A -4 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD ARG A -3 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD GLY A -2 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER A -1 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS A 0 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD MET B -20 UNP G4RFI7 INITIATING METHIONINE
SEQADV 5DWD GLY B -19 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER B -18 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER B -17 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B -16 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B -15 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B -14 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B -13 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B -12 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B -11 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B -10 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER B -9 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER B -8 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD GLY B -7 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD LEU B -6 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD VAL B -5 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD PRO B -4 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD ARG B -3 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD GLY B -2 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD SER B -1 UNP G4RFI7 EXPRESSION TAG
SEQADV 5DWD HIS B 0 UNP G4RFI7 EXPRESSION TAG
SEQRES 1 A 240 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 A 240 GLY LEU VAL PRO ARG GLY SER HIS MET THR GLU PRO VAL
SEQRES 3 A 240 LYS LEU SER GLY PRO MET LEU PRO ALA VAL SER GLY ALA
SEQRES 4 A 240 ALA LYS SER LEU VAL VAL LEU LEU HIS GLY TYR GLY SER
SEQRES 5 A 240 ASP GLY ARG ASP LEU ILE ALA LEU GLY GLN PHE TRP ARG
SEQRES 6 A 240 ASP SER PHE PRO ASP THR MET PHE VAL ALA PRO ASN ALA
SEQRES 7 A 240 PRO HIS VAL CYS GLY GLY ASN PRO PHE GLY TYR GLU TRP
SEQRES 8 A 240 PHE PRO LEU ASP LEU GLU ARG ASP ARG THR LEU ALA ARG
SEQRES 9 A 240 LEU ALA GLY ALA GLU THR ALA HIS PRO VAL LEU ASP ALA
SEQRES 10 A 240 PHE LEU ALA ASP LEU TRP ALA GLN THR GLY LEU GLY PRO
SEQRES 11 A 240 ALA ASP THR ILE LEU VAL GLY PHE SER GLN GLY ALA MET
SEQRES 12 A 240 MET ALA LEU TYR THR GLY LEU ARG LEU PRO GLU PRO LEU
SEQRES 13 A 240 LYS ALA ILE ILE ALA PHE SER GLY LEU ILE VAL ALA PRO
SEQRES 14 A 240 GLU LYS LEU GLU ALA GLU ILE ALA SER LYS PRO PRO VAL
SEQRES 15 A 240 LEU LEU ILE HIS GLY ASP LEU ASP ASP VAL VAL PRO VAL
SEQRES 16 A 240 ILE GLY SER GLU THR ALA LEU PRO LYS LEU ILE ASP LEU
SEQRES 17 A 240 GLY ILE ASP ALA ARG LEU HIS ILE SER GLN GLY SER GLY
SEQRES 18 A 240 HIS THR ILE ALA GLN ASP GLY LEU ASP THR ALA THR ALA
SEQRES 19 A 240 PHE LEU ARG GLU ILE LEU
SEQRES 1 B 240 MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER
SEQRES 2 B 240 GLY LEU VAL PRO ARG GLY SER HIS MET THR GLU PRO VAL
SEQRES 3 B 240 LYS LEU SER GLY PRO MET LEU PRO ALA VAL SER GLY ALA
SEQRES 4 B 240 ALA LYS SER LEU VAL VAL LEU LEU HIS GLY TYR GLY SER
SEQRES 5 B 240 ASP GLY ARG ASP LEU ILE ALA LEU GLY GLN PHE TRP ARG
SEQRES 6 B 240 ASP SER PHE PRO ASP THR MET PHE VAL ALA PRO ASN ALA
SEQRES 7 B 240 PRO HIS VAL CYS GLY GLY ASN PRO PHE GLY TYR GLU TRP
SEQRES 8 B 240 PHE PRO LEU ASP LEU GLU ARG ASP ARG THR LEU ALA ARG
SEQRES 9 B 240 LEU ALA GLY ALA GLU THR ALA HIS PRO VAL LEU ASP ALA
SEQRES 10 B 240 PHE LEU ALA ASP LEU TRP ALA GLN THR GLY LEU GLY PRO
SEQRES 11 B 240 ALA ASP THR ILE LEU VAL GLY PHE SER GLN GLY ALA MET
SEQRES 12 B 240 MET ALA LEU TYR THR GLY LEU ARG LEU PRO GLU PRO LEU
SEQRES 13 B 240 LYS ALA ILE ILE ALA PHE SER GLY LEU ILE VAL ALA PRO
SEQRES 14 B 240 GLU LYS LEU GLU ALA GLU ILE ALA SER LYS PRO PRO VAL
SEQRES 15 B 240 LEU LEU ILE HIS GLY ASP LEU ASP ASP VAL VAL PRO VAL
SEQRES 16 B 240 ILE GLY SER GLU THR ALA LEU PRO LYS LEU ILE ASP LEU
SEQRES 17 B 240 GLY ILE ASP ALA ARG LEU HIS ILE SER GLN GLY SER GLY
SEQRES 18 B 240 HIS THR ILE ALA GLN ASP GLY LEU ASP THR ALA THR ALA
SEQRES 19 B 240 PHE LEU ARG GLU ILE LEU
HET 1PG B 301 17
HET GOL B 302 6
HETNAM 1PG 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-
HETNAM 2 1PG ETHANOL
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 1PG C11 H24 O6
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *325(H2 O)
HELIX 1 AA1 ASP A 32 ASP A 45 1 14
HELIX 2 AA2 ARG A 79 GLY A 106 1 28
HELIX 3 AA3 GLY A 108 ALA A 110 5 3
HELIX 4 AA4 SER A 118 LEU A 129 1 12
HELIX 5 AA5 ALA A 147 ILE A 155 1 9
HELIX 6 AA6 VAL A 174 LEU A 187 1 14
HELIX 7 AA7 ALA A 204 LEU A 219 1 16
HELIX 8 AA8 ASP B 32 ASP B 45 1 14
HELIX 9 AA9 ARG B 79 GLY B 106 1 28
HELIX 10 AB1 GLY B 108 ALA B 110 5 3
HELIX 11 AB2 SER B 118 LEU B 129 1 12
HELIX 12 AB3 ALA B 147 ILE B 155 1 9
HELIX 13 AB4 VAL B 174 LEU B 187 1 14
HELIX 14 AB5 ALA B 204 LEU B 219 1 16
SHEET 1 AA1 7 MET A 11 LEU A 12 0
SHEET 2 AA1 7 THR A 50 VAL A 53 -1 O PHE A 52 N LEU A 12
SHEET 3 AA1 7 SER A 21 LEU A 26 1 N LEU A 25 O VAL A 53
SHEET 4 AA1 7 THR A 112 PHE A 117 1 O ILE A 113 N LEU A 22
SHEET 5 AA1 7 ALA A 137 PHE A 141 1 O PHE A 141 N GLY A 116
SHEET 6 AA1 7 VAL A 161 GLY A 166 1 O LEU A 162 N ALA A 140
SHEET 7 AA1 7 ALA A 191 SER A 196 1 O ARG A 192 N LEU A 163
SHEET 1 AA2 2 HIS A 59 CYS A 61 0
SHEET 2 AA2 2 ASN A 64 GLU A 69 -1 O GLU A 69 N HIS A 59
SHEET 1 AA3 7 MET B 11 LEU B 12 0
SHEET 2 AA3 7 THR B 50 VAL B 53 -1 O PHE B 52 N LEU B 12
SHEET 3 AA3 7 SER B 21 LEU B 26 1 N LEU B 25 O VAL B 53
SHEET 4 AA3 7 THR B 112 PHE B 117 1 O VAL B 115 N VAL B 24
SHEET 5 AA3 7 ALA B 137 PHE B 141 1 O PHE B 141 N GLY B 116
SHEET 6 AA3 7 VAL B 161 GLY B 166 1 O LEU B 162 N ALA B 140
SHEET 7 AA3 7 ALA B 191 SER B 196 1 O ARG B 192 N LEU B 163
SHEET 1 AA4 2 HIS B 59 CYS B 61 0
SHEET 2 AA4 2 ASN B 64 GLU B 69 -1 O GLU B 69 N HIS B 59
SITE 1 AC1 7 TYR A 29 GLY A 63 GLY B 63 ASN B 64
SITE 2 AC1 7 ARG B 79 ARG B 83 HOH B 532
SITE 1 AC2 10 GLY A 30 SER A 31 ASP A 35 ASN A 64
SITE 2 AC2 10 PHE A 66 HOH A 367 ASP B 35 ASN B 64
SITE 3 AC2 10 PHE B 66 HOH B 433
CRYST1 41.772 73.398 66.403 90.00 102.37 90.00 P 1 21 1 4
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 0.023939 0.000000 0.005251 0.00000
SCALE2 0.000000 0.013624 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015418 0.00000
TER 1591 LEU A 219
TER 3232 LEU B 219
MASTER 382 0 2 14 18 0 5 6 3578 2 23 38
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