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HEADER HYDROLASE 29-JAN-09 2ZYS
TITLE A. FULGIDUS LIPASE WITH FATTY ACID FRAGMENT AND CHLORIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE, PUTATIVE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 GENE: AF_1763;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-23A(+)
KEYWDS LIPASE, ARCHAEOGLOBUS FULGIDUS, FATTY ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.K.CHEN,T.P.KO,R.T.GUO,A.H.WANG
REVDAT 1 16-JUN-09 2ZYS 0
JRNL AUTH C.K.CHEN,G.C.LEE,T.P.KO,R.T.GUO,L.M.HUANG,H.J.LIU,
JRNL AUTH 2 Y.F.HO,J.F.SHAW,A.H.WANG
JRNL TITL STRUCTURE OF THE ALKALOHYPERTHERMOPHILIC
JRNL TITL 2 ARCHAEOGLOBUS FULGIDUS LIPASE CONTAINS A UNIQUE
JRNL TITL 3 C-TERMINAL DOMAIN ESSENTIAL FOR LONG-CHAIN
JRNL TITL 4 SUBSTRATE BINDING.
JRNL REF J.MOL.BIOL. 2009
JRNL REFN ESSN 1089-8638
JRNL PMID 19447113
JRNL DOI 10.1016/J.JMB.2009.05.017
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 10287
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 SET) : 0.184
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 542
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.21
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE : 0.4570
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 37
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3632
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 14
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.46
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : 1.90
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZYS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB028595.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10557
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 2ZYH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 100MM CAPS PH 10.5,
REMARK 280 200MM NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 29.51050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.26575
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.75525
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A 1
REMARK 465 ARG A 2
REMARK 465 GLY A 3
REMARK 465 LEU A 4
REMARK 465 ALA A 5
REMARK 465 VAL A 6
REMARK 465 LEU A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 VAL A 11
REMARK 465 PHE A 12
REMARK 465 ALA A 13
REMARK 465 VAL A 14
REMARK 465 GLN A 15
REMARK 465 VAL A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
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 GLY A 190 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 LEU A 357 CA - CB - CG ANGL. DEV. = 16.5 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 SER A 34 -178.12 -175.59
REMARK 500 TYR A 50 123.48 -30.34
REMARK 500 GLU A 70 5.72 -60.30
REMARK 500 GLU A 81 -54.54 -12.98
REMARK 500 GLU A 120 -9.35 -48.87
REMARK 500 SER A 136 -127.13 48.83
REMARK 500 SER A 149 173.66 176.72
REMARK 500 ASP A 163 49.99 34.33
REMARK 500 ALA A 185 34.53 -96.10
REMARK 500 LEU A 186 61.09 -157.83
REMARK 500 ALA A 188 -2.66 -52.95
REMARK 500 HIS A 210 -77.15 -2.04
REMARK 500 ALA A 233 -73.94 -47.81
REMARK 500 ALA A 255 -40.94 65.29
REMARK 500 ASN A 257 27.21 48.45
REMARK 500 GLU A 271 3.99 -48.70
REMARK 500 ASP A 323 132.24 -39.44
REMARK 500 TRP A 326 21.49 -140.46
REMARK 500 LEU A 336 35.14 -90.45
REMARK 500 ASP A 337 82.91 -45.86
REMARK 500 LYS A 363 105.10 175.78
REMARK 500 CYS A 387 58.30 -108.74
REMARK 500 THR A 388 -172.36 -67.61
REMARK 500 ARG A 406 106.78 -58.21
REMARK 500 SER A 412 77.69 -103.02
REMARK 500 PHE A 426 -0.94 78.23
REMARK 500 ALA A 436 37.80 -80.31
REMARK 500 LYS A 477 8.96 -68.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 473 0.08 SIDE_CHAIN
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 505 DISTANCE = 8.17 ANGSTROMS
REMARK 525 HOH A 509 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH A 514 DISTANCE = 8.50 ANGSTROMS
REMARK 525 HOH A 522 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH A 525 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 529 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH A 530 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH A 533 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A 536 DISTANCE = 8.99 ANGSTROMS
REMARK 525 HOH A 537 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 538 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH A 539 DISTANCE = 7.77 ANGSTROMS
REMARK 525 HOH A 543 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH A 553 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 562 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH A 568 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH A 570 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 572 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH A 577 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH A 584 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH A 585 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 591 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH A 595 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH A 598 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A 599 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A 606 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH A 608 DISTANCE = 7.05 ANGSTROMS
REMARK 525 HOH A 612 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A 614 DISTANCE = 8.99 ANGSTROMS
REMARK 525 HOH A 615 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH A 619 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 621 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH A 623 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH A 629 DISTANCE = 6.98 ANGSTROMS
REMARK 525 HOH A 638 DISTANCE = 7.33 ANGSTROMS
REMARK 525 HOH A 639 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH A 640 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH A 641 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH A 643 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH A 644 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH A 647 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A 648 DISTANCE = 7.74 ANGSTROMS
REMARK 525 HOH A 649 DISTANCE = 7.12 ANGSTROMS
REMARK 525 HOH A 651 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH A 654 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 656 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A 657 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH A 660 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A 662 DISTANCE = 7.51 ANGSTROMS
REMARK 525 HOH A 665 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A 666 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A 668 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH A 669 DISTANCE = 8.55 ANGSTROMS
REMARK 525 HOH A 670 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH A 671 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH A 675 DISTANCE = 8.96 ANGSTROMS
REMARK 525 HOH A 678 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 681 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH A 682 DISTANCE = 10.10 ANGSTROMS
REMARK 525 HOH A 683 DISTANCE = 9.68 ANGSTROMS
REMARK 525 HOH A 686 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A 687 DISTANCE = 9.55 ANGSTROMS
REMARK 525 HOH A 689 DISTANCE = 7.48 ANGSTROMS
REMARK 525 HOH A 690 DISTANCE = 8.19 ANGSTROMS
REMARK 525 HOH A 691 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH A 692 DISTANCE = 8.31 ANGSTROMS
REMARK 525 HOH A 693 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH A 694 DISTANCE = 7.28 ANGSTROMS
REMARK 525 HOH A 695 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A 696 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH A 697 DISTANCE = 8.54 ANGSTROMS
REMARK 525 HOH A 698 DISTANCE = 8.62 ANGSTROMS
REMARK 525 HOH A 701 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH A 702 DISTANCE = 9.24 ANGSTROMS
REMARK 525 HOH A 703 DISTANCE = 9.29 ANGSTROMS
REMARK 525 HOH A 704 DISTANCE = 8.83 ANGSTROMS
REMARK 525 HOH A 705 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 706 DISTANCE = 7.62 ANGSTROMS
REMARK 525 HOH A 707 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH A 708 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 710 DISTANCE = 7.23 ANGSTROMS
REMARK 525 HOH A 712 DISTANCE = 10.08 ANGSTROMS
REMARK 525 HOH A 713 DISTANCE = 10.32 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZYH RELATED DB: PDB
REMARK 900 RELATED ID: 2ZYI RELATED DB: PDB
REMARK 900 RELATED ID: 2ZYR RELATED DB: PDB
DBREF 2ZYS A 1 474 UNP O28511 O28511_ARCFU 1 474
SEQADV 2ZYS VAL A 475 UNP O28511 EXPRESSION TAG
SEQADV 2ZYS ASP A 476 UNP O28511 EXPRESSION TAG
SEQADV 2ZYS LYS A 477 UNP O28511 EXPRESSION TAG
SEQADV 2ZYS LEU A 478 UNP O28511 EXPRESSION TAG
SEQADV 2ZYS ALA A 479 UNP O28511 EXPRESSION TAG
SEQRES 1 A 479 MET ARG GLY LEU ALA VAL LEU VAL LEU LEU VAL PHE ALA
SEQRES 2 A 479 VAL GLN VAL ALA ALA ALA GLU ASP PHE ARG PRO VAL VAL
SEQRES 3 A 479 PHE VAL HIS GLY LEU ALA GLY SER ALA GLY GLN PHE GLU
SEQRES 4 A 479 SER GLN GLY MET ARG PHE ALA ALA ASN GLY TYR PRO ALA
SEQRES 5 A 479 GLU TYR VAL LYS THR PHE GLU TYR ASP THR ILE SER TRP
SEQRES 6 A 479 ALA LEU VAL VAL GLU THR ASP MET LEU PHE SER GLY LEU
SEQRES 7 A 479 GLY SER GLU PHE GLY LEU ASN ILE SER GLN ILE ILE ASP
SEQRES 8 A 479 PRO GLU THR LEU ASP LYS ILE LEU SER LYS SER ARG GLU
SEQRES 9 A 479 ARG LEU ILE ASP GLU THR PHE SER ARG LEU ASP ARG VAL
SEQRES 10 A 479 ILE ASP GLU ALA LEU ALA GLU SER GLY ALA ASP LYS VAL
SEQRES 11 A 479 ASP LEU VAL GLY HIS SER MET GLY THR PHE PHE LEU VAL
SEQRES 12 A 479 ARG TYR VAL ASN SER SER PRO GLU ARG ALA ALA LYS VAL
SEQRES 13 A 479 ALA HIS LEU ILE LEU LEU ASP GLY VAL TRP GLY VAL ASP
SEQRES 14 A 479 ALA PRO GLU GLY ILE PRO THR LEU ALA VAL PHE GLY ASN
SEQRES 15 A 479 PRO LYS ALA LEU PRO ALA LEU GLY LEU PRO GLU GLU LYS
SEQRES 16 A 479 VAL VAL TYR ASN ALA THR ASN VAL TYR PHE ASN ASN MET
SEQRES 17 A 479 THR HIS VAL GLN LEU CYS THR SER PRO GLU THR PHE ALA
SEQRES 18 A 479 VAL MET PHE GLU PHE ILE ASN GLY TYR LYS PRO ALA THR
SEQRES 19 A 479 THR ASP ILE VAL PRO GLN ASP GLY ASP TYR VAL LYS VAL
SEQRES 20 A 479 LYS GLY LYS PHE LEU ALA PHE ALA THR ASN GLY ASP VAL
SEQRES 21 A 479 SER GLY TRP LEU SER ILE TYR PRO ILE ASP GLU ASN GLY
SEQRES 22 A 479 LYS ARG LEU THR ARG LEU PRO VAL LYS PHE MET ARG VAL
SEQRES 23 A 479 LYS GLY ASP PHE GLU VAL ARG LEU ARG LYS GLY GLN LEU
SEQRES 24 A 479 TYR GLU PHE GLN PHE ARG LYS ASP PHE SER PRO ILE ILE
SEQRES 25 A 479 TYR HIS TYR TYR ARG ALA PRO PHE VAL ARG ASP ASP LEU
SEQRES 26 A 479 TRP ALA ARG PHE LEU VAL SER LYS PRO PRO LEU ASP VAL
SEQRES 27 A 479 GLU LEU LEU ILE LEU PRO GLU ARG LEU SER PRO ALA ALA
SEQRES 28 A 479 LYS GLU THR SER GLY LEU LEU LEU ILE ARG TYR LYS GLU
SEQRES 29 A 479 MET ILE GLY GLU TYR ASP GLU GLU ILE GLY GLY VAL ASP
SEQRES 30 A 479 GLU VAL TYR VAL ASN GLY VAL ASN VAL CYS THR GLU ARG
SEQRES 31 A 479 ILE CYS PRO ILE GLU ARG ALA VAL ASN GLY LEU TRP VAL
SEQRES 32 A 479 PHE ASP ARG GLY ALA ASP GLY LYS SER ASP LEU ASP ARG
SEQRES 33 A 479 GLU VAL VAL ARG TYR SER ILE MET PRO PHE MET SER ALA
SEQRES 34 A 479 ALA ASP LEU VAL VAL PRO ALA GLU GLY THR ILE SER ILE
SEQRES 35 A 479 ALA VAL LYS SER ARG THR GLY GLY GLU GLU SER PHE THR
SEQRES 36 A 479 ILE PRO ALA TRP SER ALA ASP ARG HIS SER ILE ILE VAL
SEQRES 37 A 479 GLN PHE SER ASP TYR ILE VAL ASP LYS LEU ALA
HET PG4 A 500 13
HET CL A 800 1
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM CL CHLORIDE ION
FORMUL 2 PG4 C8 H18 O5
FORMUL 3 CL CL 1-
FORMUL 4 HOH *214(H2 O)
HELIX 1 1 SER A 34 GLN A 37 5 4
HELIX 2 2 PHE A 38 ALA A 47 1 10
HELIX 3 3 PRO A 51 GLU A 53 5 3
HELIX 4 4 ASP A 61 VAL A 69 1 9
HELIX 5 5 SER A 80 GLN A 88 1 9
HELIX 6 6 ASP A 91 SER A 100 1 10
HELIX 7 7 SER A 102 GLY A 126 1 25
HELIX 8 8 SER A 136 ASN A 147 1 12
HELIX 9 9 SER A 149 LYS A 155 1 7
HELIX 10 10 PRO A 183 GLY A 190 5 8
HELIX 11 11 VAL A 211 SER A 216 1 6
HELIX 12 12 PRO A 217 GLY A 229 1 13
HELIX 13 13 ASP A 337 LEU A 341 5 5
HELIX 14 14 ILE A 342 LEU A 347 1 6
HELIX 15 15 SER A 348 THR A 354 5 7
HELIX 16 16 VAL A 418 SER A 422 5 5
SHEET 1 A 6 VAL A 55 PHE A 58 0
SHEET 2 A 6 VAL A 25 VAL A 28 1 N PHE A 27 O PHE A 58
SHEET 3 A 6 VAL A 130 HIS A 135 1 O VAL A 133 N VAL A 28
SHEET 4 A 6 VAL A 156 LEU A 162 1 O ALA A 157 N VAL A 130
SHEET 5 A 6 THR A 176 GLY A 181 1 O LEU A 177 N LEU A 161
SHEET 6 A 6 THR A 201 PHE A 205 1 O VAL A 203 N PHE A 180
SHEET 1 B 3 ASP A 289 ARG A 295 0
SHEET 2 B 3 TYR A 244 ALA A 253 -1 N VAL A 245 O LEU A 294
SHEET 3 B 3 ARG A 328 VAL A 331 1 O PHE A 329 N LYS A 250
SHEET 1 C 8 LYS A 282 LYS A 287 0
SHEET 2 C 8 SER A 261 PRO A 268 -1 N ILE A 266 O LYS A 282
SHEET 3 C 8 TYR A 300 LYS A 306 -1 O ARG A 305 N TRP A 263
SHEET 4 C 8 ILE A 312 ARG A 317 -1 O TYR A 315 N PHE A 302
SHEET 5 C 8 HIS A 464 GLN A 469 1 O ILE A 467 N TYR A 316
SHEET 6 C 8 LEU A 357 ILE A 360 1 N LEU A 358 O ILE A 466
SHEET 7 C 8 GLY A 400 PHE A 404 -1 O LEU A 401 N LEU A 359
SHEET 8 C 8 ALA A 429 ASP A 431 1 O ALA A 430 N TRP A 402
SHEET 1 D 4 VAL A 384 ASN A 385 0
SHEET 2 D 4 GLU A 378 VAL A 381 -1 N VAL A 381 O VAL A 384
SHEET 3 D 4 THR A 439 LYS A 445 -1 O ALA A 443 N TYR A 380
SHEET 4 D 4 GLU A 451 PRO A 457 -1 O GLU A 452 N VAL A 444
CISPEP 1 PRO A 334 PRO A 335 0 0.36
SITE 1 AC1 7 LEU A 31 ALA A 32 VAL A 211 PHE A 254
SITE 2 AC1 7 LEU A 358 ASN A 399 GLY A 400
SITE 1 AC2 2 VAL A 419 ARG A 420
CRYST1 99.552 99.552 59.021 90.00 90.00 90.00 P 43 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 0.010045 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010045 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016943 0.00000
TER 3633 ALA A 479
MASTER 427 0 2 16 21 0 3 6 3860 1 13 37
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