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HEADER HYDROLASE 28-JAN-09 2ZYR
TITLE A. FULGIDUS LIPASE WITH FATTY ACID FRAGMENT AND MAGNESIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
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 2ZYR 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. 1.77 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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
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) (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 90064
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) : 0.178
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4527
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.83
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 76.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 396
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 : 7246
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 1255
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.89
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.019
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 2ZYR 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 RCSB028594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 4.2.2
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 : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94247
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.34400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
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 (%): 45.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16M MAGNESIUM CHLORIDE, 0.08M
REMARK 280 TRIS HCL, 10% PEG4000, 20% GLYCEROL , PH 8.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.14450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.94250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.33350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.94250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.14450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.33350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 465 GLU A 20
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 GLY B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 VAL B 6
REMARK 465 LEU B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 VAL B 11
REMARK 465 PHE B 12
REMARK 465 ALA B 13
REMARK 465 VAL B 14
REMARK 465 GLN B 15
REMARK 465 VAL B 16
REMARK 465 ALA B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
REMARK 465 GLU B 20
REMARK 465 VAL B 475
REMARK 465 ASP B 476
REMARK 465 LYS B 477
REMARK 465 LEU B 478
REMARK 465 ALA B 479
REMARK 465 ALA B 480
REMARK 465 ALA B 481
REMARK 465 LEU B 482
REMARK 465 GLU B 483
REMARK 465 HIS B 484
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 787 O HOH A 788 1.89
REMARK 500 OG SER B 136 O HOH B 870 2.04
REMARK 500 O HOH A 829 O HOH A 850 2.05
REMARK 500 O HOH A 653 O HOH A 1084 2.09
REMARK 500 OE2 GLU B 39 O HOH B 513 2.10
REMARK 500 O HOH B 566 O HOH B 812 2.10
REMARK 500 O HOH B 633 O HOH B 1241 2.14
REMARK 500 O GLU B 437 O HOH B 947 2.14
REMARK 500 O HOH B 604 O HOH B 1113 2.15
REMARK 500 O HOH B 649 O HOH B 1247 2.15
REMARK 500 O HOH A 535 O HOH A 1139 2.16
REMARK 500 O HOH B 560 O HOH B 561 2.17
REMARK 500 OH TYR B 473 O HOH B 1202 2.18
REMARK 500 O HOH B 730 O HOH B 731 2.18
REMARK 500 O HOH B 597 O HOH B 905 2.18
REMARK 500 O HOH A 503 O HOH A 991 2.19
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 B 23 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU B 213 CA - CB - CG ANGL. DEV. = 14.5 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 136 -119.49 55.57
REMARK 500 GLU A 194 146.44 -172.82
REMARK 500 ALA A 255 -41.48 72.41
REMARK 500 LEU A 336 72.08 -111.45
REMARK 500 LYS A 363 112.34 -178.18
REMARK 500 SER B 136 -119.79 54.34
REMARK 500 LEU B 186 59.41 -148.66
REMARK 500 ALA B 255 -36.11 69.30
REMARK 500 LEU B 336 69.29 -116.58
REMARK 500 LYS B 363 117.17 -172.39
REMARK 500 ALA B 436 22.76 -77.30
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 B 539 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 559 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH B 573 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B 574 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A 593 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH A 598 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH A 600 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH B 612 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH B 616 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 626 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 636 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B 644 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 665 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH B 696 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A 766 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH A 776 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH B 788 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH B 801 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A 806 DISTANCE = 6.53 ANGSTROMS
REMARK 525 HOH A 834 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A 837 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH A 862 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A 869 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH B 925 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 931 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 937 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B 951 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH B 990 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH B1014 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH B1093 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A 929 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH B1107 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH B1111 DISTANCE = 7.93 ANGSTROMS
REMARK 525 HOH B1151 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH B1158 DISTANCE = 8.07 ANGSTROMS
REMARK 525 HOH B1162 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 971 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH B1173 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH B1179 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A 983 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH B1204 DISTANCE = 7.38 ANGSTROMS
REMARK 525 HOH A1005 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH A1010 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH B1225 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH B1227 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH B1232 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH A1024 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B1246 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH B1250 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A1075 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A1082 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH A1127 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A1130 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH A1136 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A1163 DISTANCE = 5.45 ANGSTROMS
REMARK 525 HOH A1164 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A1253 DISTANCE = 5.16 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 1PE B 500
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 158 NE2
REMARK 620 2 HOH A 732 O 95.4
REMARK 620 3 HOH A 680 O 95.8 82.4
REMARK 620 4 HOH A 679 O 175.9 85.7 88.3
REMARK 620 5 HOH A 682 O 89.1 97.2 175.1 86.8
REMARK 620 6 HOH A 681 O 90.1 174.5 96.2 89.0 83.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 405 OD1
REMARK 620 2 ARG A 406 O 84.1
REMARK 620 3 ASP A 409 OD2 80.1 89.3
REMARK 620 4 LYS A 411 O 98.2 177.3 89.6
REMARK 620 5 ASP A 431 OD1 92.3 91.3 172.2 90.1
REMARK 620 6 HOH A 845 O 151.2 84.5 73.5 92.8 114.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2005 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 158 NE2
REMARK 620 2 HOH B 867 O 170.4
REMARK 620 3 HOH B 727 O 87.6 101.0
REMARK 620 4 HOH B1235 O 96.8 85.5 103.9
REMARK 620 5 HOH B1236 O 93.0 78.1 175.6 80.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B2004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 405 OD1
REMARK 620 2 ARG B 406 O 96.0
REMARK 620 3 LYS B 411 O 85.5 177.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A2002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 873 O
REMARK 620 2 HOH A1138 O 96.7
REMARK 620 3 HOH A 870 O 114.3 89.0
REMARK 620 4 HOH A 872 O 158.9 92.6 84.7
REMARK 620 5 HOH A 874 O 89.9 173.4 87.5 81.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A2001
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A2002
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A2003
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 500
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2004
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2005
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: 2ZYS RELATED DB: PDB
DBREF 2ZYR A 1 474 UNP O28511 O28511_ARCFU 1 474
DBREF 2ZYR B 1 474 UNP O28511 O28511_ARCFU 1 474
SEQADV 2ZYR VAL A 475 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ASP A 476 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR LYS A 477 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR LEU A 478 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ALA A 479 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ALA A 480 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ALA A 481 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR LEU A 482 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR GLU A 483 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR HIS A 484 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR VAL B 475 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ASP B 476 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR LYS B 477 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR LEU B 478 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ALA B 479 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ALA B 480 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR ALA B 481 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR LEU B 482 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR GLU B 483 UNP O28511 EXPRESSION TAG
SEQADV 2ZYR HIS B 484 UNP O28511 EXPRESSION TAG
SEQRES 1 A 484 MET ARG GLY LEU ALA VAL LEU VAL LEU LEU VAL PHE ALA
SEQRES 2 A 484 VAL GLN VAL ALA ALA ALA GLU ASP PHE ARG PRO VAL VAL
SEQRES 3 A 484 PHE VAL HIS GLY LEU ALA GLY SER ALA GLY GLN PHE GLU
SEQRES 4 A 484 SER GLN GLY MET ARG PHE ALA ALA ASN GLY TYR PRO ALA
SEQRES 5 A 484 GLU TYR VAL LYS THR PHE GLU TYR ASP THR ILE SER TRP
SEQRES 6 A 484 ALA LEU VAL VAL GLU THR ASP MET LEU PHE SER GLY LEU
SEQRES 7 A 484 GLY SER GLU PHE GLY LEU ASN ILE SER GLN ILE ILE ASP
SEQRES 8 A 484 PRO GLU THR LEU ASP LYS ILE LEU SER LYS SER ARG GLU
SEQRES 9 A 484 ARG LEU ILE ASP GLU THR PHE SER ARG LEU ASP ARG VAL
SEQRES 10 A 484 ILE ASP GLU ALA LEU ALA GLU SER GLY ALA ASP LYS VAL
SEQRES 11 A 484 ASP LEU VAL GLY HIS SER MET GLY THR PHE PHE LEU VAL
SEQRES 12 A 484 ARG TYR VAL ASN SER SER PRO GLU ARG ALA ALA LYS VAL
SEQRES 13 A 484 ALA HIS LEU ILE LEU LEU ASP GLY VAL TRP GLY VAL ASP
SEQRES 14 A 484 ALA PRO GLU GLY ILE PRO THR LEU ALA VAL PHE GLY ASN
SEQRES 15 A 484 PRO LYS ALA LEU PRO ALA LEU GLY LEU PRO GLU GLU LYS
SEQRES 16 A 484 VAL VAL TYR ASN ALA THR ASN VAL TYR PHE ASN ASN MET
SEQRES 17 A 484 THR HIS VAL GLN LEU CYS THR SER PRO GLU THR PHE ALA
SEQRES 18 A 484 VAL MET PHE GLU PHE ILE ASN GLY TYR LYS PRO ALA THR
SEQRES 19 A 484 THR ASP ILE VAL PRO GLN ASP GLY ASP TYR VAL LYS VAL
SEQRES 20 A 484 LYS GLY LYS PHE LEU ALA PHE ALA THR ASN GLY ASP VAL
SEQRES 21 A 484 SER GLY TRP LEU SER ILE TYR PRO ILE ASP GLU ASN GLY
SEQRES 22 A 484 LYS ARG LEU THR ARG LEU PRO VAL LYS PHE MET ARG VAL
SEQRES 23 A 484 LYS GLY ASP PHE GLU VAL ARG LEU ARG LYS GLY GLN LEU
SEQRES 24 A 484 TYR GLU PHE GLN PHE ARG LYS ASP PHE SER PRO ILE ILE
SEQRES 25 A 484 TYR HIS TYR TYR ARG ALA PRO PHE VAL ARG ASP ASP LEU
SEQRES 26 A 484 TRP ALA ARG PHE LEU VAL SER LYS PRO PRO LEU ASP VAL
SEQRES 27 A 484 GLU LEU LEU ILE LEU PRO GLU ARG LEU SER PRO ALA ALA
SEQRES 28 A 484 LYS GLU THR SER GLY LEU LEU LEU ILE ARG TYR LYS GLU
SEQRES 29 A 484 MET ILE GLY GLU TYR ASP GLU GLU ILE GLY GLY VAL ASP
SEQRES 30 A 484 GLU VAL TYR VAL ASN GLY VAL ASN VAL CYS THR GLU ARG
SEQRES 31 A 484 ILE CYS PRO ILE GLU ARG ALA VAL ASN GLY LEU TRP VAL
SEQRES 32 A 484 PHE ASP ARG GLY ALA ASP GLY LYS SER ASP LEU ASP ARG
SEQRES 33 A 484 GLU VAL VAL ARG TYR SER ILE MET PRO PHE MET SER ALA
SEQRES 34 A 484 ALA ASP LEU VAL VAL PRO ALA GLU GLY THR ILE SER ILE
SEQRES 35 A 484 ALA VAL LYS SER ARG THR GLY GLY GLU GLU SER PHE THR
SEQRES 36 A 484 ILE PRO ALA TRP SER ALA ASP ARG HIS SER ILE ILE VAL
SEQRES 37 A 484 GLN PHE SER ASP TYR ILE VAL ASP LYS LEU ALA ALA ALA
SEQRES 38 A 484 LEU GLU HIS
SEQRES 1 B 484 MET ARG GLY LEU ALA VAL LEU VAL LEU LEU VAL PHE ALA
SEQRES 2 B 484 VAL GLN VAL ALA ALA ALA GLU ASP PHE ARG PRO VAL VAL
SEQRES 3 B 484 PHE VAL HIS GLY LEU ALA GLY SER ALA GLY GLN PHE GLU
SEQRES 4 B 484 SER GLN GLY MET ARG PHE ALA ALA ASN GLY TYR PRO ALA
SEQRES 5 B 484 GLU TYR VAL LYS THR PHE GLU TYR ASP THR ILE SER TRP
SEQRES 6 B 484 ALA LEU VAL VAL GLU THR ASP MET LEU PHE SER GLY LEU
SEQRES 7 B 484 GLY SER GLU PHE GLY LEU ASN ILE SER GLN ILE ILE ASP
SEQRES 8 B 484 PRO GLU THR LEU ASP LYS ILE LEU SER LYS SER ARG GLU
SEQRES 9 B 484 ARG LEU ILE ASP GLU THR PHE SER ARG LEU ASP ARG VAL
SEQRES 10 B 484 ILE ASP GLU ALA LEU ALA GLU SER GLY ALA ASP LYS VAL
SEQRES 11 B 484 ASP LEU VAL GLY HIS SER MET GLY THR PHE PHE LEU VAL
SEQRES 12 B 484 ARG TYR VAL ASN SER SER PRO GLU ARG ALA ALA LYS VAL
SEQRES 13 B 484 ALA HIS LEU ILE LEU LEU ASP GLY VAL TRP GLY VAL ASP
SEQRES 14 B 484 ALA PRO GLU GLY ILE PRO THR LEU ALA VAL PHE GLY ASN
SEQRES 15 B 484 PRO LYS ALA LEU PRO ALA LEU GLY LEU PRO GLU GLU LYS
SEQRES 16 B 484 VAL VAL TYR ASN ALA THR ASN VAL TYR PHE ASN ASN MET
SEQRES 17 B 484 THR HIS VAL GLN LEU CYS THR SER PRO GLU THR PHE ALA
SEQRES 18 B 484 VAL MET PHE GLU PHE ILE ASN GLY TYR LYS PRO ALA THR
SEQRES 19 B 484 THR ASP ILE VAL PRO GLN ASP GLY ASP TYR VAL LYS VAL
SEQRES 20 B 484 LYS GLY LYS PHE LEU ALA PHE ALA THR ASN GLY ASP VAL
SEQRES 21 B 484 SER GLY TRP LEU SER ILE TYR PRO ILE ASP GLU ASN GLY
SEQRES 22 B 484 LYS ARG LEU THR ARG LEU PRO VAL LYS PHE MET ARG VAL
SEQRES 23 B 484 LYS GLY ASP PHE GLU VAL ARG LEU ARG LYS GLY GLN LEU
SEQRES 24 B 484 TYR GLU PHE GLN PHE ARG LYS ASP PHE SER PRO ILE ILE
SEQRES 25 B 484 TYR HIS TYR TYR ARG ALA PRO PHE VAL ARG ASP ASP LEU
SEQRES 26 B 484 TRP ALA ARG PHE LEU VAL SER LYS PRO PRO LEU ASP VAL
SEQRES 27 B 484 GLU LEU LEU ILE LEU PRO GLU ARG LEU SER PRO ALA ALA
SEQRES 28 B 484 LYS GLU THR SER GLY LEU LEU LEU ILE ARG TYR LYS GLU
SEQRES 29 B 484 MET ILE GLY GLU TYR ASP GLU GLU ILE GLY GLY VAL ASP
SEQRES 30 B 484 GLU VAL TYR VAL ASN GLY VAL ASN VAL CYS THR GLU ARG
SEQRES 31 B 484 ILE CYS PRO ILE GLU ARG ALA VAL ASN GLY LEU TRP VAL
SEQRES 32 B 484 PHE ASP ARG GLY ALA ASP GLY LYS SER ASP LEU ASP ARG
SEQRES 33 B 484 GLU VAL VAL ARG TYR SER ILE MET PRO PHE MET SER ALA
SEQRES 34 B 484 ALA ASP LEU VAL VAL PRO ALA GLU GLY THR ILE SER ILE
SEQRES 35 B 484 ALA VAL LYS SER ARG THR GLY GLY GLU GLU SER PHE THR
SEQRES 36 B 484 ILE PRO ALA TRP SER ALA ASP ARG HIS SER ILE ILE VAL
SEQRES 37 B 484 GLN PHE SER ASP TYR ILE VAL ASP LYS LEU ALA ALA ALA
SEQRES 38 B 484 LEU GLU HIS
HET 1PE A 500 16
HET MG A2001 1
HET MG A2002 1
HET MG A2003 1
HET 1PE B 500 13
HET MG B2004 1
HET MG B2005 1
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM MG MAGNESIUM ION
HETSYN 1PE PEG400
FORMUL 3 1PE 2(C10 H22 O6)
FORMUL 4 MG 5(MG 2+)
FORMUL 10 HOH *1255(H2 O)
HELIX 1 1 SER A 34 GLN A 37 5 4
HELIX 2 2 PHE A 38 ASN A 48 1 11
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 GLY A 77 GLY A 79 5 3
HELIX 6 6 SER A 80 SER A 87 1 8
HELIX 7 7 GLN A 88 ILE A 90 5 3
HELIX 8 8 ASP A 91 SER A 100 1 10
HELIX 9 9 SER A 102 GLY A 126 1 25
HELIX 10 10 SER A 136 SER A 148 1 13
HELIX 11 11 SER A 149 LYS A 155 1 7
HELIX 12 12 PRO A 183 LEU A 186 5 4
HELIX 13 13 THR A 209 SER A 216 1 8
HELIX 14 14 SER A 216 GLY A 229 1 14
HELIX 15 15 ASP A 337 LEU A 341 5 5
HELIX 16 16 ILE A 342 LEU A 347 1 6
HELIX 17 17 SER A 348 GLU A 353 5 6
HELIX 18 18 PRO A 393 ALA A 397 5 5
HELIX 19 19 ASP A 405 ASP A 409 5 5
HELIX 20 20 VAL A 418 SER A 422 5 5
HELIX 21 21 ASP A 476 HIS A 484 1 9
HELIX 22 22 SER B 34 GLN B 37 5 4
HELIX 23 23 PHE B 38 ASN B 48 1 11
HELIX 24 24 PRO B 51 GLU B 53 5 3
HELIX 25 25 ASP B 61 VAL B 69 1 9
HELIX 26 26 GLY B 79 GLN B 88 1 10
HELIX 27 27 ASP B 91 SER B 100 1 10
HELIX 28 28 SER B 102 GLY B 126 1 25
HELIX 29 29 SER B 136 SER B 148 1 13
HELIX 30 30 SER B 149 LYS B 155 1 7
HELIX 31 31 ASN B 182 GLY B 190 5 9
HELIX 32 32 THR B 209 SER B 216 1 8
HELIX 33 33 SER B 216 GLY B 229 1 14
HELIX 34 34 ASP B 337 LEU B 341 5 5
HELIX 35 35 ILE B 342 LEU B 347 1 6
HELIX 36 36 SER B 348 GLU B 353 5 6
HELIX 37 37 PRO B 393 ALA B 397 5 5
HELIX 38 38 ASP B 405 ASP B 409 5 5
HELIX 39 39 VAL B 418 SER B 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 VAL A 25 O LYS A 56
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 LEU A 162 N GLY A 134
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 PHE A 205 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 247 O VAL A 292
SHEET 3 B 3 ASP A 324 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 GLY A 262 O VAL A 286
SHEET 3 C 8 TYR A 300 LYS A 306 -1 O GLN A 303 N SER A 265
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 GLN A 469 N TYR A 316
SHEET 6 C 8 LEU A 357 MET A 365 1 N ILE A 360 O VAL A 468
SHEET 7 C 8 VAL A 398 PHE A 404 -1 O VAL A 403 N LEU A 357
SHEET 8 C 8 MET A 427 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 PHE A 454 N ILE A 442
SHEET 1 E 6 VAL B 55 PHE B 58 0
SHEET 2 E 6 VAL B 25 VAL B 28 1 N VAL B 25 O LYS B 56
SHEET 3 E 6 VAL B 130 HIS B 135 1 O VAL B 133 N VAL B 28
SHEET 4 E 6 VAL B 156 LEU B 162 1 O ALA B 157 N VAL B 130
SHEET 5 E 6 THR B 176 PHE B 180 1 O LEU B 177 N LEU B 161
SHEET 6 E 6 THR B 201 TYR B 204 1 O THR B 201 N ALA B 178
SHEET 1 F 3 ASP B 289 ARG B 295 0
SHEET 2 F 3 TYR B 244 ALA B 253 -1 N VAL B 245 O LEU B 294
SHEET 3 F 3 ASP B 324 VAL B 331 1 O PHE B 329 N LYS B 250
SHEET 1 G 8 LYS B 282 LYS B 287 0
SHEET 2 G 8 SER B 261 PRO B 268 -1 N LEU B 264 O MET B 284
SHEET 3 G 8 TYR B 300 LYS B 306 -1 O GLN B 303 N SER B 265
SHEET 4 G 8 ILE B 312 ARG B 317 -1 O TYR B 313 N PHE B 304
SHEET 5 G 8 HIS B 464 GLN B 469 1 O ILE B 467 N TYR B 316
SHEET 6 G 8 LEU B 357 ILE B 360 1 N ILE B 360 O VAL B 468
SHEET 7 G 8 GLY B 400 PHE B 404 -1 O VAL B 403 N LEU B 357
SHEET 8 G 8 MET B 427 ASP B 431 1 O ALA B 430 N TRP B 402
SHEET 1 H 4 VAL B 384 ASN B 385 0
SHEET 2 H 4 GLU B 378 VAL B 381 -1 N VAL B 381 O VAL B 384
SHEET 3 H 4 THR B 439 LYS B 445 -1 O ALA B 443 N TYR B 380
SHEET 4 H 4 GLU B 451 PRO B 457 -1 O PHE B 454 N ILE B 442
LINK NE2 HIS A 158 MG MG A2001 1555 1555 2.24
LINK OD1 ASP A 405 MG MG A2003 1555 1555 2.35
LINK O ARG A 406 MG MG A2003 1555 1555 2.34
LINK OD2 ASP A 409 MG MG A2003 1555 1555 2.48
LINK O LYS A 411 MG MG A2003 1555 1555 2.33
LINK OD1 ASP A 431 MG MG A2003 1555 1555 2.49
LINK NE2 HIS B 158 MG MG B2005 1555 1555 2.31
LINK OD1 ASP B 405 MG MG B2004 1555 1555 2.15
LINK O ARG B 406 MG MG B2004 1555 1555 2.16
LINK O LYS B 411 MG MG B2004 1555 1555 2.10
LINK MG MG A2001 O HOH A 732 1555 1555 1.76
LINK MG MG A2001 O HOH A 680 1555 1555 2.23
LINK MG MG A2001 O HOH A 679 1555 1555 2.21
LINK MG MG A2001 O HOH A 682 1555 1555 2.21
LINK MG MG A2001 O HOH A 681 1555 1555 2.14
LINK MG MG A2002 O HOH A 873 1555 1555 1.87
LINK MG MG A2002 O HOH A1138 1555 1555 2.12
LINK MG MG A2002 O HOH A 870 1555 1555 2.37
LINK MG MG A2002 O HOH A 872 1555 1555 2.08
LINK MG MG A2002 O HOH A 874 1555 1555 2.01
LINK MG MG A2003 O HOH A 845 1555 1555 2.44
LINK MG MG B2005 O HOH B 867 1555 1555 2.21
LINK MG MG B2005 O HOH B 727 1555 1555 2.11
LINK MG MG B2005 O HOH B1235 1555 1555 2.17
LINK MG MG B2005 O HOH B1236 1555 1555 1.88
CISPEP 1 PRO A 334 PRO A 335 0 0.91
CISPEP 2 PRO B 334 PRO B 335 0 0.28
SITE 1 AC1 7 LEU A 31 HIS A 135 PHE A 254 LEU A 330
SITE 2 AC1 7 SER A 332 GLU A 339 PHE A 426
SITE 1 AC2 6 HIS A 158 HOH A 679 HOH A 680 HOH A 681
SITE 2 AC2 6 HOH A 682 HOH A 732
SITE 1 AC3 5 HOH A 870 HOH A 872 HOH A 873 HOH A 874
SITE 2 AC3 5 HOH A1138
SITE 1 AC4 6 ASP A 405 ARG A 406 ASP A 409 LYS A 411
SITE 2 AC4 6 ASP A 431 HOH A 845
SITE 1 AC5 5 LEU B 31 ALA B 32 VAL B 338 PHE B 426
SITE 2 AC5 5 HOH B 871
SITE 1 AC6 6 ASP B 405 ARG B 406 ASP B 409 LYS B 411
SITE 2 AC6 6 ASP B 431 HOH B 804
SITE 1 AC7 6 HIS B 158 HOH B 726 HOH B 727 HOH B 867
SITE 2 AC7 6 HOH B1235 HOH B1236
CRYST1 52.289 106.667 175.885 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019124 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009375 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005686 0.00000
TER 3661 HIS A 484
TER 7248 ILE B 474
MASTER 509 0 7 39 42 0 14 6 8535 2 63 76
END |