HEADER HYDROLASE 01-OCT-02 1MWY
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF ZNTA IN THE APO-FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZNTA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, (RESIDUES 46-118);
COMPND 5 SYNONYM: LEAD, CADMIUM, ZINC AND MERCURY TRANSPORTING ATPASE;
COMPND 6 EC: 3.6.3.3, 3.6.3.5;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ZNTA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11C
KEYWDS OPEN-FACED BETA-SANDWICH FOLD, BETA-ALPHA-BETA-BETA-ALPHA-BETA,
KEYWDS 2 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.A.FINNEY,C.E.OUTTEN,
AUTHOR 2 T.V.O'HALLORAN
REVDAT 3 23-FEB-22 1MWY 1 REMARK
REVDAT 2 24-FEB-09 1MWY 1 VERSN
REVDAT 1 06-NOV-02 1MWY 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.A.FINNEY,C.E.OUTTEN,
JRNL AUTH 2 T.V.O'HALLORAN
JRNL TITL A NEW ZINC-PROTEIN COORDINATION SITE IN INTRACELLULAR METAL
JRNL TITL 2 TRAFFICKING: SOLUTION STRUCTURE OF THE APO AND ZN(II) FORMS
JRNL TITL 3 OF ZNTA (46-118)
JRNL REF J.MOL.BIOL. V. 323 883 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12417201
JRNL DOI 10.1016/S0022-2836(02)01007-0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, AMBER 5.0
REMARK 3 AUTHORS : BRUKER SOFTWARE (XWINNMR), CASE D.A., PEARLMAN
REMARK 3 D.A. ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1772 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS AND 87 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1MWY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017263.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 100 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM U-15N APO-ZNTA(46-118),
REMARK 210 100 MM PHOSPHATE BUFFER; 2.0 MM
REMARK 210 UNLABELLED APO-ZNTA(46-118), 100
REMARK 210 MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; 2D
REMARK 210 NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 700 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, CORMA, XEASY 3.2,
REMARK 210 XWINNMR 1.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 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 1 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 1 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -9.8 DEGREES
REMARK 500 1 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 1 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 2 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 2 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -9.8 DEGREES
REMARK 500 2 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 2 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 3 TRP A 8 CD2 - CE2 - CZ2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 3 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -9.0 DEGREES
REMARK 500 3 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -9.4 DEGREES
REMARK 500 3 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 4 TRP A 8 NE1 - CE2 - CZ2 ANGL. DEV. = 11.3 DEGREES
REMARK 500 4 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 4 TRP A 8 CG - CD2 - CE3 ANGL. DEV. = 7.5 DEGREES
REMARK 500 4 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 4 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 5 TRP A 8 CD2 - CE2 - CZ2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 5 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 5 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -9.4 DEGREES
REMARK 500 5 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 5 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 6 TRP A 8 CD2 - CE2 - CZ2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 6 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 6 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -10.2 DEGREES
REMARK 500 6 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 6 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 7 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 7 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -9.9 DEGREES
REMARK 500 7 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 7 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 8 TRP A 8 NE1 - CE2 - CZ2 ANGL. DEV. = 12.3 DEGREES
REMARK 500 8 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -9.2 DEGREES
REMARK 500 8 TRP A 8 CG - CD2 - CE3 ANGL. DEV. = 8.5 DEGREES
REMARK 500 8 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 8 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -8.3 DEGREES
REMARK 500 9 TRP A 8 CD2 - CE2 - CZ2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 9 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 9 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -9.5 DEGREES
REMARK 500 9 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 10 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 10 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -10.1 DEGREES
REMARK 500 10 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 10 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 11 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 11 TRP A 8 CE2 - CD2 - CE3 ANGL. DEV. = -9.5 DEGREES
REMARK 500 11 TRP A 8 CE3 - CZ3 - CH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 11 TRP A 8 CZ3 - CH2 - CZ2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 12 TRP A 8 CD2 - CE2 - CZ2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 12 TRP A 8 NE1 - CE2 - CD2 ANGL. DEV. = -9.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 130 ANGLE DEVIATIONS.
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 1 ALA A 17 -47.28 -174.60
REMARK 500 1 LEU A 29 -119.43 -71.87
REMARK 500 1 ALA A 30 -48.91 -174.21
REMARK 500 1 ASN A 33 21.37 -142.84
REMARK 500 1 GLN A 34 143.18 -178.99
REMARK 500 1 ALA A 40 -50.43 68.33
REMARK 500 1 ASN A 50 151.04 163.21
REMARK 500 2 ALA A 17 -47.28 -174.60
REMARK 500 2 LEU A 29 -119.43 -71.87
REMARK 500 2 ALA A 30 -48.91 -174.21
REMARK 500 2 ASN A 33 21.37 -142.84
REMARK 500 2 GLN A 34 143.18 -178.99
REMARK 500 2 ALA A 40 -50.43 68.33
REMARK 500 2 ASN A 50 151.04 163.21
REMARK 500 3 MET A 13 95.71 -69.79
REMARK 500 3 CYS A 15 -95.57 -155.16
REMARK 500 3 ALA A 16 -58.94 -175.82
REMARK 500 3 LEU A 29 -109.22 -66.33
REMARK 500 3 ALA A 30 -49.85 176.67
REMARK 500 3 ALA A 40 -48.30 74.97
REMARK 500 3 ASP A 49 56.24 -92.68
REMARK 500 3 ASN A 50 150.13 165.69
REMARK 500 3 ASP A 69 100.58 -54.42
REMARK 500 3 ALA A 72 -76.01 -78.62
REMARK 500 3 ALA A 73 -47.11 -160.04
REMARK 500 4 CYS A 15 145.43 168.02
REMARK 500 4 ALA A 17 -50.93 -170.34
REMARK 500 4 LEU A 29 -108.63 -65.72
REMARK 500 4 ALA A 30 -51.05 177.99
REMARK 500 4 ASN A 33 -52.13 -124.80
REMARK 500 4 PHE A 39 77.75 -69.21
REMARK 500 4 ALA A 40 -62.15 -168.94
REMARK 500 4 THR A 41 48.85 -93.29
REMARK 500 4 GLU A 42 32.20 31.49
REMARK 500 4 ASN A 50 151.82 157.53
REMARK 500 4 ILE A 52 21.07 -141.80
REMARK 500 4 ASP A 69 103.41 -27.64
REMARK 500 5 MET A 13 35.71 -73.12
REMARK 500 5 CYS A 15 -75.32 -158.34
REMARK 500 5 ALA A 16 -65.33 157.51
REMARK 500 5 LEU A 29 -115.74 -72.23
REMARK 500 5 ALA A 30 -48.92 -177.10
REMARK 500 5 ALA A 40 -37.35 149.79
REMARK 500 5 GLU A 42 36.96 39.32
REMARK 500 5 ASP A 49 58.31 -95.90
REMARK 500 5 ASN A 50 157.65 161.45
REMARK 500 5 ALA A 72 -80.92 -65.35
REMARK 500 6 MET A 13 86.85 -69.30
REMARK 500 6 CYS A 15 -94.99 -147.52
REMARK 500 6 ALA A 16 -58.47 -171.80
REMARK 500
REMARK 500 THIS ENTRY HAS 290 RAMACHANDRAN OUTLIERS.
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 ALA A 73 GLU A 74 10 145.24
REMARK 500 LEU A 44 VAL A 45 18 148.66
REMARK 500 ALA A 73 GLU A 74 19 149.66
REMARK 500 ALA A 73 GLU A 74 26 -141.88
REMARK 500 LEU A 44 VAL A 45 28 149.07
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 1 ARG A 5 0.08 SIDE CHAIN
REMARK 500 1 ARG A 20 0.09 SIDE CHAIN
REMARK 500 1 PHE A 39 0.09 SIDE CHAIN
REMARK 500 1 TYR A 65 0.08 SIDE CHAIN
REMARK 500 2 ARG A 5 0.08 SIDE CHAIN
REMARK 500 2 ARG A 20 0.09 SIDE CHAIN
REMARK 500 2 PHE A 39 0.09 SIDE CHAIN
REMARK 500 2 TYR A 65 0.08 SIDE CHAIN
REMARK 500 3 PHE A 39 0.09 SIDE CHAIN
REMARK 500 3 ARG A 53 0.10 SIDE CHAIN
REMARK 500 4 TYR A 65 0.07 SIDE CHAIN
REMARK 500 5 TYR A 6 0.07 SIDE CHAIN
REMARK 500 6 PHE A 39 0.08 SIDE CHAIN
REMARK 500 6 TYR A 65 0.09 SIDE CHAIN
REMARK 500 7 TYR A 6 0.09 SIDE CHAIN
REMARK 500 8 ARG A 5 0.08 SIDE CHAIN
REMARK 500 8 ARG A 53 0.14 SIDE CHAIN
REMARK 500 8 ARG A 68 0.10 SIDE CHAIN
REMARK 500 9 ARG A 27 0.08 SIDE CHAIN
REMARK 500 9 PHE A 39 0.09 SIDE CHAIN
REMARK 500 10 TYR A 6 0.07 SIDE CHAIN
REMARK 500 10 ARG A 27 0.09 SIDE CHAIN
REMARK 500 10 PHE A 39 0.13 SIDE CHAIN
REMARK 500 10 ARG A 53 0.14 SIDE CHAIN
REMARK 500 11 PHE A 39 0.10 SIDE CHAIN
REMARK 500 12 ARG A 20 0.08 SIDE CHAIN
REMARK 500 12 PHE A 39 0.10 SIDE CHAIN
REMARK 500 12 ARG A 53 0.11 SIDE CHAIN
REMARK 500 13 PHE A 39 0.09 SIDE CHAIN
REMARK 500 14 ARG A 53 0.12 SIDE CHAIN
REMARK 500 15 TYR A 65 0.07 SIDE CHAIN
REMARK 500 16 PHE A 39 0.13 SIDE CHAIN
REMARK 500 16 TYR A 65 0.07 SIDE CHAIN
REMARK 500 17 TYR A 6 0.12 SIDE CHAIN
REMARK 500 17 PHE A 39 0.10 SIDE CHAIN
REMARK 500 17 TYR A 65 0.14 SIDE CHAIN
REMARK 500 18 ARG A 5 0.11 SIDE CHAIN
REMARK 500 18 TYR A 65 0.08 SIDE CHAIN
REMARK 500 19 ARG A 53 0.11 SIDE CHAIN
REMARK 500 20 TYR A 6 0.11 SIDE CHAIN
REMARK 500 20 PHE A 39 0.09 SIDE CHAIN
REMARK 500 21 ARG A 53 0.11 SIDE CHAIN
REMARK 500 22 PHE A 39 0.11 SIDE CHAIN
REMARK 500 22 TYR A 65 0.09 SIDE CHAIN
REMARK 500 23 PHE A 39 0.09 SIDE CHAIN
REMARK 500 24 TYR A 6 0.09 SIDE CHAIN
REMARK 500 24 PHE A 39 0.09 SIDE CHAIN
REMARK 500 24 ARG A 53 0.10 SIDE CHAIN
REMARK 500 25 ARG A 53 0.12 SIDE CHAIN
REMARK 500 25 TYR A 65 0.10 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 56 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MWZ RELATED DB: PDB
DBREF 1MWY A 2 74 UNP P37617 ATZN_ECOLI 46 118
SEQRES 1 A 73 SER GLY THR ARG TYR SER TRP LYS VAL SER GLY MET ASP
SEQRES 2 A 73 CYS ALA ALA CYS ALA ARG LYS VAL GLU ASN ALA VAL ARG
SEQRES 3 A 73 GLN LEU ALA GLY VAL ASN GLN VAL GLN VAL LEU PHE ALA
SEQRES 4 A 73 THR GLU LYS LEU VAL VAL ASP ALA ASP ASN ASP ILE ARG
SEQRES 5 A 73 ALA GLN VAL GLU SER ALA LEU GLN LYS ALA GLY TYR SER
SEQRES 6 A 73 LEU ARG ASP GLU GLN ALA ALA GLU
HELIX 1 1 ALA A 17 GLN A 28 1 12
HELIX 2 2 ILE A 52 GLY A 64 1 13
SHEET 1 A 4 VAL A 32 LEU A 38 0
SHEET 2 A 4 LYS A 43 ALA A 48 -1 O VAL A 45 N GLN A 36
SHEET 3 A 4 THR A 4 SER A 11 -1 N TYR A 6 O VAL A 46
SHEET 4 A 4 SER A 66 ASP A 69 -1 O ARG A 68 N LYS A 9
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
