HEADER METAL TRANSPORT 18-JUL-06 2HQ3
TITLE SOLUTION NMR STRUCTURE OF THE APO-NOSL PROTEIN FROM ACHROMOBACTER
TITLE 2 CYCLOCLASTES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOSL PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACHROMOBACTER CYCLOCLASTES;
SOURCE 3 ORGANISM_TAXID: 223;
SOURCE 4 STRAIN: IAM1013;
SOURCE 5 GENE: NOSL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-20B+
KEYWDS ALPHA BETA TOPOLOGY, METAL TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.M.TAUBNER,M.A.MCGUIRL,D.M.DOOLEY,V.COPIE
REVDAT 3 09-MAR-22 2HQ3 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2HQ3 1 VERSN
REVDAT 1 24-OCT-06 2HQ3 0
JRNL AUTH L.M.TAUBNER,M.A.MCGUIRL,D.M.DOOLEY,V.COPIE
JRNL TITL STRUCTURAL STUDIES OF APO NOSL, AN ACCESSORY PROTEIN OF THE
JRNL TITL 2 NITROUS OXIDE REDUCTASE SYSTEM: INSIGHTS FROM STRUCTURAL
JRNL TITL 3 HOMOLOGY WITH MERB, A MERCURY RESISTANCE PROTEIN.
JRNL REF BIOCHEMISTRY V. 45 12240 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 17014077
JRNL DOI 10.1021/BI061089+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.1
REMARK 3 AUTHORS : BRUKER INC. (XWINNMR),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES,PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038627.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM NOSL, U-15N, 13C; 100MM
REMARK 210 SODIUM PHOSPHATE; 1MM EDTA; 1MM
REMARK 210 DTT; 90% H2O, 10% D2O; 1.0 MM
REMARK 210 NOSL, U-15N; 100MM SODIUM
REMARK 210 PHOSPHATE; 1MM EDTA; 1MM DTT; 95%
REMARK 210 H2O, 5% D2O; 1.0 MM NOSL, U-15N,
REMARK 210 13C; 100MM SODIUM PHOSPHATE;
REMARK 210 1MM EDTA; 1MM DTT; > 95% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HNCO; HNCACB; CBCA(CO)NH;
REMARK 210 C(CO)NH; HCC(CO)NH; 1H-13C-CT
REMARK 210 HSQC; HCCH-TOCSY; 3D 15N NOESY;
REMARK 210 15N NOESY-HSQC; 13C NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.4, NMRVIEW 5.0, ARIA
REMARK 210 1.2
REMARK 210 METHOD USED : AMBIGUOUS RESTRAINTS FOR
REMARK 210 ITERATIVE ASSIGNMENTS (ARIA 1.2),
REMARK 210 TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING.
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: SEQUENTIAL AND INTRA-RESIDUE 1H, 15N, AND 13C BACKBONE AND
REMARK 210 SIDE-CHAIN CHEMICAL SHIFT ASSIGNMENTS WERE EXTRACTED FROM A
REMARK 210 SERIES OF DOUBLE AND TRIPLE RESONANCE NMR EXPERIMENTS (HNCA,
REMARK 210 HNCO, HNCACB, CBCA(CO)NH, C(CO)NH, HCC(CO)NH, 1H-13C-CT HSQC,AND
REMARK 210 HCCH-TOCSY) CONDUCTED ON A DRX600. NOE DATA WERE OBTAINED FROM
REMARK 210 3D 15N NOESY EXPERIMENTS WITH MIXING TIMES (TMIX) OF 100, 120,
REMARK 210 AND 140 MSEC AND FROM 3D HCHC-NOESY (TMIX=140 MSEC) SPECTRA
REMARK 210 ACQUIRED AT 600 MHZ. ADDITIONAL 15N NOESY-HSQC AND 13C NOESY-
REMARK 210 HSQC EXPERIMENTS (NOE MIXING TIMES OF 120 MSEC) WERE ACQUIRED ON
REMARK 210 A VARIAN 800 INOVA (800 MHZ) INSTRUMENT.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASP A 2
REMARK 465 LYS A 3
REMARK 465 GLU A 4
REMARK 465 ASP A 5
REMARK 465 VAL A 6
REMARK 465 ALA A 7
REMARK 465 GLN A 8
REMARK 465 SER A 9
REMARK 465 ILE A 10
REMARK 465 VAL A 11
REMARK 465 PRO A 12
REMARK 465 GLN A 13
REMARK 465 ASP A 14
REMARK 465 MET A 15
REMARK 465 THR A 16
REMARK 465 PRO A 17
REMARK 465 GLU A 18
REMARK 465 THR A 19
REMARK 465 LEU A 20
REMARK 465 GLY A 21
REMARK 465 HIS A 22
REMARK 465 TYR A 23
REMARK 465 CYS A 24
REMARK 465 GLN A 25
REMARK 465 MET A 26
REMARK 465 ASN A 27
REMARK 465 LEU A 28
REMARK 465 LEU A 29
REMARK 465 GLU A 30
REMARK 465 HIS A 31
REMARK 465 PRO A 32
REMARK 465 GLY A 33
REMARK 465 PRO A 34
REMARK 465 ASP A 161
REMARK 465 TYR A 162
REMARK 465 LEU A 163
REMARK 465 GLY A 164
REMARK 465 ARG A 165
REMARK 465 LEU A 166
REMARK 465 ARG A 167
REMARK 465 ALA A 168
REMARK 465 LEU A 169
REMARK 465 PRO A 170
REMARK 465 HIS A 171
REMARK 465 PRO A 172
REMARK 465 ALA A 173
REMARK 465 GLY A 174
REMARK 465 GLY A 175
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 GLY A 77 HA ALA A 78 0.44
REMARK 500 HA2 GLY A 77 H ALA A 78 0.64
REMARK 500 C GLU A 63 H GLN A 64 0.77
REMARK 500 O GLU A 63 H GLN A 64 0.79
REMARK 500 C ALA A 78 H ALA A 79 0.80
REMARK 500 O GLU A 63 N GLN A 64 0.81
REMARK 500 CA GLY A 77 H ALA A 78 0.84
REMARK 500 O GLY A 77 CA ALA A 78 0.84
REMARK 500 O ALA A 78 N ALA A 79 0.85
REMARK 500 C MET A 76 H GLY A 77 0.87
REMARK 500 C ASP A 159 H GLU A 160 0.92
REMARK 500 O MET A 76 N GLY A 77 0.94
REMARK 500 C ARG A 106 H GLY A 107 0.98
REMARK 500 C ARG A 105 H ARG A 106 0.99
REMARK 500 C GLY A 77 CA ALA A 78 1.00
REMARK 500 O ASP A 159 N GLU A 160 1.02
REMARK 500 C GLN A 64 H ILE A 65 1.02
REMARK 500 C ALA A 157 H ASP A 158 1.04
REMARK 500 C GLY A 77 HA ALA A 78 1.05
REMARK 500 C GLY A 77 H ALA A 78 1.07
REMARK 500 HA2 GLY A 77 N ALA A 78 1.08
REMARK 500 O ARG A 105 N ARG A 106 1.09
REMARK 500 C GLU A 150 H THR A 151 1.09
REMARK 500 CA GLY A 77 N ALA A 78 1.09
REMARK 500 O ARG A 106 N GLY A 107 1.10
REMARK 500 C GLY A 87 H ASP A 88 1.14
REMARK 500 O GLN A 64 N ILE A 65 1.16
REMARK 500 O ALA A 157 N ASP A 158 1.18
REMARK 500 O ASP A 159 H GLU A 160 1.19
REMARK 500 O GLY A 77 N ALA A 78 1.20
REMARK 500 O GLU A 150 N THR A 151 1.21
REMARK 500 HA3 GLY A 77 H ALA A 78 1.22
REMARK 500 O GLU A 150 H GLY A 152 1.24
REMARK 500 C GLY A 107 H GLY A 108 1.25
REMARK 500 HA3 GLY A 77 N ALA A 78 1.28
REMARK 500 O GLY A 87 N ASP A 88 1.29
REMARK 500 C ASP A 158 H ASP A 159 1.30
REMARK 500 C ASP A 88 H GLY A 89 1.33
REMARK 500 C PRO A 155 H ARG A 156 1.33
REMARK 500 O ALA A 78 CA ALA A 79 1.38
REMARK 500 O ARG A 105 H ARG A 106 1.38
REMARK 500 O GLY A 107 N GLY A 108 1.39
REMARK 500 O ARG A 106 H GLY A 107 1.40
REMARK 500 O ALA A 78 H GLY A 80 1.41
REMARK 500 O ALA A 78 H ALA A 79 1.41
REMARK 500 N ALA A 79 H GLY A 80 1.43
REMARK 500 O MET A 76 H GLY A 77 1.45
REMARK 500 O ASP A 88 N GLY A 89 1.45
REMARK 500 O GLY A 77 H ALA A 79 1.47
REMARK 500 O MET A 76 HA2 GLY A 77 1.47
REMARK 500
REMARK 500 THIS ENTRY HAS 76 CLOSE CONTACTS
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 LYS A 35 CD LYS A 35 CE -0.789
REMARK 500 LYS A 35 CE LYS A 35 NZ -0.584
REMARK 500 GLN A 37 CD GLN A 37 OE1 -0.610
REMARK 500 GLN A 37 CD GLN A 37 NE2 -0.671
REMARK 500 PHE A 39 CB PHE A 39 CG -0.127
REMARK 500 PHE A 39 CG PHE A 39 CD2 -0.612
REMARK 500 PHE A 39 CG PHE A 39 CD1 -0.555
REMARK 500 PHE A 39 CE1 PHE A 39 CZ -0.607
REMARK 500 PHE A 39 CZ PHE A 39 CE2 -0.552
REMARK 500 GLU A 41 CD GLU A 41 OE1 -0.709
REMARK 500 GLU A 41 CD GLU A 41 OE2 -0.612
REMARK 500 SER A 43 CB SER A 43 OG -0.170
REMARK 500 LEU A 47 CG LEU A 47 CD1 -0.270
REMARK 500 LEU A 47 CG LEU A 47 CD2 -0.268
REMARK 500 PHE A 48 CB PHE A 48 CG -0.312
REMARK 500 PHE A 48 CG PHE A 48 CD2 -0.892
REMARK 500 PHE A 48 CG PHE A 48 CD1 -0.715
REMARK 500 PHE A 48 CD1 PHE A 48 CE1 -0.287
REMARK 500 PHE A 48 CE1 PHE A 48 CZ -0.891
REMARK 500 PHE A 48 CZ PHE A 48 CE2 -0.712
REMARK 500 PHE A 48 CE2 PHE A 48 CD2 -0.288
REMARK 500 PHE A 49 CB PHE A 49 CG -0.143
REMARK 500 PHE A 49 CG PHE A 49 CD2 -0.823
REMARK 500 PHE A 49 CG PHE A 49 CD1 -0.652
REMARK 500 PHE A 49 CD1 PHE A 49 CE1 -0.130
REMARK 500 PHE A 49 CE1 PHE A 49 CZ -0.822
REMARK 500 PHE A 49 CZ PHE A 49 CE2 -0.651
REMARK 500 PHE A 49 CE2 PHE A 49 CD2 -0.129
REMARK 500 SER A 50 CB SER A 50 OG -0.360
REMARK 500 GLN A 51 CD GLN A 51 OE1 -0.504
REMARK 500 GLN A 51 CD GLN A 51 NE2 -0.520
REMARK 500 ARG A 53 CZ ARG A 53 NH1 -0.139
REMARK 500 ASP A 54 CG ASP A 54 OD1 -0.595
REMARK 500 ASP A 54 CG ASP A 54 OD2 -0.466
REMARK 500 TYR A 58 CB TYR A 58 CG -0.247
REMARK 500 TYR A 58 CG TYR A 58 CD2 -0.721
REMARK 500 TYR A 58 CG TYR A 58 CD1 -0.851
REMARK 500 TYR A 58 CD1 TYR A 58 CE1 -0.231
REMARK 500 TYR A 58 CE1 TYR A 58 CZ -0.738
REMARK 500 TYR A 58 CZ TYR A 58 OH -0.220
REMARK 500 TYR A 58 CZ TYR A 58 CE2 -0.868
REMARK 500 TYR A 58 CE2 TYR A 58 CD2 -0.230
REMARK 500 ARG A 60 CD ARG A 60 NE -0.873
REMARK 500 ARG A 60 NE ARG A 60 CZ -0.277
REMARK 500 ARG A 60 CZ ARG A 60 NH1 -0.705
REMARK 500 ARG A 60 CZ ARG A 60 NH2 -0.858
REMARK 500 PRO A 62 C PRO A 62 O -0.264
REMARK 500 PRO A 62 C GLU A 63 N -0.205
REMARK 500 GLU A 63 CA GLU A 63 CB -0.214
REMARK 500 GLU A 63 CB GLU A 63 CG -0.407
REMARK 500
REMARK 500 THIS ENTRY HAS 330 BOND DEVIATIONS.
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 LYS A 35 CG - CD - CE ANGL. DEV. = 61.3 DEGREES
REMARK 500 LYS A 35 CD - CE - NZ ANGL. DEV. = 66.8 DEGREES
REMARK 500 GLN A 37 OE1 - CD - NE2 ANGL. DEV. = -72.3 DEGREES
REMARK 500 GLN A 37 CG - CD - OE1 ANGL. DEV. = 34.6 DEGREES
REMARK 500 GLN A 37 CG - CD - NE2 ANGL. DEV. = 37.5 DEGREES
REMARK 500 PHE A 39 CB - CG - CD2 ANGL. DEV. = 22.1 DEGREES
REMARK 500 PHE A 39 CD1 - CG - CD2 ANGL. DEV. = -46.8 DEGREES
REMARK 500 PHE A 39 CB - CG - CD1 ANGL. DEV. = 24.7 DEGREES
REMARK 500 PHE A 39 CG - CD1 - CE1 ANGL. DEV. = 24.9 DEGREES
REMARK 500 PHE A 39 CG - CD2 - CE2 ANGL. DEV. = 22.0 DEGREES
REMARK 500 PHE A 39 CD1 - CE1 - CZ ANGL. DEV. = 22.0 DEGREES
REMARK 500 PHE A 39 CE1 - CZ - CE2 ANGL. DEV. = -47.2 DEGREES
REMARK 500 PHE A 39 CZ - CE2 - CD2 ANGL. DEV. = 25.0 DEGREES
REMARK 500 GLU A 41 OE1 - CD - OE2 ANGL. DEV. = 102.3 DEGREES
REMARK 500 GLU A 41 CG - CD - OE1 ANGL. DEV. = 50.2 DEGREES
REMARK 500 GLU A 41 CG - CD - OE2 ANGL. DEV. = 52.1 DEGREES
REMARK 500 PHE A 48 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 PHE A 48 CB - CG - CD2 ANGL. DEV. = 42.6 DEGREES
REMARK 500 PHE A 48 CD1 - CG - CD2 ANGL. DEV. = -90.4 DEGREES
REMARK 500 PHE A 48 CB - CG - CD1 ANGL. DEV. = 47.9 DEGREES
REMARK 500 PHE A 48 CG - CD1 - CE1 ANGL. DEV. = 47.6 DEGREES
REMARK 500 PHE A 48 CG - CD2 - CE2 ANGL. DEV. = 42.9 DEGREES
REMARK 500 PHE A 48 CD1 - CE1 - CZ ANGL. DEV. = 43.4 DEGREES
REMARK 500 PHE A 48 CE1 - CZ - CE2 ANGL. DEV. = -91.6 DEGREES
REMARK 500 PHE A 48 CZ - CE2 - CD2 ANGL. DEV. = 48.0 DEGREES
REMARK 500 PHE A 49 CB - CG - CD2 ANGL. DEV. = 53.8 DEGREES
REMARK 500 PHE A 49 CD1 - CG - CD2 ANGL. DEV. = 108.5 DEGREES
REMARK 500 PHE A 49 CB - CG - CD1 ANGL. DEV. = 54.9 DEGREES
REMARK 500 PHE A 49 CG - CD1 - CE1 ANGL. DEV. = 55.0 DEGREES
REMARK 500 PHE A 49 CG - CD2 - CE2 ANGL. DEV. = 53.6 DEGREES
REMARK 500 PHE A 49 CD1 - CE1 - CZ ANGL. DEV. = 54.2 DEGREES
REMARK 500 PHE A 49 CE1 - CZ - CE2 ANGL. DEV. = 110.0 DEGREES
REMARK 500 PHE A 49 CZ - CE2 - CD2 ANGL. DEV. = 55.6 DEGREES
REMARK 500 GLN A 51 OE1 - CD - NE2 ANGL. DEV. = -45.5 DEGREES
REMARK 500 GLN A 51 CG - CD - OE1 ANGL. DEV. = 20.7 DEGREES
REMARK 500 GLN A 51 CG - CD - NE2 ANGL. DEV. = 24.6 DEGREES
REMARK 500 ARG A 53 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 54 OD1 - CG - OD2 ANGL. DEV. = -49.1 DEGREES
REMARK 500 ASP A 54 CB - CG - OD1 ANGL. DEV. = 20.2 DEGREES
REMARK 500 ASP A 54 CB - CG - OD2 ANGL. DEV. = 29.0 DEGREES
REMARK 500 TYR A 58 CB - CG - CD2 ANGL. DEV. = 54.5 DEGREES
REMARK 500 TYR A 58 CD1 - CG - CD2 ANGL. DEV. = 108.7 DEGREES
REMARK 500 TYR A 58 CB - CG - CD1 ANGL. DEV. = 54.3 DEGREES
REMARK 500 TYR A 58 CG - CD1 - CE1 ANGL. DEV. = 53.6 DEGREES
REMARK 500 TYR A 58 CG - CD2 - CE2 ANGL. DEV. = 54.5 DEGREES
REMARK 500 TYR A 58 CD1 - CE1 - CZ ANGL. DEV. = 56.0 DEGREES
REMARK 500 TYR A 58 OH - CZ - CE2 ANGL. DEV. = 54.5 DEGREES
REMARK 500 TYR A 58 CE1 - CZ - OH ANGL. DEV. = 55.8 DEGREES
REMARK 500 TYR A 58 CE1 - CZ - CE2 ANGL. DEV. = 110.3 DEGREES
REMARK 500 TYR A 58 CZ - CE2 - CD2 ANGL. DEV. = 54.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 272 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 PRO A 62 1.55 -58.19
REMARK 500 GLU A 63 92.39 -58.67
REMARK 500 ILE A 65 -31.71 -130.22
REMARK 500 ASP A 75 109.70 -56.17
REMARK 500 MET A 76 79.50 -156.48
REMARK 500 ALA A 79 -5.50 79.87
REMARK 500 GLN A 85 160.30 61.77
REMARK 500 ARG A 106 -137.82 -171.60
REMARK 500 GLU A 130 -73.79 -154.23
REMARK 500 GLU A 150 -44.28 66.42
REMARK 500 THR A 151 -0.80 10.28
REMARK 500 PRO A 155 -72.61 -62.91
REMARK 500 ALA A 157 33.85 -169.58
REMARK 500 ASP A 159 -81.74 -104.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5595 RELATED DB: BMRB
REMARK 900 NMR CHEMICAL SHIFT ASSIGNMENTS
REMARK 900 RELATED ID: 2HPU RELATED DB: PDB
REMARK 900 SOLUTION NMR STRUCTURE OF THE APO-NOSL PROTEIN FROM ACHROMOBACTER
REMARK 900 CYCLOCLASTES
DBREF 2HQ3 A 3 175 UNP O68481 O68481_ACHCY 21 193
SEQADV 2HQ3 MET A 1 UNP O68481 CLONING ARTIFACT
SEQADV 2HQ3 ASP A 2 UNP O68481 CLONING ARTIFACT
SEQRES 1 A 175 MET ASP LYS GLU ASP VAL ALA GLN SER ILE VAL PRO GLN
SEQRES 2 A 175 ASP MET THR PRO GLU THR LEU GLY HIS TYR CYS GLN MET
SEQRES 3 A 175 ASN LEU LEU GLU HIS PRO GLY PRO LYS ALA GLN ILE PHE
SEQRES 4 A 175 LEU GLU GLY SER PRO ALA PRO LEU PHE PHE SER GLN VAL
SEQRES 5 A 175 ARG ASP ALA ILE ALA TYR ALA ARG GLY PRO GLU GLN ILE
SEQRES 6 A 175 ALA PRO ILE LEU VAL ILE TYR VAL ASN ASP MET GLY ALA
SEQRES 7 A 175 ALA GLY ALA THR TRP ASP GLN PRO GLY ASP GLY ASN TRP
SEQRES 8 A 175 ILE ALA ALA ASP LYS ALA PHE TYR VAL VAL GLY SER ALA
SEQRES 9 A 175 ARG ARG GLY GLY MET GLY ALA PRO GLU ALA VAL PRO PHE
SEQRES 10 A 175 SER SER ARG ASP GLU ALA ALA ALA PHE VAL LEU ALA GLU
SEQRES 11 A 175 GLY GLY GLN VAL LEU ALA LEU ALA ASP ILE THR ASP ALA
SEQRES 12 A 175 MET VAL LEU THR PRO VAL GLU THR GLY SER GLU PRO ARG
SEQRES 13 A 175 ALA ASP ASP GLU ASP TYR LEU GLY ARG LEU ARG ALA LEU
SEQRES 14 A 175 PRO HIS PRO ALA GLY GLY
HELIX 1 1 GLN A 51 ARG A 60 1 10
HELIX 2 2 SER A 119 GLU A 130 1 12
HELIX 3 3 ALA A 138 ILE A 140 5 3
HELIX 4 4 THR A 141 LEU A 146 1 6
SHEET 1 A 4 PRO A 46 PHE A 49 0
SHEET 2 A 4 ALA A 36 LEU A 40 -1 N ALA A 36 O PHE A 49
SHEET 3 A 4 ILE A 68 ASP A 75 -1 O TYR A 72 N GLN A 37
SHEET 4 A 4 ASN A 90 ALA A 93 -1 O ASN A 90 N ASP A 75
SHEET 1 B 3 ALA A 114 PHE A 117 0
SHEET 2 B 3 PHE A 98 GLY A 102 -1 N PHE A 98 O PHE A 117
SHEET 3 B 3 GLY A 132 ALA A 136 -1 O LEU A 135 N TYR A 99
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
(ATOM LINES ARE NOT SHOWN.)
END
