Header list of 1j3g.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 31-JAN-03 1J3G
TITLE SOLUTION STRUCTURE OF CITROBACTER FREUNDII AMPD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMPD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMPD;
COMPND 5 EC: 3.5.1.28;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CITROBACTER FREUNDII;
SOURCE 3 ORGANISM_TAXID: 546;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-9A
KEYWDS MIXED ALPHA-BETA, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.LIEPINSH,C.GENEREUX,D.DEHARENG,B.JORIS,G.OTTING
REVDAT 4 23-FEB-22 1J3G 1 REMARK
REVDAT 3 24-FEB-09 1J3G 1 VERSN
REVDAT 2 01-APR-03 1J3G 1 JRNL
REVDAT 1 18-FEB-03 1J3G 0
SPRSDE 18-FEB-03 1J3G 1IYA 1J2S
JRNL AUTH E.LIEPINSH,C.GENEREUX,D.DEHARENG,B.JORIS,G.OTTING
JRNL TITL NMR STRUCTURE OF CITROBACTER FREUNDII AMPD, COMPARISON WITH
JRNL TITL 2 BACTERIOPHAGE T7 LYSOZYME AND HOMOLOGY WITH PGRP DOMAINS
JRNL REF J.MOL.BIOL. V. 327 833 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12654266
JRNL DOI 10.1016/S0022-2836(03)00185-2
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PROSA 3.6, OPAL 2.6
REMARK 3 AUTHORS : GUENTERT (PROSA),
REMARK 3 P.LUGINBUHL,P.GUNTERT,M.BILLETER,K.WUTHRICH (OPAL)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J3G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000005582.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.3MM AMPD U-15N,13C; 0.3MM AMPD
REMARK 210 U-15N; 0.3MM AMPD
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHB; DQF-COSY;
REMARK 210 CT-HMQC-HN
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 970326, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BY TRIPLE-RESONANCE AND 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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
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 1 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 TYR A 19 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 SER A 37 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 2 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 3 ASP A 164 OD1 - CG - OD2 ANGL. DEV. = -11.4 DEGREES
REMARK 500 3 ASP A 164 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 4 ASP A 20 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 4 ARG A 105 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 5 ASP A 20 CB - CG - OD1 ANGL. DEV. = -5.6 DEGREES
REMARK 500 5 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 5 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 5 ASP A 164 OD1 - CG - OD2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 5 ASP A 164 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 5 ARG A 173 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 6 ARG A 173 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 7 SER A 37 N - CA - C ANGL. DEV. = -16.6 DEGREES
REMARK 500 8 ASP A 164 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 9 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 9 TYR A 19 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 10 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 10 ASP A 164 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 11 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 11 TYR A 19 CB - CG - CD1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 11 HIS A 34 CA - CB - CG ANGL. DEV. = 10.6 DEGREES
REMARK 500 11 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 12 PHE A 64 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 12 TYR A 102 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 12 ASP A 164 OD1 - CG - OD2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 12 ASP A 164 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 15 SER A 37 N - CA - C ANGL. DEV. = -17.3 DEGREES
REMARK 500 16 SER A 37 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 16 ASP A 164 OD1 - CG - OD2 ANGL. DEV. = -11.6 DEGREES
REMARK 500 16 ASP A 164 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 17 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 17 ASP A 164 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 18 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 18 TYR A 87 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 18 ASP A 164 OD1 - CG - OD2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 18 ARG A 175 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 19 ASP A 164 OD1 - CG - OD2 ANGL. DEV. = -12.2 DEGREES
REMARK 500 19 ASP A 164 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 20 TYR A 19 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 20 TYR A 19 CB - CG - CD1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 20 ARG A 22 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 20 SER A 37 N - CA - C ANGL. DEV. = -17.1 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 1 CYS A 21 118.13 -165.66
REMARK 500 1 SER A 29 79.39 -172.24
REMARK 500 1 LEU A 38 -48.40 -142.20
REMARK 500 1 PRO A 40 44.30 -84.48
REMARK 500 1 ALA A 74 -154.00 -95.83
REMARK 500 1 HIS A 75 -67.16 -131.15
REMARK 500 1 VAL A 88 92.10 79.84
REMARK 500 1 PRO A 89 -175.76 -61.70
REMARK 500 1 PHE A 90 5.49 -58.34
REMARK 500 1 LYS A 92 82.17 85.81
REMARK 500 1 ARG A 93 138.05 -32.56
REMARK 500 1 HIS A 96 63.13 -158.23
REMARK 500 1 ALA A 97 -56.83 -164.96
REMARK 500 1 ALA A 124 114.03 -25.90
REMARK 500 1 THR A 126 77.06 65.59
REMARK 500 1 ASP A 127 -33.71 -23.22
REMARK 500 1 ALA A 146 -52.45 -152.25
REMARK 500 1 ALA A 158 -53.54 -156.67
REMARK 500 1 ASP A 164 -178.87 -175.84
REMARK 500 1 PRO A 167 -98.31 -78.13
REMARK 500 1 ASP A 170 82.08 42.95
REMARK 500 1 PRO A 180 54.92 -95.26
REMARK 500 1 MET A 186 -95.43 57.54
REMARK 500 2 PRO A 23 40.19 -78.05
REMARK 500 2 SER A 29 77.16 -170.83
REMARK 500 2 LEU A 38 -66.09 -142.66
REMARK 500 2 PRO A 58 69.74 -69.63
REMARK 500 2 SER A 73 133.64 -172.33
REMARK 500 2 ALA A 74 -154.69 -96.46
REMARK 500 2 HIS A 75 -59.21 -132.48
REMARK 500 2 VAL A 88 91.46 63.75
REMARK 500 2 PRO A 89 -169.90 -58.89
REMARK 500 2 PHE A 90 24.15 -69.85
REMARK 500 2 LYS A 92 81.48 85.96
REMARK 500 2 ARG A 93 145.16 -34.89
REMARK 500 2 HIS A 96 63.18 -159.38
REMARK 500 2 ALA A 97 -70.74 -165.73
REMARK 500 2 PHE A 111 37.98 -81.48
REMARK 500 2 ILE A 113 56.96 -104.62
REMARK 500 2 ALA A 124 113.45 -24.12
REMARK 500 2 THR A 126 77.86 59.57
REMARK 500 2 ASP A 127 -33.14 -23.06
REMARK 500 2 ALA A 146 -48.35 -153.27
REMARK 500 2 ASN A 156 40.54 -87.74
REMARK 500 2 ALA A 158 -53.79 -164.24
REMARK 500 2 PRO A 167 -74.65 -75.72
REMARK 500 2 PRO A 180 40.10 -80.22
REMARK 500 2 SER A 182 64.31 -159.56
REMARK 500 2 HIS A 183 116.03 -164.10
REMARK 500 3 GLU A 10 58.21 38.88
REMARK 500
REMARK 500 THIS ENTRY HAS 520 RAMACHANDRAN OUTLIERS.
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 13 0.10 SIDE CHAIN
REMARK 500 1 HIS A 69 0.11 SIDE CHAIN
REMARK 500 1 ARG A 93 0.11 SIDE CHAIN
REMARK 500 1 ARG A 105 0.10 SIDE CHAIN
REMARK 500 1 PHE A 111 0.08 SIDE CHAIN
REMARK 500 2 HIS A 69 0.08 SIDE CHAIN
REMARK 500 2 ARG A 105 0.09 SIDE CHAIN
REMARK 500 3 ARG A 12 0.08 SIDE CHAIN
REMARK 500 3 HIS A 69 0.08 SIDE CHAIN
REMARK 500 4 ARG A 79 0.08 SIDE CHAIN
REMARK 500 4 ARG A 175 0.09 SIDE CHAIN
REMARK 500 5 TYR A 102 0.08 SIDE CHAIN
REMARK 500 5 TYR A 125 0.09 SIDE CHAIN
REMARK 500 5 ARG A 173 0.10 SIDE CHAIN
REMARK 500 6 HIS A 18 0.11 SIDE CHAIN
REMARK 500 6 HIS A 69 0.09 SIDE CHAIN
REMARK 500 6 TYR A 102 0.07 SIDE CHAIN
REMARK 500 6 ARG A 175 0.08 SIDE CHAIN
REMARK 500 7 ARG A 12 0.08 SIDE CHAIN
REMARK 500 7 ARG A 79 0.16 SIDE CHAIN
REMARK 500 7 ARG A 80 0.15 SIDE CHAIN
REMARK 500 8 ARG A 22 0.08 SIDE CHAIN
REMARK 500 8 HIS A 96 0.10 SIDE CHAIN
REMARK 500 8 TYR A 125 0.08 SIDE CHAIN
REMARK 500 9 HIS A 69 0.10 SIDE CHAIN
REMARK 500 9 ARG A 71 0.10 SIDE CHAIN
REMARK 500 10 ARG A 79 0.08 SIDE CHAIN
REMARK 500 12 ARG A 12 0.08 SIDE CHAIN
REMARK 500 12 ARG A 79 0.19 SIDE CHAIN
REMARK 500 12 ARG A 105 0.10 SIDE CHAIN
REMARK 500 12 ARG A 175 0.07 SIDE CHAIN
REMARK 500 13 ARG A 79 0.10 SIDE CHAIN
REMARK 500 14 HIS A 96 0.10 SIDE CHAIN
REMARK 500 14 TYR A 125 0.08 SIDE CHAIN
REMARK 500 15 HIS A 69 0.09 SIDE CHAIN
REMARK 500 15 ARG A 105 0.11 SIDE CHAIN
REMARK 500 16 ARG A 22 0.16 SIDE CHAIN
REMARK 500 16 ARG A 79 0.15 SIDE CHAIN
REMARK 500 16 TYR A 102 0.11 SIDE CHAIN
REMARK 500 16 ARG A 161 0.09 SIDE CHAIN
REMARK 500 16 ARG A 175 0.09 SIDE CHAIN
REMARK 500 17 HIS A 69 0.10 SIDE CHAIN
REMARK 500 17 ARG A 105 0.13 SIDE CHAIN
REMARK 500 18 ARG A 12 0.11 SIDE CHAIN
REMARK 500 18 ARG A 22 0.08 SIDE CHAIN
REMARK 500 18 ARG A 71 0.08 SIDE CHAIN
REMARK 500 18 ARG A 173 0.17 SIDE CHAIN
REMARK 500 19 ARG A 13 0.11 SIDE CHAIN
REMARK 500 20 ARG A 12 0.14 SIDE CHAIN
REMARK 500 20 HIS A 69 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 53 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 12 MET A 1 12.67
REMARK 500
REMARK 500 REMARK: NULL
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 ZN A 210 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 34 ND1
REMARK 620 2 HIS A 154 ND1 97.2
REMARK 620 3 ASP A 164 OD1 98.0 92.4
REMARK 620 4 ASP A 164 OD2 99.6 144.9 54.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 210
DBREF 1J3G A 1 187 UNP P82974 AMPD_CITFR 1 187
SEQRES 1 A 187 MET LEU LEU ASP GLU GLY TRP LEU ALA GLU ALA ARG ARG
SEQRES 2 A 187 VAL PRO SER PRO HIS TYR ASP CYS ARG PRO ASP ASP GLU
SEQRES 3 A 187 ASN PRO SER LEU LEU VAL VAL HIS ASN ILE SER LEU PRO
SEQRES 4 A 187 PRO GLY GLU PHE GLY GLY PRO TRP ILE ASP ALA LEU PHE
SEQRES 5 A 187 THR GLY THR ILE ASP PRO ASN ALA HIS PRO TYR PHE ALA
SEQRES 6 A 187 GLY ILE ALA HIS LEU ARG VAL SER ALA HIS CYS LEU ILE
SEQRES 7 A 187 ARG ARG ASP GLY GLU ILE VAL GLN TYR VAL PRO PHE ASP
SEQRES 8 A 187 LYS ARG ALA TRP HIS ALA GLY VAL SER SER TYR GLN GLY
SEQRES 9 A 187 ARG GLU ARG CYS ASN ASP PHE SER ILE GLY ILE GLU LEU
SEQRES 10 A 187 GLU GLY THR ASP THR LEU ALA TYR THR ASP ALA GLN TYR
SEQRES 11 A 187 GLN GLN LEU ALA ALA VAL THR ASN ALA LEU ILE THR ARG
SEQRES 12 A 187 TYR PRO ALA ILE ALA ASN ASN MET THR GLY HIS CYS ASN
SEQRES 13 A 187 ILE ALA PRO GLU ARG LYS THR ASP PRO GLY PRO SER PHE
SEQRES 14 A 187 ASP TRP ALA ARG PHE ARG ALA LEU VAL THR PRO SER SER
SEQRES 15 A 187 HIS LYS GLU MET THR
HET ZN A 210 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLY A 45 GLY A 54 1 10
HELIX 2 2 HIS A 61 ALA A 68 1 8
HELIX 3 3 ASP A 127 TYR A 144 1 18
HELIX 4 4 ALA A 146 ASN A 149 5 4
HELIX 5 5 ASP A 170 VAL A 178 1 9
SHEET 1 A 2 LEU A 3 ASP A 4 0
SHEET 2 A 2 TRP A 7 LEU A 8 -1 O TRP A 7 N ASP A 4
SHEET 1 B 5 ARG A 12 ARG A 13 0
SHEET 2 B 5 GLU A 83 GLN A 86 1 O GLN A 86 N ARG A 12
SHEET 3 B 5 CYS A 76 ARG A 79 -1 N LEU A 77 O VAL A 85
SHEET 4 B 5 GLU A 116 GLU A 118 1 O GLU A 118 N ILE A 78
SHEET 5 B 5 ASN A 35 ILE A 36 1 N ILE A 36 O LEU A 117
SHEET 1 C 2 LEU A 31 VAL A 32 0
SHEET 2 C 2 MET A 151 THR A 152 1 O THR A 152 N LEU A 31
SHEET 1 D 2 SER A 100 TYR A 102 0
SHEET 2 D 2 ARG A 105 ARG A 107 -1 O ARG A 107 N SER A 100
LINK ND1 HIS A 34 ZN ZN A 210 1555 1555 2.28
LINK ND1 HIS A 154 ZN ZN A 210 1555 1555 2.27
LINK OD1 ASP A 164 ZN ZN A 210 1555 1555 2.28
LINK OD2 ASP A 164 ZN ZN A 210 1555 1555 2.23
SITE 1 AC1 3 HIS A 34 HIS A 154 ASP A 164
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
Complete list - b 23 2 Bytes