Header list of 1u7j.pdb file
Complete list - r 2 2 Bytes
HEADER DE NOVO PROTEIN 04-AUG-04 1U7J
TITLE SOLUTION STRUCTURE OF A DIIRON PROTEIN MODEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FOUR-HELIX BUNDLE MODEL;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
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: PET15B
KEYWDS DIIRON PROTEINS, FOUR-HELIX BUNDLE, PROTEIN DESIGN, INTER-HELICAL
KEYWDS 2 LOOPS, DE NOVO PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR O.MAGLIO,F.NASTRI,J.R.CALHOUN,S.LAHR,V.PAVONE,W.F.DEGRADO,A.LOMBARDI
REVDAT 3 02-MAR-22 1U7J 1 REMARK LINK
REVDAT 2 24-FEB-09 1U7J 1 VERSN
REVDAT 1 01-MAR-05 1U7J 0
JRNL AUTH S.J.LAHR,D.E.ENGEL,S.E.STAYROOK,O.MAGLIO,B.NORTH,S.GEREMIA,
JRNL AUTH 2 A.LOMBARDI,W.F.DEGRADO
JRNL TITL ANALYSIS AND DESIGN OF TURNS IN ALPHA-HELICAL HAIRPINS
JRNL REF J.MOL.BIOL. V. 346 1441 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15713492
JRNL DOI 10.1016/J.JMB.2004.12.016
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.PASTERNAK,J.KAPLAN,J.D.LEAR,W.F.DEGRADO
REMARK 1 TITL PROTON AND METAL ION-DEPENDENT ASSEMBLY OF A MODEL DIIRON
REMARK 1 TITL 2 PROTEIN
REMARK 1 REF PROTEIN SCI. V. 10 958 2001
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 11316876
REMARK 1 DOI 10.1110/PS.52101
REMARK 1 REFERENCE 2
REMARK 1 AUTH O.MAGLIO,F.NASTRI,V.PAVONE,A.LOMBARDI,W.F.DEGRADO
REMARK 1 TITL PREORGANIZATION OF MOLECULAR BINDING SITES IN DESIGNED
REMARK 1 TITL 2 DIIRON PROTEINS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 100 3772 2003
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 12655072
REMARK 1 DOI 10.1073/PNAS.0730771100
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.LOMBARDI,C.M.SUMMA,S.GEREMIA,L.RANDACCIO,V.PAVONE,
REMARK 1 AUTH 2 W.F.DEGRADO
REMARK 1 TITL INAUGURAL ARTICLE: RETROSTRUCTURAL ANALYSIS OF
REMARK 1 TITL 2 METALLOPROTEINS: APPLICATION TO THE DESIGN OF A MINIMAL
REMARK 1 TITL 3 MODEL FOR DIIRON PROTEINS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 97 6298 2000
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 10841536
REMARK 1 DOI 10.1073/PNAS.97.12.6298
REMARK 1 REFERENCE 4
REMARK 1 AUTH D.E.ENGEL,S.J.LAHR,S.E.STAYROOK,S.GEREMIA,W.F.DEGRADO
REMARK 1 TITL ANALYSIS AND DESIGN OF TURNS IN ALPHA-HELICAL HAIRPINS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, AMBER 7.0
REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), CASE ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U7J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023343.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM PROTEIN CONCENTRATION;
REMARK 210 50MM PHOSPHATE BUFFER; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; DQF-COSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING, ENERGY
REMARK 210 RESTRAINED MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.6 DEGREES
REMARK 500 1 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.6 DEGREES
REMARK 500 2 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 2 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.5 DEGREES
REMARK 500 3 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 3 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -15.9 DEGREES
REMARK 500 4 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.4 DEGREES
REMARK 500 4 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 4 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.2 DEGREES
REMARK 500 4 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 5 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.9 DEGREES
REMARK 500 5 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.2 DEGREES
REMARK 500 6 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.9 DEGREES
REMARK 500 6 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.3 DEGREES
REMARK 500 7 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.4 DEGREES
REMARK 500 7 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 7 ARG B 19 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.8 DEGREES
REMARK 500 8 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -15.6 DEGREES
REMARK 500 9 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.9 DEGREES
REMARK 500 9 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -15.8 DEGREES
REMARK 500 10 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 10 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 11 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.6 DEGREES
REMARK 500 11 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 12 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 12 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.4 DEGREES
REMARK 500 13 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.4 DEGREES
REMARK 500 13 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -15.8 DEGREES
REMARK 500 14 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.2 DEGREES
REMARK 500 14 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.9 DEGREES
REMARK 500 15 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 15 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 16 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 16 GLU A 37 OE1 - CD - OE2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 16 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.0 DEGREES
REMARK 500 16 GLU B 37 OE1 - CD - OE2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 17 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 17 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 18 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -15.7 DEGREES
REMARK 500 18 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.2 DEGREES
REMARK 500 19 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.1 DEGREES
REMARK 500 19 ARG A 19 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 19 ARG B 5 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 19 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.0 DEGREES
REMARK 500 20 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -16.0 DEGREES
REMARK 500 20 GLU B 11 OE1 - CD - OE2 ANGL. DEV. = -16.3 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 TYR A 3 -56.48 -129.40
REMARK 500 1 ASP B 2 -7.06 -148.57
REMARK 500 2 TYR A 3 -62.32 -172.89
REMARK 500 2 ILE A 47 -7.96 -59.51
REMARK 500 2 TYR B 3 -38.16 -152.13
REMARK 500 3 TYR B 3 -39.58 -160.05
REMARK 500 3 LYS B 9 0.28 -69.11
REMARK 500 3 ALA B 14 46.09 -72.09
REMARK 500 3 MET B 15 -48.06 -149.65
REMARK 500 4 TYR A 3 -63.37 -145.64
REMARK 500 4 ALA A 14 52.03 -68.74
REMARK 500 4 MET A 15 -53.10 -160.62
REMARK 500 4 GLU A 37 6.26 -67.77
REMARK 500 4 ASP B 2 -56.49 -173.25
REMARK 500 4 SER B 22 -50.70 -124.80
REMARK 500 4 ASN B 48 -76.86 -82.05
REMARK 500 5 ALA A 21 40.48 -78.23
REMARK 500 5 TYR B 3 -39.56 -165.97
REMARK 500 5 LYS B 9 4.45 -66.29
REMARK 500 5 VAL B 25 -50.97 -135.32
REMARK 500 6 TYR A 3 -42.95 -158.39
REMARK 500 6 ALA A 14 40.22 -70.34
REMARK 500 6 MET A 15 -52.08 -139.32
REMARK 500 6 TYR B 3 -46.96 -137.16
REMARK 500 6 SER B 22 -50.15 -125.24
REMARK 500 7 ASP A 2 19.36 48.04
REMARK 500 7 LYS A 9 4.98 -69.79
REMARK 500 7 SER A 22 -49.99 -133.97
REMARK 500 7 TYR B 3 -155.95 -131.25
REMARK 500 7 ASN B 48 15.02 -140.68
REMARK 500 8 ALA A 14 42.72 -72.44
REMARK 500 8 MET A 15 -43.02 -149.28
REMARK 500 8 TYR B 3 -46.89 -155.51
REMARK 500 8 MET B 15 -50.50 -151.73
REMARK 500 8 HIS B 40 -0.66 -57.74
REMARK 500 9 TYR A 3 -67.92 -151.52
REMARK 500 9 HIS A 40 -9.41 -54.77
REMARK 500 9 TYR B 3 -67.78 -127.77
REMARK 500 9 LYS B 9 1.57 -66.16
REMARK 500 9 ALA B 21 41.17 -80.37
REMARK 500 10 ASP A 2 -34.63 -171.37
REMARK 500 10 VAL A 25 -57.19 -144.53
REMARK 500 10 ASP A 27 129.84 48.87
REMARK 500 10 HIS A 40 -6.30 -57.08
REMARK 500 10 TYR B 3 -51.34 -143.96
REMARK 500 11 ASP A 2 -20.17 176.26
REMARK 500 11 LYS A 9 2.89 -65.88
REMARK 500 11 ALA A 14 59.68 -67.52
REMARK 500 11 MET A 15 -51.78 -158.31
REMARK 500 11 VAL A 25 -69.12 -151.53
REMARK 500
REMARK 500 THIS ENTRY HAS 103 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 TYR A 3 LEU A 4 7 -149.73
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 50 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 11 OE2
REMARK 620 2 GLU A 11 OE1 64.9
REMARK 620 3 GLU A 37 OE1 127.5 91.7
REMARK 620 4 HIS A 40 ND1 100.2 162.0 89.9
REMARK 620 5 GLU B 37 OE2 116.3 104.5 114.8 91.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 150 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 37 OE2
REMARK 620 2 GLU B 11 OE2 113.0
REMARK 620 3 GLU B 11 OE1 105.1 65.2
REMARK 620 4 GLU B 37 OE1 109.5 136.0 93.2
REMARK 620 5 HIS B 40 ND1 91.4 98.7 160.3 91.3
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 ZN A 50
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 150
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EC5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FOUR-HELIX BUNDLE MODEL
REMARK 900 RELATED ID: 1JMO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FOUR-HELIX BUNDLE MODEL
REMARK 900 RELATED ID: 1JMB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FOUR-HELIX BUNDLE MODEL
REMARK 900 RELATED ID: 1NVO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF FOUR-HELIX BUNDLE MODEL
REMARK 900 RELATED ID: 1U7M RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF FOUR-HELIX BUNDLE MODEL, DUE FERRI(II) TURN
REMARK 900 MUTANT'
DBREF 1U7J A 1 49 PDB 1U7J 1U7J 1 49
DBREF 1U7J B 1 49 PDB 1U7J 1U7J 1 49
SEQRES 1 A 49 MET ASP TYR LEU ARG GLU LEU TYR LYS LEU GLU GLN GLN
SEQRES 2 A 49 ALA MET LYS LEU TYR ARG GLU ALA SER GLU ARG VAL GLY
SEQRES 3 A 49 ASP PRO VAL LEU ALA LYS ILE LEU GLU ASP GLU GLU LYS
SEQRES 4 A 49 HIS ILE GLU TRP LEU GLU THR ILE ASN GLY
SEQRES 1 B 49 MET ASP TYR LEU ARG GLU LEU TYR LYS LEU GLU GLN GLN
SEQRES 2 B 49 ALA MET LYS LEU TYR ARG GLU ALA SER GLU ARG VAL GLY
SEQRES 3 B 49 ASP PRO VAL LEU ALA LYS ILE LEU GLU ASP GLU GLU LYS
SEQRES 4 B 49 HIS ILE GLU TRP LEU GLU THR ILE ASN GLY
HET ZN A 50 1
HET ZN B 150 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 LEU A 4 GLY A 26 1 23
HELIX 2 2 ASP A 27 ILE A 47 1 21
HELIX 3 3 ASP B 2 GLY B 26 1 25
HELIX 4 4 ASP B 27 ILE B 47 1 21
LINK OE2 GLU A 11 ZN ZN A 50 1555 1555 1.80
LINK OE1 GLU A 11 ZN ZN A 50 1555 1555 1.91
LINK OE1 GLU A 37 ZN ZN A 50 1555 1555 1.79
LINK OE2 GLU A 37 ZN ZN B 150 1555 1555 1.78
LINK ND1 HIS A 40 ZN ZN A 50 1555 1555 2.11
LINK ZN ZN A 50 OE2 GLU B 37 1555 1555 1.78
LINK OE2 GLU B 11 ZN ZN B 150 1555 1555 1.82
LINK OE1 GLU B 11 ZN ZN B 150 1555 1555 1.88
LINK OE1 GLU B 37 ZN ZN B 150 1555 1555 1.80
LINK ND1 HIS B 40 ZN ZN B 150 1555 1555 2.10
SITE 1 AC1 4 GLU A 11 GLU A 37 HIS A 40 GLU B 37
SITE 1 AC2 4 GLU A 37 GLU B 11 GLU B 37 HIS B 40
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 - r 2 2 Bytes