HEADER DNA BINDING PROTEIN 01-MAY-92 1BBO
TITLE HIGH-RESOLUTION SOLUTION STRUCTURE OF THE DOUBLE CYS2*HIS2 ZINC FINGER
TITLE 2 FROM THE HUMAN ENHANCER BINDING PROTEIN MBP-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HUMAN ENHANCER-BINDING PROTEIN MBP-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 60
AUTHOR G.M.CLORE,J.G.OMICHINSKI,A.M.GRONENBORN
REVDAT 6 15-NOV-23 1BBO 1 ATOM
REVDAT 5 16-FEB-22 1BBO 1 KEYWDS REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1BBO 1 VERSN
REVDAT 3 15-MAY-95 1BBO 1 REMARK
REVDAT 2 15-JAN-95 1BBO 1 SOURCE
REVDAT 1 31-OCT-93 1BBO 0
JRNL AUTH J.G.OMICHINSKI,G.M.CLORE,M.ROBIEN,K.SAKAGUCHI,E.APPELLA,
JRNL AUTH 2 A.M.GRONENBORN
JRNL TITL HIGH-RESOLUTION SOLUTION STRUCTURE OF THE DOUBLE CYS2HIS2
JRNL TITL 2 ZINC FINGER FROM THE HUMAN ENHANCER BINDING PROTEIN MBP-1.
JRNL REF BIOCHEMISTRY V. 31 3907 1992
JRNL REFN ISSN 0006-2960
JRNL PMID 1567844
JRNL DOI 10.1021/BI00131A004
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL
REMARK 3 STATISTICS ARE GIVEN IN THE JRNL REFERENCE ABOVE.
REMARK 3
REMARK 3 THE STRUCTURES ARE BASED ON 1135 INTERPROTON DISTANCE
REMARK 3 RESTRAINTS DERIVED FROM NOE MEASUREMENTS; AND 55 PHI, 44
REMARK 3 PSI AND 45 CHI1 TORSION ANGLE RESTRAINTS DERIVED FROM
REMARK 3 COUPLING CONSTANTS AND NOE DATA, USING THE CONFORMATIONAL
REMARK 3 GRID SEARCH PROGRAM STEREOSEARCH (M. NILGES, G. M. CLORE,
REMARK 3 AND A. M. GRONENBORN, (1990) BIOPOLYMERS 29, 813.
REMARK 3
REMARK 3 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID
REMARK 3 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED
REMARK 3 ANNEALING METHOD (M. NILGES, G. M. CLORE, AND A. M.
REMARK 3 GRONENBORN, FEBS LETT. 229, 317-324 (1988)).
REMARK 3
REMARK 3 A TOTAL OF 30 STRUCTURES WERE CALCULATED. AS THERE IS SOME
REMARK 3 UNCERTAINTY IN THE EXACT ORIENTATION OF THE N- AND C-
REMARK 3 TERMINAL FINGERS RELATIVE TO EACH OTHER, THE COORDINATES
REMARK 3 ARE PRESENTED TWICE. IN MODELS 1 THROUGH 30, THE
REMARK 3 COORDINATES ARE BEST FITTED TO THE N-TERMINAL DOMAIN
REMARK 3 (RESIDUES 2 - 28). IN MODELS 31 THROUGH 60, THE
REMARK 3 COORDINATES ARE BEST FITTED TO THE C-TERMINAL DOMAIN
REMARK 3 (RESIDUES 27 - 55). THE ANGLE BETWEEN THE LONG AXES OF THE
REMARK 3 HELICES (RESIDUES 13 - 25 AND 41 - 55 FROM THE N- AND C-
REMARK 3 TERMINAL FINGERS, RESPECTIVELY) ADOPT A RANGE OF VALUES
REMARK 3 CENTERED AROUND A MEAN OF 47 DEGREES WITH A STANDARD
REMARK 3 DEVIATION OF +/- 5 DEGREES. CONSEQUENTLY, NO AVERAGE
REMARK 3 STRUCTURE IS GIVEN.
REMARK 3
REMARK 3 THE NUMBERS IN LAST COLUMN IN THE COORDINATE FILES HAVE NO
REMARK 3 MEANING.
REMARK 3
REMARK 3 ALL THE INTERPROTON DISTANCE AND TORSION ANGLE RESTRAINTS
REMARK 3 ARE INCLUDED HERE AS A SEPARATE FILE: MBP_EXPT_DATA.DAT
REMARK 4
REMARK 4 1BBO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171565.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 60
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 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 1 HIS A 20 CG HIS A 20 ND1 -0.093
REMARK 500 1 HIS A 31 CG HIS A 31 ND1 -0.116
REMARK 500 1 HIS A 48 CG HIS A 48 ND1 -0.092
REMARK 500 1 HIS A 54 CG HIS A 54 ND1 -0.092
REMARK 500 2 HIS A 20 CG HIS A 20 ND1 -0.093
REMARK 500 2 HIS A 31 CG HIS A 31 ND1 -0.115
REMARK 500 2 HIS A 48 CG HIS A 48 ND1 -0.092
REMARK 500 2 HIS A 54 CG HIS A 54 ND1 -0.091
REMARK 500 3 HIS A 20 CG HIS A 20 ND1 -0.092
REMARK 500 3 HIS A 31 CG HIS A 31 ND1 -0.116
REMARK 500 3 HIS A 48 CG HIS A 48 ND1 -0.091
REMARK 500 4 HIS A 20 CG HIS A 20 ND1 -0.093
REMARK 500 4 HIS A 31 CG HIS A 31 ND1 -0.117
REMARK 500 4 HIS A 48 CG HIS A 48 ND1 -0.093
REMARK 500 4 HIS A 54 CG HIS A 54 ND1 -0.092
REMARK 500 5 HIS A 20 CG HIS A 20 ND1 -0.094
REMARK 500 5 HIS A 31 CG HIS A 31 ND1 -0.116
REMARK 500 5 HIS A 48 CG HIS A 48 ND1 -0.092
REMARK 500 5 HIS A 54 CG HIS A 54 ND1 -0.094
REMARK 500 6 HIS A 20 CG HIS A 20 ND1 -0.093
REMARK 500 6 HIS A 31 CG HIS A 31 ND1 -0.115
REMARK 500 6 HIS A 48 CG HIS A 48 ND1 -0.091
REMARK 500 6 HIS A 54 CG HIS A 54 ND1 -0.092
REMARK 500 7 HIS A 20 CG HIS A 20 ND1 -0.094
REMARK 500 7 HIS A 31 CG HIS A 31 ND1 -0.117
REMARK 500 7 HIS A 48 CG HIS A 48 ND1 -0.093
REMARK 500 7 HIS A 54 CG HIS A 54 ND1 -0.092
REMARK 500 8 HIS A 20 CG HIS A 20 ND1 -0.091
REMARK 500 8 HIS A 31 CG HIS A 31 ND1 -0.117
REMARK 500 8 HIS A 48 CG HIS A 48 ND1 -0.091
REMARK 500 8 HIS A 54 CG HIS A 54 ND1 -0.091
REMARK 500 9 HIS A 20 CG HIS A 20 ND1 -0.095
REMARK 500 9 HIS A 31 CG HIS A 31 ND1 -0.116
REMARK 500 9 HIS A 48 CG HIS A 48 ND1 -0.091
REMARK 500 9 HIS A 54 CG HIS A 54 ND1 -0.092
REMARK 500 10 HIS A 20 CG HIS A 20 ND1 -0.095
REMARK 500 10 HIS A 31 CG HIS A 31 ND1 -0.115
REMARK 500 10 HIS A 48 CG HIS A 48 ND1 -0.092
REMARK 500 10 HIS A 54 CG HIS A 54 ND1 -0.092
REMARK 500 11 HIS A 20 CG HIS A 20 ND1 -0.093
REMARK 500 11 HIS A 31 CG HIS A 31 ND1 -0.115
REMARK 500 11 HIS A 48 CG HIS A 48 ND1 -0.091
REMARK 500 11 HIS A 54 CG HIS A 54 ND1 -0.091
REMARK 500 12 HIS A 20 CG HIS A 20 ND1 -0.093
REMARK 500 12 HIS A 31 CG HIS A 31 ND1 -0.117
REMARK 500 12 HIS A 48 CG HIS A 48 ND1 -0.092
REMARK 500 12 HIS A 54 CG HIS A 54 ND1 -0.090
REMARK 500 13 HIS A 20 CG HIS A 20 ND1 -0.091
REMARK 500 13 HIS A 31 CG HIS A 31 ND1 -0.118
REMARK 500 13 HIS A 48 CG HIS A 48 ND1 -0.091
REMARK 500
REMARK 500 THIS ENTRY HAS 236 BOND 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 TYR A 2 66.29 -152.81
REMARK 500 1 GLU A 6 -70.11 -90.90
REMARK 500 1 LYS A 18 -38.31 -35.49
REMARK 500 1 THR A 25 -110.76 -95.68
REMARK 500 1 ASP A 26 31.24 -149.38
REMARK 500 1 VAL A 27 47.48 -96.53
REMARK 500 1 TYR A 34 -63.94 -142.75
REMARK 500 1 CYS A 35 -174.68 -68.21
REMARK 500 1 ALA A 53 -86.23 -52.97
REMARK 500 1 LYS A 56 48.86 -76.94
REMARK 500 2 LYS A 12 10.81 -63.30
REMARK 500 2 PRO A 14 -70.96 -63.49
REMARK 500 2 THR A 25 -93.17 -94.20
REMARK 500 2 ASP A 26 23.56 -156.90
REMARK 500 2 VAL A 27 50.11 -97.19
REMARK 500 2 TYR A 34 -72.90 -118.55
REMARK 500 2 CYS A 35 -169.20 -59.39
REMARK 500 2 LYS A 52 8.48 -68.52
REMARK 500 2 ALA A 53 -94.80 -44.67
REMARK 500 2 SER A 55 -41.78 -155.19
REMARK 500 3 TYR A 2 45.08 -156.01
REMARK 500 3 THR A 25 -100.02 -91.84
REMARK 500 3 ASP A 26 28.50 -159.58
REMARK 500 3 VAL A 27 46.50 -91.81
REMARK 500 3 TYR A 34 -44.32 -141.45
REMARK 500 3 ALA A 53 -76.21 -47.33
REMARK 500 3 HIS A 54 106.54 -170.61
REMARK 500 4 GLU A 6 -69.65 -90.37
REMARK 500 4 THR A 25 -100.10 -84.00
REMARK 500 4 ASP A 26 27.12 -151.28
REMARK 500 4 VAL A 27 45.27 -100.99
REMARK 500 4 TYR A 30 94.96 -66.11
REMARK 500 4 TYR A 34 -67.93 -144.40
REMARK 500 4 CYS A 35 -165.25 -62.43
REMARK 500 4 SER A 51 155.28 -44.58
REMARK 500 4 LYS A 52 9.83 -69.29
REMARK 500 4 ALA A 53 -93.61 -46.28
REMARK 500 4 SER A 55 61.15 -162.33
REMARK 500 4 LYS A 56 -88.19 -49.92
REMARK 500 5 TYR A 2 47.35 -143.69
REMARK 500 5 GLU A 6 -69.51 -91.23
REMARK 500 5 LYS A 12 11.07 -64.78
REMARK 500 5 THR A 25 -99.37 -96.99
REMARK 500 5 ASP A 26 28.11 -157.38
REMARK 500 5 VAL A 27 46.26 -101.92
REMARK 500 5 TYR A 34 -65.87 -142.44
REMARK 500 5 CYS A 35 -166.24 -64.86
REMARK 500 5 SER A 51 156.63 -44.70
REMARK 500 5 ALA A 53 -87.26 -46.51
REMARK 500 5 SER A 55 -34.48 -151.67
REMARK 500
REMARK 500 THIS ENTRY HAS 643 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 10 0.30 SIDE CHAIN
REMARK 500 1 ARG A 22 0.20 SIDE CHAIN
REMARK 500 1 ARG A 28 0.26 SIDE CHAIN
REMARK 500 2 ARG A 10 0.28 SIDE CHAIN
REMARK 500 2 ARG A 22 0.16 SIDE CHAIN
REMARK 500 2 ARG A 28 0.27 SIDE CHAIN
REMARK 500 3 ARG A 10 0.20 SIDE CHAIN
REMARK 500 3 ARG A 22 0.32 SIDE CHAIN
REMARK 500 3 ARG A 28 0.15 SIDE CHAIN
REMARK 500 4 ARG A 10 0.30 SIDE CHAIN
REMARK 500 4 ARG A 22 0.32 SIDE CHAIN
REMARK 500 4 ARG A 28 0.27 SIDE CHAIN
REMARK 500 5 ARG A 10 0.20 SIDE CHAIN
REMARK 500 5 ARG A 22 0.31 SIDE CHAIN
REMARK 500 6 ARG A 10 0.21 SIDE CHAIN
REMARK 500 6 ARG A 22 0.15 SIDE CHAIN
REMARK 500 6 ARG A 28 0.28 SIDE CHAIN
REMARK 500 7 ARG A 10 0.28 SIDE CHAIN
REMARK 500 7 ARG A 22 0.28 SIDE CHAIN
REMARK 500 7 ARG A 28 0.32 SIDE CHAIN
REMARK 500 8 ARG A 10 0.32 SIDE CHAIN
REMARK 500 8 ARG A 22 0.27 SIDE CHAIN
REMARK 500 9 ARG A 10 0.32 SIDE CHAIN
REMARK 500 9 ARG A 28 0.32 SIDE CHAIN
REMARK 500 10 ARG A 10 0.32 SIDE CHAIN
REMARK 500 10 ARG A 22 0.30 SIDE CHAIN
REMARK 500 10 ARG A 28 0.20 SIDE CHAIN
REMARK 500 11 ARG A 10 0.29 SIDE CHAIN
REMARK 500 11 ARG A 22 0.23 SIDE CHAIN
REMARK 500 11 ARG A 28 0.26 SIDE CHAIN
REMARK 500 12 ARG A 10 0.28 SIDE CHAIN
REMARK 500 12 ARG A 22 0.27 SIDE CHAIN
REMARK 500 12 ARG A 28 0.32 SIDE CHAIN
REMARK 500 13 ARG A 10 0.26 SIDE CHAIN
REMARK 500 13 ARG A 22 0.30 SIDE CHAIN
REMARK 500 13 ARG A 28 0.21 SIDE CHAIN
REMARK 500 14 ARG A 10 0.29 SIDE CHAIN
REMARK 500 14 ARG A 22 0.24 SIDE CHAIN
REMARK 500 14 ARG A 28 0.20 SIDE CHAIN
REMARK 500 15 ARG A 10 0.19 SIDE CHAIN
REMARK 500 15 ARG A 28 0.31 SIDE CHAIN
REMARK 500 16 ARG A 10 0.26 SIDE CHAIN
REMARK 500 16 ARG A 22 0.28 SIDE CHAIN
REMARK 500 16 ARG A 28 0.29 SIDE CHAIN
REMARK 500 17 ARG A 10 0.26 SIDE CHAIN
REMARK 500 17 ARG A 22 0.31 SIDE CHAIN
REMARK 500 17 ARG A 28 0.23 SIDE CHAIN
REMARK 500 18 ARG A 10 0.25 SIDE CHAIN
REMARK 500 18 ARG A 22 0.20 SIDE CHAIN
REMARK 500 18 ARG A 28 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 166 PLANE DEVIATIONS.
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 60 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 4 SG
REMARK 620 2 CYS A 7 SG 111.2
REMARK 620 3 HIS A 20 NE2 111.7 110.6
REMARK 620 4 HIS A 24 NE2 110.9 101.2 110.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 61 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 32 SG
REMARK 620 2 CYS A 35 SG 112.6
REMARK 620 3 HIS A 48 NE2 113.7 110.5
REMARK 620 4 HIS A 54 NE2 112.8 92.7 112.7
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 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 61
DBREF 1BBO A 1 57 UNP P15822 ZEP1_HUMAN 2086 2142
SEQADV 1BBO ABA A 11 UNP P15822 CYS 2096 CONFLICT
SEQRES 1 A 57 LYS TYR ILE CYS GLU GLU CYS GLY ILE ARG ABA LYS LYS
SEQRES 2 A 57 PRO SER MET LEU LYS LYS HIS ILE ARG THR HIS THR ASP
SEQRES 3 A 57 VAL ARG PRO TYR HIS CYS THR TYR CYS ASN PHE SER PHE
SEQRES 4 A 57 LYS THR LYS GLY ASN LEU THR LYS HIS MET LYS SER LYS
SEQRES 5 A 57 ALA HIS SER LYS LYS
MODRES 1BBO ABA A 11 ALA ALPHA-AMINOBUTYRIC ACID
HET ABA A 11 13
HET ZN A 60 1
HET ZN A 61 1
HETNAM ABA ALPHA-AMINOBUTYRIC ACID
HETNAM ZN ZINC ION
FORMUL 1 ABA C4 H9 N O2
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 LYS A 13 HIS A 24 1 12
HELIX 2 2 THR A 41 SER A 51 1 11
SHEET 1 A 2 TYR A 30 HIS A 31 0
SHEET 2 A 2 SER A 38 PHE A 39 -1 N PHE A 39 O TYR A 30
LINK C ARG A 10 N ABA A 11 1555 1555 1.31
LINK C ABA A 11 N LYS A 12 1555 1555 1.30
LINK SG CYS A 4 ZN ZN A 60 1555 1555 2.29
LINK SG CYS A 7 ZN ZN A 60 1555 1555 2.29
LINK NE2 HIS A 20 ZN ZN A 60 1555 1555 2.00
LINK NE2 HIS A 24 ZN ZN A 60 1555 1555 1.98
LINK SG CYS A 32 ZN ZN A 61 1555 1555 2.31
LINK SG CYS A 35 ZN ZN A 61 1555 1555 2.30
LINK NE2 HIS A 48 ZN ZN A 61 1555 1555 2.00
LINK NE2 HIS A 54 ZN ZN A 61 1555 1555 1.99
SITE 1 AC1 4 CYS A 4 CYS A 7 HIS A 20 HIS A 24
SITE 1 AC2 4 CYS A 32 CYS A 35 HIS A 48 HIS A 54
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
