Header list of 3btb.pdb file
Complete list - 16 20 Bytes
HEADER TRANSMEMBRANE 07-SEP-97 3BTB
TITLE NMR SOLUTION STRUCTURE OF A BAND 3 PEPTIDE INHIBITOR BOUND TO
TITLE 2 GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BAND 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GLYCOLYTIC ENZYME-BINDING DOMAIN, N-TERMINAL 15 RESIDUES OF
COMPND 5 BAND 3 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS BAND 3, G3PDH, EXCHANGE TRANSFER, FAST EXCHANGE, TRANSMEMBRANE,
KEYWDS 2 GLYCOPROTEIN, ANION EXCHANGE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.Z.EISENMESSER,C.B.POST
REVDAT 3 16-MAR-22 3BTB 1 REMARK LINK
REVDAT 2 24-FEB-09 3BTB 1 VERSN
REVDAT 1 28-JAN-98 3BTB 0
JRNL AUTH E.Z.EISENMESSER,C.B.POST
JRNL TITL INSIGHTS INTO TYROSINE PHOSPHORYLATION CONTROL OF
JRNL TITL 2 PROTEIN-PROTEIN ASSOCIATION FROM THE NMR STRUCTURE OF A BAND
JRNL TITL 3 3 PEPTIDE INHIBITOR BOUND TO GLYCERALDEHYDE-3-PHOSPHATE
JRNL TITL 4 DEHYDROGENASE.
JRNL REF BIOCHEMISTRY V. 37 867 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9454576
JRNL DOI 10.1021/BI971445B
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3BTB 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_1000178895.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS 600
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CHARMM, XPLOR
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 GOOD GEOMETRY
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 H2 MET A 1 OE1 GLU A 3 1.55
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 2 GLU A 9 C - N - CA ANGL. DEV. = 15.1 DEGREES
REMARK 500 3 TYR A 8 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 4 TYR A 8 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 7 GLU A 9 C - N - CA ANGL. DEV. = 15.2 DEGREES
REMARK 500 8 TYR A 8 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 14 ASP A 10 CB - CA - C ANGL. DEV. = 12.7 DEGREES
REMARK 500 16 TYR A 8 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 16 MET A 12 CG - SD - CE ANGL. DEV. = -10.8 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 GLU A 2 58.40 -158.46
REMARK 500 1 ASP A 7 37.29 -93.02
REMARK 500 1 ASP A 10 0.47 83.37
REMARK 500 2 GLU A 2 -145.42 -95.52
REMARK 500 2 GLU A 3 86.50 -69.11
REMARK 500 2 GLN A 5 -45.00 -132.46
REMARK 500 2 ASP A 7 38.38 -74.54
REMARK 500 2 GLU A 9 64.48 39.32
REMARK 500 2 MET A 12 -57.45 -124.97
REMARK 500 2 GLU A 13 -64.72 -141.92
REMARK 500 3 ASP A 7 33.85 -55.83
REMARK 500 3 TYR A 8 -71.71 -138.65
REMARK 500 3 ASP A 10 -74.75 -157.95
REMARK 500 4 GLU A 9 29.15 40.33
REMARK 500 4 ASP A 10 -78.09 -151.99
REMARK 500 5 ASP A 7 61.06 -62.62
REMARK 500 5 TYR A 8 -71.68 -97.07
REMARK 500 5 GLU A 9 77.78 54.17
REMARK 500 5 MET A 12 22.10 -143.00
REMARK 500 6 GLU A 3 59.28 -58.75
REMARK 500 6 GLN A 5 -39.49 -154.15
REMARK 500 6 ASP A 7 48.61 -92.63
REMARK 500 6 GLU A 9 71.19 30.13
REMARK 500 6 MET A 12 37.88 -148.98
REMARK 500 6 GLU A 13 -163.55 -110.97
REMARK 500 6 GLU A 14 60.15 -64.24
REMARK 500 7 GLU A 2 71.31 -153.09
REMARK 500 7 ASP A 7 78.02 -50.48
REMARK 500 7 TYR A 8 -82.10 -129.58
REMARK 500 7 ASP A 10 -69.69 -143.87
REMARK 500 8 GLU A 3 45.35 -80.54
REMARK 500 8 ASP A 7 9.35 -61.43
REMARK 500 8 GLU A 9 68.27 30.39
REMARK 500 8 GLU A 14 43.21 -59.29
REMARK 500 9 GLU A 2 61.59 -159.05
REMARK 500 9 GLU A 3 -58.20 -159.46
REMARK 500 9 TYR A 8 -54.81 -157.32
REMARK 500 9 GLU A 9 83.96 37.61
REMARK 500 9 GLU A 14 53.17 -50.06
REMARK 500 10 GLU A 2 77.07 -171.96
REMARK 500 10 GLU A 3 56.85 -92.73
REMARK 500 10 GLN A 5 -50.56 -135.75
REMARK 500 10 ASP A 7 49.16 -61.31
REMARK 500 10 GLU A 9 68.04 29.26
REMARK 500 10 MET A 12 64.76 -101.44
REMARK 500 11 ASP A 7 17.78 -65.88
REMARK 500 11 GLU A 9 75.12 36.24
REMARK 500 11 GLU A 13 -68.00 -105.87
REMARK 500 12 ASP A 7 38.15 -76.08
REMARK 500 12 GLU A 9 71.84 41.41
REMARK 500
REMARK 500 THIS ENTRY HAS 87 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 16
DBREF 3BTB A 1 15 UNP P02730 B3AT_HUMAN 1 15
SEQRES 1 A 16 MET GLU GLU LEU GLN ASP ASP TYR GLU ASP MET MET GLU
SEQRES 2 A 16 GLU ASN NH2
HET NH2 A 16 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
LINK C ASN A 15 N NH2 A 16 1555 1555 1.35
SITE 1 AC1 2 GLU A 14 ASN A 15
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 - 16 20 Bytes