Header list of 2alb.pdb file
Complete list - r 9 2 Bytes
HEADER ISOMERASE 05-AUG-05 2ALB
TITLE NMR STRUCTURE OF THE N-TERMINAL DOMAIN A OF THE GLYCOPROTEIN CHAPERONE
TITLE 2 ERP57
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE A3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DISULFIDE ISOMERASE ER-60, ERP60, 58 KDA MICROSOMAL PROTEIN,
COMPND 5 P58, ERP57, 58 KDA GLUCOSE REGULATED PROTEIN;
COMPND 6 EC: 5.3.4.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS THIOREDOXIN FOLD, ISOMERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.SILVENNOINEN,H.TOSSAVAINEN,J.MYLLYHARJU,P.PERMI
REVDAT 3 09-MAR-22 2ALB 1 REMARK
REVDAT 2 24-FEB-09 2ALB 1 VERSN
REVDAT 1 15-AUG-06 2ALB 0
JRNL AUTH L.SILVENNOINEN,H.TOSSAVAINEN,J.MYLLYHARJU,P.PERMI
JRNL TITL NMR STRUCTURE OF THE N-TERMINAL DOMAIN A OF THE GLYCOPROTEIN
JRNL TITL 2 CHAPERONE ERP57
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, AMBER 8.0
REMARK 3 AUTHORS : VARIAN ASSOCIATES INC. (VNMR), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ALB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034029.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 0.8-2.5 MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.110, CYANA 2.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 4 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 9 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 9 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 10 ARG A 83 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 13 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 16 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 18 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.6 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 5 63.77 -106.85
REMARK 500 1 ASN A 10 -12.51 -142.13
REMARK 500 1 ILE A 53 -45.97 -132.99
REMARK 500 1 SER A 74 11.02 52.64
REMARK 500 1 ASP A 84 28.39 48.77
REMARK 500 1 SER A 112 9.66 57.82
REMARK 500 2 ASN A 64 47.80 -146.91
REMARK 500 2 VAL A 73 51.08 -69.29
REMARK 500 2 ASP A 84 28.80 48.32
REMARK 500 3 ASN A 10 -12.89 -143.68
REMARK 500 3 HIS A 35 -14.22 -141.05
REMARK 500 3 ALA A 111 10.21 58.32
REMARK 500 4 GLU A 5 70.93 -119.56
REMARK 500 4 ASP A 17 48.08 -80.11
REMARK 500 4 ASN A 64 49.88 -143.18
REMARK 500 4 SER A 74 9.96 -51.24
REMARK 500 4 ARG A 95 45.63 -81.37
REMARK 500 5 PRO A 31 30.02 -58.34
REMARK 500 5 HIS A 35 -31.93 -135.03
REMARK 500 5 ASN A 64 44.80 -142.60
REMARK 500 5 ASP A 84 25.20 48.29
REMARK 500 5 PRO A 94 -4.20 -53.63
REMARK 500 6 ASP A 84 25.91 49.79
REMARK 500 6 ASP A 92 53.40 -149.65
REMARK 500 7 ASN A 10 -14.51 -142.03
REMARK 500 7 ASP A 17 32.32 -79.94
REMARK 500 7 PHE A 29 -156.38 -153.48
REMARK 500 7 TRP A 32 108.60 -57.44
REMARK 500 7 ASN A 64 45.69 -142.69
REMARK 500 7 ASP A 92 46.31 -145.18
REMARK 500 8 ASN A 10 -14.45 -141.85
REMARK 500 8 ARG A 14 -37.46 -133.80
REMARK 500 8 ASP A 17 39.21 -79.50
REMARK 500 8 ILE A 53 -47.21 -131.84
REMARK 500 8 ASP A 84 25.75 47.40
REMARK 500 8 ALA A 111 24.86 46.79
REMARK 500 8 SER A 112 -15.31 -140.21
REMARK 500 9 GLU A 12 1.31 -67.99
REMARK 500 9 PRO A 31 2.73 -63.39
REMARK 500 9 SER A 74 -18.26 62.58
REMARK 500 9 ASP A 92 41.12 -144.52
REMARK 500 10 ASN A 10 -34.08 -131.18
REMARK 500 10 ILE A 53 -51.47 -129.73
REMARK 500 11 ASN A 10 -12.81 -147.63
REMARK 500 11 GLU A 12 2.29 -66.79
REMARK 500 11 ILE A 53 -40.26 -136.36
REMARK 500 11 ASP A 84 27.62 48.30
REMARK 500 11 ALA A 111 14.65 59.04
REMARK 500 12 GLU A 12 0.42 -63.17
REMARK 500 12 PRO A 31 29.73 -77.17
REMARK 500
REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6308 RELATED DB: BMRB
DBREF 2ALB A 1 113 UNP P30101 PDIA3_HUMAN 25 137
SEQRES 1 A 113 SER ASP VAL LEU GLU LEU THR ASP ASP ASN PHE GLU SER
SEQRES 2 A 113 ARG ILE SER ASP THR GLY SER ALA GLY LEU MET LEU VAL
SEQRES 3 A 113 GLU PHE PHE ALA PRO TRP CYS GLY HIS CYS LYS ARG LEU
SEQRES 4 A 113 ALA PRO GLU TYR GLU ALA ALA ALA THR ARG LEU LYS GLY
SEQRES 5 A 113 ILE VAL PRO LEU ALA LYS VAL ASP CYS THR ALA ASN THR
SEQRES 6 A 113 ASN THR CYS ASN LYS TYR GLY VAL SER GLY TYR PRO THR
SEQRES 7 A 113 LEU LYS ILE PHE ARG ASP GLY GLU GLU ALA GLY ALA TYR
SEQRES 8 A 113 ASP GLY PRO ARG THR ALA ASP GLY ILE VAL SER HIS LEU
SEQRES 9 A 113 LYS LYS GLN ALA GLY PRO ALA SER VAL
HELIX 1 1 ASN A 10 ILE A 15 1 6
HELIX 2 2 SER A 16 THR A 18 5 3
HELIX 3 3 GLY A 34 LEU A 50 1 17
HELIX 4 4 ASN A 64 TYR A 71 1 8
HELIX 5 5 THR A 96 GLY A 109 1 14
SHEET 1 A 5 LEU A 4 GLU A 5 0
SHEET 2 A 5 LEU A 56 ASP A 60 1 O LYS A 58 N LEU A 4
SHEET 3 A 5 LEU A 23 PHE A 29 1 N GLU A 27 O ALA A 57
SHEET 4 A 5 THR A 78 ARG A 83 -1 O THR A 78 N PHE A 28
SHEET 5 A 5 GLU A 86 GLU A 87 -1 O GLU A 86 N ARG A 83
CISPEP 1 TYR A 76 PRO A 77 1 -4.78
CISPEP 2 TYR A 76 PRO A 77 2 -5.35
CISPEP 3 TYR A 76 PRO A 77 3 3.15
CISPEP 4 TYR A 76 PRO A 77 4 -2.40
CISPEP 5 TYR A 76 PRO A 77 5 -2.70
CISPEP 6 TYR A 76 PRO A 77 6 1.08
CISPEP 7 TYR A 76 PRO A 77 7 3.40
CISPEP 8 TYR A 76 PRO A 77 8 2.15
CISPEP 9 TYR A 76 PRO A 77 9 2.17
CISPEP 10 TYR A 76 PRO A 77 10 1.10
CISPEP 11 TYR A 76 PRO A 77 11 -1.18
CISPEP 12 TYR A 76 PRO A 77 12 -10.19
CISPEP 13 TYR A 76 PRO A 77 13 1.81
CISPEP 14 TYR A 76 PRO A 77 14 2.76
CISPEP 15 TYR A 76 PRO A 77 15 -0.97
CISPEP 16 TYR A 76 PRO A 77 16 5.02
CISPEP 17 TYR A 76 PRO A 77 17 -5.59
CISPEP 18 TYR A 76 PRO A 77 18 -4.67
CISPEP 19 TYR A 76 PRO A 77 19 0.09
CISPEP 20 TYR A 76 PRO A 77 20 -5.43
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 9 2 Bytes