Header list of 1aqs.pdb file
Complete list - 16 20 Bytes
HEADER METALLOTHIONEIN 31-JUL-97 1AQS
TITLE CU-METALLOTHIONEIN FROM SACCHAROMYCES CEREVISIAE, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CU-METALLOTHIONEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CU-MT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 STRAIN: 2180
KEYWDS METALLOTHIONEIN, COPPER DETOXIFICATION, METAL-THIOLATE CLUSTER
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.W.PETERSON,S.S.NARULA,I.M.ARMITAGE
REVDAT 3 16-FEB-22 1AQS 1 REMARK LINK
REVDAT 2 24-FEB-09 1AQS 1 VERSN
REVDAT 1 24-DEC-97 1AQS 0
JRNL AUTH C.W.PETERSON,S.S.NARULA,I.M.ARMITAGE
JRNL TITL 3D SOLUTION STRUCTURE OF COPPER AND SILVER-SUBSTITUTED YEAST
JRNL TITL 2 METALLOTHIONEINS.
JRNL REF FEBS LETT. V. 379 85 1996
JRNL REFN ISSN 0014-5793
JRNL PMID 8566237
JRNL DOI 10.1016/0014-5793(95)01492-6
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1AQS 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_1000171142.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; AG-FILTERED COSY; RELAY
REMARK 210 -COSY; TOCSY; NOESY; 1H-109AG
REMARK 210 HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM-500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 LYS A 41
REMARK 465 SER A 42
REMARK 465 GLU A 43
REMARK 465 GLU A 44
REMARK 465 THR A 45
REMARK 465 LYS A 46
REMARK 465 LYS A 47
REMARK 465 SER A 48
REMARK 465 CYS A 49
REMARK 465 CYS A 50
REMARK 465 SER A 51
REMARK 465 GLY A 52
REMARK 465 LYS A 53
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 3 -66.96 -141.07
REMARK 500 1 HIS A 5 -91.34 -145.20
REMARK 500 1 GLU A 6 95.01 -160.16
REMARK 500 1 CYS A 11 -151.13 -55.17
REMARK 500 1 SER A 23 43.92 -160.27
REMARK 500 1 PRO A 27 -167.35 -79.35
REMARK 500 1 THR A 28 45.31 -86.91
REMARK 500 1 CYS A 30 51.30 -99.94
REMARK 500 1 ASP A 34 -128.79 -144.42
REMARK 500 1 LYS A 35 32.13 -85.10
REMARK 500 1 CYS A 36 102.67 -48.97
REMARK 500 1 CYS A 38 -164.51 -66.61
REMARK 500 2 GLU A 3 -91.70 -95.47
REMARK 500 2 HIS A 5 -100.82 -160.59
REMARK 500 2 CYS A 11 -154.91 -55.28
REMARK 500 2 ASN A 17 88.60 -62.19
REMARK 500 2 LYS A 22 11.30 -144.77
REMARK 500 2 SER A 23 25.88 -148.66
REMARK 500 2 SER A 25 56.17 -95.71
REMARK 500 2 THR A 28 43.11 -89.92
REMARK 500 2 CYS A 30 52.53 -93.31
REMARK 500 2 ASP A 34 -132.56 -126.26
REMARK 500 2 CYS A 36 103.98 -49.40
REMARK 500 3 HIS A 5 -95.27 -158.25
REMARK 500 3 CYS A 11 -149.56 -54.87
REMARK 500 3 SER A 23 43.06 -160.58
REMARK 500 3 SER A 25 50.84 -107.73
REMARK 500 3 THR A 28 44.83 -89.99
REMARK 500 3 CYS A 30 52.35 -98.84
REMARK 500 3 LYS A 35 35.49 -160.28
REMARK 500 3 PRO A 37 46.80 -84.29
REMARK 500 3 CYS A 38 -162.77 -72.90
REMARK 500 4 HIS A 5 -87.94 -159.09
REMARK 500 4 GLU A 6 97.56 -160.49
REMARK 500 4 CYS A 11 -145.79 -54.65
REMARK 500 4 SER A 23 41.93 -160.77
REMARK 500 4 SER A 25 52.21 -101.34
REMARK 500 4 THR A 28 44.89 -88.59
REMARK 500 4 CYS A 30 52.47 -93.97
REMARK 500 4 LYS A 35 35.00 -160.58
REMARK 500 5 ASN A 2 -40.54 -152.57
REMARK 500 5 HIS A 5 -83.35 -142.46
REMARK 500 5 GLU A 6 97.18 -160.28
REMARK 500 5 CYS A 11 -150.26 -55.12
REMARK 500 5 ASN A 16 -72.08 -86.04
REMARK 500 5 SER A 23 41.56 -160.16
REMARK 500 5 SER A 25 53.43 -98.85
REMARK 500 5 THR A 28 45.29 -88.86
REMARK 500 5 LYS A 35 36.87 -160.48
REMARK 500 5 PRO A 37 47.23 -83.93
REMARK 500
REMARK 500 THIS ENTRY HAS 104 RAMACHANDRAN OUTLIERS.
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 CU1 A 54 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 7 SG
REMARK 620 2 CYS A 9 SG 95.5
REMARK 620 3 CYS A 24 SG 131.0 131.8
REMARK 620 4 CU1 A 57 CU 134.0 103.5 55.9
REMARK 620 5 CU1 A 60 CU 92.4 66.8 115.1 59.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 56 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 7 SG
REMARK 620 2 CYS A 20 SG 146.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 60 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 9 SG
REMARK 620 2 CYS A 14 SG 100.6
REMARK 620 3 CYS A 38 SG 161.8 97.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 55 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 14 SG 129.4
REMARK 620 3 CYS A 36 SG 103.7 125.6
REMARK 620 4 CU1 A 58 CU 59.1 123.2 91.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 58 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 CYS A 30 SG 147.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 57 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 24 SG
REMARK 620 2 CYS A 26 SG 108.9
REMARK 620 3 CYS A 38 SG 131.0 119.9
REMARK 620 4 CU1 A 60 CU 107.3 107.2 55.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 59 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 26 SG
REMARK 620 2 CYS A 30 SG 100.2
REMARK 620 3 CYS A 36 SG 152.7 106.4
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 54
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 55
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 58
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 59
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 60
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQR RELATED DB: PDB
DBREF 1AQS A 1 53 UNP P07215 MTCU_YEAST 9 61
SEQRES 1 A 53 GLN ASN GLU GLY HIS GLU CYS GLN CYS GLN CYS GLY SER
SEQRES 2 A 53 CYS LYS ASN ASN GLU GLN CYS GLN LYS SER CYS SER CYS
SEQRES 3 A 53 PRO THR GLY CYS ASN SER ASP ASP LYS CYS PRO CYS GLY
SEQRES 4 A 53 ASN LYS SER GLU GLU THR LYS LYS SER CYS CYS SER GLY
SEQRES 5 A 53 LYS
HET CU1 A 54 1
HET CU1 A 55 1
HET CU1 A 56 1
HET CU1 A 57 1
HET CU1 A 58 1
HET CU1 A 59 1
HET CU1 A 60 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 7(CU 1+)
LINK SG CYS A 7 CU CU1 A 54 1555 1555 2.36
LINK SG CYS A 7 CU CU1 A 56 1555 1555 2.45
LINK SG CYS A 9 CU CU1 A 54 1555 1555 2.26
LINK SG CYS A 9 CU CU1 A 60 1555 1555 2.48
LINK SG CYS A 11 CU CU1 A 55 1555 1555 2.45
LINK SG CYS A 11 CU CU1 A 58 1555 1555 2.44
LINK SG CYS A 14 CU CU1 A 55 1555 1555 2.25
LINK SG CYS A 14 CU CU1 A 60 1555 1555 2.27
LINK SG CYS A 20 CU CU1 A 56 1555 1555 2.25
LINK SG CYS A 24 CU CU1 A 54 1555 1555 2.48
LINK SG CYS A 24 CU CU1 A 57 1555 1555 2.45
LINK SG CYS A 26 CU CU1 A 57 1555 1555 2.25
LINK SG CYS A 26 CU CU1 A 59 1555 1555 2.25
LINK SG CYS A 30 CU CU1 A 58 1555 1555 2.25
LINK SG CYS A 30 CU CU1 A 59 1555 1555 2.28
LINK SG CYS A 36 CU CU1 A 55 1555 1555 2.28
LINK SG CYS A 36 CU CU1 A 59 1555 1555 2.25
LINK SG CYS A 38 CU CU1 A 57 1555 1555 2.30
LINK SG CYS A 38 CU CU1 A 60 1555 1555 2.25
LINK CU CU1 A 54 CU CU1 A 57 1555 1555 2.73
LINK CU CU1 A 54 CU CU1 A 60 1555 1555 2.24
LINK CU CU1 A 55 CU CU1 A 58 1555 1555 2.50
LINK CU CU1 A 57 CU CU1 A 60 1555 1555 2.50
SITE 1 AC1 7 CYS A 7 CYS A 9 CYS A 24 CYS A 38
SITE 2 AC1 7 CU1 A 56 CU1 A 57 CU1 A 60
SITE 1 AC2 7 CYS A 9 CYS A 11 CYS A 14 CYS A 36
SITE 2 AC2 7 CU1 A 58 CU1 A 59 CU1 A 60
SITE 1 AC3 7 CYS A 7 CYS A 14 CYS A 20 CYS A 24
SITE 2 AC3 7 CYS A 38 CU1 A 54 CU1 A 60
SITE 1 AC4 7 CYS A 24 SER A 25 CYS A 26 CYS A 38
SITE 2 AC4 7 CU1 A 54 CU1 A 59 CU1 A 60
SITE 1 AC5 6 CYS A 9 CYS A 11 CYS A 30 CYS A 36
SITE 2 AC5 6 CU1 A 55 CU1 A 59
SITE 1 AC6 8 CYS A 26 CYS A 30 CYS A 36 CYS A 38
SITE 2 AC6 8 CU1 A 55 CU1 A 57 CU1 A 58 CU1 A 60
SITE 1 AC7 9 CYS A 7 CYS A 9 CYS A 14 CYS A 38
SITE 2 AC7 9 CU1 A 54 CU1 A 55 CU1 A 56 CU1 A 57
SITE 3 AC7 9 CU1 A 59
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