Header list of 1xfq.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 15-SEP-04 1XFQ
TITLE STRUCTURE OF THE BLUE SHIFTED INTERMEDIATE STATE OF THE PHOTOACTIVE
TITLE 2 YELLOW PROTEIN LACKING THE N-TERMINAL PART
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOACTIVE YELLOW PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 26-125;
COMPND 5 SYNONYM: PYP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALORHODOSPIRA HALOPHILA;
SOURCE 3 ORGANISM_TAXID: 1053;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PAS DOMAIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.BERNARD,K.HOUBEN,N.M.DERIX,D.MARKS,M.A.VAN DER HORST,
AUTHOR 2 K.J.HELLINGWERF,R.BOELENS,R.KAPTEIN,N.A.VAN NULAND
REVDAT 3 02-MAR-22 1XFQ 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1XFQ 1 VERSN
REVDAT 1 16-AUG-05 1XFQ 0
JRNL AUTH C.BERNARD,K.HOUBEN,N.M.DERIX,D.MARKS,M.A.VAN DER HORST,
JRNL AUTH 2 K.J.HELLINGWERF,R.BOELENS,R.KAPTEIN,N.A.VAN NULAND
JRNL TITL THE SOLUTION STRUCTURE OF A TRANSIENT PHOTORECEPTOR
JRNL TITL 2 INTERMEDIATE: DELTA25 PHOTOACTIVE YELLOW PROTEIN
JRNL REF STRUCTURE V. 13 953 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 16004868
JRNL DOI 10.1016/J.STR.2005.04.017
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, CNS 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XFQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030311.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM DELTA25-PYP, 15N-13C, 50MM
REMARK 210 PHOSPHATE BUFFER; 1MM DELTA25-
REMARK 210 PYP 15N, 50MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; CBCA(CO)NH; 3D 15N TOCSY
REMARK 210 -HSQC; 3D_15N-SEPARATED_NOESY;
REMARK 210 2D NOESY; 2D TOCSY; HNCO; HNCACB;
REMARK 210 13C FILTERED 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0.4, CNS 1.2
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 GLU A 19
REMARK 465 SER A 20
REMARK 465 ASP A 21
REMARK 465 ASP A 22
REMARK 465 ASP A 23
REMARK 465 ASP A 24
REMARK 465 LYS A 25
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 ILE A 31 CA ILE A 31 CB -0.205
REMARK 500 1 ILE A 39 CA ILE A 39 CB -0.216
REMARK 500 1 ILE A 49 CA ILE A 49 CB -0.219
REMARK 500 1 THR A 50 CA THR A 50 CB -0.197
REMARK 500 1 VAL A 57 CA VAL A 57 CB -0.213
REMARK 500 1 ILE A 58 CA ILE A 58 CB -0.205
REMARK 500 1 VAL A 66 CA VAL A 66 CB -0.211
REMARK 500 1 THR A 70 CA THR A 70 CB -0.207
REMARK 500 1 VAL A 83 CA VAL A 83 CB -0.217
REMARK 500 1 THR A 90 CA THR A 90 CB -0.195
REMARK 500 1 THR A 95 CA THR A 95 CB -0.209
REMARK 500 1 THR A 101 CA THR A 101 CB -0.210
REMARK 500 1 THR A 103 CA THR A 103 CB -0.216
REMARK 500 1 VAL A 105 CA VAL A 105 CB -0.218
REMARK 500 1 VAL A 107 CA VAL A 107 CB -0.217
REMARK 500 1 VAL A 120 CA VAL A 120 CB -0.210
REMARK 500 1 VAL A 122 CA VAL A 122 CB -0.208
REMARK 500 1 VAL A 125 CA VAL A 125 CB -0.216
REMARK 500 2 ILE A 31 CA ILE A 31 CB -0.214
REMARK 500 2 ILE A 39 CA ILE A 39 CB -0.213
REMARK 500 2 ILE A 49 CA ILE A 49 CB -0.212
REMARK 500 2 THR A 50 CA THR A 50 CB -0.209
REMARK 500 2 VAL A 57 CA VAL A 57 CB -0.216
REMARK 500 2 ILE A 58 CA ILE A 58 CB -0.198
REMARK 500 2 VAL A 66 CA VAL A 66 CB -0.212
REMARK 500 2 THR A 70 CA THR A 70 CB -0.196
REMARK 500 2 VAL A 83 CA VAL A 83 CB -0.216
REMARK 500 2 THR A 90 CA THR A 90 CB -0.204
REMARK 500 2 THR A 95 CA THR A 95 CB -0.212
REMARK 500 2 THR A 101 CA THR A 101 CB -0.204
REMARK 500 2 THR A 103 CA THR A 103 CB -0.213
REMARK 500 2 VAL A 105 CA VAL A 105 CB -0.212
REMARK 500 2 VAL A 107 CA VAL A 107 CB -0.212
REMARK 500 2 VAL A 120 CA VAL A 120 CB -0.210
REMARK 500 2 VAL A 122 CA VAL A 122 CB -0.214
REMARK 500 2 VAL A 125 CA VAL A 125 CB -0.213
REMARK 500 3 ILE A 31 CA ILE A 31 CB -0.215
REMARK 500 3 ILE A 39 CA ILE A 39 CB -0.215
REMARK 500 3 ILE A 49 CA ILE A 49 CB -0.208
REMARK 500 3 THR A 50 CA THR A 50 CB -0.208
REMARK 500 3 VAL A 57 CA VAL A 57 CB -0.205
REMARK 500 3 ILE A 58 CA ILE A 58 CB -0.206
REMARK 500 3 VAL A 66 CA VAL A 66 CB -0.207
REMARK 500 3 THR A 70 CA THR A 70 CB -0.211
REMARK 500 3 VAL A 83 CA VAL A 83 CB -0.220
REMARK 500 3 THR A 90 CA THR A 90 CB -0.193
REMARK 500 3 THR A 95 CA THR A 95 CB -0.198
REMARK 500 3 THR A 101 CA THR A 101 CB -0.213
REMARK 500 3 THR A 103 CA THR A 103 CB -0.210
REMARK 500 3 VAL A 105 CA VAL A 105 CB -0.213
REMARK 500
REMARK 500 THIS ENTRY HAS 360 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 ALA A 44 -32.53 176.18
REMARK 500 1 GLU A 46 40.46 -147.45
REMARK 500 1 LYS A 55 32.20 -99.05
REMARK 500 1 ILE A 58 166.66 50.73
REMARK 500 1 TYR A 76 -113.60 50.40
REMARK 500 1 ASN A 87 48.65 -157.18
REMARK 500 1 TYR A 98 -166.51 -100.31
REMARK 500 1 MET A 100 33.40 -95.74
REMARK 500 2 ALA A 44 13.04 -170.20
REMARK 500 2 PRO A 54 36.94 -83.40
REMARK 500 2 ILE A 58 73.53 37.85
REMARK 500 2 PHE A 62 79.09 34.82
REMARK 500 2 VAL A 66 78.72 54.79
REMARK 500 2 ALA A 67 105.95 -39.56
REMARK 500 2 GLU A 74 43.65 -80.10
REMARK 500 2 TYR A 76 -96.98 52.22
REMARK 500 2 ASN A 87 54.63 -164.00
REMARK 500 2 LEU A 88 96.11 -65.37
REMARK 500 2 ASP A 97 -168.14 63.94
REMARK 500 2 TYR A 98 2.84 -155.74
REMARK 500 2 LEU A 113 1.27 -67.07
REMARK 500 2 SER A 117 151.32 179.25
REMARK 500 3 GLU A 46 103.18 67.57
REMARK 500 3 ILE A 49 47.75 33.97
REMARK 500 3 GLN A 56 44.32 -107.16
REMARK 500 3 LYS A 60 90.45 -69.25
REMARK 500 3 ALA A 67 110.27 -38.22
REMARK 500 3 CYS A 69 179.43 61.94
REMARK 500 3 TYR A 76 -106.30 54.15
REMARK 500 3 ASN A 87 55.75 -162.85
REMARK 500 3 LEU A 88 83.61 -69.07
REMARK 500 3 ASP A 97 -123.18 -84.44
REMARK 500 3 MET A 100 21.72 48.25
REMARK 500 3 PRO A 102 -73.84 -80.07
REMARK 500 4 GLN A 56 -46.94 -161.81
REMARK 500 4 ASP A 65 120.21 -172.07
REMARK 500 4 VAL A 66 37.33 -150.35
REMARK 500 4 ALA A 67 106.45 61.86
REMARK 500 4 SER A 72 79.29 57.02
REMARK 500 4 GLU A 74 -49.92 -167.63
REMARK 500 4 ASN A 87 50.19 -158.89
REMARK 500 4 TYR A 98 -149.37 177.50
REMARK 500 4 PRO A 102 86.82 -56.41
REMARK 500 5 ALA A 27 145.39 69.35
REMARK 500 5 GLU A 46 -178.82 68.14
REMARK 500 5 THR A 50 49.22 -95.00
REMARK 500 5 ILE A 58 73.44 38.70
REMARK 500 5 LYS A 64 141.64 -170.15
REMARK 500 5 ASN A 87 62.61 -169.96
REMARK 500 5 LEU A 88 102.35 -38.45
REMARK 500
REMARK 500 THIS ENTRY HAS 221 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 HC4 A 169
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XFN RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE GROUND STATE
DBREF 1XFQ A 26 125 UNP P16113 PYP_ECTHA 26 125
SEQADV 1XFQ HIS A 13 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ HIS A 14 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ HIS A 15 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ HIS A 16 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ HIS A 17 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ HIS A 18 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ GLU A 19 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ SER A 20 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ ASP A 21 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ ASP A 22 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ ASP A 23 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ ASP A 24 UNP P16113 EXPRESSION TAG
SEQADV 1XFQ LYS A 25 UNP P16113 EXPRESSION TAG
SEQRES 1 A 113 HIS HIS HIS HIS HIS HIS GLU SER ASP ASP ASP ASP LYS
SEQRES 2 A 113 LEU ALA PHE GLY ALA ILE GLN LEU ASP GLY ASP GLY ASN
SEQRES 3 A 113 ILE LEU GLN TYR ASN ALA ALA GLU GLY ASP ILE THR GLY
SEQRES 4 A 113 ARG ASP PRO LYS GLN VAL ILE GLY LYS ASN PHE PHE LYS
SEQRES 5 A 113 ASP VAL ALA PRO CYS THR ASP SER PRO GLU PHE TYR GLY
SEQRES 6 A 113 LYS PHE LYS GLU GLY VAL ALA SER GLY ASN LEU ASN THR
SEQRES 7 A 113 MET PHE GLU TYR THR PHE ASP TYR GLN MET THR PRO THR
SEQRES 8 A 113 LYS VAL LYS VAL HIS MET LYS LYS ALA LEU SER GLY ASP
SEQRES 9 A 113 SER TYR TRP VAL PHE VAL LYS ARG VAL
HET HC4 A 169 18
HETNAM HC4 4'-HYDROXYCINNAMIC ACID
HETSYN HC4 PARA-COUMARIC ACID
FORMUL 2 HC4 C9 H8 O3
HELIX 1 1 LYS A 78 GLY A 86 1 9
SHEET 1 A 5 ILE A 39 ASN A 43 0
SHEET 2 A 5 ALA A 30 ASP A 34 -1 N ALA A 30 O ASN A 43
SHEET 3 A 5 SER A 117 ARG A 124 -1 O VAL A 120 N ILE A 31
SHEET 4 A 5 VAL A 105 LYS A 111 -1 N LYS A 110 O TRP A 119
SHEET 5 A 5 THR A 90 TYR A 94 -1 N PHE A 92 O VAL A 107
LINK SG CYS A 69 C1 HC4 A 169 1555 1555 1.82
SITE 1 AC1 1 CYS A 69
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