Header list of 1fpw.pdb file
Complete list - b 23 2 Bytes
HEADER METAL BINDING PROTEIN 31-AUG-00 1FPW
TITLE STRUCTURE OF YEAST FREQUENIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-BINDING PROTEIN NCS-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: YEAST FREQUENIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932
KEYWDS EF-HAND, CALCIUM, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.B.AMES,K.B.HENDRICKS,T.STRAHL,I.G.HUTTNER,J.THORNER
REVDAT 4 23-FEB-22 1FPW 1 REMARK LINK
REVDAT 3 24-FEB-09 1FPW 1 VERSN
REVDAT 2 06-DEC-00 1FPW 1 ATOM
REVDAT 1 18-OCT-00 1FPW 0
JRNL AUTH J.B.AMES,K.B.HENDRICKS,T.STRAHL,I.G.HUTTNER,N.HAMASAKI,
JRNL AUTH 2 J.THORNER
JRNL TITL STRUCTURE AND CALCIUM-BINDING PROPERTIES OF FRQ1, A NOVEL
JRNL TITL 2 CALCIUM SENSOR IN THE YEAST SACCHAROMYCES CEREVISIAE.
JRNL REF BIOCHEMISTRY V. 39 12149 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11015193
JRNL DOI 10.1021/BI0012890
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FPW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1000011799.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 0.05
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MILLIMOLAR PROTEIN
REMARK 210 CONCENTRATION
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 MET A 1 CB CG SD CE
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 HD21 ASN A 77 H GLY A 78 1.18
REMARK 500 HH11 ARG A 45 HD21 ASN A 66 1.22
REMARK 500 HG1 THR A 137 H LEU A 138 1.34
REMARK 500 HD22 ASN A 111 OE2 GLU A 120 1.40
REMARK 500 O ASP A 12 H LEU A 16 1.47
REMARK 500 O TRP A 30 H PHE A 34 1.48
REMARK 500 O SER A 9 H ASP A 11 1.51
REMARK 500 O HIS A 81 H PHE A 85 1.54
REMARK 500 O ILE A 86 H SER A 90 1.55
REMARK 500 O PRO A 145 H VAL A 149 1.57
REMARK 500 O HIS A 112 H GLY A 114 1.59
REMARK 500 OH TYR A 129 HH21 ARG A 148 1.60
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 TRP A 30 CG TRP A 30 CD2 -0.126
REMARK 500 1 HIS A 31 CG HIS A 31 ND1 -0.120
REMARK 500 1 HIS A 67 CG HIS A 67 ND1 -0.120
REMARK 500 1 HIS A 81 CG HIS A 81 ND1 -0.120
REMARK 500 1 TRP A 103 CG TRP A 103 CD2 -0.112
REMARK 500 1 HIS A 112 CG HIS A 112 ND1 -0.120
REMARK 500 2 TRP A 30 CG TRP A 30 CD2 -0.129
REMARK 500 2 HIS A 31 CG HIS A 31 ND1 -0.120
REMARK 500 2 HIS A 67 CG HIS A 67 ND1 -0.121
REMARK 500 2 HIS A 81 CG HIS A 81 ND1 -0.121
REMARK 500 2 TRP A 103 CG TRP A 103 CD2 -0.115
REMARK 500 2 HIS A 112 CG HIS A 112 ND1 -0.120
REMARK 500 3 TRP A 30 CG TRP A 30 CD2 -0.124
REMARK 500 3 HIS A 31 CG HIS A 31 ND1 -0.121
REMARK 500 3 HIS A 67 CG HIS A 67 ND1 -0.120
REMARK 500 3 HIS A 81 CG HIS A 81 ND1 -0.118
REMARK 500 3 TRP A 103 CG TRP A 103 CD2 -0.117
REMARK 500 3 HIS A 112 CG HIS A 112 ND1 -0.121
REMARK 500 4 TRP A 30 CG TRP A 30 CD2 -0.116
REMARK 500 4 HIS A 31 CG HIS A 31 ND1 -0.121
REMARK 500 4 HIS A 67 CG HIS A 67 ND1 -0.121
REMARK 500 4 HIS A 81 CG HIS A 81 ND1 -0.121
REMARK 500 4 TRP A 103 CG TRP A 103 CD2 -0.114
REMARK 500 4 HIS A 112 CG HIS A 112 ND1 -0.121
REMARK 500 5 TRP A 30 CG TRP A 30 CD2 -0.126
REMARK 500 5 HIS A 31 CG HIS A 31 ND1 -0.120
REMARK 500 5 HIS A 67 CG HIS A 67 ND1 -0.123
REMARK 500 5 HIS A 81 CG HIS A 81 ND1 -0.120
REMARK 500 5 TRP A 103 CG TRP A 103 CD2 -0.124
REMARK 500 5 HIS A 112 CG HIS A 112 ND1 -0.121
REMARK 500 6 TRP A 30 CG TRP A 30 CD2 -0.113
REMARK 500 6 HIS A 31 CG HIS A 31 ND1 -0.122
REMARK 500 6 HIS A 67 CG HIS A 67 ND1 -0.121
REMARK 500 6 HIS A 81 CG HIS A 81 ND1 -0.122
REMARK 500 6 TRP A 103 CG TRP A 103 CD2 -0.126
REMARK 500 6 HIS A 112 CG HIS A 112 ND1 -0.122
REMARK 500 7 TRP A 30 CG TRP A 30 CD2 -0.117
REMARK 500 7 HIS A 31 CG HIS A 31 ND1 -0.122
REMARK 500 7 HIS A 67 CG HIS A 67 ND1 -0.121
REMARK 500 7 HIS A 81 CG HIS A 81 ND1 -0.121
REMARK 500 7 TRP A 103 CG TRP A 103 CD2 -0.115
REMARK 500 7 HIS A 112 CG HIS A 112 ND1 -0.121
REMARK 500 8 TRP A 30 CG TRP A 30 CD2 -0.126
REMARK 500 8 HIS A 31 CG HIS A 31 ND1 -0.120
REMARK 500 8 HIS A 67 CG HIS A 67 ND1 -0.120
REMARK 500 8 HIS A 81 CG HIS A 81 ND1 -0.118
REMARK 500 8 TRP A 103 CG TRP A 103 CD2 -0.111
REMARK 500 8 HIS A 112 CG HIS A 112 ND1 -0.118
REMARK 500 9 TRP A 30 CG TRP A 30 CD2 -0.111
REMARK 500 9 HIS A 31 CG HIS A 31 ND1 -0.121
REMARK 500
REMARK 500 THIS ENTRY HAS 120 BOND DEVIATIONS.
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 1 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 TRP A 30 NE1 - CE2 - CZ2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 1 TRP A 30 NE1 - CE2 - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 1 TRP A 30 CE2 - CD2 - CG ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 TRP A 30 CG - CD2 - CE3 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 TRP A 103 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP A 103 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 1 TRP A 103 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 TRP A 30 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 2 TRP A 30 NE1 - CE2 - CZ2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 2 TRP A 30 NE1 - CE2 - CD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 2 TRP A 30 CG - CD2 - CE3 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 103 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 TRP A 103 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 103 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 2 TRP A 103 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 3 TRP A 30 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 3 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 3 TRP A 30 NE1 - CE2 - CZ2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 3 TRP A 30 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 3 TRP A 103 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 TRP A 103 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 103 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 3 TRP A 103 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 4 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP A 30 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 4 TRP A 30 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 4 TRP A 103 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 4 TRP A 103 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TRP A 103 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 4 TRP A 103 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 5 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 5 TRP A 30 NE1 - CE2 - CZ2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 5 TRP A 30 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 5 TRP A 30 CG - CD2 - CE3 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 TRP A 103 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 5 TRP A 103 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 5 TRP A 103 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 5 TRP A 103 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 6 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 6 TRP A 30 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 6 TRP A 30 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 6 TRP A 103 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 6 TRP A 103 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 6 TRP A 103 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 6 TRP A 103 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 7 TRP A 30 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 7 TRP A 30 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 7 TRP A 30 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 146 ANGLE 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 LYS A 4 -132.75 -83.22
REMARK 500 1 SER A 6 10.87 -170.78
REMARK 500 1 LEU A 8 -89.91 -101.25
REMARK 500 1 LYS A 10 -57.03 63.57
REMARK 500 1 LEU A 16 -0.54 -56.55
REMARK 500 1 LYS A 17 165.40 -49.63
REMARK 500 1 SER A 19 -73.43 -151.52
REMARK 500 1 THR A 20 66.28 21.59
REMARK 500 1 TYR A 21 31.72 -87.74
REMARK 500 1 PHE A 22 68.55 -155.75
REMARK 500 1 ASP A 23 150.84 -38.02
REMARK 500 1 ARG A 25 -27.44 -39.53
REMARK 500 1 GLU A 26 -70.59 -90.72
REMARK 500 1 PRO A 61 78.67 -68.82
REMARK 500 1 GLU A 62 -73.10 -107.49
REMARK 500 1 LEU A 68 -70.40 -52.78
REMARK 500 1 VAL A 71 32.90 -79.65
REMARK 500 1 PHE A 72 -142.15 -130.39
REMARK 500 1 ASP A 73 170.56 59.02
REMARK 500 1 LYS A 74 -26.81 -146.33
REMARK 500 1 ASN A 76 51.59 39.42
REMARK 500 1 PHE A 82 -71.03 -37.62
REMARK 500 1 ARG A 94 161.28 60.82
REMARK 500 1 THR A 96 -113.30 -172.18
REMARK 500 1 LEU A 97 -157.27 -95.52
REMARK 500 1 GLU A 98 -17.05 -48.81
REMARK 500 1 ASN A 111 -114.49 -87.56
REMARK 500 1 HIS A 112 9.07 -177.41
REMARK 500 1 ASP A 113 32.54 -65.58
REMARK 500 1 MET A 131 -78.78 -96.29
REMARK 500 1 SER A 134 -4.40 -162.17
REMARK 500 1 THR A 137 -91.56 -85.10
REMARK 500 1 LEU A 138 -62.45 -162.54
REMARK 500 1 ALA A 143 117.01 -175.53
REMARK 500 1 ASP A 157 51.17 -90.03
REMARK 500 1 LYS A 158 35.00 -74.96
REMARK 500 1 GLU A 160 103.47 55.41
REMARK 500 1 ASP A 161 13.66 -165.60
REMARK 500 1 VAL A 175 -98.06 -88.40
REMARK 500 1 ASP A 176 95.44 -27.60
REMARK 500 1 PRO A 177 82.64 -68.90
REMARK 500 1 SER A 178 -49.69 -169.05
REMARK 500 2 LYS A 10 -68.63 -128.51
REMARK 500 2 LEU A 16 -80.11 -61.37
REMARK 500 2 LYS A 17 123.64 67.10
REMARK 500 2 GLN A 18 19.02 45.08
REMARK 500 2 THR A 20 -58.80 -131.09
REMARK 500 2 TYR A 21 -26.37 67.08
REMARK 500 2 ASP A 23 179.50 53.58
REMARK 500 2 PHE A 56 62.32 -155.15
REMARK 500
REMARK 500 THIS ENTRY HAS 749 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 24 0.08 SIDE CHAIN
REMARK 500 1 ARG A 25 0.11 SIDE CHAIN
REMARK 500 1 ARG A 36 0.26 SIDE CHAIN
REMARK 500 1 ARG A 45 0.31 SIDE CHAIN
REMARK 500 1 ARG A 94 0.32 SIDE CHAIN
REMARK 500 1 ARG A 170 0.12 SIDE CHAIN
REMARK 500 2 ARG A 24 0.23 SIDE CHAIN
REMARK 500 2 ARG A 36 0.30 SIDE CHAIN
REMARK 500 2 ARG A 45 0.21 SIDE CHAIN
REMARK 500 2 ARG A 94 0.13 SIDE CHAIN
REMARK 500 2 ARG A 148 0.13 SIDE CHAIN
REMARK 500 2 ARG A 170 0.28 SIDE CHAIN
REMARK 500 3 ARG A 24 0.30 SIDE CHAIN
REMARK 500 3 ARG A 25 0.23 SIDE CHAIN
REMARK 500 3 ARG A 36 0.24 SIDE CHAIN
REMARK 500 3 ARG A 45 0.32 SIDE CHAIN
REMARK 500 3 ARG A 94 0.32 SIDE CHAIN
REMARK 500 3 ARG A 148 0.25 SIDE CHAIN
REMARK 500 3 ARG A 170 0.27 SIDE CHAIN
REMARK 500 4 ARG A 24 0.28 SIDE CHAIN
REMARK 500 4 ARG A 25 0.29 SIDE CHAIN
REMARK 500 4 ARG A 36 0.25 SIDE CHAIN
REMARK 500 4 ARG A 45 0.32 SIDE CHAIN
REMARK 500 4 ARG A 94 0.28 SIDE CHAIN
REMARK 500 4 ARG A 148 0.31 SIDE CHAIN
REMARK 500 4 ARG A 170 0.18 SIDE CHAIN
REMARK 500 5 ARG A 24 0.28 SIDE CHAIN
REMARK 500 5 ARG A 25 0.12 SIDE CHAIN
REMARK 500 5 ARG A 36 0.26 SIDE CHAIN
REMARK 500 5 ARG A 45 0.20 SIDE CHAIN
REMARK 500 5 ARG A 94 0.11 SIDE CHAIN
REMARK 500 5 ARG A 148 0.31 SIDE CHAIN
REMARK 500 5 ARG A 170 0.08 SIDE CHAIN
REMARK 500 6 ARG A 24 0.25 SIDE CHAIN
REMARK 500 6 ARG A 25 0.14 SIDE CHAIN
REMARK 500 6 ARG A 36 0.16 SIDE CHAIN
REMARK 500 6 ARG A 45 0.16 SIDE CHAIN
REMARK 500 6 ARG A 148 0.23 SIDE CHAIN
REMARK 500 6 ARG A 170 0.28 SIDE CHAIN
REMARK 500 7 ARG A 24 0.28 SIDE CHAIN
REMARK 500 7 ARG A 25 0.08 SIDE CHAIN
REMARK 500 7 ARG A 36 0.31 SIDE CHAIN
REMARK 500 7 ARG A 45 0.32 SIDE CHAIN
REMARK 500 7 ARG A 94 0.32 SIDE CHAIN
REMARK 500 7 ARG A 148 0.31 SIDE CHAIN
REMARK 500 7 ARG A 170 0.31 SIDE CHAIN
REMARK 500 8 ARG A 24 0.26 SIDE CHAIN
REMARK 500 8 ARG A 25 0.17 SIDE CHAIN
REMARK 500 8 ARG A 36 0.21 SIDE CHAIN
REMARK 500 8 ARG A 45 0.14 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 129 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 CA A 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 73 OD1
REMARK 620 2 ASP A 75 OD2 127.4
REMARK 620 3 ASP A 75 OD1 78.0 50.5
REMARK 620 4 ASN A 77 OD1 106.4 58.6 58.3
REMARK 620 5 ASN A 77 ND2 63.3 88.0 51.8 43.2
REMARK 620 6 PHE A 79 O 77.5 124.9 109.6 67.7 58.2
REMARK 620 7 HIS A 81 NE2 139.5 67.2 111.7 111.9 153.5 128.9
REMARK 620 8 GLU A 84 OE1 65.1 144.3 133.9 156.7 123.1 89.0 83.4
REMARK 620 9 GLU A 84 OE2 77.9 96.7 97.6 152.5 133.5 138.3 62.1 49.9
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 109 OD1
REMARK 620 2 ASN A 111 OD1 57.8
REMARK 620 3 ASP A 113 OD2 109.6 84.8
REMARK 620 4 ASP A 113 OD1 71.4 51.5 40.8
REMARK 620 5 TYR A 115 O 64.2 97.6 65.2 58.1
REMARK 620 6 ILE A 116 N 82.0 137.2 96.6 105.0 47.1
REMARK 620 7 ILE A 116 O 128.3 170.9 98.0 134.5 91.4 51.3
REMARK 620 8 THR A 117 OG1 152.6 108.3 91.0 120.9 143.1 114.4 63.1
REMARK 620 9 THR A 117 N 112.7 130.7 135.2 175.9 122.6 75.6 42.7 55.8
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 157 OD1
REMARK 620 2 ASN A 159 OD1 66.7
REMARK 620 3 ASP A 161 OD1 52.5 66.8
REMARK 620 4 ASP A 161 OD2 95.4 57.4 49.8
REMARK 620 5 TYR A 163 O 83.1 136.3 69.8 97.5
REMARK 620 6 GLU A 168 OE2 151.6 95.7 142.6 92.8 122.8
REMARK 620 7 GLU A 168 OE1 100.1 58.1 124.9 98.3 163.5 51.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
DBREF 1FPW A 1 190 UNP Q06389 NCS1_YEAST 1 190
SEQRES 1 A 190 MET GLY ALA LYS THR SER LYS LEU SER LYS ASP ASP LEU
SEQRES 2 A 190 THR CYS LEU LYS GLN SER THR TYR PHE ASP ARG ARG GLU
SEQRES 3 A 190 ILE GLN GLN TRP HIS LYS GLY PHE LEU ARG ASP CYS PRO
SEQRES 4 A 190 SER GLY GLN LEU ALA ARG GLU ASP PHE VAL LYS ILE TYR
SEQRES 5 A 190 LYS GLN PHE PHE PRO PHE GLY SER PRO GLU ASP PHE ALA
SEQRES 6 A 190 ASN HIS LEU PHE THR VAL PHE ASP LYS ASP ASN ASN GLY
SEQRES 7 A 190 PHE ILE HIS PHE GLU GLU PHE ILE THR VAL LEU SER THR
SEQRES 8 A 190 THR SER ARG GLY THR LEU GLU GLU LYS LEU SER TRP ALA
SEQRES 9 A 190 PHE GLU LEU TYR ASP LEU ASN HIS ASP GLY TYR ILE THR
SEQRES 10 A 190 PHE ASP GLU MET LEU THR ILE VAL ALA SER VAL TYR LYS
SEQRES 11 A 190 MET MET GLY SER MET VAL THR LEU ASN GLU ASP GLU ALA
SEQRES 12 A 190 THR PRO GLU MET ARG VAL LYS LYS ILE PHE LYS LEU MET
SEQRES 13 A 190 ASP LYS ASN GLU ASP GLY TYR ILE THR LEU ASP GLU PHE
SEQRES 14 A 190 ARG GLU GLY SER LYS VAL ASP PRO SER ILE ILE GLY ALA
SEQRES 15 A 190 LEU ASN LEU TYR ASP GLY LEU ILE
HET CA A 500 1
HET CA A 501 1
HET CA A 502 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
HELIX 1 1 LYS A 10 LYS A 17 1 8
HELIX 2 2 ASP A 23 CYS A 38 1 16
HELIX 3 3 ARG A 45 PHE A 56 1 12
HELIX 4 4 GLU A 62 VAL A 71 1 10
HELIX 5 5 HIS A 81 SER A 93 1 13
HELIX 6 6 GLU A 98 ASP A 109 1 12
HELIX 7 7 PHE A 118 LYS A 130 1 13
HELIX 8 8 THR A 144 ASP A 157 1 14
HELIX 9 9 LEU A 166 VAL A 175 1 10
HELIX 10 10 SER A 178 GLY A 188 1 11
SHEET 1 A 2 LEU A 43 ALA A 44 0
SHEET 2 A 2 PHE A 79 ILE A 80 -1 N ILE A 80 O LEU A 43
SHEET 1 B 2 TYR A 115 THR A 117 0
SHEET 2 B 2 TYR A 163 THR A 165 -1 O ILE A 164 N ILE A 116
LINK OD1 ASP A 73 CA CA A 500 1555 1555 2.45
LINK OD2 ASP A 75 CA CA A 500 1555 1555 2.56
LINK OD1 ASP A 75 CA CA A 500 1555 1555 2.57
LINK OD1 ASN A 77 CA CA A 500 1555 1555 2.57
LINK ND2 ASN A 77 CA CA A 500 1555 1555 3.16
LINK O PHE A 79 CA CA A 500 1555 1555 2.57
LINK NE2 HIS A 81 CA CA A 500 1555 1555 1.62
LINK OE1 GLU A 84 CA CA A 500 1555 1555 2.57
LINK OE2 GLU A 84 CA CA A 500 1555 1555 2.60
LINK OD1 ASP A 109 CA CA A 501 1555 1555 2.63
LINK OD1 ASN A 111 CA CA A 501 1555 1555 2.75
LINK OD2 ASP A 113 CA CA A 501 1555 1555 3.31
LINK OD1 ASP A 113 CA CA A 501 1555 1555 2.81
LINK O TYR A 115 CA CA A 501 1555 1555 1.69
LINK N ILE A 116 CA CA A 501 1555 1555 2.96
LINK O ILE A 116 CA CA A 501 1555 1555 3.07
LINK OG1 THR A 117 CA CA A 501 1555 1555 2.71
LINK N THR A 117 CA CA A 501 1555 1555 2.97
LINK OE1 GLU A 120 CA CA A 501 1555 1555 2.58
LINK OE2 GLU A 120 CA CA A 501 1555 1555 2.51
LINK OD1 ASP A 157 CA CA A 502 1555 1555 2.51
LINK OD1 ASN A 159 CA CA A 502 1555 1555 2.55
LINK OD1 ASP A 161 CA CA A 502 1555 1555 2.70
LINK OD2 ASP A 161 CA CA A 502 1555 1555 2.46
LINK O TYR A 163 CA CA A 502 1555 1555 2.53
LINK OE2 GLU A 168 CA CA A 502 1555 1555 2.57
LINK OE1 GLU A 168 CA CA A 502 1555 1555 2.44
SITE 1 AC1 6 ASP A 73 ASP A 75 ASN A 77 PHE A 79
SITE 2 AC1 6 HIS A 81 GLU A 84
SITE 1 AC2 7 ASP A 109 ASN A 111 ASP A 113 TYR A 115
SITE 2 AC2 7 ILE A 116 THR A 117 GLU A 120
SITE 1 AC3 6 ASP A 157 ASN A 159 ASP A 161 TYR A 163
SITE 2 AC3 6 ILE A 164 GLU A 168
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 - b 23 2 Bytes