Header list of 1q80.pdb file
Complete list - b 5 2 Bytes
HEADER METAL BINDING PROTEIN 20-AUG-03 1Q80
TITLE SOLUTION STRUCTURE AND DYNAMICS OF NEREIS SARCOPLASMIC CALCIUM BINDING
TITLE 2 PROTEIN
CAVEAT 1Q80 CHIRALITY ERRORS IN MODELS 2,11,13
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARCOPLASMIC CALCIUM-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SCP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEANTHES DIVERSICOLOR;
SOURCE 3 ORGANISM_TAXID: 6352;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PDIA17/PHSP234;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PET22B;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNDNER04
KEYWDS ALL-ALPHA, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 17
AUTHOR G.RABAH,R.POPESCU,J.A.COX,Y.ENGELBORGHS,C.T.CRAESCU
REVDAT 4 05-FEB-20 1Q80 1 REMARK
REVDAT 3 24-FEB-09 1Q80 1 VERSN
REVDAT 2 10-MAY-05 1Q80 1 JRNL
REVDAT 1 21-SEP-04 1Q80 0
JRNL AUTH G.RABAH,R.POPESCU,J.A.COX,Y.ENGELBORGHS,C.T.CRAESCU
JRNL TITL SOLUTION STRUCTURE AND INTERNAL DYNAMICS OF NSCP, A COMPACT
JRNL TITL 2 CALCIUM-BINDING PROTEIN.
JRNL REF FEBS J. V. 272 2022 2005
JRNL REFN ISSN 1742-464X
JRNL PMID 15819893
JRNL DOI 10.1111/J.1742-4658.2005.04629.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.T.CRAESCU,B.PRECHEUR,A.VAN RIEL,H.SAKAMOTO,J.A.COX,
REMARK 1 AUTH 2 Y.ENGELBORGHS
REMARK 1 TITL 1H AND 15N RESONANCE ASSIGNMENT OF THE CALCIUM-BOUND FORM OF
REMARK 1 TITL 2 THE NEREIS DIVERSICOLOR SARCOPLASMIC CA(2+)-BINDING PROTEIN
REMARK 1 REF J.BIOMOL.NMR V. 12 565 1998
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008361202496
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII 2, DISCOVER 3
REMARK 3 AUTHORS : ACCELRYS (DGII), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE CALCULATION USED 1859 NOE
REMARK 3 RESTRAINTS, 188 HYDROGEN BOND RESTRAINTS AND 262 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1Q80 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000020031.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 5MM CACL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM NSCP U-15N; 50MM TRIS
REMARK 210 BUFFER, PH 6.5; 5MM CACL2; 95%
REMARK 210 H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; HMQCJ
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX I2000, DISCOVER 3
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 17
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 17
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 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 O VAL A 168 H PHE A 169 0.66
REMARK 500 C VAL A 168 H PHE A 169 1.25
REMARK 500 HG SER A 146 OE1 GLU A 149 1.34
REMARK 500 HG SER A 1 OD2 ASP A 161 1.35
REMARK 500 HG SER A 112 OE2 GLU A 115 1.40
REMARK 500 HG SER A 90 OE2 GLU A 93 1.44
REMARK 500 O TRP A 57 HG1 THR A 62 1.45
REMARK 500 HZ3 LYS A 37 OE1 GLU A 38 1.50
REMARK 500 O THR A 74 HG SER A 78 1.51
REMARK 500 HZ1 LYS A 42 OE2 GLU A 44 1.52
REMARK 500 O MET A 50 HG1 THR A 54 1.56
REMARK 500 OD1 ASP A 114 HZ3 LYS A 127 1.56
REMARK 500 HH TYR A 116 OG SER A 133 1.59
REMARK 500 HZ1 LYS A 9 OE1 GLU A 72 1.59
REMARK 500 OD1 ASP A 163 HZ3 LYS A 167 1.60
REMARK 500 O VAL A 168 N PHE A 169 1.62
REMARK 500 O TRP A 57 OG1 THR A 62 2.14
REMARK 500 O GLN A 6 OG1 THR A 10 2.19
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 VAL A 174 C VAL A 174 OXT 0.140
REMARK 500 2 VAL A 174 C VAL A 174 OXT 0.135
REMARK 500 3 VAL A 174 C VAL A 174 OXT 0.141
REMARK 500 4 HIS A 45 CG HIS A 45 CD2 0.056
REMARK 500 4 VAL A 174 C VAL A 174 OXT 0.141
REMARK 500 5 VAL A 174 C VAL A 174 OXT 0.138
REMARK 500 6 HIS A 45 CG HIS A 45 CD2 0.059
REMARK 500 6 VAL A 174 C VAL A 174 OXT 0.136
REMARK 500 7 VAL A 174 C VAL A 174 OXT 0.144
REMARK 500 8 VAL A 174 C VAL A 174 OXT 0.135
REMARK 500 9 HIS A 45 CG HIS A 45 CD2 0.055
REMARK 500 9 VAL A 174 C VAL A 174 OXT 0.143
REMARK 500 10 VAL A 174 C VAL A 174 OXT 0.141
REMARK 500 11 VAL A 174 C VAL A 174 OXT 0.142
REMARK 500 12 VAL A 174 C VAL A 174 OXT 0.143
REMARK 500 13 VAL A 174 C VAL A 174 OXT 0.135
REMARK 500 14 VAL A 174 C VAL A 174 OXT 0.142
REMARK 500 15 VAL A 174 C VAL A 174 OXT 0.135
REMARK 500 16 HIS A 45 CG HIS A 45 CD2 0.061
REMARK 500 16 VAL A 174 C VAL A 174 OXT 0.142
REMARK 500 17 VAL A 174 C VAL A 174 OXT 0.144
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 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 1 HIS A 45 ND1 - CE1 - NE2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 1 ASN A 59 OD1 - CG - ND2 ANGL. DEV. = -38.8 DEGREES
REMARK 500 1 THR A 62 N - CA - CB ANGL. DEV. = -12.0 DEGREES
REMARK 500 1 LYS A 84 CA - CB - CG ANGL. DEV. = 17.6 DEGREES
REMARK 500 1 VAL A 92 CA - CB - CG1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 1 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 VAL A 168 O - C - N ANGL. DEV. = -41.2 DEGREES
REMARK 500 2 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 2 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 HIS A 45 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 2 TRP A 57 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 2 THR A 62 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 2 ASN A 85 OD1 - CG - ND2 ANGL. DEV. = -38.5 DEGREES
REMARK 500 2 VAL A 92 CA - CB - CG1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 2 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 2 ASP A 142 O - C - N ANGL. DEV. = -45.1 DEGREES
REMARK 500 2 VAL A 168 O - C - N ANGL. DEV. = -41.2 DEGREES
REMARK 500 3 THR A 10 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 3 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 3 ALA A 43 CA - C - O ANGL. DEV. = -22.5 DEGREES
REMARK 500 3 ALA A 43 CA - C - N ANGL. DEV. = 42.0 DEGREES
REMARK 500 3 ALA A 43 O - C - N ANGL. DEV. = -60.9 DEGREES
REMARK 500 3 HIS A 45 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 3 THR A 62 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 3 VAL A 83 CA - C - O ANGL. DEV. = -18.3 DEGREES
REMARK 500 3 VAL A 83 CA - C - N ANGL. DEV. = 13.6 DEGREES
REMARK 500 3 VAL A 83 O - C - N ANGL. DEV. = -51.0 DEGREES
REMARK 500 3 VAL A 92 CA - CB - CG1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 3 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 3 ARG A 101 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG A 113 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 3 VAL A 168 O - C - N ANGL. DEV. = -40.6 DEGREES
REMARK 500 3 TRP A 170 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 4 THR A 10 CA - CB - CG2 ANGL. DEV. = 11.8 DEGREES
REMARK 500 4 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 4 LYS A 37 O - C - N ANGL. DEV. = -38.9 DEGREES
REMARK 500 4 HIS A 45 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 4 THR A 62 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 4 LYS A 68 O - C - N ANGL. DEV. = -37.6 DEGREES
REMARK 500 4 VAL A 83 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 4 VAL A 83 N - CA - CB ANGL. DEV. = -13.4 DEGREES
REMARK 500 4 ARG A 101 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 267 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 ALA A 43 -47.60 -25.46
REMARK 500 1 PHE A 60 -65.00 -127.28
REMARK 500 1 ASP A 104 54.87 -63.25
REMARK 500 1 ASN A 109 18.92 83.51
REMARK 500 1 ASP A 138 70.84 -64.24
REMARK 500 1 ASP A 163 -109.24 -95.29
REMARK 500 1 SER A 164 -167.22 64.81
REMARK 500 2 LYS A 19 9.84 57.14
REMARK 500 2 GLU A 38 45.95 -104.17
REMARK 500 2 PHE A 60 -66.54 -126.00
REMARK 500 2 ALA A 88 42.66 -83.32
REMARK 500 2 ASP A 104 73.24 -67.37
REMARK 500 2 GLU A 107 45.26 72.94
REMARK 500 2 ASN A 109 20.09 101.29
REMARK 500 2 ASP A 138 75.92 -63.68
REMARK 500 2 ASP A 161 -73.75 -82.47
REMARK 500 2 ASP A 163 -124.29 -165.82
REMARK 500 2 SER A 164 -112.08 56.72
REMARK 500 2 ASN A 166 -11.78 65.88
REMARK 500 2 PRO A 172 46.80 -76.64
REMARK 500 2 LEU A 173 113.39 53.14
REMARK 500 3 LYS A 19 9.82 54.37
REMARK 500 3 GLU A 44 -15.52 -48.23
REMARK 500 3 PHE A 60 -67.59 -127.14
REMARK 500 3 ASP A 104 55.52 -66.28
REMARK 500 3 GLU A 107 10.03 80.09
REMARK 500 3 ASN A 109 19.98 80.02
REMARK 500 3 ASP A 138 72.99 -66.95
REMARK 500 3 ASP A 161 -68.26 -132.50
REMARK 500 3 ASP A 163 -51.88 -159.52
REMARK 500 3 SER A 164 90.12 -64.51
REMARK 500 3 THR A 165 164.79 54.63
REMARK 500 4 LYS A 19 14.10 52.39
REMARK 500 4 GLU A 38 -13.17 -156.69
REMARK 500 4 SER A 39 -150.82 -101.29
REMARK 500 4 GLU A 40 -85.12 -101.00
REMARK 500 4 MET A 41 151.02 63.64
REMARK 500 4 ALA A 43 -78.24 26.80
REMARK 500 4 PHE A 60 -64.65 -132.07
REMARK 500 4 GLU A 107 33.96 73.98
REMARK 500 4 ASN A 109 18.28 82.61
REMARK 500 4 LEU A 123 -6.82 -59.72
REMARK 500 4 LEU A 125 -123.65 -127.82
REMARK 500 4 ASP A 126 133.76 -171.67
REMARK 500 4 ASP A 138 84.41 -64.20
REMARK 500 4 SER A 164 -98.24 -157.27
REMARK 500 4 THR A 165 -38.85 -153.00
REMARK 500 4 PHE A 169 -8.17 -51.62
REMARK 500 5 ALA A 43 -77.20 -45.60
REMARK 500 5 GLU A 44 -19.79 -40.64
REMARK 500
REMARK 500 THIS ENTRY HAS 177 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 25 0.12 SIDE CHAIN
REMARK 500 1 ASN A 59 0.16 SIDE CHAIN
REMARK 500 1 PHE A 100 0.08 SIDE CHAIN
REMARK 500 2 ASN A 85 0.17 SIDE CHAIN
REMARK 500 3 ARG A 14 0.10 SIDE CHAIN
REMARK 500 3 ARG A 34 0.12 SIDE CHAIN
REMARK 500 4 ARG A 25 0.08 SIDE CHAIN
REMARK 500 4 ASN A 166 0.15 SIDE CHAIN
REMARK 500 7 ARG A 25 0.12 SIDE CHAIN
REMARK 500 7 ARG A 34 0.07 SIDE CHAIN
REMARK 500 7 ARG A 113 0.09 SIDE CHAIN
REMARK 500 7 PHE A 157 0.08 SIDE CHAIN
REMARK 500 8 ARG A 34 0.12 SIDE CHAIN
REMARK 500 9 ARG A 25 0.12 SIDE CHAIN
REMARK 500 10 ARG A 25 0.12 SIDE CHAIN
REMARK 500 10 ARG A 34 0.11 SIDE CHAIN
REMARK 500 11 GLN A 6 0.17 SIDE CHAIN
REMARK 500 11 ASN A 160 0.15 SIDE CHAIN
REMARK 500 12 ASN A 59 0.17 SIDE CHAIN
REMARK 500 12 ASN A 85 0.17 SIDE CHAIN
REMARK 500 13 GLN A 6 0.16 SIDE CHAIN
REMARK 500 13 ARG A 14 0.14 SIDE CHAIN
REMARK 500 13 ASN A 77 0.16 SIDE CHAIN
REMARK 500 14 ARG A 14 0.10 SIDE CHAIN
REMARK 500 14 ARG A 25 0.08 SIDE CHAIN
REMARK 500 14 ARG A 34 0.12 SIDE CHAIN
REMARK 500 14 HIS A 45 0.14 SIDE CHAIN
REMARK 500 14 ASN A 160 0.16 SIDE CHAIN
REMARK 500 15 HIS A 45 0.09 SIDE CHAIN
REMARK 500 16 ARG A 113 0.17 SIDE CHAIN
REMARK 500 17 ARG A 25 0.16 SIDE CHAIN
REMARK 500 17 ARG A 34 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 VAL A 168 46.04
REMARK 500 2 ASP A 142 56.78
REMARK 500 2 VAL A 168 46.54
REMARK 500 3 ALA A 43 -169.00
REMARK 500 3 VAL A 83 -70.41
REMARK 500 3 VAL A 168 45.47
REMARK 500 4 LYS A 37 47.64
REMARK 500 4 LYS A 68 -45.97
REMARK 500 5 ARG A 14 83.61
REMARK 500 5 MET A 41 -21.12
REMARK 500 5 ALA A 43 -162.74
REMARK 500 5 VAL A 168 43.16
REMARK 500 6 LYS A 42 34.34
REMARK 500 6 GLU A 87 40.90
REMARK 500 6 LYS A 167 63.11
REMARK 500 7 GLY A 66 -41.65
REMARK 500 7 GLU A 87 41.56
REMARK 500 7 ASN A 166 -49.58
REMARK 500 8 GLY A 66 -41.73
REMARK 500 9 MET A 41 46.17
REMARK 500 9 GLY A 67 -48.13
REMARK 500 9 LYS A 68 46.26
REMARK 500 9 LEU A 125 50.09
REMARK 500 10 GLU A 40 -47.39
REMARK 500 10 MET A 41 45.51
REMARK 500 10 ALA A 43 -153.96
REMARK 500 10 GLU A 44 -62.01
REMARK 500 10 LYS A 68 -164.97
REMARK 500 10 GLU A 87 40.19
REMARK 500 11 MET A 41 47.27
REMARK 500 11 ALA A 43 -168.80
REMARK 500 11 PHE A 60 -51.97
REMARK 500 11 VAL A 168 46.36
REMARK 500 12 MET A 41 -47.83
REMARK 500 12 GLY A 66 -62.53
REMARK 500 12 VAL A 168 46.09
REMARK 500 13 GLU A 40 53.68
REMARK 500 13 MET A 159 -50.13
REMARK 500 13 THR A 165 -141.47
REMARK 500 14 GLU A 40 -37.85
REMARK 500 14 ALA A 43 -151.40
REMARK 500 14 GLU A 44 -55.61
REMARK 500 14 VAL A 64 -145.94
REMARK 500 14 GLY A 66 -42.46
REMARK 500 14 ASN A 160 -39.78
REMARK 500 14 ASP A 163 39.56
REMARK 500 15 LYS A 37 56.30
REMARK 500 15 MET A 41 152.98
REMARK 500 15 ALA A 43 -172.13
REMARK 500 15 PHE A 60 -44.43
REMARK 500
REMARK 500 THIS ENTRY HAS 54 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4129 RELATED DB: BMRB
REMARK 900 THE SAME PROTEIN, ONLY CHEMICAL SHIFTS OF PROTON AND 15N RESONANCES
DBREF 1Q80 A 1 174 UNP P04571 SCP_NERDI 1 174
SEQRES 1 A 174 SER ASP LEU TRP VAL GLN LYS MET LYS THR TYR PHE ASN
SEQRES 2 A 174 ARG ILE ASP PHE ASP LYS ASP GLY ALA ILE THR ARG MET
SEQRES 3 A 174 ASP PHE GLU SER MET ALA GLU ARG PHE ALA LYS GLU SER
SEQRES 4 A 174 GLU MET LYS ALA GLU HIS ALA LYS VAL LEU MET ASP SER
SEQRES 5 A 174 LEU THR GLY VAL TRP ASP ASN PHE LEU THR ALA VAL ALA
SEQRES 6 A 174 GLY GLY LYS GLY ILE ASP GLU THR THR PHE ILE ASN SER
SEQRES 7 A 174 MET LYS GLU MET VAL LYS ASN PRO GLU ALA LYS SER VAL
SEQRES 8 A 174 VAL GLU GLY PRO LEU PRO LEU PHE PHE ARG ALA VAL ASP
SEQRES 9 A 174 THR ASN GLU ASP ASN ASN ILE SER ARG ASP GLU TYR GLY
SEQRES 10 A 174 ILE PHE PHE GLY MET LEU GLY LEU ASP LYS THR MET ALA
SEQRES 11 A 174 PRO ALA SER PHE ASP ALA ILE ASP THR ASN ASN ASP GLY
SEQRES 12 A 174 LEU LEU SER LEU GLU GLU PHE VAL ILE ALA GLY SER ASP
SEQRES 13 A 174 PHE PHE MET ASN ASP GLY ASP SER THR ASN LYS VAL PHE
SEQRES 14 A 174 TRP GLY PRO LEU VAL
HELIX 1 1 SER A 1 ASP A 16 1 16
HELIX 2 2 THR A 24 SER A 39 1 16
HELIX 3 3 GLU A 44 PHE A 60 1 17
HELIX 4 4 LEU A 61 VAL A 64 5 4
HELIX 5 5 GLU A 72 VAL A 83 1 12
HELIX 6 6 ALA A 88 GLY A 94 1 7
HELIX 7 7 GLY A 94 ASP A 104 1 11
HELIX 8 8 SER A 112 GLY A 124 1 13
HELIX 9 9 ASP A 126 THR A 128 5 3
HELIX 10 10 MET A 129 ASP A 138 1 10
HELIX 11 11 SER A 146 ASN A 160 1 15
SHEET 1 A 2 ALA A 22 ILE A 23 0
SHEET 2 A 2 ILE A 70 ASP A 71 -1 O ILE A 70 N ILE A 23
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 5 2 Bytes