Header list of 1ikc.pdb file
Complete list - b 23 2 Bytes
HEADER TOXIN 03-MAY-01 1IKC
TITLE NMR STRUCTURE OF ALPHA-BUNGAROTOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LONG NEUROTOXIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-BUNGAROTOXIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BUNGARUS MULTICINCTUS;
SOURCE 3 ORGANISM_COMMON: MANY-BANDED KRAIT;
SOURCE 4 ORGANISM_TAXID: 8616
KEYWDS ALPHA-BUNGAROTOXIN, TOXIN, NICOTINIC-ACETILCHOLINE RECEPTOR
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR N.NICCOLAI,O.SPIGA,A.CIUTTI
REVDAT 5 23-FEB-22 1IKC 1 REMARK
REVDAT 4 24-FEB-09 1IKC 1 VERSN
REVDAT 3 27-FEB-02 1IKC 1 JRNL REMARK
REVDAT 2 13-JUN-01 1IKC 1 TITLE
REVDAT 1 16-MAY-01 1IKC 0
JRNL AUTH M.SCARSELLI,O.SPIGA,A.CIUTTI,A.BERNINI,L.BRACCI,B.LELLI,
JRNL AUTH 2 L.LOZZI,D.CALAMANDREI,D.DI MARO,S.KLEIN,N.NICCOLAI
JRNL TITL NMR STRUCTURE OF ALPHA-BUNGAROTOXIN FREE AND BOUND TO A
JRNL TITL 2 MIMOTOPE OF THE NICOTINIC ACETYLCHOLINE RECEPTOR.
JRNL REF BIOCHEMISTRY V. 41 1457 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11814338
JRNL DOI 10.1021/BI011012F
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH O.SPIGA,A.BERNINI,M.SCARSELLI,A.CIUTTI,L.BRACCI,L.LOZZI,
REMARK 1 AUTH 2 B.LELLI,D.DI MARO,D.CALAMANDREI,N.NICCOLAI
REMARK 1 TITL PEPTIDE-PROTEIN INTERACTIONS STUDIED BY SURFACE PLASMON AND
REMARK 1 TITL 2 NUCLEAR MAGNETIC RESONANCES
REMARK 1 REF FEBS LETT. V. 511 33 2002
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(01)03274-4
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, AMBER 4.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IKC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013361.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.67
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 0.5MM ALPHA-BUNGAROTOXIN; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2DTOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.1, NMRVIEW 4.1, DIANA
REMARK 210 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 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 2 HIS A 68 CG HIS A 68 ND1 -0.122
REMARK 500 2 HIS A 68 NE2 HIS A 68 CD2 -0.079
REMARK 500 3 THR A 5 CB THR A 5 OG1 -0.143
REMARK 500 3 HIS A 68 NE2 HIS A 68 CD2 -0.075
REMARK 500 4 TRP A 28 CE2 TRP A 28 CD2 -0.092
REMARK 500 4 HIS A 68 NE2 HIS A 68 CD2 -0.068
REMARK 500 5 CYS A 29 CB CYS A 29 SG -0.109
REMARK 500 6 HIS A 68 NE2 HIS A 68 CD2 -0.066
REMARK 500 7 HIS A 68 CB HIS A 68 CG 0.150
REMARK 500 7 HIS A 68 CG HIS A 68 CD2 -0.206
REMARK 500 7 HIS A 68 CG HIS A 68 ND1 -0.159
REMARK 500 8 HIS A 68 NE2 HIS A 68 CD2 -0.087
REMARK 500 9 HIS A 68 CG HIS A 68 ND1 -0.091
REMARK 500 9 HIS A 68 CE1 HIS A 68 NE2 -0.093
REMARK 500 9 HIS A 68 NE2 HIS A 68 CD2 -0.093
REMARK 500 10 HIS A 68 NE2 HIS A 68 CD2 -0.066
REMARK 500 11 TRP A 28 CE2 TRP A 28 CD2 -0.105
REMARK 500 12 HIS A 68 NE2 HIS A 68 CD2 -0.094
REMARK 500 13 HIS A 68 NE2 HIS A 68 CD2 -0.088
REMARK 500 14 THR A 5 CB THR A 5 OG1 -0.130
REMARK 500 15 HIS A 68 CB HIS A 68 CG 0.166
REMARK 500 15 HIS A 68 CG HIS A 68 CD2 -0.248
REMARK 500 15 HIS A 68 CG HIS A 68 ND1 -0.161
REMARK 500 15 GLN A 71 CD GLN A 71 NE2 -0.268
REMARK 500 16 HIS A 68 NE2 HIS A 68 CD2 -0.087
REMARK 500 17 LYS A 64 CE LYS A 64 NZ 0.154
REMARK 500 18 HIS A 68 NE2 HIS A 68 CD2 -0.088
REMARK 500 19 TRP A 28 CE2 TRP A 28 CD2 -0.083
REMARK 500 19 HIS A 68 CG HIS A 68 ND1 -0.125
REMARK 500 19 HIS A 68 ND1 HIS A 68 CE1 -0.092
REMARK 500 19 HIS A 68 NE2 HIS A 68 CD2 -0.078
REMARK 500 20 GLN A 71 CD GLN A 71 OE1 -0.149
REMARK 500 21 TRP A 28 CG TRP A 28 CD2 -0.103
REMARK 500 21 TRP A 28 CD1 TRP A 28 NE1 -0.137
REMARK 500 21 TRP A 28 CE2 TRP A 28 CZ2 -0.163
REMARK 500 21 HIS A 68 NE2 HIS A 68 CD2 -0.084
REMARK 500 22 LYS A 64 CE LYS A 64 NZ -0.184
REMARK 500 22 HIS A 68 NE2 HIS A 68 CD2 -0.072
REMARK 500 23 LYS A 64 CE LYS A 64 NZ -0.197
REMARK 500 23 HIS A 68 NE2 HIS A 68 CD2 -0.091
REMARK 500 24 HIS A 68 CE1 HIS A 68 NE2 -0.106
REMARK 500 24 HIS A 68 NE2 HIS A 68 CD2 -0.079
REMARK 500 25 LYS A 64 CE LYS A 64 NZ 0.172
REMARK 500 26 CYS A 16 CB CYS A 16 SG 0.110
REMARK 500 26 TRP A 28 NE1 TRP A 28 CE2 -0.079
REMARK 500 26 HIS A 68 NE2 HIS A 68 CD2 -0.094
REMARK 500 27 HIS A 68 CE1 HIS A 68 NE2 -0.074
REMARK 500 27 HIS A 68 NE2 HIS A 68 CD2 -0.180
REMARK 500 27 GLN A 71 CD GLN A 71 OE1 -0.171
REMARK 500 28 TRP A 28 CG TRP A 28 CD2 -0.105
REMARK 500
REMARK 500 THIS ENTRY HAS 58 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 VAL A 2 CG1 - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 1 CYS A 3 CA - CB - SG ANGL. DEV. = 11.2 DEGREES
REMARK 500 1 THR A 5 CA - CB - CG2 ANGL. DEV. = -13.1 DEGREES
REMARK 500 1 ALA A 13 N - CA - CB ANGL. DEV. = 9.7 DEGREES
REMARK 500 1 VAL A 14 O - C - N ANGL. DEV. = 9.7 DEGREES
REMARK 500 1 CYS A 16 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 1 VAL A 40 CG1 - CB - CG2 ANGL. DEV. = -12.4 DEGREES
REMARK 500 1 CYS A 44 CB - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 1 CYS A 44 N - CA - CB ANGL. DEV. = 17.2 DEGREES
REMARK 500 1 THR A 58 CA - CB - CG2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 1 CYS A 65 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 CYS A 3 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 2 THR A 5 OG1 - CB - CG2 ANGL. DEV. = -31.6 DEGREES
REMARK 500 2 ALA A 13 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 2 VAL A 14 O - C - N ANGL. DEV. = 9.9 DEGREES
REMARK 500 2 LEU A 22 CB - CG - CD1 ANGL. DEV. = 14.8 DEGREES
REMARK 500 2 TYR A 24 CG - CD1 - CE1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 2 TYR A 24 CZ - CE2 - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 VAL A 40 CG1 - CB - CG2 ANGL. DEV. = -14.5 DEGREES
REMARK 500 2 CYS A 44 CA - CB - SG ANGL. DEV. = 14.1 DEGREES
REMARK 500 2 LYS A 64 CD - CE - NZ ANGL. DEV. = 17.1 DEGREES
REMARK 500 2 HIS A 68 CG - ND1 - CE1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 3 VAL A 2 CG1 - CB - CG2 ANGL. DEV. = 10.3 DEGREES
REMARK 500 3 CYS A 3 CA - CB - SG ANGL. DEV. = 9.5 DEGREES
REMARK 500 3 THR A 5 OG1 - CB - CG2 ANGL. DEV. = -31.2 DEGREES
REMARK 500 3 ALA A 13 N - CA - CB ANGL. DEV. = 9.9 DEGREES
REMARK 500 3 VAL A 14 O - C - N ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 LEU A 22 CB - CG - CD1 ANGL. DEV. = 14.8 DEGREES
REMARK 500 3 TYR A 24 CG - CD1 - CE1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 3 ASP A 30 CB - CG - OD1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 3 VAL A 40 CG1 - CB - CG2 ANGL. DEV. = -16.8 DEGREES
REMARK 500 3 CYS A 44 CA - CB - SG ANGL. DEV. = 14.2 DEGREES
REMARK 500 3 LYS A 64 CD - CE - NZ ANGL. DEV. = 14.7 DEGREES
REMARK 500 4 VAL A 2 CG1 - CB - CG2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 4 CYS A 3 CA - CB - SG ANGL. DEV. = 9.8 DEGREES
REMARK 500 4 THR A 5 OG1 - CB - CG2 ANGL. DEV. = -31.3 DEGREES
REMARK 500 4 THR A 5 O - C - N ANGL. DEV. = 10.1 DEGREES
REMARK 500 4 ALA A 13 N - CA - CB ANGL. DEV. = 10.8 DEGREES
REMARK 500 4 VAL A 14 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 4 CYS A 16 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 4 LEU A 22 CB - CG - CD1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 4 TYR A 24 CG - CD1 - CE1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 4 TYR A 24 CG - CD2 - CE2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 4 TYR A 24 CZ - CE2 - CD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 4 VAL A 40 CG1 - CB - CG2 ANGL. DEV. = -16.7 DEGREES
REMARK 500 4 CYS A 44 N - CA - CB ANGL. DEV. = 9.4 DEGREES
REMARK 500 4 VAL A 57 CG1 - CB - CG2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 4 LYS A 64 CD - CE - NZ ANGL. DEV. = 18.8 DEGREES
REMARK 500 5 CYS A 3 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 5 ALA A 7 N - CA - CB ANGL. DEV. = 8.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 446 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 VAL A 2 -101.22 -168.74
REMARK 500 1 THR A 5 -108.76 -143.23
REMARK 500 1 ALA A 7 67.90 127.76
REMARK 500 1 THR A 8 62.41 82.28
REMARK 500 1 SER A 9 -149.68 106.68
REMARK 500 1 ILE A 11 -153.94 58.50
REMARK 500 1 SER A 12 36.20 -174.95
REMARK 500 1 ALA A 13 -32.88 105.43
REMARK 500 1 VAL A 14 -77.79 10.30
REMARK 500 1 THR A 15 32.22 107.17
REMARK 500 1 CYS A 16 -157.43 63.78
REMARK 500 1 PRO A 17 -148.43 -76.40
REMARK 500 1 PRO A 18 -108.03 -72.58
REMARK 500 1 GLU A 20 63.58 64.08
REMARK 500 1 ASN A 21 153.67 101.00
REMARK 500 1 LEU A 22 151.45 96.67
REMARK 500 1 MET A 27 164.53 78.82
REMARK 500 1 TRP A 28 -40.48 167.18
REMARK 500 1 CYS A 29 60.53 -116.57
REMARK 500 1 ASP A 30 -80.70 17.94
REMARK 500 1 ALA A 31 3.27 -177.88
REMARK 500 1 CYS A 33 40.71 35.78
REMARK 500 1 SER A 35 -170.40 93.05
REMARK 500 1 ARG A 36 -131.72 59.82
REMARK 500 1 VAL A 39 77.97 -119.81
REMARK 500 1 GLU A 41 -51.82 -126.67
REMARK 500 1 LEU A 42 75.00 0.67
REMARK 500 1 CYS A 44 163.86 46.18
REMARK 500 1 ALA A 45 39.82 -164.24
REMARK 500 1 ALA A 46 -93.92 131.15
REMARK 500 1 CYS A 48 84.69 40.19
REMARK 500 1 PRO A 49 7.22 -69.18
REMARK 500 1 SER A 50 -43.37 82.53
REMARK 500 1 LYS A 51 -134.03 67.22
REMARK 500 1 TYR A 54 -158.76 37.23
REMARK 500 1 GLU A 55 -101.91 -28.13
REMARK 500 1 THR A 58 -157.92 177.35
REMARK 500 1 CYS A 59 108.73 -179.96
REMARK 500 1 CYS A 60 -161.40 -113.53
REMARK 500 1 SER A 61 50.93 159.25
REMARK 500 1 ASP A 63 -29.54 107.64
REMARK 500 1 LYS A 64 168.47 173.51
REMARK 500 1 CYS A 65 53.83 164.59
REMARK 500 1 ASN A 66 50.96 -155.11
REMARK 500 1 PRO A 67 -158.38 -70.57
REMARK 500 1 HIS A 68 117.48 177.00
REMARK 500 1 PRO A 69 -166.31 -71.87
REMARK 500 1 LYS A 70 -86.96 53.82
REMARK 500 1 GLN A 71 -158.29 62.86
REMARK 500 1 PRO A 73 44.70 -74.91
REMARK 500
REMARK 500 THIS ENTRY HAS 1536 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 43 CYS A 44 14 -149.52
REMARK 500 GLY A 43 CYS A 44 16 -148.83
REMARK 500 GLY A 43 CYS A 44 20 -148.93
REMARK 500 GLY A 43 CYS A 44 26 -149.50
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 TYR A 54 0.08 SIDE CHAIN
REMARK 500 2 TYR A 24 0.10 SIDE CHAIN
REMARK 500 2 HIS A 68 0.17 SIDE CHAIN
REMARK 500 3 TYR A 24 0.10 SIDE CHAIN
REMARK 500 4 TYR A 24 0.10 SIDE CHAIN
REMARK 500 5 TYR A 54 0.08 SIDE CHAIN
REMARK 500 6 TYR A 24 0.10 SIDE CHAIN
REMARK 500 6 HIS A 68 0.15 SIDE CHAIN
REMARK 500 7 TYR A 24 0.10 SIDE CHAIN
REMARK 500 8 TYR A 24 0.10 SIDE CHAIN
REMARK 500 9 TYR A 24 0.09 SIDE CHAIN
REMARK 500 9 HIS A 68 0.14 SIDE CHAIN
REMARK 500 10 TYR A 24 0.10 SIDE CHAIN
REMARK 500 10 HIS A 68 0.18 SIDE CHAIN
REMARK 500 11 TYR A 24 0.10 SIDE CHAIN
REMARK 500 12 TYR A 24 0.10 SIDE CHAIN
REMARK 500 13 TYR A 24 0.10 SIDE CHAIN
REMARK 500 14 TYR A 24 0.10 SIDE CHAIN
REMARK 500 14 HIS A 68 0.16 SIDE CHAIN
REMARK 500 15 TYR A 24 0.10 SIDE CHAIN
REMARK 500 16 TYR A 24 0.10 SIDE CHAIN
REMARK 500 17 TYR A 24 0.14 SIDE CHAIN
REMARK 500 17 HIS A 68 0.15 SIDE CHAIN
REMARK 500 18 TYR A 24 0.11 SIDE CHAIN
REMARK 500 19 TYR A 24 0.10 SIDE CHAIN
REMARK 500 19 HIS A 68 0.15 SIDE CHAIN
REMARK 500 20 TYR A 24 0.11 SIDE CHAIN
REMARK 500 21 TYR A 24 0.11 SIDE CHAIN
REMARK 500 22 TYR A 24 0.10 SIDE CHAIN
REMARK 500 23 TYR A 24 0.10 SIDE CHAIN
REMARK 500 24 TYR A 24 0.10 SIDE CHAIN
REMARK 500 24 HIS A 68 0.10 SIDE CHAIN
REMARK 500 25 TYR A 24 0.13 SIDE CHAIN
REMARK 500 25 HIS A 68 0.12 SIDE CHAIN
REMARK 500 26 TYR A 24 0.11 SIDE CHAIN
REMARK 500 27 TYR A 24 0.12 SIDE CHAIN
REMARK 500 28 TYR A 24 0.10 SIDE CHAIN
REMARK 500 28 TYR A 54 0.09 SIDE CHAIN
REMARK 500 29 TYR A 24 0.08 SIDE CHAIN
REMARK 500 29 HIS A 68 0.16 SIDE CHAIN
REMARK 500 30 TYR A 24 0.15 SIDE CHAIN
REMARK 500 30 ASN A 66 0.12 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 THR A 6 15.16
REMARK 500 3 GLY A 37 11.13
REMARK 500 3 GLN A 71 10.58
REMARK 500 4 GLY A 37 10.29
REMARK 500 5 VAL A 2 -11.26
REMARK 500 5 THR A 6 15.12
REMARK 500 5 CYS A 44 11.05
REMARK 500 6 GLY A 43 10.14
REMARK 500 8 GLY A 43 10.24
REMARK 500 10 GLY A 43 10.32
REMARK 500 11 VAL A 2 -12.94
REMARK 500 11 GLY A 37 10.34
REMARK 500 12 GLY A 37 10.52
REMARK 500 12 GLY A 43 10.31
REMARK 500 13 GLY A 37 10.31
REMARK 500 13 GLY A 43 10.31
REMARK 500 14 THR A 6 13.93
REMARK 500 15 VAL A 2 -12.97
REMARK 500 16 THR A 6 13.49
REMARK 500 16 GLY A 37 10.38
REMARK 500 16 GLY A 43 10.03
REMARK 500 17 THR A 6 16.53
REMARK 500 17 LEU A 42 10.68
REMARK 500 18 THR A 6 14.17
REMARK 500 18 GLY A 37 10.14
REMARK 500 18 GLY A 43 10.11
REMARK 500 19 THR A 6 15.21
REMARK 500 19 GLY A 43 10.81
REMARK 500 20 TYR A 24 11.29
REMARK 500 20 LEU A 42 17.83
REMARK 500 21 TYR A 24 10.55
REMARK 500 21 PRO A 67 12.27
REMARK 500 22 GLY A 37 10.71
REMARK 500 23 THR A 15 11.01
REMARK 500 23 CYS A 44 10.54
REMARK 500 26 CYS A 44 10.74
REMARK 500 27 LEU A 42 12.22
REMARK 500 28 GLY A 37 10.33
REMARK 500 28 GLY A 43 10.64
REMARK 500 29 THR A 58 -13.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HN7 RELATED DB: PDB
REMARK 900 1HN7 CONTAINS THE SAME PROTEIN COMPLEXED WITH A PEPTIDE
REMARK 900 RELATED ID: 1HOY RELATED DB: PDB
REMARK 900 1HOY CONTAINS THE SAME PROTEIN COMPLEXED WITH A PEPTIDE
REMARK 900 RELATED ID: 1IK8 RELATED DB: PDB
REMARK 900 1IK8 CONTAINS THE MINIMIZED AVERAGE STRUCTURE
DBREF 1IKC A 1 74 UNP P60615 NXL1A_BUNMU 1 74
SEQRES 1 A 74 ILE VAL CYS HIS THR THR ALA THR SER PRO ILE SER ALA
SEQRES 2 A 74 VAL THR CYS PRO PRO GLY GLU ASN LEU CYS TYR ARG LYS
SEQRES 3 A 74 MET TRP CYS ASP ALA PHE CYS SER SER ARG GLY LYS VAL
SEQRES 4 A 74 VAL GLU LEU GLY CYS ALA ALA THR CYS PRO SER LYS LYS
SEQRES 5 A 74 PRO TYR GLU GLU VAL THR CYS CYS SER THR ASP LYS CYS
SEQRES 6 A 74 ASN PRO HIS PRO LYS GLN ARG PRO GLY
SHEET 1 A 2 MET A 27 TRP A 28 0
SHEET 2 A 2 VAL A 39 VAL A 40 -1 O VAL A 39 N TRP A 28
SSBOND 1 CYS A 3 CYS A 23 1555 1555 2.01
SSBOND 2 CYS A 16 CYS A 44 1555 1555 1.99
SSBOND 3 CYS A 29 CYS A 33 1555 1555 2.01
SSBOND 4 CYS A 48 CYS A 59 1555 1555 2.04
SSBOND 5 CYS A 60 CYS A 65 1555 1555 2.04
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