Header list of 1as5.pdb file
Complete list - 16 20 Bytes
HEADER NEUROTOXIN 13-AUG-97 1AS5
TITLE SOLUTION STRUCTURE OF CONOTOXIN Y-PIIIE FROM CONUS PURPURASCENS, NMR,
TITLE 2 14 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONOTOXIN Y-PIIIE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: CONOTOXIN Y-PIIIE CONTAINS THE SAME DISULFIDE BONDING
COMPND 6 PATTERN AS THE MU-CONOTOXINS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CONUS PURPURASCENS;
SOURCE 3 ORGANISM_TAXID: 41690
KEYWDS CONOTOXIN, NEUROTOXIN, ACETYLCHOLINE
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR S.S.MITCHELL,K.SHON,M.P.FOSTER,B.M.OLIVERA,C.M.IRELAND
REVDAT 3 16-FEB-22 1AS5 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1AS5 1 VERSN
REVDAT 1 14-OCT-98 1AS5 0
JRNL AUTH S.S.MITCHELL,K.J.SHON,M.P.FOSTER,D.R.DAVIS,B.M.OLIVERA,
JRNL AUTH 2 C.M.IRELAND
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF CONOTOXIN PSI-PIIIE,
JRNL TITL 2 AN ACETYLCHOLINE GATED ION CHANNEL ANTAGONIST.
JRNL REF BIOCHEMISTRY V. 37 1215 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9477946
JRNL DOI 10.1021/BI972186T
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BIOSYM, BIOSYM
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NO REFINEMENT WAS DONE
REMARK 4
REMARK 4 1AS5 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_1000171191.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 277
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 6 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O/D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; DQF-COSY; PE-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY 500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED
REMARK 210 WITH IRMA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION,
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED ON THE SYNTHETIC PEPTIDE. NOE
REMARK 210 BUILD UP CURVES (100, 200, AND 400 MS) WERE GENERATED FOR
REMARK 210 ANALYSIS BY USING IRMA.
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 HYP A 2 HH TYR A 13 1.48
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 HIS A 1 CG HIS A 1 CD2 0.061
REMARK 500 2 HIS A 1 CG HIS A 1 CD2 0.060
REMARK 500 3 HIS A 1 CG HIS A 1 CD2 0.062
REMARK 500 4 HIS A 1 CG HIS A 1 CD2 0.062
REMARK 500 5 HIS A 1 CG HIS A 1 CD2 0.061
REMARK 500 6 HIS A 1 CG HIS A 1 CD2 0.057
REMARK 500 7 HIS A 1 CG HIS A 1 CD2 0.068
REMARK 500 8 HIS A 1 CG HIS A 1 CD2 0.060
REMARK 500 9 HIS A 1 CG HIS A 1 CD2 0.062
REMARK 500 10 HIS A 1 CG HIS A 1 CD2 0.061
REMARK 500 11 HIS A 1 CG HIS A 1 CD2 0.062
REMARK 500 12 HIS A 1 CG HIS A 1 CD2 0.067
REMARK 500 13 HIS A 1 CG HIS A 1 CD2 0.065
REMARK 500 14 HIS A 1 CG HIS A 1 CD2 0.067
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 HIS A 1 CA - CB - CG ANGL. DEV. = 10.7 DEGREES
REMARK 500 1 HIS A 1 ND1 - CE1 - NE2 ANGL. DEV. = 8.1 DEGREES
REMARK 500 1 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 1 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 1 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 1 CYS A 22 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 1 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 1 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 2 HIS A 1 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 2 CYS A 4 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 2 CYS A 4 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 CYS A 10 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 2 CYS A 10 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 2 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 2 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 2 TYR A 13 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 2 TYR A 13 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 CYS A 22 CB - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 2 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 3 HIS A 1 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 3 CYS A 4 N - CA - CB ANGL. DEV. = -19.0 DEGREES
REMARK 500 3 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 TYR A 13 CA - CB - CG ANGL. DEV. = 12.2 DEGREES
REMARK 500 3 CYS A 22 CB - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 3 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 4 HIS A 1 CA - CB - CG ANGL. DEV. = 10.6 DEGREES
REMARK 500 4 HIS A 1 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 4 CYS A 10 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 4 CYS A 10 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 4 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 4 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 4 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 4 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 4 GLN A 23 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 4 ARG A 24 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 4 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 5 HIS A 1 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 5 CYS A 4 N - CA - CB ANGL. DEV. = -15.3 DEGREES
REMARK 500 5 CYS A 10 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 5 ARG A 11 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 5 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 5 ARG A 12 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 145 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 HYP A 2 -162.18 -61.73
REMARK 500 1 HYP A 3 163.39 -46.83
REMARK 500 1 TYR A 7 -9.42 67.57
REMARK 500 1 HYP A 14 52.11 13.56
REMARK 500 1 CYS A 21 40.37 19.90
REMARK 500 1 CYS A 22 -77.93 -123.53
REMARK 500 1 GLN A 23 142.30 5.39
REMARK 500 2 HYP A 2 -158.24 -64.09
REMARK 500 2 CYS A 5 2.60 -68.02
REMARK 500 2 TYR A 7 -16.72 69.22
REMARK 500 2 HYP A 14 53.86 18.55
REMARK 500 2 ALA A 19 92.56 -68.06
REMARK 500 2 CYS A 21 16.37 -48.73
REMARK 500 2 GLN A 23 145.33 -17.29
REMARK 500 3 HYP A 2 -150.07 -61.73
REMARK 500 3 TYR A 7 -46.40 -28.04
REMARK 500 3 HYP A 14 8.95 17.78
REMARK 500 3 CYS A 16 -66.00 -139.94
REMARK 500 3 ALA A 19 80.68 -66.24
REMARK 500 3 CYS A 21 -29.01 -33.07
REMARK 500 3 CYS A 22 -76.43 -102.79
REMARK 500 3 GLN A 23 148.69 -11.57
REMARK 500 4 HYP A 2 -161.73 -60.61
REMARK 500 4 HYP A 3 163.24 -48.41
REMARK 500 4 TYR A 7 -12.65 76.74
REMARK 500 4 HYP A 14 52.50 16.77
REMARK 500 4 CYS A 21 34.62 19.77
REMARK 500 4 CYS A 22 -26.08 -140.26
REMARK 500 5 HYP A 2 -147.65 -61.41
REMARK 500 5 CYS A 5 11.51 -69.48
REMARK 500 5 HYP A 14 -13.22 17.60
REMARK 500 5 CYS A 16 -20.20 -140.95
REMARK 500 5 SER A 18 2.94 -66.17
REMARK 500 5 ALA A 19 85.33 -61.03
REMARK 500 5 CYS A 21 -23.41 -30.75
REMARK 500 5 GLN A 23 145.58 -14.28
REMARK 500 6 HYP A 2 -143.21 -60.59
REMARK 500 6 HYP A 3 173.03 -56.95
REMARK 500 6 TYR A 7 -5.76 68.71
REMARK 500 6 HYP A 14 -15.54 15.23
REMARK 500 6 CYS A 21 41.85 20.11
REMARK 500 6 CYS A 22 -49.43 -145.32
REMARK 500 7 HYP A 2 -160.33 -74.01
REMARK 500 7 HYP A 3 173.15 -48.64
REMARK 500 7 TYR A 7 -19.73 81.45
REMARK 500 7 CYS A 10 93.61 -66.87
REMARK 500 7 ARG A 11 126.59 -32.10
REMARK 500 7 HYP A 14 -19.15 3.52
REMARK 500 7 CYS A 21 -36.71 -14.20
REMARK 500 7 CYS A 22 -72.23 -106.57
REMARK 500
REMARK 500 THIS ENTRY HAS 99 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 HYP A 2 HYP A 3 1 133.86
REMARK 500 CYS A 16 SER A 17 1 -108.72
REMARK 500 SER A 17 SER A 18 1 149.78
REMARK 500 CYS A 22 GLN A 23 1 131.77
REMARK 500 HYP A 2 HYP A 3 2 135.55
REMARK 500 TYR A 13 HYP A 14 2 135.74
REMARK 500 CYS A 16 SER A 17 2 -106.83
REMARK 500 CYS A 21 CYS A 22 2 149.60
REMARK 500 CYS A 22 GLN A 23 2 145.30
REMARK 500 HYP A 2 HYP A 3 3 136.16
REMARK 500 CYS A 10 ARG A 11 3 147.19
REMARK 500 TYR A 13 HYP A 14 3 128.91
REMARK 500 GLY A 15 CYS A 16 3 -139.74
REMARK 500 CYS A 16 SER A 17 3 -94.05
REMARK 500 SER A 20 CYS A 21 3 141.66
REMARK 500 HYP A 2 HYP A 3 4 135.93
REMARK 500 TYR A 13 HYP A 14 4 144.09
REMARK 500 CYS A 16 SER A 17 4 -107.61
REMARK 500 CYS A 22 GLN A 23 4 -55.81
REMARK 500 HYP A 2 HYP A 3 5 129.77
REMARK 500 TYR A 13 HYP A 14 5 134.73
REMARK 500 CYS A 16 SER A 17 5 -123.74
REMARK 500 SER A 17 SER A 18 5 149.22
REMARK 500 HYP A 2 HYP A 3 6 123.94
REMARK 500 ARG A 12 TYR A 13 6 -136.45
REMARK 500 TYR A 13 HYP A 14 6 133.78
REMARK 500 CYS A 16 SER A 17 6 -121.99
REMARK 500 SER A 17 SER A 18 6 146.19
REMARK 500 CYS A 22 GLN A 23 6 -31.55
REMARK 500 HYP A 2 HYP A 3 7 130.11
REMARK 500 CYS A 10 ARG A 11 7 146.19
REMARK 500 TYR A 13 HYP A 14 7 139.84
REMARK 500 CYS A 16 SER A 17 7 -108.15
REMARK 500 CYS A 22 GLN A 23 7 149.23
REMARK 500 HYP A 2 HYP A 3 8 130.79
REMARK 500 TYR A 13 HYP A 14 8 137.14
REMARK 500 CYS A 16 SER A 17 8 -107.86
REMARK 500 HYP A 2 HYP A 3 9 134.52
REMARK 500 TYR A 13 HYP A 14 9 142.39
REMARK 500 CYS A 16 SER A 17 9 -106.34
REMARK 500 SER A 17 SER A 18 9 148.41
REMARK 500 CYS A 22 GLN A 23 9 140.36
REMARK 500 HYP A 2 HYP A 3 10 136.23
REMARK 500 TYR A 13 HYP A 14 10 140.39
REMARK 500 CYS A 16 SER A 17 10 -110.99
REMARK 500 HYP A 2 HYP A 3 11 136.00
REMARK 500 TYR A 13 HYP A 14 11 133.60
REMARK 500 CYS A 16 SER A 17 11 -110.57
REMARK 500 SER A 20 CYS A 21 11 141.43
REMARK 500 HYP A 2 HYP A 3 12 133.20
REMARK 500
REMARK 500 THIS ENTRY HAS 63 NON CIS, NON-TRANS OMEGA 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 11 0.08 SIDE CHAIN
REMARK 500 1 TYR A 13 0.21 SIDE CHAIN
REMARK 500 2 TYR A 13 0.08 SIDE CHAIN
REMARK 500 3 TYR A 13 0.08 SIDE CHAIN
REMARK 500 4 ARG A 11 0.08 SIDE CHAIN
REMARK 500 4 TYR A 13 0.13 SIDE CHAIN
REMARK 500 5 TYR A 13 0.16 SIDE CHAIN
REMARK 500 6 TYR A 13 0.17 SIDE CHAIN
REMARK 500 7 ARG A 11 0.14 SIDE CHAIN
REMARK 500 8 TYR A 13 0.13 SIDE CHAIN
REMARK 500 9 ARG A 11 0.09 SIDE CHAIN
REMARK 500 9 TYR A 13 0.14 SIDE CHAIN
REMARK 500 10 ARG A 11 0.08 SIDE CHAIN
REMARK 500 10 TYR A 13 0.15 SIDE CHAIN
REMARK 500 11 TYR A 13 0.10 SIDE CHAIN
REMARK 500 12 ARG A 11 0.09 SIDE CHAIN
REMARK 500 12 TYR A 13 0.16 SIDE CHAIN
REMARK 500 13 ARG A 11 0.08 SIDE CHAIN
REMARK 500 13 TYR A 13 0.15 SIDE CHAIN
REMARK 500 14 TYR A 13 0.10 SIDE CHAIN
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 NH2 A 25
DBREF 1AS5 A 1 24 UNP P56529 CXP3E_CONPU 3 26
SEQADV 1AS5 HYP A 2 UNP P56529 PRO 4 CONFLICT
SEQADV 1AS5 HYP A 3 UNP P56529 PRO 5 CONFLICT
SEQADV 1AS5 HYP A 14 UNP P56529 PRO 16 CONFLICT
SEQRES 1 A 25 HIS HYP HYP CYS CYS LEU TYR GLY LYS CYS ARG ARG TYR
SEQRES 2 A 25 HYP GLY CYS SER SER ALA SER CYS CYS GLN ARG NH2
MODRES 1AS5 HYP A 2 PRO 4-HYDROXYPROLINE
MODRES 1AS5 HYP A 3 PRO 4-HYDROXYPROLINE
MODRES 1AS5 HYP A 14 PRO 4-HYDROXYPROLINE
HET HYP A 2 15
HET HYP A 3 15
HET HYP A 14 15
HET NH2 A 25 3
HETNAM HYP 4-HYDROXYPROLINE
HETNAM NH2 AMINO GROUP
HETSYN HYP HYDROXYPROLINE
FORMUL 1 HYP 3(C5 H9 N O3)
FORMUL 1 NH2 H2 N
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.00
SSBOND 2 CYS A 5 CYS A 21 1555 1555 2.00
SSBOND 3 CYS A 10 CYS A 22 1555 1555 1.99
LINK C HIS A 1 N HYP A 2 1555 1555 1.40
LINK C HYP A 2 N HYP A 3 1555 1555 1.40
LINK C HYP A 3 N CYS A 4 1555 1555 1.37
LINK C TYR A 13 N HYP A 14 1555 1555 1.42
LINK C HYP A 14 N GLY A 15 1555 1555 1.33
LINK C ARG A 24 N NH2 A 25 1555 1555 1.33
SITE 1 AC1 1 ARG A 24
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