Header list of 1c2u.pdb file
Complete list - 3 20 Bytes
HEADER TOXIN 27-JUL-99 1C2U
TITLE SOLUTION STRUCTURE OF [ABU3,35]SHK12-28,17-32
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNTHETIC PEPTIDE ANALOGUE OF SHK TOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PEPTIDE IS NATURALLY FOUND IN STICHODACTYLA HELIANTHUS.
KEYWDS SHK TOXIN, POTASSIUM CHANNEL, DISULPHIDE BONDS, ANALOGUES, STRUCTURE-
KEYWDS 2 FUNCTION, SOLUTION STRUCTURE, TOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.W.PENNINGTON,M.D.LANIGAN,K.KALMAN,V.M.MANHIR,H.RAUER,C.T.MCVAUGH,
AUTHOR 2 D.BEHM,D.DONALDSON,K.G.CHANDY,W.R.KEM,R.S.NORTON
REVDAT 4 03-NOV-21 1C2U 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1C2U 1 VERSN
REVDAT 2 01-APR-03 1C2U 1 JRNL
REVDAT 1 10-NOV-99 1C2U 0
JRNL AUTH M.W.PENNINGTON,M.D.LANIGAN,K.KALMAN,V.M.MAHNIR,H.RAUER,
JRNL AUTH 2 C.T.MCVAUGH,D.BEHM,D.DONALDSON,K.G.CHANDY,W.R.KEM,R.S.NORTON
JRNL TITL ROLE OF DISULFIDE BONDS IN THE STRUCTURE AND POTASSIUM
JRNL TITL 2 CHANNEL BLOCKING ACTIVITY OF SHK TOXIN.
JRNL REF BIOCHEMISTRY V. 38 14549 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10545177
JRNL DOI 10.1021/BI991282M
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, X-PLOR 1.3, CHARMM 19
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR), BROOKS
REMARK 3 (CHARMM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 328 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS AND 26 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1C2U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000009409.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293.0
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 5.6 MM PEPTIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 5.6 MM [ABU3,35]SHK12-28,17-32;
REMARK 210 90% H2O, 10% D2O (V/V)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D-TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3.7, DYANA 1.4
REMARK 210 METHOD USED : THE STRUCTURES WERE REFINED
REMARK 210 USING DISTANCE GEOMETRY,
REMARK 210 SIMULATED ANNEALING AND
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 2 HIS A 19 NE2 HIS A 19 CD2 -0.068
REMARK 500 3 HIS A 19 NE2 HIS A 19 CD2 -0.068
REMARK 500 4 HIS A 19 NE2 HIS A 19 CD2 -0.071
REMARK 500 5 HIS A 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 6 HIS A 19 NE2 HIS A 19 CD2 -0.071
REMARK 500 7 HIS A 19 NE2 HIS A 19 CD2 -0.069
REMARK 500 8 HIS A 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 9 HIS A 19 NE2 HIS A 19 CD2 -0.071
REMARK 500 10 HIS A 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 11 HIS A 19 NE2 HIS A 19 CD2 -0.068
REMARK 500 12 HIS A 19 NE2 HIS A 19 CD2 -0.069
REMARK 500 13 HIS A 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 14 HIS A 19 NE2 HIS A 19 CD2 -0.072
REMARK 500 15 HIS A 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 16 HIS A 19 NE2 HIS A 19 CD2 -0.071
REMARK 500 17 HIS A 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 18 HIS A 19 NE2 HIS A 19 CD2 -0.070
REMARK 500 19 HIS A 19 NE2 HIS A 19 CD2 -0.069
REMARK 500 20 HIS A 19 NE2 HIS A 19 CD2 -0.073
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 11 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 1 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 1 ARG A 29 NH1 - CZ - NH2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 1 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 2 CYS A 32 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 3 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 4 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 4 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 5 ARG A 1 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 5 ARG A 24 NH1 - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 5 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 5 CYS A 28 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 6 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 7 ARG A 11 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 7 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 7 CYS A 28 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 7 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 8 CYS A 28 CA - CB - SG ANGL. DEV. = 7.5 DEGREES
REMARK 500 8 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 9 ARG A 1 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 9 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 9 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 10 ARG A 24 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 10 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 11 ARG A 1 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 11 ARG A 11 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 11 CYS A 28 CA - CB - SG ANGL. DEV. = 10.6 DEGREES
REMARK 500 11 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 12 ARG A 11 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 12 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 12 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 13 ARG A 1 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 13 ARG A 11 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 13 CYS A 28 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 13 ARG A 29 NH1 - CZ - NH2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 13 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 13 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 14 ARG A 11 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 14 CYS A 28 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 14 ARG A 29 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 15 ARG A 24 NH1 - CZ - NH2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 15 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 15 CYS A 28 CA - CB - SG ANGL. DEV. = 11.3 DEGREES
REMARK 500 15 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 16 ARG A 24 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 16 CYS A 28 CA - CB - SG ANGL. DEV. = 9.6 DEGREES
REMARK 500 16 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 17 ARG A 11 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 65 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 ABA A 3 170.67 -52.00
REMARK 500 1 ASP A 5 -126.03 -146.29
REMARK 500 1 THR A 6 -24.84 -33.41
REMARK 500 1 PRO A 8 66.54 -40.34
REMARK 500 1 LYS A 9 66.02 -18.80
REMARK 500 1 SER A 10 -101.67 -144.14
REMARK 500 1 GLN A 16 -66.97 -151.50
REMARK 500 1 CYS A 17 -44.56 -29.57
REMARK 500 1 LYS A 18 71.22 -172.21
REMARK 500 1 HIS A 19 -84.44 -29.56
REMARK 500 1 ALA A 21 -12.47 179.72
REMARK 500 1 LEU A 25 -79.06 -90.78
REMARK 500 1 SER A 26 -43.81 178.71
REMARK 500 1 PHE A 27 -64.50 -159.77
REMARK 500 1 ARG A 29 -89.62 -176.55
REMARK 500 2 SER A 2 -165.49 -121.31
REMARK 500 2 ABA A 3 -166.44 -101.09
REMARK 500 2 ILE A 4 -120.80 -111.39
REMARK 500 2 PRO A 8 83.58 -57.48
REMARK 500 2 SER A 10 -123.10 -121.39
REMARK 500 2 GLN A 16 -52.03 -158.30
REMARK 500 2 CYS A 17 -55.74 -29.86
REMARK 500 2 LYS A 18 77.87 -168.61
REMARK 500 2 HIS A 19 -87.84 -29.92
REMARK 500 2 SER A 20 77.00 -68.24
REMARK 500 2 ALA A 21 -12.80 179.80
REMARK 500 2 LEU A 25 -74.07 -91.50
REMARK 500 2 SER A 26 -50.85 178.01
REMARK 500 2 PHE A 27 -63.28 -161.08
REMARK 500 2 ARG A 29 -56.40 -166.91
REMARK 500 2 LYS A 30 -79.22 -66.25
REMARK 500 2 THR A 34 -75.04 -100.83
REMARK 500 3 ABA A 3 155.53 -47.55
REMARK 500 3 ILE A 4 -92.45 -113.30
REMARK 500 3 ASP A 5 -105.58 -120.19
REMARK 500 3 THR A 6 1.25 -56.76
REMARK 500 3 LYS A 9 73.02 -68.55
REMARK 500 3 SER A 10 -109.52 -147.79
REMARK 500 3 GLN A 16 -60.28 -157.34
REMARK 500 3 LYS A 18 75.21 -174.05
REMARK 500 3 HIS A 19 -94.21 -28.80
REMARK 500 3 SER A 20 34.71 -69.17
REMARK 500 3 SER A 26 -67.56 177.85
REMARK 500 3 PHE A 27 -52.11 -157.09
REMARK 500 3 ARG A 29 -88.54 -167.75
REMARK 500 3 THR A 34 -78.41 -102.27
REMARK 500 4 SER A 2 -150.53 -70.79
REMARK 500 4 ILE A 4 -120.96 -114.65
REMARK 500 4 THR A 6 -121.78 -100.80
REMARK 500 4 SER A 10 -107.87 -119.88
REMARK 500
REMARK 500 THIS ENTRY HAS 300 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 1 0.30 SIDE CHAIN
REMARK 500 1 ARG A 11 0.28 SIDE CHAIN
REMARK 500 1 ARG A 24 0.32 SIDE CHAIN
REMARK 500 1 ARG A 29 0.27 SIDE CHAIN
REMARK 500 2 ARG A 1 0.32 SIDE CHAIN
REMARK 500 2 ARG A 24 0.32 SIDE CHAIN
REMARK 500 2 ARG A 29 0.29 SIDE CHAIN
REMARK 500 3 ARG A 1 0.32 SIDE CHAIN
REMARK 500 3 ARG A 11 0.32 SIDE CHAIN
REMARK 500 3 ARG A 24 0.32 SIDE CHAIN
REMARK 500 3 ARG A 29 0.31 SIDE CHAIN
REMARK 500 4 ARG A 1 0.27 SIDE CHAIN
REMARK 500 4 ARG A 11 0.32 SIDE CHAIN
REMARK 500 4 ARG A 24 0.30 SIDE CHAIN
REMARK 500 4 ARG A 29 0.24 SIDE CHAIN
REMARK 500 5 ARG A 1 0.32 SIDE CHAIN
REMARK 500 5 ARG A 11 0.31 SIDE CHAIN
REMARK 500 5 ARG A 24 0.32 SIDE CHAIN
REMARK 500 5 ARG A 29 0.31 SIDE CHAIN
REMARK 500 6 ARG A 1 0.32 SIDE CHAIN
REMARK 500 6 ARG A 11 0.30 SIDE CHAIN
REMARK 500 6 ARG A 24 0.19 SIDE CHAIN
REMARK 500 6 ARG A 29 0.27 SIDE CHAIN
REMARK 500 7 ARG A 1 0.32 SIDE CHAIN
REMARK 500 7 ARG A 11 0.31 SIDE CHAIN
REMARK 500 7 ARG A 24 0.32 SIDE CHAIN
REMARK 500 7 ARG A 29 0.32 SIDE CHAIN
REMARK 500 8 ARG A 1 0.28 SIDE CHAIN
REMARK 500 8 ARG A 11 0.30 SIDE CHAIN
REMARK 500 8 ARG A 24 0.18 SIDE CHAIN
REMARK 500 8 ARG A 29 0.32 SIDE CHAIN
REMARK 500 9 ARG A 1 0.33 SIDE CHAIN
REMARK 500 9 ARG A 11 0.31 SIDE CHAIN
REMARK 500 9 ARG A 24 0.28 SIDE CHAIN
REMARK 500 9 ARG A 29 0.25 SIDE CHAIN
REMARK 500 10 ARG A 1 0.32 SIDE CHAIN
REMARK 500 10 ARG A 11 0.29 SIDE CHAIN
REMARK 500 10 ARG A 24 0.30 SIDE CHAIN
REMARK 500 10 ARG A 29 0.30 SIDE CHAIN
REMARK 500 11 ARG A 1 0.32 SIDE CHAIN
REMARK 500 11 ARG A 11 0.31 SIDE CHAIN
REMARK 500 11 ARG A 24 0.12 SIDE CHAIN
REMARK 500 11 ARG A 29 0.31 SIDE CHAIN
REMARK 500 12 ARG A 1 0.32 SIDE CHAIN
REMARK 500 12 ARG A 11 0.32 SIDE CHAIN
REMARK 500 12 ARG A 24 0.32 SIDE CHAIN
REMARK 500 12 ARG A 29 0.32 SIDE CHAIN
REMARK 500 13 ARG A 1 0.32 SIDE CHAIN
REMARK 500 13 ARG A 11 0.32 SIDE CHAIN
REMARK 500 13 ARG A 29 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1C2U A 1 35 UNP P29187 TXSHK_STOHE 1 35
SEQADV 1C2U ABA A 3 UNP P29187 CYS 3 ENGINEERED MUTATION
SEQADV 1C2U ALA A 21 UNP P29187 MET 21 ENGINEERED MUTATION
SEQADV 1C2U ABA A 35 UNP P29187 CYS 35 ENGINEERED MUTATION
SEQRES 1 A 35 ARG SER ABA ILE ASP THR ILE PRO LYS SER ARG CYS THR
SEQRES 2 A 35 ALA PHE GLN CYS LYS HIS SER ALA LYS TYR ARG LEU SER
SEQRES 3 A 35 PHE CYS ARG LYS THR CYS GLY THR ABA
MODRES 1C2U ABA A 3 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 1C2U ABA A 35 ALA ALPHA-AMINOBUTYRIC ACID
HET ABA A 3 13
HET ABA A 35 14
HETNAM ABA ALPHA-AMINOBUTYRIC ACID
FORMUL 1 ABA 2(C4 H9 N O2)
SSBOND 1 CYS A 12 CYS A 28 1555 1555 2.03
SSBOND 2 CYS A 17 CYS A 32 1555 1555 2.01
LINK C SER A 2 N ABA A 3 1555 1555 1.31
LINK C ABA A 3 N ILE A 4 1555 1555 1.31
LINK C THR A 34 N ABA A 35 1555 1555 1.31
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 - 3 20 Bytes