Header list of 1p4s.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 24-APR-03 1P4S
TITLE SOLUTION STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ADENYLATE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ATP-AMP TRANSPHOSPHORYLASE;
COMPND 5 EC: 2.7.4.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: ADK OR RV0733 OR MT0757 OR MTV041.07;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BLI5/PHL20;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.MIRON,H.MUNIER-LEHMANN,C.T.CRAESCU
REVDAT 3 23-FEB-22 1P4S 1 REMARK
REVDAT 2 24-FEB-09 1P4S 1 VERSN
REVDAT 1 20-JAN-04 1P4S 0
JRNL AUTH S.MIRON,H.MUNIER-LEHMANN,C.T.CRAESCU
JRNL TITL STRUCTURAL AND DYNAMIC STUDIES ON LIGAND-FREE ADENYLATE
JRNL TITL 2 KINASE FROM MYCOBACTERIUM TUBERCULOSIS REVEALED A CLOSED
JRNL TITL 3 CONFORMATION THAT CAN BE RELATED TO THE REDUCED CATALYTIC
JRNL TITL 4 ACTIVITY.
JRNL REF BIOCHEMISTRY V. 43 67 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 14705932
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INSIGHT II
REMARK 3 AUTHORS : MSI
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A 1809 ARE NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 191 DIHEDRAL ANGLE RESTRAINTS,159 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1P4S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000019006.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1.2 MM ADENYLATE KINASE 15N,
REMARK 210 13C, 50MM POTASSIUM PHOSPHATE
REMARK 210 BUFFER PH 7.1; 1.0 MM ADENYLATE
REMARK 210 KINASE 50MM POTASSIUM PHOSPHATE
REMARK 210 BUFFER PH 7.1; 1.2 MM ADENYLATE
REMARK 210 KINASE 50MM POTASSIUM PHOSPHATE
REMARK 210 BUFFER PH 7.1; 1.2 MM ADENYLATE
REMARK 210 KINASE 15N, 50MM POTASSIUM
REMARK 210 PHOSPHATE BUFFER PH 7.1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, TOCSY, COSY; 3D 15N
REMARK 210 NOESY-HSQC, TOCSY-HSQC; 3D 15N,
REMARK 210 13C HNCA, HNCOCA, HNCACB,
REMARK 210 HNCOCACB, HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING PROTOCOL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 RESTRAINT VIOLATIONS AND LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12
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 HA LEU A 120 HB2 ARG A 123 1.16
REMARK 500 O GLU A 98 HB3 ARG A 102 1.20
REMARK 500 O MET A 99 HB3 ARG A 103 1.33
REMARK 500 O LEU A 152 HB2 ARG A 156 1.35
REMARK 500 C ARG A 123 H LEU A 124 1.40
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 3 HIS A 97 CG HIS A 97 CD2 0.056
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 2 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 1 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 VAL A 47 CA - CB - CG1 ANGL. DEV. = 13.4 DEGREES
REMARK 500 1 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 51 CA - C - O ANGL. DEV. = -34.2 DEGREES
REMARK 500 1 ARG A 51 O - C - N ANGL. DEV. = -13.9 DEGREES
REMARK 500 1 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ASN A 74 N - CA - C ANGL. DEV. = 16.8 DEGREES
REMARK 500 1 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 HIS A 97 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 VAL A 119 CA - CB - CG2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 1 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 LEU A 124 C - N - CA ANGL. DEV. = 18.5 DEGREES
REMARK 500 1 LEU A 124 N - CA - C ANGL. DEV. = 18.6 DEGREES
REMARK 500 1 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 174 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 177 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 2 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 ARG A 36 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 VAL A 47 CA - CB - CG1 ANGL. DEV. = 12.6 DEGREES
REMARK 500 2 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 51 CA - C - O ANGL. DEV. = -33.9 DEGREES
REMARK 500 2 ARG A 51 O - C - N ANGL. DEV. = -13.4 DEGREES
REMARK 500 2 TYR A 52 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 2 TYR A 52 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 2 ARG A 71 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 HIS A 97 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 123 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 129 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 145 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 LEU A 152 CA - CB - CG ANGL. DEV. = 17.3 DEGREES
REMARK 500 2 TYR A 154 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 2 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 174 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 504 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 11 -46.27 -27.29
REMARK 500 1 LYS A 13 -78.09 -172.47
REMARK 500 1 LYS A 44 -41.49 105.84
REMARK 500 1 TYR A 52 -66.22 -27.64
REMARK 500 1 ASN A 74 -28.11 -32.26
REMARK 500 1 PHE A 81 138.93 -176.18
REMARK 500 1 PRO A 87 70.97 -68.79
REMARK 500 1 ASP A 108 -77.04 -100.25
REMARK 500 1 ARG A 123 47.74 -25.15
REMARK 500 1 LEU A 124 27.13 36.04
REMARK 500 1 ARG A 127 110.51 153.30
REMARK 500 1 ARG A 129 -157.25 -146.24
REMARK 500 1 ALA A 130 56.92 -149.88
REMARK 500 1 THR A 133 -165.72 -57.14
REMARK 500 1 ASP A 134 -62.45 70.64
REMARK 500 1 MET A 168 -65.31 -91.39
REMARK 500 1 LEU A 179 -60.03 -102.29
REMARK 500 2 LYS A 13 -92.94 64.80
REMARK 500 2 THR A 43 -65.62 -92.16
REMARK 500 2 LYS A 44 -55.68 128.81
REMARK 500 2 ASN A 73 8.64 -66.81
REMARK 500 2 PHE A 81 135.76 178.58
REMARK 500 2 PRO A 87 70.87 -65.30
REMARK 500 2 ASP A 108 -68.04 -90.33
REMARK 500 2 ARG A 127 -115.61 -150.13
REMARK 500 2 ARG A 129 128.16 158.01
REMARK 500 2 ASP A 132 57.90 -91.54
REMARK 500 2 THR A 133 -118.33 -129.32
REMARK 500 2 GLU A 147 26.73 -140.34
REMARK 500 3 ALA A 11 -80.49 -72.13
REMARK 500 3 LYS A 13 -84.71 153.56
REMARK 500 3 THR A 43 125.29 49.45
REMARK 500 3 LYS A 44 -24.12 -142.46
REMARK 500 3 TYR A 52 -62.23 -28.28
REMARK 500 3 PHE A 81 132.53 -172.63
REMARK 500 3 PRO A 87 72.64 -67.53
REMARK 500 3 ASP A 108 -65.58 -97.76
REMARK 500 3 ARG A 127 -94.92 -149.12
REMARK 500 3 ALA A 130 45.87 -95.10
REMARK 500 3 THR A 133 -79.50 -5.35
REMARK 500 4 LYS A 13 -74.87 170.56
REMARK 500 4 LYS A 44 -40.52 105.87
REMARK 500 4 ASP A 62 -46.12 81.89
REMARK 500 4 ASN A 73 23.43 -75.80
REMARK 500 4 PHE A 81 135.32 -178.39
REMARK 500 4 PRO A 87 70.70 -66.13
REMARK 500 4 ASP A 108 -76.23 -96.50
REMARK 500 4 ARG A 129 112.03 -164.40
REMARK 500 4 ASP A 132 62.00 -116.62
REMARK 500 4 THR A 133 -109.79 -140.45
REMARK 500
REMARK 500 THIS ENTRY HAS 316 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 ARG A 51 TYR A 52 1 146.00
REMARK 500 ARG A 51 TYR A 52 2 149.35
REMARK 500 THR A 43 LYS A 44 3 146.13
REMARK 500 ARG A 51 TYR A 52 3 147.99
REMARK 500 ARG A 51 TYR A 52 4 146.73
REMARK 500 ARG A 51 TYR A 52 5 148.90
REMARK 500 ARG A 51 TYR A 52 6 146.51
REMARK 500 ARG A 51 TYR A 52 7 146.49
REMARK 500 ARG A 51 TYR A 52 9 146.86
REMARK 500 ARG A 51 TYR A 52 10 147.87
REMARK 500 ARG A 51 TYR A 52 11 146.74
REMARK 500 ARG A 51 TYR A 52 12 146.54
REMARK 500 ASN A 73 ASN A 74 12 146.57
REMARK 500 ASN A 74 PRO A 75 12 149.52
REMARK 500 ARG A 51 TYR A 52 13 145.85
REMARK 500 ARG A 51 TYR A 52 14 144.03
REMARK 500 LYS A 160 THR A 161 14 149.51
REMARK 500 ASP A 163 ALA A 164 14 -147.66
REMARK 500 ARG A 51 TYR A 52 15 147.87
REMARK 500 ARG A 51 TYR A 52 16 146.22
REMARK 500 ARG A 51 TYR A 52 17 145.52
REMARK 500 LYS A 160 THR A 161 17 149.93
REMARK 500 ARG A 51 TYR A 52 18 147.21
REMARK 500 LYS A 160 THR A 161 18 -146.10
REMARK 500 THR A 161 VAL A 162 18 -146.69
REMARK 500 VAL A 165 GLY A 166 18 -149.19
REMARK 500 ARG A 51 TYR A 52 19 145.22
REMARK 500 ARG A 51 TYR A 52 20 146.10
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 154 0.07 SIDE CHAIN
REMARK 500 1 TYR A 155 0.08 SIDE CHAIN
REMARK 500 2 ARG A 2 0.09 SIDE CHAIN
REMARK 500 2 TYR A 52 0.08 SIDE CHAIN
REMARK 500 2 TYR A 154 0.10 SIDE CHAIN
REMARK 500 2 TYR A 155 0.08 SIDE CHAIN
REMARK 500 3 TYR A 154 0.11 SIDE CHAIN
REMARK 500 3 TYR A 155 0.08 SIDE CHAIN
REMARK 500 4 TYR A 154 0.09 SIDE CHAIN
REMARK 500 4 TYR A 155 0.08 SIDE CHAIN
REMARK 500 5 TYR A 52 0.12 SIDE CHAIN
REMARK 500 5 TYR A 86 0.07 SIDE CHAIN
REMARK 500 5 TYR A 154 0.09 SIDE CHAIN
REMARK 500 6 TYR A 155 0.07 SIDE CHAIN
REMARK 500 7 PHE A 35 0.08 SIDE CHAIN
REMARK 500 7 TYR A 154 0.07 SIDE CHAIN
REMARK 500 7 TYR A 155 0.11 SIDE CHAIN
REMARK 500 8 TYR A 154 0.07 SIDE CHAIN
REMARK 500 9 TYR A 86 0.08 SIDE CHAIN
REMARK 500 9 ARG A 88 0.08 SIDE CHAIN
REMARK 500 9 TYR A 155 0.09 SIDE CHAIN
REMARK 500 10 TYR A 155 0.09 SIDE CHAIN
REMARK 500 11 TYR A 154 0.11 SIDE CHAIN
REMARK 500 11 TYR A 155 0.10 SIDE CHAIN
REMARK 500 12 TYR A 154 0.10 SIDE CHAIN
REMARK 500 12 TYR A 155 0.10 SIDE CHAIN
REMARK 500 14 TYR A 155 0.09 SIDE CHAIN
REMARK 500 15 TYR A 154 0.08 SIDE CHAIN
REMARK 500 15 TYR A 155 0.11 SIDE CHAIN
REMARK 500 16 TYR A 154 0.08 SIDE CHAIN
REMARK 500 16 TYR A 155 0.12 SIDE CHAIN
REMARK 500 17 TYR A 155 0.13 SIDE CHAIN
REMARK 500 18 TYR A 154 0.08 SIDE CHAIN
REMARK 500 18 TYR A 155 0.10 SIDE CHAIN
REMARK 500 19 TYR A 155 0.09 SIDE CHAIN
REMARK 500 20 TYR A 155 0.10 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 ARG A 51 46.21
REMARK 500 2 ARG A 51 46.09
REMARK 500 3 ARG A 51 47.42
REMARK 500 4 ARG A 51 46.26
REMARK 500 5 ARG A 51 49.92
REMARK 500 6 ARG A 51 44.21
REMARK 500 7 ARG A 51 45.97
REMARK 500 8 ARG A 51 -41.92
REMARK 500 9 ARG A 51 45.91
REMARK 500 10 ARG A 51 48.31
REMARK 500 11 ARG A 51 46.73
REMARK 500 12 ARG A 51 46.52
REMARK 500 13 ARG A 51 47.97
REMARK 500 14 LYS A 23 -19.85
REMARK 500 14 ARG A 51 45.13
REMARK 500 15 ARG A 51 45.47
REMARK 500 16 ARG A 51 44.98
REMARK 500 17 ARG A 51 45.10
REMARK 500 17 LYS A 160 11.50
REMARK 500 18 ARG A 51 46.50
REMARK 500 18 THR A 161 17.37
REMARK 500 19 ARG A 51 46.58
REMARK 500 20 ARG A 51 46.23
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1P4S A 1 181 UNP P69440 KAD_MYCTU 1 181
SEQRES 1 A 181 MET ARG VAL LEU LEU LEU GLY PRO PRO GLY ALA GLY LYS
SEQRES 2 A 181 GLY THR GLN ALA VAL LYS LEU ALA GLU LYS LEU GLY ILE
SEQRES 3 A 181 PRO GLN ILE SER THR GLY GLU LEU PHE ARG ARG ASN ILE
SEQRES 4 A 181 GLU GLU GLY THR LYS LEU GLY VAL GLU ALA LYS ARG TYR
SEQRES 5 A 181 LEU ASP ALA GLY ASP LEU VAL PRO SER ASP LEU THR ASN
SEQRES 6 A 181 GLU LEU VAL ASP ASP ARG LEU ASN ASN PRO ASP ALA ALA
SEQRES 7 A 181 ASN GLY PHE ILE LEU ASP GLY TYR PRO ARG SER VAL GLU
SEQRES 8 A 181 GLN ALA LYS ALA LEU HIS GLU MET LEU GLU ARG ARG GLY
SEQRES 9 A 181 THR ASP ILE ASP ALA VAL LEU GLU PHE ARG VAL SER GLU
SEQRES 10 A 181 GLU VAL LEU LEU GLU ARG LEU LYS GLY ARG GLY ARG ALA
SEQRES 11 A 181 ASP ASP THR ASP ASP VAL ILE LEU ASN ARG MET LYS VAL
SEQRES 12 A 181 TYR ARG ASP GLU THR ALA PRO LEU LEU GLU TYR TYR ARG
SEQRES 13 A 181 ASP GLN LEU LYS THR VAL ASP ALA VAL GLY THR MET ASP
SEQRES 14 A 181 GLU VAL PHE ALA ARG ALA LEU ARG ALA LEU GLY LYS
HELIX 1 1 LYS A 13 GLY A 25 1 13
HELIX 2 2 GLY A 32 GLY A 42 1 11
HELIX 3 3 LYS A 44 ASP A 54 1 11
HELIX 4 4 PRO A 60 ASN A 73 1 14
HELIX 5 5 SER A 89 GLU A 101 1 13
HELIX 6 6 GLU A 117 ARG A 123 1 7
HELIX 7 7 ASP A 134 LEU A 159 1 26
HELIX 8 8 MET A 168 LEU A 179 1 12
SHEET 1 A 5 GLN A 28 SER A 30 0
SHEET 2 A 5 ILE A 82 ASP A 84 1 O ILE A 82 N ILE A 29
SHEET 3 A 5 VAL A 3 LEU A 6 1 N VAL A 3 O LEU A 83
SHEET 4 A 5 ALA A 109 ARG A 114 1 O LEU A 111 N LEU A 4
SHEET 5 A 5 LYS A 160 ASP A 163 1 O VAL A 162 N ARG A 114
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