Header list of 1ti3.pdb file
Complete list - r 2 2 Bytes
HEADER OXIDOREDUCTASE 02-JUN-04 1TI3
TITLE SOLUTION STRUCTURE OF THE THIOREDOXIN H1 FROM POPLAR, A CPPC ACTIVE
TITLE 2 SITE VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOREDOXIN H;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PTTRXH1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: POPULUS TREMULA;
SOURCE 3 ORGANISM_TAXID: 113636
KEYWDS OXIDOREDUCTASE, THIOREDOXIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.COUDEVYLLE,A.THUREAU,C.HEMMERLIN,E.GELHAYE,J.P.JACQUOT,M.T.CUNG
REVDAT 3 02-MAR-22 1TI3 1 REMARK
REVDAT 2 24-FEB-09 1TI3 1 VERSN
REVDAT 1 14-DEC-04 1TI3 0
JRNL AUTH N.COUDEVYLLE,A.THUREAU,C.HEMMERLIN,E.GELHAYE,J.P.JACQUOT,
JRNL AUTH 2 M.T.CUNG
JRNL TITL SOLUTION STRUCTURE OF A NATURAL CPPC ACTIVE SITE VARIANT,
JRNL TITL 2 THE REDUCED FORM OF THIOREDOXIN H1 FROM POPLAR.
JRNL REF BIOCHEMISTRY V. 44 2001 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15697225
JRNL DOI 10.1021/BI047816N
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TI3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022655.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1.85 MM TRXH1, 50 MM PHOSPHATE
REMARK 210 BUFFER, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA
REMARK 210 METHOD USED : NULL
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: 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 1 GLU A 2 CD GLU A 2 OE2 0.175
REMARK 500 1 GLU A 3 CD GLU A 3 OE2 0.141
REMARK 500 1 HIS A 10 CG HIS A 10 CD2 0.066
REMARK 500 1 GLU A 17 CD GLU A 17 OE2 0.089
REMARK 500 1 HIS A 18 CG HIS A 18 CD2 0.083
REMARK 500 1 GLU A 20 CD GLU A 20 OE2 0.094
REMARK 500 1 ASP A 32 CG ASP A 32 OD2 0.159
REMARK 500 1 GLU A 50 CD GLU A 50 OE2 0.140
REMARK 500 1 GLU A 67 CD GLU A 67 OE2 0.146
REMARK 500 1 GLU A 73 CD GLU A 73 OE2 0.131
REMARK 500 1 GLU A 74 CD GLU A 74 OE2 0.125
REMARK 500 1 GLU A 78 CD GLU A 78 OE1 -0.076
REMARK 500 1 MET A 80 N MET A 80 CA 0.134
REMARK 500 1 MET A 80 C PRO A 81 N 0.122
REMARK 500 1 PRO A 81 CA PRO A 81 CB 0.117
REMARK 500 1 ASP A 88 CG ASP A 88 OD2 0.141
REMARK 500 1 ASP A 93 CG ASP A 93 OD2 0.152
REMARK 500 1 ASP A 99 CG ASP A 99 OD2 0.171
REMARK 500 1 HIS A 110 CG HIS A 110 CD2 0.063
REMARK 500 2 GLU A 2 CD GLU A 2 OE2 0.106
REMARK 500 2 GLU A 3 CD GLU A 3 OE2 0.140
REMARK 500 2 GLU A 17 CD GLU A 17 OE1 -0.087
REMARK 500 2 GLU A 17 CD GLU A 17 OE2 0.078
REMARK 500 2 GLU A 20 CD GLU A 20 OE2 0.120
REMARK 500 2 ASP A 66 CG ASP A 66 OD2 0.155
REMARK 500 2 GLU A 67 CD GLU A 67 OE2 0.103
REMARK 500 2 GLU A 73 CD GLU A 73 OE2 0.152
REMARK 500 2 GLU A 74 CD GLU A 74 OE2 0.137
REMARK 500 2 GLU A 78 CD GLU A 78 OE2 0.142
REMARK 500 2 ASP A 93 CG ASP A 93 OD2 0.139
REMARK 500 2 HIS A 110 CG HIS A 110 CD2 0.057
REMARK 500 2 ALA A 113 C ALA A 113 OXT 0.149
REMARK 500 3 GLU A 2 CD GLU A 2 OE2 0.167
REMARK 500 3 GLU A 3 CD GLU A 3 OE2 0.082
REMARK 500 3 HIS A 10 CG HIS A 10 CD2 0.112
REMARK 500 3 TRP A 15 CG TRP A 15 CD2 -0.103
REMARK 500 3 TRP A 15 CG TRP A 15 CD1 0.089
REMARK 500 3 GLU A 17 CD GLU A 17 OE2 0.086
REMARK 500 3 GLU A 20 CD GLU A 20 OE2 0.104
REMARK 500 3 GLU A 50 CD GLU A 50 OE2 0.142
REMARK 500 3 GLU A 67 CD GLU A 67 OE2 0.168
REMARK 500 3 GLU A 74 CD GLU A 74 OE2 0.094
REMARK 500 3 TRP A 75 CE2 TRP A 75 CD2 0.085
REMARK 500 3 GLU A 78 CD GLU A 78 OE2 0.093
REMARK 500 3 PRO A 81 CD PRO A 81 N -0.092
REMARK 500 3 ASP A 93 CG ASP A 93 OD2 0.165
REMARK 500 3 HIS A 110 CG HIS A 110 CD2 0.075
REMARK 500 4 GLU A 2 CD GLU A 2 OE2 0.143
REMARK 500 4 GLU A 3 CD GLU A 3 OE2 0.087
REMARK 500 4 GLU A 17 CD GLU A 17 OE2 0.102
REMARK 500
REMARK 500 THIS ENTRY HAS 319 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 PHE A 33 CB - CG - CD2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 1 LEU A 61 CB - CA - C ANGL. DEV. = 12.6 DEGREES
REMARK 500 1 ASP A 66 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 1 ASP A 66 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP A 75 CD1 - NE1 - CE2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 ASN A 76 N - CA - CB ANGL. DEV. = 12.2 DEGREES
REMARK 500 1 VAL A 77 CG1 - CB - CG2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 1 PRO A 81 CA - C - O ANGL. DEV. = 15.8 DEGREES
REMARK 500 1 PRO A 81 CA - C - N ANGL. DEV. = -14.6 DEGREES
REMARK 500 1 PHE A 83 CB - CG - CD1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 ILE A 84 CB - CA - C ANGL. DEV. = 14.5 DEGREES
REMARK 500 1 LEU A 86 CB - CG - CD1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 1 ASP A 88 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 ASP A 88 CB - CG - OD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 1 ASP A 93 CB - CG - OD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 1 ASP A 93 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 ALA A 98 N - CA - CB ANGL. DEV. = -10.7 DEGREES
REMARK 500 1 ASP A 99 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 1 LEU A 103 CB - CA - C ANGL. DEV. = 14.4 DEGREES
REMARK 500 1 HIS A 110 CG - ND1 - CE1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 1 HIS A 110 ND1 - CE1 - NE2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 2 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 ASP A 13 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 2 ASP A 13 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 2 TRP A 15 CD1 - NE1 - CE2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 2 HIS A 18 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 ASP A 32 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 2 ASP A 32 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 37 CD1 - NE1 - CE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 2 PHE A 55 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 2 PRO A 56 C - N - CA ANGL. DEV. = 12.0 DEGREES
REMARK 500 2 ASP A 66 CB - CG - OD1 ANGL. DEV. = 9.2 DEGREES
REMARK 500 2 ASP A 66 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 2 TRP A 75 NE1 - CE2 - CZ2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 2 ASN A 76 N - CA - CB ANGL. DEV. = 13.7 DEGREES
REMARK 500 2 MET A 80 CB - CA - C ANGL. DEV. = 14.4 DEGREES
REMARK 500 2 THR A 82 O - C - N ANGL. DEV. = 11.5 DEGREES
REMARK 500 2 PHE A 85 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 2 ASP A 88 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 ASP A 88 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 2 LYS A 90 CB - CA - C ANGL. DEV. = 13.6 DEGREES
REMARK 500 2 VAL A 92 CA - CB - CG2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 2 ASP A 99 CB - CG - OD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 2 ASP A 99 CB - CG - OD2 ANGL. DEV. = -12.3 DEGREES
REMARK 500 2 HIS A 110 ND1 - CE1 - NE2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 HIS A 10 ND1 - CE1 - NE2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 3 ASP A 13 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 3 THR A 14 CA - CB - CG2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 3 ASP A 32 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 3 THR A 34 CA - CB - CG2 ANGL. DEV. = 10.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 477 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 HIS A 10 -42.81 -141.55
REMARK 500 1 TRP A 37 90.73 -59.86
REMARK 500 1 CYS A 38 89.63 -175.52
REMARK 500 1 LEU A 68 54.35 -148.99
REMARK 500 1 ASN A 76 97.69 151.15
REMARK 500 1 VAL A 77 76.16 -154.38
REMARK 500 1 ASP A 88 49.01 -62.86
REMARK 500 1 LYS A 90 -167.11 56.18
REMARK 500 1 LEU A 91 101.25 -56.22
REMARK 500 2 HIS A 10 -20.91 -150.28
REMARK 500 2 GLN A 26 76.33 -64.03
REMARK 500 2 TRP A 37 69.73 -69.47
REMARK 500 2 CYS A 38 82.46 -156.63
REMARK 500 2 ASN A 57 3.64 -61.89
REMARK 500 2 LEU A 68 56.83 -143.03
REMARK 500 2 ASN A 76 81.72 151.29
REMARK 500 2 ASP A 88 56.30 -60.53
REMARK 500 2 LYS A 90 -167.79 68.86
REMARK 500 2 LEU A 91 107.24 -51.43
REMARK 500 2 ALA A 98 105.70 -161.97
REMARK 500 3 HIS A 10 -16.27 -151.87
REMARK 500 3 LYS A 23 88.70 -62.36
REMARK 500 3 GLN A 26 82.23 -60.54
REMARK 500 3 TRP A 37 75.43 -61.39
REMARK 500 3 CYS A 38 84.44 -163.95
REMARK 500 3 ASN A 57 0.03 -57.49
REMARK 500 3 LEU A 68 57.21 -148.69
REMARK 500 3 ASN A 76 83.98 149.69
REMARK 500 3 ASP A 88 16.54 -52.68
REMARK 500 3 LYS A 90 -171.75 63.27
REMARK 500 3 LEU A 91 105.78 -56.42
REMARK 500 3 ASP A 99 130.41 -173.34
REMARK 500 3 ALA A 111 -29.60 -39.60
REMARK 500 3 THR A 112 -84.44 -71.87
REMARK 500 4 HIS A 10 -22.65 -148.11
REMARK 500 4 VAL A 12 -19.11 -49.34
REMARK 500 4 GLN A 26 77.01 -62.49
REMARK 500 4 TRP A 37 88.53 -56.43
REMARK 500 4 CYS A 38 105.49 -165.50
REMARK 500 4 LEU A 68 50.39 -154.64
REMARK 500 4 ASN A 76 93.81 143.06
REMARK 500 4 ASP A 88 52.62 -57.47
REMARK 500 4 LYS A 90 -167.71 56.74
REMARK 500 4 LEU A 91 100.35 -58.06
REMARK 500 4 ALA A 98 101.83 -166.57
REMARK 500 5 HIS A 10 -11.98 -150.13
REMARK 500 5 GLU A 17 -70.34 -57.57
REMARK 500 5 LYS A 23 96.50 -65.73
REMARK 500 5 GLN A 26 78.09 -67.86
REMARK 500 5 CYS A 38 92.62 -166.04
REMARK 500
REMARK 500 THIS ENTRY HAS 212 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 CYS A 9 HIS A 10 1 -147.72
REMARK 500 SER A 36 TRP A 37 1 143.45
REMARK 500 VAL A 77 GLU A 78 1 148.00
REMARK 500 ASN A 57 VAL A 58 2 -149.52
REMARK 500 TRP A 75 ASN A 76 2 148.40
REMARK 500 VAL A 77 GLU A 78 2 138.58
REMARK 500 PRO A 81 THR A 82 2 -144.62
REMARK 500 TRP A 75 ASN A 76 3 148.22
REMARK 500 PRO A 81 THR A 82 3 -147.77
REMARK 500 PRO A 81 THR A 82 4 -148.72
REMARK 500 LYS A 87 ASP A 88 4 145.78
REMARK 500 ASN A 57 VAL A 58 5 -145.43
REMARK 500 PRO A 81 THR A 82 5 -147.04
REMARK 500 LYS A 54 PHE A 55 6 -147.02
REMARK 500 PRO A 81 THR A 82 6 -140.22
REMARK 500 LYS A 87 ASP A 88 6 148.19
REMARK 500 ASN A 57 VAL A 58 7 -148.16
REMARK 500 VAL A 58 THR A 59 7 149.90
REMARK 500 TRP A 75 ASN A 76 7 146.65
REMARK 500 VAL A 77 GLU A 78 7 148.18
REMARK 500 PRO A 81 THR A 82 7 -142.60
REMARK 500 ASN A 57 VAL A 58 8 -142.75
REMARK 500 VAL A 77 GLU A 78 8 149.53
REMARK 500 VAL A 63 ASP A 64 9 148.86
REMARK 500 TRP A 75 ASN A 76 9 147.07
REMARK 500 PRO A 81 THR A 82 9 -136.84
REMARK 500 LYS A 87 ASP A 88 9 143.83
REMARK 500 ALA A 79 MET A 80 10 143.95
REMARK 500 LYS A 87 ASP A 88 10 147.07
REMARK 500 VAL A 77 GLU A 78 11 146.36
REMARK 500 PRO A 81 THR A 82 11 -141.02
REMARK 500 CYS A 9 HIS A 10 12 -149.56
REMARK 500 VAL A 31 ASP A 32 12 149.60
REMARK 500 TRP A 75 ASN A 76 12 148.85
REMARK 500 VAL A 77 GLU A 78 12 148.46
REMARK 500 PRO A 81 THR A 82 12 -140.42
REMARK 500 PRO A 81 THR A 82 13 -137.55
REMARK 500 TRP A 75 ASN A 76 14 149.38
REMARK 500 PRO A 81 THR A 82 14 -136.91
REMARK 500 VAL A 77 GLU A 78 15 140.36
REMARK 500 PRO A 81 THR A 82 15 -142.68
REMARK 500 PRO A 81 THR A 82 16 -130.15
REMARK 500 VAL A 77 GLU A 78 17 143.94
REMARK 500 PRO A 81 THR A 82 17 -147.06
REMARK 500 LYS A 27 LEU A 28 18 148.86
REMARK 500 VAL A 77 GLU A 78 18 149.96
REMARK 500 ALA A 79 MET A 80 18 149.41
REMARK 500 PRO A 81 THR A 82 18 -140.76
REMARK 500 ASN A 57 VAL A 58 19 -148.99
REMARK 500 VAL A 63 ASP A 64 19 146.86
REMARK 500
REMARK 500 THIS ENTRY HAS 54 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 HIS A 110 0.10 SIDE CHAIN
REMARK 500 2 PHE A 19 0.08 SIDE CHAIN
REMARK 500 2 PHE A 33 0.06 SIDE CHAIN
REMARK 500 2 PHE A 48 0.07 SIDE CHAIN
REMARK 500 2 PHE A 55 0.08 SIDE CHAIN
REMARK 500 2 GLU A 78 0.08 SIDE CHAIN
REMARK 500 2 PHE A 83 0.07 SIDE CHAIN
REMARK 500 2 HIS A 110 0.16 SIDE CHAIN
REMARK 500 3 PHE A 48 0.07 SIDE CHAIN
REMARK 500 4 HIS A 10 0.10 SIDE CHAIN
REMARK 500 4 PHE A 33 0.09 SIDE CHAIN
REMARK 500 4 HIS A 110 0.14 SIDE CHAIN
REMARK 500 5 PHE A 48 0.14 SIDE CHAIN
REMARK 500 6 HIS A 10 0.11 SIDE CHAIN
REMARK 500 6 PHE A 48 0.12 SIDE CHAIN
REMARK 500 6 HIS A 110 0.14 SIDE CHAIN
REMARK 500 7 PHE A 48 0.08 SIDE CHAIN
REMARK 500 8 PHE A 48 0.12 SIDE CHAIN
REMARK 500 8 PHE A 85 0.09 SIDE CHAIN
REMARK 500 9 PHE A 48 0.10 SIDE CHAIN
REMARK 500 10 HIS A 18 0.07 SIDE CHAIN
REMARK 500 10 PHE A 19 0.09 SIDE CHAIN
REMARK 500 10 PHE A 83 0.09 SIDE CHAIN
REMARK 500 11 HIS A 110 0.15 SIDE CHAIN
REMARK 500 12 HIS A 18 0.06 SIDE CHAIN
REMARK 500 12 PHE A 83 0.08 SIDE CHAIN
REMARK 500 12 HIS A 110 0.17 SIDE CHAIN
REMARK 500 13 HIS A 110 0.16 SIDE CHAIN
REMARK 500 15 PHE A 48 0.11 SIDE CHAIN
REMARK 500 15 PHE A 83 0.07 SIDE CHAIN
REMARK 500 16 PHE A 48 0.08 SIDE CHAIN
REMARK 500 16 PHE A 83 0.08 SIDE CHAIN
REMARK 500 17 PHE A 48 0.08 SIDE CHAIN
REMARK 500 18 PHE A 48 0.11 SIDE CHAIN
REMARK 500 18 HIS A 110 0.12 SIDE CHAIN
REMARK 500 19 HIS A 110 0.10 SIDE CHAIN
REMARK 500 20 PHE A 85 0.07 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 4 ASN A 57 10.66
REMARK 500 8 LYS A 54 10.12
REMARK 500 8 PRO A 81 12.90
REMARK 500 12 VAL A 77 -12.11
REMARK 500 13 ALA A 35 10.45
REMARK 500 13 GLU A 74 -11.59
REMARK 500 14 GLY A 4 -10.68
REMARK 500 14 MET A 80 -15.32
REMARK 500 16 MET A 80 -16.19
REMARK 500 16 PRO A 81 11.18
REMARK 500 16 ALA A 98 -11.47
REMARK 500 17 VAL A 77 -13.48
REMARK 500 18 VAL A 71 -10.15
REMARK 500 19 PRO A 81 11.00
REMARK 500 20 THR A 82 -12.06
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TI3 A 1 113 UNP Q8S3L3 Q8S3L3_9ROSI 2 114
SEQRES 1 A 113 ALA GLU GLU GLY GLN VAL ILE ALA CYS HIS THR VAL ASP
SEQRES 2 A 113 THR TRP LYS GLU HIS PHE GLU LYS GLY LYS GLY SER GLN
SEQRES 3 A 113 LYS LEU ILE VAL VAL ASP PHE THR ALA SER TRP CYS PRO
SEQRES 4 A 113 PRO CYS LYS MET ILE ALA PRO ILE PHE ALA GLU LEU ALA
SEQRES 5 A 113 LYS LYS PHE PRO ASN VAL THR PHE LEU LYS VAL ASP VAL
SEQRES 6 A 113 ASP GLU LEU LYS ALA VAL ALA GLU GLU TRP ASN VAL GLU
SEQRES 7 A 113 ALA MET PRO THR PHE ILE PHE LEU LYS ASP GLY LYS LEU
SEQRES 8 A 113 VAL ASP LYS THR VAL GLY ALA ASP LYS ASP GLY LEU PRO
SEQRES 9 A 113 THR LEU VAL ALA LYS HIS ALA THR ALA
HELIX 1 1 THR A 11 LYS A 23 1 13
HELIX 2 2 CYS A 38 PHE A 55 1 18
HELIX 3 3 LEU A 68 VAL A 77 1 10
HELIX 4 4 ASP A 101 ALA A 113 1 13
SHEET 1 A 5 VAL A 6 CYS A 9 0
SHEET 2 A 5 VAL A 58 ASP A 64 1 O ASP A 64 N CYS A 9
SHEET 3 A 5 LEU A 28 THR A 34 1 N ASP A 32 O VAL A 63
SHEET 4 A 5 THR A 82 LYS A 87 -1 O ILE A 84 N VAL A 31
SHEET 5 A 5 LYS A 90 VAL A 96 -1 O THR A 95 N PHE A 83
CISPEP 1 MET A 80 PRO A 81 1 1.26
CISPEP 2 MET A 80 PRO A 81 2 -1.23
CISPEP 3 MET A 80 PRO A 81 3 -8.75
CISPEP 4 MET A 80 PRO A 81 4 -12.51
CISPEP 5 MET A 80 PRO A 81 5 -4.55
CISPEP 6 MET A 80 PRO A 81 6 -4.35
CISPEP 7 MET A 80 PRO A 81 7 -3.58
CISPEP 8 MET A 80 PRO A 81 8 -12.61
CISPEP 9 MET A 80 PRO A 81 9 -4.50
CISPEP 10 MET A 80 PRO A 81 10 -5.16
CISPEP 11 MET A 80 PRO A 81 11 5.08
CISPEP 12 MET A 80 PRO A 81 12 -15.63
CISPEP 13 MET A 80 PRO A 81 13 -17.85
CISPEP 14 MET A 80 PRO A 81 14 -18.90
CISPEP 15 MET A 80 PRO A 81 15 3.30
CISPEP 16 MET A 80 PRO A 81 16 -21.07
CISPEP 17 MET A 80 PRO A 81 17 -1.01
CISPEP 18 MET A 80 PRO A 81 18 -8.05
CISPEP 19 MET A 80 PRO A 81 19 3.07
CISPEP 20 MET A 80 PRO A 81 20 0.68
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 - r 2 2 Bytes