Header list of 1i8g.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE/ISOMERASE 14-MAR-01 1I8G
TITLE SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25
TITLE 2 PHOSPHOTHREONINE PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: M-PHASE INDUCER PHOSPHATASE 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 63-72;
COMPND 5 EC: 3.1.3.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: WW DOMAIN (RESIDUES 6-44);
COMPND 11 EC: 5.2.1.8;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE LIGAND PHOSPHOPEPTIDE WAS SYNTHESIZED FROM RINK
SOURCE 4 AMIDE RESIN USING THE FMOC STRATEGY AND ACTIVATION BY HBTU AND HOBT
SOURCE 5 IN A 431A PEPTIDE SYNTHESIZER. THE SEQUENCE OF THE PEPTIDE IS
SOURCE 6 NATURALLY FOUND IN XENOPUS LAEVIS (AFRICAN CLAWED FROG).;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: THE PIN1 WW DOMAIN WAS OBTAINED BY PEPTIDE SYNTHESIS
SOURCE 10 USING THE BOC-BENZYL STRATEGY AND THE HBTU IN SITU ACTIVATION
SOURCE 11 PROTOCOL ON AN APPLIED 430A PEPTIDE SYNTHESIZER. THE SEQUENCE OF THE
SOURCE 12 PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS CELL DIVISION, NUCLEAR PROTEIN, HYDROLASE-ISOMERASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR R.WINTJENS,J.-M.WIERUSZESKI,H.DROBECQ,G.LIPPENS,I.LANDRIEU
REVDAT 4 23-FEB-22 1I8G 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1I8G 1 VERSN
REVDAT 2 01-APR-03 1I8G 1 JRNL
REVDAT 1 18-JUL-01 1I8G 0
JRNL AUTH R.WINTJENS,J.M.WIERUSZESKI,H.DROBECQ,P.ROUSSELOT-PAILLEY,
JRNL AUTH 2 L.BUEE,G.LIPPENS,I.LANDRIEU
JRNL TITL 1H NMR STUDY ON THE BINDING OF PIN1 TRP-TRP DOMAIN WITH
JRNL TITL 2 PHOSPHOTHREONINE PEPTIDES.
JRNL REF J.BIOL.CHEM. V. 276 25150 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11313338
JRNL DOI 10.1074/JBC.M010327200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, DISCOVER 2.98
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), MOLECULAR SIMULATION INC.
REMARK 3 (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYBRID OF DISTANCE GEOMETRY / SIMULATED ANNEALING PROTOCOL
REMARK 3 MINIMIZATION PROCEDURE USING CVFF AS FORCE FIELD
REMARK 4
REMARK 4 1I8G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013035.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : SAMPLE OF 1MM WW DOMAIN / 4.5 MM
REMARK 210 CDC25 LIGAND BUFFER OF 50 MM
REMARK 210 DEUTERED TRIS-D2O, PH 6.4, 100
REMARK 210 MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 O1P TPO A 5 HG SER B 11 1.45
REMARK 500 O2P TPO A 5 HH21 ARG B 12 1.58
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 TRP B 6 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 1 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 TYR B 19 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 TYR B 19 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 HIS B 22 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 1 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 2 TRP B 6 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 2 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 2 HIS B 22 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 ARG B 31 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 2 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG B 31 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 TRP B 6 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 3 TRP B 6 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 ARG B 12 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 3 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 HIS B 22 ND1 - CE1 - NE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 3 ARG B 31 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 3 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 TRP B 6 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 4 TRP B 6 CD1 - NE1 - CE2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 4 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 4 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 4 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 HIS B 22 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 4 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 TRP B 6 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 5 TRP B 6 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 5 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 5 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 5 HIS B 22 ND1 - CE1 - NE2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 5 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ARG B 31 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 6 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 6 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 6 ARG B 12 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 6 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 HIS B 22 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 6 ARG B 31 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 TRP B 6 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 7 TRP B 6 CD1 - NE1 - CE2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 7 ARG B 9 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 ARG B 12 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 7 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 76 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 THR A 8 77.96 91.27
REMARK 500 1 ARG B 12 4.67 54.32
REMARK 500 1 SER B 13 -58.87 69.09
REMARK 500 1 ARG B 16 -122.45 -117.12
REMARK 500 1 ASN B 25 69.95 78.69
REMARK 500 1 PRO B 32 31.76 -67.50
REMARK 500 1 SER B 33 -34.09 73.07
REMARK 500 1 SER B 36 -140.68 -83.60
REMARK 500 2 LEU A 4 77.31 74.89
REMARK 500 2 VAL A 7 -138.92 -94.32
REMARK 500 2 ASP A 9 -113.83 -96.67
REMARK 500 2 LEU B 2 168.59 48.55
REMARK 500 2 SER B 11 -93.11 -76.49
REMARK 500 2 SER B 13 -74.54 69.95
REMARK 500 2 ASN B 25 69.43 79.31
REMARK 500 2 ARG B 31 123.99 -34.04
REMARK 500 2 SER B 33 -88.92 -151.89
REMARK 500 2 SER B 37 -68.21 65.63
REMARK 500 3 LEU B 2 175.83 -53.22
REMARK 500 3 SER B 11 -96.11 -112.86
REMARK 500 3 SER B 13 -81.18 64.99
REMARK 500 3 ASN B 25 73.10 81.81
REMARK 500 3 GLN B 28 -165.95 -123.08
REMARK 500 3 PRO B 32 26.87 -68.14
REMARK 500 3 SER B 33 -55.81 69.64
REMARK 500 3 SER B 38 68.67 64.10
REMARK 500 4 PRO A 3 -152.52 -88.29
REMARK 500 4 TPO A 5 72.98 -154.23
REMARK 500 4 THR A 8 110.04 73.54
REMARK 500 4 GLU B 7 -155.69 -150.73
REMARK 500 4 ARG B 12 -86.52 64.59
REMARK 500 4 SER B 13 89.68 -161.38
REMARK 500 4 ARG B 16 -134.14 -113.90
REMARK 500 4 ASN B 25 -35.79 162.59
REMARK 500 4 GLN B 28 -151.43 -143.57
REMARK 500 4 ARG B 31 133.98 99.06
REMARK 500 4 SER B 33 -75.38 -152.84
REMARK 500 4 ASN B 35 71.08 -106.84
REMARK 500 4 SER B 38 70.57 67.21
REMARK 500 5 VAL A 7 -140.24 -100.85
REMARK 500 5 LEU B 2 -174.59 46.13
REMARK 500 5 ARG B 9 -153.42 -101.54
REMARK 500 5 SER B 13 -63.96 69.12
REMARK 500 5 ARG B 16 -152.21 -112.86
REMARK 500 5 ASN B 25 67.10 76.27
REMARK 500 5 SER B 33 -87.20 -153.16
REMARK 500 5 SER B 36 -75.53 -88.62
REMARK 500 5 SER B 37 -31.03 71.15
REMARK 500 6 VAL A 7 -149.74 53.39
REMARK 500 6 THR A 8 30.58 -149.48
REMARK 500
REMARK 500 THIS ENTRY HAS 103 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 LEU A 4 TPO A 5 1 126.57
REMARK 500 ASP A 9 LEU A 10 1 149.71
REMARK 500 ARG B 12 SER B 13 1 -145.57
REMARK 500 GLY B 34 ASN B 35 1 138.61
REMARK 500 TRP B 6 GLU B 7 2 149.07
REMARK 500 GLU B 30 ARG B 31 2 149.88
REMARK 500 GLU A 1 GLN A 2 3 142.59
REMARK 500 LYS B 1 LEU B 2 3 147.81
REMARK 500 TRP B 6 GLU B 7 3 133.89
REMARK 500 SER B 37 SER B 38 3 -136.93
REMARK 500 VAL A 7 THR A 8 4 -148.65
REMARK 500 ASP A 9 LEU A 10 4 132.49
REMARK 500 TRP B 6 GLU B 7 4 144.30
REMARK 500 TRP B 29 GLU B 30 4 -144.06
REMARK 500 SER B 38 GLY B 39 4 -147.67
REMARK 500 TRP B 6 GLU B 7 5 140.48
REMARK 500 GLN A 2 PRO A 3 7 143.83
REMARK 500 TRP B 6 GLU B 7 7 139.62
REMARK 500 PRO B 32 SER B 33 7 -141.36
REMARK 500 SER B 38 GLY B 39 7 -143.37
REMARK 500 ASP A 9 LEU A 10 8 133.23
REMARK 500 TRP B 6 GLU B 7 8 148.75
REMARK 500 VAL B 17 TYR B 18 8 144.92
REMARK 500 SER B 38 GLY B 39 8 143.00
REMARK 500 PRO B 32 SER B 33 9 -126.84
REMARK 500 SER B 38 GLY B 39 9 136.22
REMARK 500 SER B 38 GLY B 39 10 -135.45
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 2 ARG B 9 0.17 SIDE CHAIN
REMARK 500 3 TYR B 19 0.07 SIDE CHAIN
REMARK 500 4 ARG B 12 0.11 SIDE CHAIN
REMARK 500 4 TYR B 19 0.07 SIDE CHAIN
REMARK 500 6 ARG B 12 0.07 SIDE CHAIN
REMARK 500 6 ARG B 31 0.10 SIDE CHAIN
REMARK 500 7 ARG B 31 0.15 SIDE CHAIN
REMARK 500 8 ARG B 12 0.09 SIDE CHAIN
REMARK 500 8 TYR B 19 0.14 SIDE CHAIN
REMARK 500 8 ARG B 31 0.13 SIDE CHAIN
REMARK 500 9 ARG B 31 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6C RELATED DB: PDB
REMARK 900 1I6C CONTAINS THE SAME PROTEIN IN A FREE (NOT COMPLEXED) FORM
REMARK 900 RELATED ID: 1I8H RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN TAU
REMARK 900 PHOSPHOTHREONINE PEPTIDE
DBREF 1I8G A 1 10 UNP P30311 MPIP3_XENLA 63 72
DBREF 1I8G B 1 39 UNP Q13526 PIN1_HUMAN 6 44
SEQADV 1I8G TPO A 5 UNP P30311 THR 67 MODIFIED RESIDUE
SEQRES 1 A 10 GLU GLN PRO LEU TPO PRO VAL THR ASP LEU
SEQRES 1 B 39 LYS LEU PRO PRO GLY TRP GLU LYS ARG MET SER ARG SER
SEQRES 2 B 39 SER GLY ARG VAL TYR TYR PHE ASN HIS ILE THR ASN ALA
SEQRES 3 B 39 SER GLN TRP GLU ARG PRO SER GLY ASN SER SER SER GLY
MODRES 1I8G TPO A 5 THR PHOSPHOTHREONINE
HET TPO A 5 17
HETNAM TPO PHOSPHOTHREONINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
SHEET 1 A 3 TRP B 6 MET B 10 0
SHEET 2 A 3 VAL B 17 ASN B 21 -1 O TYR B 18 N ARG B 9
SHEET 3 A 3 ALA B 26 GLN B 28 -1 O ALA B 26 N ASN B 21
LINK C LEU A 4 N TPO A 5 1555 1555 1.34
LINK C TPO A 5 N PRO A 6 1555 1555 1.37
CRYST1 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 - 23 20 Bytes