Header list of 1q7x.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 20-AUG-03 1Q7X
TITLE SOLUTION STRUCTURE OF THE ALTERNATIVELY SPLICED PDZ2 DOMAIN (PDZ2B) OF
TITLE 2 PTP-BAS (HPTP1E)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PDZ2B DOMAIN OF PTP-BAS (HPTP1E);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PTP1E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C600;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX2T
KEYWDS PHOSPHATASE, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS 2 GENOMICS, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.KACHEL,K.S.ERDMANN,W.KREMER,P.WOLFF,W.GRONWALD,R.HEUMANN,
AUTHOR 2 H.R.KALBITZER,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 02-MAR-22 1Q7X 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1Q7X 1 VERSN
REVDAT 1 02-DEC-03 1Q7X 0
JRNL AUTH N.KACHEL,K.S.ERDMANN,W.KREMER,P.WOLFF,W.GRONWALD,R.HEUMANN,
JRNL AUTH 2 H.R.KALBITZER
JRNL TITL STRUCTURE DETERMINATION AND LIGAND INTERACTIONS OF THE PDZ2B
JRNL TITL 2 DOMAIN OF PTP-BAS (HPTP1E): SPLICING INDUCED MODULATION OF
JRNL TITL 3 LIGAND SPECIFICITY.
JRNL REF J.MOL.BIOL. V. 334 143 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14596806
JRNL DOI 10.1016/J.JMB.2003.09.026
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1648 NOE
REMARK 3 -DERIVED DISTANCE RESTRAINTS AND 80 TORSION ANGLE RESTRAINTS
REMARK 3 ACQUIRED BY TALOS
REMARK 4
REMARK 4 1Q7X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000020028.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE, 150MM
REMARK 210 SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PDZ2B U-15N, 13C; 50MM
REMARK 210 PHOSPHATE BUFFER WITH 150MM
REMARK 210 SODIUM CHLORIDE; 2MM PDZ2B U-15N;
REMARK 210 50MM PHOSPHATE BUFFER WITH
REMARK 210 150MM SODIUM CHLORIDE; 2MM PDZ2B
REMARK 210 UNLABELED; 50MM PHOSPHATE BUFFER
REMARK 210 WITH 150MM SODIUM CHLORIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, AUREMOL 1.1, CNS
REMARK 210 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 H VAL A 46 H GLY A 64 1.30
REMARK 500 O ALA A 69 HD23 LEU A 96 1.48
REMARK 500 O LYS A 81 HB2 GLU A 85 1.49
REMARK 500 H VAL A 70 O VAL A 73 1.51
REMARK 500 O PHE A 11 H LEU A 98 1.53
REMARK 500 O GLY A 23 H ILE A 50 1.58
REMARK 500 O LEU A 22 N ALA A 55 2.14
REMARK 500 O THR A 79 N LYS A 81 2.15
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 PHE A 30 CB PHE A 30 CG -0.128
REMARK 500 2 PHE A 30 CB PHE A 30 CG -0.128
REMARK 500 3 PHE A 30 CB PHE A 30 CG -0.128
REMARK 500 4 PHE A 30 CB PHE A 30 CG -0.110
REMARK 500 5 PHE A 30 CB PHE A 30 CG -0.112
REMARK 500 6 PHE A 30 CB PHE A 30 CG -0.112
REMARK 500 7 PHE A 30 CB PHE A 30 CG -0.127
REMARK 500 8 PHE A 30 CB PHE A 30 CG -0.112
REMARK 500 9 PHE A 30 CB PHE A 30 CG -0.111
REMARK 500 10 PHE A 30 CB PHE A 30 CG -0.110
REMARK 500 11 PHE A 30 CB PHE A 30 CG -0.126
REMARK 500 12 PHE A 30 CB PHE A 30 CG -0.111
REMARK 500 13 PHE A 30 CB PHE A 30 CG -0.128
REMARK 500 14 PHE A 30 CB PHE A 30 CG -0.112
REMARK 500 15 PHE A 30 CB PHE A 30 CG -0.112
REMARK 500 16 PHE A 30 CB PHE A 30 CG -0.111
REMARK 500 17 PHE A 30 CB PHE A 30 CG -0.111
REMARK 500 18 PHE A 30 CB PHE A 30 CG -0.112
REMARK 500 19 PHE A 30 CB PHE A 30 CG -0.126
REMARK 500 20 PHE A 30 CB PHE A 30 CG -0.111
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 4 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 4 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 5 PHE A 30 CB - CG - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 5 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 6 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 6 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 8 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 8 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 9 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 9 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 10 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 10 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 12 PHE A 30 CB - CG - CD2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 12 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 14 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 14 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 15 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 15 PHE A 30 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 16 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 16 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 17 PHE A 30 CB - CG - CD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 17 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 18 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 18 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 20 PHE A 30 CB - CG - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 20 PHE A 30 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
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 ASP A 9 -138.81 174.85
REMARK 500 1 LYS A 17 91.26 -41.35
REMARK 500 1 ASN A 18 -58.06 -135.87
REMARK 500 1 SER A 21 35.28 -166.12
REMARK 500 1 LEU A 22 179.57 167.41
REMARK 500 1 LYS A 32 43.89 179.32
REMARK 500 1 VAL A 35 -140.52 160.35
REMARK 500 1 ASN A 36 22.80 -144.60
REMARK 500 1 THR A 37 -54.68 -1.71
REMARK 500 1 SER A 38 54.98 178.02
REMARK 500 1 HIS A 41 -31.45 -138.83
REMARK 500 1 ALA A 48 -143.25 82.55
REMARK 500 1 ILE A 50 163.42 -43.90
REMARK 500 1 ALA A 54 -112.87 46.11
REMARK 500 1 ARG A 60 57.15 -119.74
REMARK 500 1 HIS A 62 108.91 132.10
REMARK 500 1 ASP A 65 -168.71 -174.07
REMARK 500 1 ASN A 71 15.72 49.09
REMARK 500 1 GLU A 76 37.46 -92.65
REMARK 500 1 THR A 79 -100.14 22.93
REMARK 500 1 HIS A 80 -79.97 18.05
REMARK 500 1 THR A 90 158.15 -40.03
REMARK 500 1 VAL A 93 108.82 171.76
REMARK 500 1 GLN A 102 -171.16 -57.58
REMARK 500 1 SER A 103 -69.23 -136.94
REMARK 500 1 THR A 105 -170.23 -61.78
REMARK 500 1 LYS A 107 -46.44 -139.92
REMARK 500 2 SER A 2 120.30 62.78
REMARK 500 2 PRO A 7 176.81 -59.07
REMARK 500 2 ASP A 9 -141.15 173.28
REMARK 500 2 LYS A 17 91.32 -41.86
REMARK 500 2 ASN A 18 -56.96 -136.65
REMARK 500 2 SER A 21 36.81 -168.68
REMARK 500 2 LEU A 22 179.29 166.79
REMARK 500 2 LYS A 32 40.33 -146.93
REMARK 500 2 VAL A 35 -154.42 160.60
REMARK 500 2 ASN A 36 23.52 -141.70
REMARK 500 2 THR A 37 -55.06 1.40
REMARK 500 2 SER A 38 37.31 -176.49
REMARK 500 2 VAL A 39 -150.54 -132.39
REMARK 500 2 ALA A 48 -143.75 81.61
REMARK 500 2 ILE A 50 161.32 -41.29
REMARK 500 2 ALA A 54 -110.74 40.03
REMARK 500 2 HIS A 62 104.91 128.88
REMARK 500 2 ASP A 65 -168.24 -174.08
REMARK 500 2 ASN A 71 17.74 43.64
REMARK 500 2 GLU A 76 34.50 -93.02
REMARK 500 2 THR A 79 -99.52 20.41
REMARK 500 2 HIS A 80 -79.91 17.78
REMARK 500 2 THR A 90 176.57 -46.21
REMARK 500
REMARK 500 THIS ENTRY HAS 560 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2 RELATED DB: TARGETDB
DBREF 1Q7X A 1 108 UNP Q12923 PTN13_HUMAN 1357 1464
SEQADV 1Q7X GLY A 1 UNP Q12923 SER 1357 CLONING ARTIFACT
SEQRES 1 A 108 GLY SER SER PRO PRO LYS PRO GLY ASP ILE PHE GLU VAL
SEQRES 2 A 108 GLU LEU ALA LYS ASN ASP ASN SER LEU GLY ILE SER VAL
SEQRES 3 A 108 THR VAL LEU PHE ASP LYS GLY GLY VAL ASN THR SER VAL
SEQRES 4 A 108 ARG HIS GLY GLY ILE TYR VAL LYS ALA VAL ILE PRO GLN
SEQRES 5 A 108 GLY ALA ALA GLU SER ASP GLY ARG ILE HIS LYS GLY ASP
SEQRES 6 A 108 ARG VAL LEU ALA VAL ASN GLY VAL SER LEU GLU GLY ALA
SEQRES 7 A 108 THR HIS LYS GLN ALA VAL GLU THR LEU ARG ASN THR GLY
SEQRES 8 A 108 GLN VAL VAL HIS LEU LEU LEU GLU LYS GLY GLN SER PRO
SEQRES 9 A 108 THR SER LYS GLU
HELIX 1 1 ALA A 54 GLY A 59 1 6
HELIX 2 2 LYS A 81 THR A 90 1 10
SHEET 1 A 4 ILE A 10 ALA A 16 0
SHEET 2 A 4 VAL A 93 GLU A 99 -1 O LEU A 98 N PHE A 11
SHEET 3 A 4 ARG A 66 VAL A 70 -1 N ALA A 69 O LEU A 97
SHEET 4 A 4 VAL A 73 SER A 74 -1 O VAL A 73 N VAL A 70
SHEET 1 B 2 ILE A 24 VAL A 26 0
SHEET 2 B 2 VAL A 46 VAL A 49 -1 O LYS A 47 N SER A 25
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