Header list of 1u5s.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 28-JUL-04 1U5S
TITLE NMR STRUCTURE OF THE COMPLEX BETWEEN NCK-2 SH3 DOMAIN AND PINCH-1 LIM4
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOPLASMIC PROTEIN NCK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIRD SH3 DOMAIN (RESIDUES 192-262);
COMPND 5 SYNONYM: NCK ADAPTOR PROTEIN 2, SH2/SH3 ADAPTOR PROTEIN NCK-BETA,
COMPND 6 NCK-2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PINCH PROTEIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: FOURTH LIM DOMAIN (RESIDUES 188-251);
COMPND 12 SYNONYM: PARTICULARLY INTERESTING NEW CYS-HIS PROTEIN, LIM AND
COMPND 13 SENESCENT CELL ANTIGEN-LIKE DOMAINS 1;
COMPND 14 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: NCK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTYB11;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: LIMS1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS PROTEIN-PROTEIN COMPLEX, BETA BARREL, BETA SHEET, ZINC FINGER, METAL
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR J.VAYNBERG,T.FUKUDA,O.VINOGRADOVA,A.VELYVIS,L.NG,C.WU,J.QIN
REVDAT 3 02-MAR-22 1U5S 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1U5S 1 VERSN
REVDAT 1 05-APR-05 1U5S 0
JRNL AUTH J.VAYNBERG,T.FUKUDA,K.CHEN,O.VINOGRADOVA,A.VELYVIS,Y.TU,
JRNL AUTH 2 L.NG,C.WU,J.QIN
JRNL TITL STRUCTURE OF AN ULTRAWEAK PROTEIN-PROTEIN COMPLEX AND ITS
JRNL TITL 2 CRUCIAL ROLE IN REGULATION OF CELL MORPHOLOGY AND MOTILITY.
JRNL REF MOL.CELL V. 17 513 2005
JRNL REFN ISSN 1097-2765
JRNL PMID 15721255
JRNL DOI 10.1016/J.MOLCEL.2004.12.031
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR, XPLOR-NIH
REMARK 3 AUTHORS : CLORE (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U5S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000023280.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0MM LIM4 OF PINCH-1 U-15N,13C,
REMARK 210 1.5MM SH3-3 OF NCK-2 UNLABELED,
REMARK 210 25MM PHOSPHATE BUFFER, 100MM
REMARK 210 NACL, 0.1MM TCEP, 90% H2O, 10%
REMARK 210 D2O; 0.6MM SH3-3 OF NCK-2 U-15N,
REMARK 210 13C, 2.5MM LIM4 OF PINCH-1, 25MM
REMARK 210 PHOSPHATE BUFFER, 100MM NACL,
REMARK 210 0.1MM TCEP, 90% H2O, 10% D2O;
REMARK 210 1.3MM SH3-3 OF NCK-2 U-15N,13C,
REMARK 210 25MM PHOSPHATE BUFFER, 100MM
REMARK 210 NACL, 0.1MM TCEP, 90% H2O, 10%
REMARK 210 D2O; 1.7MM LIM4 OF PINCH-1, U-
REMARK 210 15N,13C 25MM PHOSPHATE BUFFER,
REMARK 210 100MM NACL, 0.1MM TCEP, 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 15N/13C-EDITED
REMARK 210 15N,13C-SEPARATED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, X-PLOR 3.1, XPLOR-NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, RIGID BODY/TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE MOST
REMARK 210 REPERESENTATIVE SIDE CHAINS
REMARK 210 ORIENTATIONS ON THE COMPLEX
REMARK 210 INTERFACE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURES OF FREE FORM SH3 AND LIM4 DOMAINS WERE
REMARK 210 DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-18
REMARK 470 RES CSSEQI ATOMS
REMARK 470 HIS A 71 O
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 ASN A 48 O GLN A 52 1.19
REMARK 500 OD1 ASN A 59 HH21 ARG B 83 1.33
REMARK 500 O GLU A 38 H ASP A 40 1.42
REMARK 500 O THR B 128 H GLN B 132 1.44
REMARK 500 O ASN A 48 H GLY A 51 1.48
REMARK 500 O GLU B 127 HD21 ASN B 131 1.51
REMARK 500 H ALA B 106 O ALA B 124 1.54
REMARK 500 O GLU A 21 H LEU A 55 1.56
REMARK 500 O PRO B 77 H ILE B 86 1.60
REMARK 500 N ASN A 48 O GLN A 52 2.18
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 B 112 CA PHE B 112 CB 0.609
REMARK 500 1 PHE B 112 CB PHE B 112 CG 0.611
REMARK 500 1 VAL B 137 C VAL B 137 O -0.753
REMARK 500 2 PHE B 112 CA PHE B 112 CB 0.610
REMARK 500 2 PHE B 112 CB PHE B 112 CG 0.612
REMARK 500 2 VAL B 137 C VAL B 137 O -0.756
REMARK 500 3 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 3 PHE B 112 CB PHE B 112 CG 0.612
REMARK 500 3 VAL B 137 C VAL B 137 O -0.754
REMARK 500 4 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 4 PHE B 112 CB PHE B 112 CG 0.612
REMARK 500 4 VAL B 137 C VAL B 137 O -0.756
REMARK 500 5 PHE B 112 CA PHE B 112 CB 0.611
REMARK 500 5 PHE B 112 CB PHE B 112 CG 0.611
REMARK 500 5 VAL B 137 C VAL B 137 O -0.755
REMARK 500 6 PHE B 112 CA PHE B 112 CB 0.608
REMARK 500 6 PHE B 112 CB PHE B 112 CG 0.612
REMARK 500 6 VAL B 137 C VAL B 137 O -0.755
REMARK 500 7 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 7 PHE B 112 CB PHE B 112 CG 0.611
REMARK 500 7 VAL B 137 C VAL B 137 O -0.755
REMARK 500 8 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 8 PHE B 112 CB PHE B 112 CG 0.612
REMARK 500 8 VAL B 137 C VAL B 137 O -0.754
REMARK 500 9 PHE B 112 CA PHE B 112 CB 0.610
REMARK 500 9 PHE B 112 CB PHE B 112 CG 0.613
REMARK 500 9 VAL B 137 C VAL B 137 O -0.756
REMARK 500 10 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 10 PHE B 112 CB PHE B 112 CG 0.613
REMARK 500 10 VAL B 137 C VAL B 137 O -0.755
REMARK 500 11 PHE B 112 CA PHE B 112 CB 0.608
REMARK 500 11 PHE B 112 CB PHE B 112 CG 0.610
REMARK 500 11 VAL B 137 C VAL B 137 O -0.754
REMARK 500 12 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 12 PHE B 112 CB PHE B 112 CG 0.611
REMARK 500 12 VAL B 137 C VAL B 137 O -0.755
REMARK 500 13 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 13 PHE B 112 CB PHE B 112 CG 0.612
REMARK 500 13 VAL B 137 C VAL B 137 O -0.753
REMARK 500 14 PHE B 112 CA PHE B 112 CB 0.610
REMARK 500 14 PHE B 112 CB PHE B 112 CG 0.613
REMARK 500 14 VAL B 137 C VAL B 137 O -0.755
REMARK 500 15 PHE B 112 CA PHE B 112 CB 0.608
REMARK 500 15 PHE B 112 CB PHE B 112 CG 0.611
REMARK 500 15 VAL B 137 C VAL B 137 O -0.755
REMARK 500 16 PHE B 112 CA PHE B 112 CB 0.608
REMARK 500 16 PHE B 112 CB PHE B 112 CG 0.611
REMARK 500 16 VAL B 137 C VAL B 137 O -0.755
REMARK 500 17 PHE B 112 CA PHE B 112 CB 0.609
REMARK 500 17 PHE B 112 CB PHE B 112 CG 0.611
REMARK 500
REMARK 500 THIS ENTRY HAS 54 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 B 112 N - CA - CB ANGL. DEV. = 24.3 DEGREES
REMARK 500 1 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 1 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.1 DEGREES
REMARK 500 1 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.8 DEGREES
REMARK 500 1 VAL B 137 CA - C - O ANGL. DEV. = -49.2 DEGREES
REMARK 500 2 PHE B 112 N - CA - CB ANGL. DEV. = 24.3 DEGREES
REMARK 500 2 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 2 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.1 DEGREES
REMARK 500 2 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.8 DEGREES
REMARK 500 2 VAL B 137 CA - C - O ANGL. DEV. = -49.1 DEGREES
REMARK 500 3 PHE B 112 N - CA - CB ANGL. DEV. = 24.4 DEGREES
REMARK 500 3 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 3 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.1 DEGREES
REMARK 500 3 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.7 DEGREES
REMARK 500 3 VAL B 137 CA - C - O ANGL. DEV. = -49.1 DEGREES
REMARK 500 4 PHE B 112 N - CA - CB ANGL. DEV. = 24.3 DEGREES
REMARK 500 4 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 4 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.0 DEGREES
REMARK 500 4 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.7 DEGREES
REMARK 500 4 VAL B 137 CA - C - O ANGL. DEV. = -49.0 DEGREES
REMARK 500 5 PHE B 112 N - CA - CB ANGL. DEV. = 24.4 DEGREES
REMARK 500 5 PHE B 112 CA - CB - CG ANGL. DEV. = -42.9 DEGREES
REMARK 500 5 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.0 DEGREES
REMARK 500 5 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.8 DEGREES
REMARK 500 5 VAL B 137 CA - C - O ANGL. DEV. = -49.2 DEGREES
REMARK 500 6 PHE B 112 N - CA - CB ANGL. DEV. = 24.3 DEGREES
REMARK 500 6 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 6 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.1 DEGREES
REMARK 500 6 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.7 DEGREES
REMARK 500 6 VAL B 137 CA - C - O ANGL. DEV. = -49.3 DEGREES
REMARK 500 7 PHE B 112 N - CA - CB ANGL. DEV. = 24.3 DEGREES
REMARK 500 7 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 7 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.1 DEGREES
REMARK 500 7 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.8 DEGREES
REMARK 500 7 VAL B 137 CA - C - O ANGL. DEV. = -49.3 DEGREES
REMARK 500 8 PHE B 112 N - CA - CB ANGL. DEV. = 24.4 DEGREES
REMARK 500 8 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 8 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.0 DEGREES
REMARK 500 8 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.8 DEGREES
REMARK 500 8 VAL B 137 CA - C - O ANGL. DEV. = -49.0 DEGREES
REMARK 500 9 PHE B 112 N - CA - CB ANGL. DEV. = 24.4 DEGREES
REMARK 500 9 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 9 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.1 DEGREES
REMARK 500 9 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.7 DEGREES
REMARK 500 9 VAL B 137 CA - C - O ANGL. DEV. = -49.3 DEGREES
REMARK 500 10 PHE B 112 N - CA - CB ANGL. DEV. = 24.4 DEGREES
REMARK 500 10 PHE B 112 CA - CB - CG ANGL. DEV. = -42.8 DEGREES
REMARK 500 10 PHE B 112 CB - CG - CD2 ANGL. DEV. = -28.1 DEGREES
REMARK 500 10 PHE B 112 CB - CG - CD1 ANGL. DEV. = 24.7 DEGREES
REMARK 500 10 VAL B 137 CA - C - O ANGL. DEV. = -49.1 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 90 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 SER A 3 35.34 -162.06
REMARK 500 1 VAL A 5 93.43 -66.08
REMARK 500 1 LEU A 6 -54.26 -121.20
REMARK 500 1 THR A 19 -151.98 -144.51
REMARK 500 1 VAL A 33 92.29 -62.92
REMARK 500 1 ASN A 39 -59.45 57.69
REMARK 500 1 ASP A 40 -47.32 165.75
REMARK 500 1 GLU A 42 9.17 131.83
REMARK 500 1 LYS A 58 3.17 -60.52
REMARK 500 1 LEU A 64 -63.14 -105.12
REMARK 500 1 PRO A 68 93.11 -59.42
REMARK 500 1 MET B 74 167.83 -49.81
REMARK 500 1 GLU B 87 61.53 -160.59
REMARK 500 1 MET B 94 17.34 57.99
REMARK 500 1 LYS B 96 -154.71 -130.16
REMARK 500 1 LYS B 107 -31.75 -138.77
REMARK 500 1 GLU B 109 47.60 71.65
REMARK 500 1 PHE B 112 57.03 -95.80
REMARK 500 1 CYS B 126 177.60 -57.53
REMARK 500 1 PHE B 134 -81.57 -158.62
REMARK 500 2 SER A 3 35.30 -162.04
REMARK 500 2 VAL A 5 93.47 -66.07
REMARK 500 2 LEU A 6 -54.42 -121.19
REMARK 500 2 THR A 19 -151.98 -144.54
REMARK 500 2 VAL A 33 92.32 -63.15
REMARK 500 2 ASN A 39 -59.33 57.52
REMARK 500 2 ASP A 40 -47.36 165.78
REMARK 500 2 GLU A 42 9.34 131.75
REMARK 500 2 LYS A 58 3.20 -60.38
REMARK 500 2 LEU A 64 -63.07 -105.13
REMARK 500 2 PRO A 68 93.22 -59.42
REMARK 500 2 MET B 74 167.89 -49.77
REMARK 500 2 GLU B 87 61.41 -160.53
REMARK 500 2 MET B 94 17.26 58.11
REMARK 500 2 LYS B 96 -154.76 -130.23
REMARK 500 2 LYS B 107 -31.78 -138.74
REMARK 500 2 GLU B 109 47.50 71.79
REMARK 500 2 PHE B 112 56.97 -95.84
REMARK 500 2 CYS B 126 177.50 -57.57
REMARK 500 2 PHE B 134 -81.63 -158.59
REMARK 500 3 SER A 3 35.31 -161.99
REMARK 500 3 VAL A 5 93.40 -66.08
REMARK 500 3 LEU A 6 -54.28 -121.25
REMARK 500 3 THR A 19 -152.09 -144.49
REMARK 500 3 VAL A 33 92.26 -63.10
REMARK 500 3 ASN A 39 -59.40 57.67
REMARK 500 3 ASP A 40 -47.48 165.77
REMARK 500 3 GLU A 42 9.24 131.87
REMARK 500 3 LYS A 58 3.31 -60.46
REMARK 500 3 LEU A 64 -63.18 -105.09
REMARK 500
REMARK 500 THIS ENTRY HAS 360 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 PHE B 112 0.08 SIDE CHAIN
REMARK 500 2 PHE B 112 0.08 SIDE CHAIN
REMARK 500 3 PHE B 112 0.08 SIDE CHAIN
REMARK 500 4 PHE B 112 0.08 SIDE CHAIN
REMARK 500 5 PHE B 112 0.08 SIDE CHAIN
REMARK 500 6 PHE B 112 0.08 SIDE CHAIN
REMARK 500 7 PHE B 112 0.08 SIDE CHAIN
REMARK 500 8 PHE B 112 0.08 SIDE CHAIN
REMARK 500 9 PHE B 112 0.08 SIDE CHAIN
REMARK 500 10 PHE B 112 0.08 SIDE CHAIN
REMARK 500 11 PHE B 112 0.08 SIDE CHAIN
REMARK 500 12 PHE B 112 0.08 SIDE CHAIN
REMARK 500 13 PHE B 112 0.08 SIDE CHAIN
REMARK 500 14 PHE B 112 0.08 SIDE CHAIN
REMARK 500 15 PHE B 112 0.08 SIDE CHAIN
REMARK 500 16 PHE B 112 0.08 SIDE CHAIN
REMARK 500 17 PHE B 112 0.08 SIDE CHAIN
REMARK 500 18 PHE B 112 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 138 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 79 SG
REMARK 620 2 CYS B 82 SG 109.6
REMARK 620 3 HIS B 99 ND1 104.8 107.9
REMARK 620 4 HIS B 102 ND1 123.1 106.4 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 139 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 105 SG
REMARK 620 2 CYS B 108 SG 104.5
REMARK 620 3 CYS B 126 SG 117.0 92.2
REMARK 620 4 HIS B 129 ND1 117.8 96.9 119.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 138
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 139
DBREF 1U5S A 1 71 UNP O43639 NCK2_HUMAN 192 262
DBREF 1U5S B 74 137 UNP P48059 PINC_HUMAN 188 251
SEQADV 1U5S GLY B 72 UNP P48059 CLONING ARTIFACT
SEQADV 1U5S SER B 73 UNP P48059 CLONING ARTIFACT
SEQRES 1 A 71 GLN GLY SER ARG VAL LEU HIS VAL VAL GLN THR LEU TYR
SEQRES 2 A 71 PRO PHE SER SER VAL THR GLU GLU GLU LEU ASN PHE GLU
SEQRES 3 A 71 LYS GLY GLU THR MET GLU VAL ILE GLU LYS PRO GLU ASN
SEQRES 4 A 71 ASP PRO GLU TRP TRP LYS CYS LYS ASN ALA ARG GLY GLN
SEQRES 5 A 71 VAL GLY LEU VAL PRO LYS ASN TYR VAL VAL VAL LEU SER
SEQRES 6 A 71 ASP GLY PRO ALA LEU HIS
SEQRES 1 B 66 GLY SER MET GLY VAL PRO ILE CYS GLY ALA CYS ARG ARG
SEQRES 2 B 66 PRO ILE GLU GLY ARG VAL VAL ASN ALA MET GLY LYS GLN
SEQRES 3 B 66 TRP HIS VAL GLU HIS PHE VAL CYS ALA LYS CYS GLU LYS
SEQRES 4 B 66 PRO PHE LEU GLY HIS ARG HIS TYR GLU ARG LYS GLY LEU
SEQRES 5 B 66 ALA TYR CYS GLU THR HIS TYR ASN GLN LEU PHE GLY ASP
SEQRES 6 B 66 VAL
HET ZN B 138 1
HET ZN B 139 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
HELIX 1 1 CYS B 126 PHE B 134 1 9
SHEET 1 A 5 GLN A 52 PRO A 57 0
SHEET 2 A 5 TRP A 43 ASN A 48 -1 N ASN A 48 O GLN A 52
SHEET 3 A 5 MET A 31 GLU A 35 -1 N GLU A 35 O LYS A 45
SHEET 4 A 5 VAL A 8 THR A 11 -1 N VAL A 9 O MET A 31
SHEET 5 A 5 VAL A 61 VAL A 63 -1 O VAL A 62 N GLN A 10
SHEET 1 B 2 ILE B 78 CYS B 79 0
SHEET 2 B 2 ARG B 84 PRO B 85 -1 O ARG B 84 N CYS B 79
SHEET 1 C 2 VAL B 90 VAL B 91 0
SHEET 2 C 2 TRP B 98 HIS B 99 -1 O TRP B 98 N VAL B 91
SHEET 1 D 2 TYR B 118 ARG B 120 0
SHEET 2 D 2 LEU B 123 TYR B 125 -1 O TYR B 125 N TYR B 118
LINK SG CYS B 79 ZN ZN B 138 1555 1555 2.30
LINK SG CYS B 82 ZN ZN B 138 1555 1555 2.30
LINK ND1 HIS B 99 ZN ZN B 138 1555 1555 2.00
LINK ND1 HIS B 102 ZN ZN B 138 1555 1555 2.00
LINK SG CYS B 105 ZN ZN B 139 1555 1555 2.30
LINK SG CYS B 108 ZN ZN B 139 1555 1555 2.30
LINK SG CYS B 126 ZN ZN B 139 1555 1555 2.30
LINK ND1 HIS B 129 ZN ZN B 139 1555 1555 2.00
SITE 1 AC1 4 CYS B 79 CYS B 82 HIS B 99 HIS B 102
SITE 1 AC2 4 CYS B 105 CYS B 108 CYS B 126 HIS B 129
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