Header list of 1z2k.pdb file
Complete list - r 2 2 Bytes
HEADER IMMUNE SYSTEM 08-MAR-05 1Z2K
TITLE NMR STRUCTURE OF THE D1 DOMAIN OF THE NATURAL KILLER CELL RECEPTOR,
TITLE 2 2B4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NATURAL KILLER CELL RECEPTOR 2B4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: D1 DOMAIN;
COMPND 5 SYNONYM: NKR2B4, NK CELL TYPE I RECEPTOR PROTEIN 2B4, CD244 ANTIGEN,
COMPND 6 NON MHC RESTRICTED KILLING ASSOCIATED;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CD244, 2B4, NMRK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS IMMUNOGLOBULIN MOTIF, BETA SANDWICH, V-DOMAIN, NATURAL KILLER CELL
KEYWDS 2 RECEPTOR, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR J.B.AMES,V.VYAS,J.D.LUSIN,R.MARIUZZA
REVDAT 3 02-MAR-22 1Z2K 1 REMARK
REVDAT 2 24-FEB-09 1Z2K 1 VERSN
REVDAT 1 03-MAY-05 1Z2K 0
JRNL AUTH J.B.AMES,V.VYAS,J.D.LUSIN,R.MARIUZZA
JRNL TITL NMR STRUCTURE OF THE NATURAL KILLER CELL RECEPTOR 2B4:
JRNL TITL 2 IMPLICATIONS FOR LIGAND RECOGNITION
JRNL REF BIOCHEMISTRY V. 44 6416 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15850375
JRNL DOI 10.1021/BI050139S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2657 RESTRAINTS, 2359 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 128
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 170 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1Z2K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032217.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM 2B4 D1 DOMAIN, U-15N,13C;
REMARK 210 50 MM PHOSPHATE BUFFER; PH 7.2;
REMARK 210 90% H2O, 10% D2O
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
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINDED USING STANDARD 2D
REMARK 210 HOMONUCLEAR NOESY AND 3D HETERONUCLEAR TECHNIQUES
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-14
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 1
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 SER A 60 H PHE A 61 1.24
REMARK 500 O VAL A 31 H TRP A 49 1.47
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 TRP A 33 CG TRP A 33 CD2 -0.121
REMARK 500 1 HIS A 41 CG HIS A 41 ND1 -0.119
REMARK 500 1 TRP A 49 CG TRP A 49 CD2 -0.126
REMARK 500 1 TRP A 56 CG TRP A 56 CD2 -0.121
REMARK 500 1 HIS A 86 CG HIS A 86 ND1 -0.120
REMARK 500 2 TRP A 33 CG TRP A 33 CD2 -0.117
REMARK 500 2 HIS A 41 CG HIS A 41 ND1 -0.121
REMARK 500 2 TRP A 49 CG TRP A 49 CD2 -0.115
REMARK 500 2 TRP A 56 CG TRP A 56 CD2 -0.114
REMARK 500 2 HIS A 86 CG HIS A 86 ND1 -0.121
REMARK 500 3 TRP A 33 CG TRP A 33 CD2 -0.117
REMARK 500 3 HIS A 41 CG HIS A 41 ND1 -0.119
REMARK 500 3 TRP A 49 CG TRP A 49 CD2 -0.116
REMARK 500 3 TRP A 56 CG TRP A 56 CD2 -0.112
REMARK 500 3 HIS A 86 CG HIS A 86 ND1 -0.121
REMARK 500 4 TRP A 33 CG TRP A 33 CD2 -0.119
REMARK 500 4 HIS A 41 CG HIS A 41 ND1 -0.120
REMARK 500 4 TRP A 49 CG TRP A 49 CD2 -0.119
REMARK 500 4 TRP A 56 CG TRP A 56 CD2 -0.114
REMARK 500 4 HIS A 86 CG HIS A 86 ND1 -0.121
REMARK 500 5 TRP A 33 CG TRP A 33 CD2 -0.115
REMARK 500 5 HIS A 41 CG HIS A 41 ND1 -0.121
REMARK 500 5 TRP A 49 CG TRP A 49 CD2 -0.107
REMARK 500 5 TRP A 56 CG TRP A 56 CD2 -0.121
REMARK 500 5 HIS A 86 CG HIS A 86 ND1 -0.121
REMARK 500 6 TRP A 33 CG TRP A 33 CD2 -0.117
REMARK 500 6 HIS A 41 CG HIS A 41 ND1 -0.122
REMARK 500 6 TRP A 49 CG TRP A 49 CD2 -0.121
REMARK 500 6 TRP A 56 CG TRP A 56 CD2 -0.123
REMARK 500 6 HIS A 86 CG HIS A 86 ND1 -0.123
REMARK 500 7 TRP A 33 CG TRP A 33 CD2 -0.118
REMARK 500 7 HIS A 41 CG HIS A 41 ND1 -0.118
REMARK 500 7 TRP A 49 CG TRP A 49 CD2 -0.126
REMARK 500 7 TRP A 56 CG TRP A 56 CD2 -0.117
REMARK 500 7 HIS A 86 CG HIS A 86 ND1 -0.122
REMARK 500 8 TRP A 33 CG TRP A 33 CD2 -0.117
REMARK 500 8 HIS A 41 CG HIS A 41 ND1 -0.122
REMARK 500 8 TRP A 49 CG TRP A 49 CD2 -0.125
REMARK 500 8 TRP A 56 CG TRP A 56 CD2 -0.115
REMARK 500 8 HIS A 86 CG HIS A 86 ND1 -0.121
REMARK 500 9 TRP A 33 CG TRP A 33 CD2 -0.114
REMARK 500 9 HIS A 41 CG HIS A 41 ND1 -0.121
REMARK 500 9 TRP A 49 CG TRP A 49 CD2 -0.123
REMARK 500 9 TRP A 56 CG TRP A 56 CD2 -0.110
REMARK 500 9 HIS A 86 CG HIS A 86 ND1 -0.121
REMARK 500 10 TRP A 33 CG TRP A 33 CD2 -0.111
REMARK 500 10 HIS A 41 CG HIS A 41 ND1 -0.115
REMARK 500 10 TRP A 56 CG TRP A 56 CD2 -0.107
REMARK 500 10 HIS A 86 CG HIS A 86 ND1 -0.115
REMARK 500 11 TRP A 33 CG TRP A 33 CD2 -0.116
REMARK 500
REMARK 500 THIS ENTRY HAS 69 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 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 1 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 1 TRP A 49 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 TRP A 49 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP A 49 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 1 TRP A 49 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 1 TRP A 49 CG - CD2 - CE3 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 TRP A 56 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 TRP A 56 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP A 56 NE1 - CE2 - CZ2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 1 TRP A 56 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 2 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 2 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 TRP A 49 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 2 TRP A 49 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 49 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 2 TRP A 49 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 2 TRP A 56 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 TRP A 56 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 56 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 2 TRP A 56 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 3 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 3 TRP A 33 CD1 - NE1 - CE2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 3 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 3 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 3 TRP A 49 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 3 TRP A 49 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 49 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 3 TRP A 49 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 3 TRP A 56 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 TRP A 56 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 3 TRP A 56 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 TRP A 56 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 4 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 4 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 4 TRP A 49 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 4 TRP A 49 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP A 49 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 4 TRP A 49 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 4 TRP A 56 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 4 TRP A 56 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 4 TRP A 56 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 4 TRP A 56 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 5 TRP A 33 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 5 TRP A 33 NE1 - CE2 - CZ2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 5 TRP A 33 NE1 - CE2 - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 5 TRP A 49 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 156 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 PRO A 3 23.68 -74.92
REMARK 500 1 ASP A 4 97.68 73.99
REMARK 500 1 SER A 13 75.20 38.82
REMARK 500 1 ASN A 23 97.35 73.34
REMARK 500 1 ILE A 24 9.25 -150.51
REMARK 500 1 GLN A 25 -7.97 59.95
REMARK 500 1 THR A 26 88.51 45.27
REMARK 500 1 ASP A 28 104.55 -52.92
REMARK 500 1 SER A 40 5.27 54.64
REMARK 500 1 HIS A 41 -159.07 -121.38
REMARK 500 1 ARG A 42 -159.80 -157.22
REMARK 500 1 ILE A 46 -107.42 68.22
REMARK 500 1 ASN A 51 83.89 51.13
REMARK 500 1 ASP A 52 27.45 45.34
REMARK 500 1 SER A 57 79.39 -158.51
REMARK 500 1 ASN A 58 80.80 158.77
REMARK 500 1 VAL A 59 96.54 -47.07
REMARK 500 1 SER A 60 2.05 174.40
REMARK 500 1 PHE A 61 38.33 -79.71
REMARK 500 1 ASP A 71 -99.06 156.43
REMARK 500 1 SER A 78 -33.84 -151.71
REMARK 500 1 ALA A 79 15.82 48.70
REMARK 500 1 LEU A 81 -15.75 -44.08
REMARK 500 1 SER A 84 100.06 -45.89
REMARK 500 1 ASN A 93 86.80 50.57
REMARK 500 1 VAL A 98 151.71 -40.14
REMARK 500 1 CYS A 99 -98.49 -168.66
REMARK 500 2 ASP A 4 106.86 -42.88
REMARK 500 2 SER A 13 81.42 35.19
REMARK 500 2 LYS A 15 79.48 -119.54
REMARK 500 2 ASN A 23 56.59 83.76
REMARK 500 2 GLN A 25 3.95 -160.33
REMARK 500 2 SER A 40 -7.99 62.85
REMARK 500 2 ILE A 46 -109.98 70.20
REMARK 500 2 ASN A 51 -60.44 65.38
REMARK 500 2 ASP A 52 32.18 -159.81
REMARK 500 2 ASN A 58 -40.84 70.71
REMARK 500 2 SER A 60 54.29 -18.14
REMARK 500 2 PHE A 61 76.76 -63.12
REMARK 500 2 SER A 62 -22.49 -148.23
REMARK 500 2 ASP A 71 -103.49 173.92
REMARK 500 2 SER A 78 -31.84 -151.74
REMARK 500 2 SER A 84 105.04 -57.49
REMARK 500 2 THR A 92 -171.88 56.64
REMARK 500 2 LYS A 97 33.92 35.90
REMARK 500 2 CYS A 99 102.57 -57.77
REMARK 500 3 PRO A 3 -161.08 -68.07
REMARK 500 3 SER A 13 83.93 33.61
REMARK 500 3 LYS A 15 60.34 -119.44
REMARK 500 3 PRO A 16 97.00 -69.81
REMARK 500
REMARK 500 THIS ENTRY HAS 317 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 ARG A 20 0.26 SIDE CHAIN
REMARK 500 1 ARG A 42 0.31 SIDE CHAIN
REMARK 500 2 ARG A 20 0.23 SIDE CHAIN
REMARK 500 3 ARG A 20 0.20 SIDE CHAIN
REMARK 500 3 ARG A 42 0.30 SIDE CHAIN
REMARK 500 4 ARG A 20 0.17 SIDE CHAIN
REMARK 500 4 ARG A 42 0.28 SIDE CHAIN
REMARK 500 5 ARG A 20 0.19 SIDE CHAIN
REMARK 500 5 ARG A 42 0.22 SIDE CHAIN
REMARK 500 6 ARG A 20 0.32 SIDE CHAIN
REMARK 500 6 ARG A 42 0.31 SIDE CHAIN
REMARK 500 7 ARG A 20 0.29 SIDE CHAIN
REMARK 500 7 ARG A 42 0.27 SIDE CHAIN
REMARK 500 8 ARG A 20 0.27 SIDE CHAIN
REMARK 500 8 ARG A 42 0.30 SIDE CHAIN
REMARK 500 9 ARG A 20 0.32 SIDE CHAIN
REMARK 500 9 ARG A 42 0.28 SIDE CHAIN
REMARK 500 10 ARG A 20 0.32 SIDE CHAIN
REMARK 500 10 ARG A 42 0.31 SIDE CHAIN
REMARK 500 10 TYR A 87 0.09 SIDE CHAIN
REMARK 500 11 ARG A 20 0.08 SIDE CHAIN
REMARK 500 11 ARG A 42 0.30 SIDE CHAIN
REMARK 500 12 ARG A 20 0.32 SIDE CHAIN
REMARK 500 12 ARG A 42 0.20 SIDE CHAIN
REMARK 500 13 ARG A 20 0.20 SIDE CHAIN
REMARK 500 13 ARG A 42 0.29 SIDE CHAIN
REMARK 500 14 ARG A 42 0.26 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Z2K A 1 109 UNP Q07763 CD244_MOUSE 21 129
SEQRES 1 A 109 ASP CYS PRO ASP SER SER GLU GLU VAL VAL GLY VAL SER
SEQRES 2 A 109 GLY LYS PRO VAL GLN LEU ARG PRO SER ASN ILE GLN THR
SEQRES 3 A 109 LYS ASP VAL SER VAL GLN TRP LYS LYS THR GLU GLN GLY
SEQRES 4 A 109 SER HIS ARG LYS ILE GLU ILE LEU ASN TRP TYR ASN ASP
SEQRES 5 A 109 GLY PRO SER TRP SER ASN VAL SER PHE SER ASP ILE TYR
SEQRES 6 A 109 GLY PHE ASP TYR GLY ASP PHE ALA LEU SER ILE LYS SER
SEQRES 7 A 109 ALA LYS LEU GLN ASP SER GLY HIS TYR LEU LEU GLU ILE
SEQRES 8 A 109 THR ASN THR GLY GLY LYS VAL CYS ASN LYS ASN PHE GLN
SEQRES 9 A 109 LEU LEU ILE LEU ASP
HELIX 1 1 LYS A 80 ASP A 83 5 4
SHEET 1 A 6 SER A 5 VAL A 12 0
SHEET 2 A 6 ASN A 100 LEU A 108 1 O GLN A 104 N GLU A 7
SHEET 3 A 6 GLY A 85 ILE A 91 -1 N TYR A 87 O PHE A 103
SHEET 4 A 6 SER A 30 GLU A 37 -1 N GLN A 32 O GLU A 90
SHEET 5 A 6 LYS A 43 TYR A 50 -1 O TRP A 49 N VAL A 31
SHEET 6 A 6 PRO A 54 SER A 57 -1 O SER A 55 N ASN A 48
SHEET 1 B 3 VAL A 17 LEU A 19 0
SHEET 2 B 3 ALA A 73 ILE A 76 -1 O LEU A 74 N LEU A 19
SHEET 3 B 3 GLY A 66 ASP A 68 -1 N ASP A 68 O ALA A 73
SSBOND 1 CYS A 2 CYS A 99 1555 1555 2.74
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