Header list of 1m39.pdb file
Complete list - b 23 2 Bytes
HEADER CELL CYCLE 27-JUN-02 1M39
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT (F86-I165) OF THE HUMAN
TITLE 2 CENTRIN 2 IN CALCIUM SATURATED FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALTRACTIN, ISOFORM 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINUS (RESIDUES 84-172);
COMPND 5 SYNONYM: CENTRIN 2;
COMPND 6 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: CEN2;
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: PET24A(+)
KEYWDS EF-HAND, CELL CYCLE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR E.MATEI,S.MIRON,Y.BLOUQUIT,P.DUCHAMBON,P.DURUSSEL,J.A.COX,C.T.CRAESCU
REVDAT 3 23-FEB-22 1M39 1 REMARK
REVDAT 2 24-FEB-09 1M39 1 VERSN
REVDAT 1 25-MAR-03 1M39 0
JRNL AUTH E.MATEI,S.MIRON,Y.BLOUQUIT,P.DUCHAMBON,P.DURUSSEL,J.A.COX,
JRNL AUTH 2 C.T.CRAESCU
JRNL TITL C-TERMINAL HALF OF HUMAN CENTRIN 2 BEHAVES LIKE A REGULATORY
JRNL TITL 2 EF-HAND DOMAIN
JRNL REF BIOCHEMISTRY V. 42 1439 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12578356
JRNL DOI 10.1021/BI0269714
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII I2000, DISCOVER I2000
REMARK 3 AUTHORS : ACCELRYS (DGII), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 1103 NOE
REMARK 3 RESTRAINTS, 35 HYDROGEN BOND RESTRAINTS AND 103 DIHEDRAL
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1M39 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016542.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : LC-HSCEN2 M84-Y172; TRIS D11 20
REMARK 210 MM BUFFER;100 MM NACL; 93% H2O,
REMARK 210 7% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINT
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 76
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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 1-25
REMARK 465 RES C SSSEQI
REMARK 465 MET A 84
REMARK 465 ASN A 85
REMARK 465 MET A 166
REMARK 465 LYS A 167
REMARK 465 LYS A 168
REMARK 465 THR A 169
REMARK 465 SER A 170
REMARK 465 LEU A 171
REMARK 465 TYR A 172
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 HG SER A 158 OE1 GLU A 159 1.44
REMARK 500 HZ1 LYS A 127 OD2 ASP A 139 1.47
REMARK 500 OE1 GLU A 99 HZ3 LYS A 100 1.50
REMARK 500 O MET A 97 HG SER A 98 1.52
REMARK 500 OD1 ASP A 115 HH22 ARG A 128 1.55
REMARK 500 HZ1 LYS A 120 OE2 GLU A 156 1.56
REMARK 500 OD2 ASP A 101 HZ1 LYS A 108 1.56
REMARK 500 HZ1 LYS A 111 OD2 ASP A 114 1.57
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 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 1 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 PHE A 113 CB - CG - CD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 LEU A 163 CB - CG - CD2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 2 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 3 ASP A 150 N - CA - CB ANGL. DEV. = -11.7 DEGREES
REMARK 500 3 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 3 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 4 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 4 VAL A 129 CA - CB - CG2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 4 ASP A 150 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 4 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 4 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 5 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 5 LEU A 133 N - CA - CB ANGL. DEV. = -17.7 DEGREES
REMARK 500 5 LEU A 133 CB - CG - CD1 ANGL. DEV. = 15.2 DEGREES
REMARK 500 5 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 5 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 6 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 LEU A 142 CB - CG - CD1 ANGL. DEV. = 20.3 DEGREES
REMARK 500 6 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 6 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 7 PHE A 113 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 7 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 VAL A 129 CA - CB - CG2 ANGL. DEV. = 12.7 DEGREES
REMARK 500 7 ASP A 147 CA - CB - CG ANGL. DEV. = 13.5 DEGREES
REMARK 500 7 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 7 LEU A 163 CB - CG - CD2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 7 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 8 PHE A 86 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 8 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 8 LEU A 142 CB - CG - CD1 ANGL. DEV. = 20.9 DEGREES
REMARK 500 8 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 9 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ALA A 149 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 9 ASP A 150 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 9 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 9 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 10 VAL A 92 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 10 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 10 ARG A 151 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 10 ARG A 164 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 11 VAL A 92 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 11 ARG A 128 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 11 LEU A 133 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 131 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 98 89.77 168.16
REMARK 500 1 GLU A 99 -79.19 -134.62
REMARK 500 1 ASP A 101 169.36 59.52
REMARK 500 1 THR A 102 100.39 -171.60
REMARK 500 1 LYS A 103 172.50 77.27
REMARK 500 1 GLU A 104 -50.85 71.94
REMARK 500 1 GLU A 117 -0.48 69.87
REMARK 500 1 LEU A 133 -73.82 -68.99
REMARK 500 1 ARG A 164 -19.99 -49.41
REMARK 500 2 GLN A 95 -37.43 57.83
REMARK 500 2 MET A 97 -46.01 63.11
REMARK 500 2 SER A 98 -71.67 -64.49
REMARK 500 2 LYS A 103 152.93 99.53
REMARK 500 2 GLU A 104 -59.12 68.19
REMARK 500 2 LEU A 137 -115.13 -90.83
REMARK 500 2 ASP A 150 60.83 -67.95
REMARK 500 3 MET A 97 -111.92 -98.19
REMARK 500 3 SER A 98 62.54 -158.77
REMARK 500 3 ASP A 101 145.79 72.83
REMARK 500 3 THR A 102 129.40 -171.41
REMARK 500 3 LYS A 103 151.99 72.32
REMARK 500 3 GLU A 104 -50.65 66.87
REMARK 500 3 GLU A 117 -9.38 78.56
REMARK 500 3 LEU A 133 -73.23 -67.47
REMARK 500 3 ASP A 150 37.31 -70.51
REMARK 500 4 SER A 98 93.63 106.41
REMARK 500 4 GLU A 99 -92.81 -128.23
REMARK 500 4 LYS A 100 -58.78 -161.87
REMARK 500 4 ASP A 101 106.21 64.22
REMARK 500 4 GLU A 104 -42.02 68.84
REMARK 500 4 ASP A 114 73.28 -68.83
REMARK 500 4 ASP A 115 -15.05 -48.73
REMARK 500 4 GLU A 117 -1.02 78.22
REMARK 500 4 LEU A 137 -125.96 -88.13
REMARK 500 4 ASP A 150 20.42 -57.89
REMARK 500 4 ASP A 154 30.83 -144.04
REMARK 500 5 MET A 97 -93.57 -128.73
REMARK 500 5 SER A 98 -68.55 -163.19
REMARK 500 5 GLU A 99 -132.94 59.59
REMARK 500 5 LYS A 100 -93.50 -137.69
REMARK 500 5 ASP A 101 78.32 64.11
REMARK 500 5 THR A 102 121.34 -174.67
REMARK 500 5 LYS A 103 -67.43 3.27
REMARK 500 5 ASP A 115 -19.55 -49.96
REMARK 500 5 GLU A 117 -20.64 80.67
REMARK 500 5 LEU A 137 -109.09 -81.20
REMARK 500 5 ASP A 150 72.04 -61.21
REMARK 500 6 ASP A 101 135.57 74.34
REMARK 500 6 THR A 102 -137.58 -109.85
REMARK 500 6 LYS A 103 -86.16 47.70
REMARK 500
REMARK 500 THIS ENTRY HAS 235 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 151 0.11 SIDE CHAIN
REMARK 500 1 PHE A 162 0.12 SIDE CHAIN
REMARK 500 2 PHE A 113 0.09 SIDE CHAIN
REMARK 500 2 PHE A 162 0.13 SIDE CHAIN
REMARK 500 3 PHE A 162 0.17 SIDE CHAIN
REMARK 500 4 PHE A 86 0.08 SIDE CHAIN
REMARK 500 4 PHE A 113 0.13 SIDE CHAIN
REMARK 500 4 ARG A 151 0.11 SIDE CHAIN
REMARK 500 4 PHE A 162 0.15 SIDE CHAIN
REMARK 500 5 PHE A 162 0.19 SIDE CHAIN
REMARK 500 6 PHE A 86 0.14 SIDE CHAIN
REMARK 500 6 ARG A 128 0.17 SIDE CHAIN
REMARK 500 6 ARG A 151 0.09 SIDE CHAIN
REMARK 500 6 PHE A 162 0.18 SIDE CHAIN
REMARK 500 7 PHE A 162 0.14 SIDE CHAIN
REMARK 500 8 ARG A 151 0.13 SIDE CHAIN
REMARK 500 8 PHE A 162 0.15 SIDE CHAIN
REMARK 500 9 PHE A 162 0.15 SIDE CHAIN
REMARK 500 10 PHE A 113 0.12 SIDE CHAIN
REMARK 500 10 ARG A 151 0.09 SIDE CHAIN
REMARK 500 10 PHE A 162 0.13 SIDE CHAIN
REMARK 500 11 PHE A 162 0.14 SIDE CHAIN
REMARK 500 12 PHE A 162 0.15 SIDE CHAIN
REMARK 500 13 PHE A 162 0.12 SIDE CHAIN
REMARK 500 14 ARG A 151 0.08 SIDE CHAIN
REMARK 500 14 PHE A 162 0.15 SIDE CHAIN
REMARK 500 15 PHE A 113 0.09 SIDE CHAIN
REMARK 500 15 ARG A 128 0.08 SIDE CHAIN
REMARK 500 15 PHE A 162 0.14 SIDE CHAIN
REMARK 500 16 PHE A 162 0.12 SIDE CHAIN
REMARK 500 17 PHE A 86 0.10 SIDE CHAIN
REMARK 500 17 ARG A 151 0.13 SIDE CHAIN
REMARK 500 17 PHE A 162 0.15 SIDE CHAIN
REMARK 500 18 PHE A 113 0.10 SIDE CHAIN
REMARK 500 18 ARG A 151 0.10 SIDE CHAIN
REMARK 500 18 PHE A 162 0.14 SIDE CHAIN
REMARK 500 19 PHE A 113 0.09 SIDE CHAIN
REMARK 500 19 ARG A 128 0.08 SIDE CHAIN
REMARK 500 19 PHE A 162 0.14 SIDE CHAIN
REMARK 500 20 PHE A 113 0.13 SIDE CHAIN
REMARK 500 20 PHE A 162 0.12 SIDE CHAIN
REMARK 500 21 PHE A 113 0.09 SIDE CHAIN
REMARK 500 21 ARG A 151 0.17 SIDE CHAIN
REMARK 500 21 PHE A 162 0.17 SIDE CHAIN
REMARK 500 22 PHE A 162 0.12 SIDE CHAIN
REMARK 500 23 PHE A 113 0.09 SIDE CHAIN
REMARK 500 23 PHE A 123 0.11 SIDE CHAIN
REMARK 500 23 PHE A 162 0.11 SIDE CHAIN
REMARK 500 24 PHE A 89 0.10 SIDE CHAIN
REMARK 500 24 PHE A 113 0.10 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 55 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1M39 A 84 172 UNP P41208 CETN2_HUMAN 84 172
SEQRES 1 A 89 MET ASN PHE GLY ASP PHE LEU THR VAL MET THR GLN LYS
SEQRES 2 A 89 MET SER GLU LYS ASP THR LYS GLU GLU ILE LEU LYS ALA
SEQRES 3 A 89 PHE LYS LEU PHE ASP ASP ASP GLU THR GLY LYS ILE SER
SEQRES 4 A 89 PHE LYS ASN LEU LYS ARG VAL ALA LYS GLU LEU GLY GLU
SEQRES 5 A 89 ASN LEU THR ASP GLU GLU LEU GLN GLU MET ILE ASP GLU
SEQRES 6 A 89 ALA ASP ARG ASP GLY ASP GLY GLU VAL SER GLU GLN GLU
SEQRES 7 A 89 PHE LEU ARG ILE MET LYS LYS THR SER LEU TYR
HELIX 1 1 PHE A 86 GLN A 95 1 10
HELIX 2 2 GLU A 104 ASP A 114 1 11
HELIX 3 3 PHE A 123 GLY A 134 1 12
HELIX 4 4 THR A 138 ASP A 150 1 13
HELIX 5 5 GLU A 159 ARG A 164 1 6
SHEET 1 A 2 LYS A 120 SER A 122 0
SHEET 2 A 2 GLU A 156 SER A 158 -1 O VAL A 157 N ILE A 121
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 - b 23 2 Bytes