Header list of 1d9s.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN 29-OCT-99 1D9S
TITLE TUMOR SUPPRESSOR P15(INK4B) STRUCTURE BY COMPARATIVE MODELING AND NMR
TITLE 2 DATA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 4 INHIBITOR B;
COMPND 3 CHAIN: A;
COMPND 4 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PGEX-2T
KEYWDS HELIX-TURN-HELIX, ANKYRIN REPEAT, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
MDLTYP MINIMIZED AVERAGE
AUTHOR C.YUAN,L.JI,T.L.SELBY,I.J.L.BYEON,M.D.TSAI
REVDAT 5 16-FEB-22 1D9S 1 REMARK
REVDAT 4 24-FEB-09 1D9S 1 VERSN
REVDAT 3 01-APR-03 1D9S 1 JRNL
REVDAT 2 18-AUG-00 1D9S 1 AUTHOR JRNL
REVDAT 1 28-JUL-00 1D9S 0
JRNL AUTH C.YUAN,J.LI,T.L.SELBY,I.J.BYEON,M.D.TSAI
JRNL TITL TUMOR SUPPRESSOR INK4: COMPARISONS OF CONFORMATIONAL
JRNL TITL 2 PROPERTIES BETWEEN P16(INK4A) AND P18(INK4C).
JRNL REF J.MOL.BIOL. V. 294 201 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10556039
JRNL DOI 10.1006/JMBI.1999.3231
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 DUE TO THE STRUCTURAL FLEXIBILITY AND INSTABILITY OF P15, ONLY A
REMARK 3 LIMITED
REMARK 3 NUMBER OF NMR CONSTRAINTS WERE COLLECTED. BECAUSE P15 SHARES MORE
REMARK 3 THAN 85%
REMARK 3 SEQUENCE HOMOLOGY WITH P16, 19 P15 STRUCTURES WERE GENERATED BY
REMARK 3 USING
REMARK 3 COMPARATIVE MODELING (MODELLER-4) WITH AN ENSEMBLE OF P16(INK4A)
REMARK 3 NMR
REMARK 3 STRUCTURES AS TEMPLATES. THE MODELING STRUCTURES WERE THEN
REMARK 3 SUBJECTED TO 1400
REMARK 3 STEPS OF RESTRAINT ENERGY MINIMIZATION (X-PLOR) WITH THE NMR DATA
REMARK 3 (672
REMARK 3 DISTANCE CONSTRAINTS). THE STRUCTURES THAT SATISFY THE NMR
REMARK 3 CONSTRAINTS WERE
REMARK 3 PICKED TO REPRESENT P15(INK4B).
REMARK 4
REMARK 4 1D9S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000009922.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.2 MM P15, U-15N; 4 MM HEPES, 1
REMARK 210 MM DTT, 5 UM EDTA; 0.2 MM P15, U-
REMARK 210 15N,13C; 4 MM HEPES, 1 MM DTT, 5
REMARK 210 UM EDTA; 0.2 MM P15, U-15N,13C;
REMARK 210 4 MM HEPES, 1 MM DTT, 5 UM EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNCA;
REMARK 210 CBCA(CO)NH; 3D_13C-SEPARATED_
REMARK 210 NOESY; 3D_13C-SEPARATED_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : MODELLER-4 4.0
REMARK 210 METHOD USED : COMPARATIVE MODELING, RESTRAINT
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 19
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
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 : 10
REMARK 210
REMARK 210 REMARK: TRIPLE-RESONANCE NMR SPECTROSCOPY WAS USED TO DETERMINE
REMARK 210 THE P15 STRUCTURE
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 O ALA A 8 H ALA A 11 1.45
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 A 84 CB - CG - CD2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 1 PHE A 84 CD1 - CG - CD2 ANGL. DEV. = -65.5 DEGREES
REMARK 500 1 PHE A 84 CB - CG - CD1 ANGL. DEV. = 18.7 DEGREES
REMARK 500 1 PHE A 84 CG - CD1 - CE1 ANGL. DEV. = -47.7 DEGREES
REMARK 500 1 PHE A 84 CG - CD2 - CE2 ANGL. DEV. = -50.8 DEGREES
REMARK 500 1 PHE A 84 CD1 - CE1 - CZ ANGL. DEV. = -50.2 DEGREES
REMARK 500 1 PHE A 84 CE1 - CZ - CE2 ANGL. DEV. = -68.6 DEGREES
REMARK 500 1 PHE A 84 CZ - CE2 - CD2 ANGL. DEV. = -47.4 DEGREES
REMARK 500 2 TYR A 123 CB - CG - CD2 ANGL. DEV. = 18.2 DEGREES
REMARK 500 2 TYR A 123 CD1 - CG - CD2 ANGL. DEV. = -65.3 DEGREES
REMARK 500 2 TYR A 123 CB - CG - CD1 ANGL. DEV. = -12.0 DEGREES
REMARK 500 2 TYR A 123 CG - CD1 - CE1 ANGL. DEV. = -51.1 DEGREES
REMARK 500 2 TYR A 123 CG - CD2 - CE2 ANGL. DEV. = -48.2 DEGREES
REMARK 500 2 TYR A 123 CD1 - CE1 - CZ ANGL. DEV. = -46.9 DEGREES
REMARK 500 2 TYR A 123 CE1 - CZ - OH ANGL. DEV. = 19.0 DEGREES
REMARK 500 2 TYR A 123 CE1 - CZ - CE2 ANGL. DEV. = -68.3 DEGREES
REMARK 500 2 TYR A 123 CZ - CE2 - CD2 ANGL. DEV. = -49.8 DEGREES
REMARK 500 4 PHE A 84 CB - CG - CD2 ANGL. DEV. = 18.4 DEGREES
REMARK 500 4 PHE A 84 CD1 - CG - CD2 ANGL. DEV. = -65.7 DEGREES
REMARK 500 4 PHE A 84 CB - CG - CD1 ANGL. DEV. = -11.9 DEGREES
REMARK 500 4 PHE A 84 CG - CD1 - CE1 ANGL. DEV. = -50.7 DEGREES
REMARK 500 4 PHE A 84 CG - CD2 - CE2 ANGL. DEV. = -47.7 DEGREES
REMARK 500 4 PHE A 84 CD1 - CE1 - CZ ANGL. DEV. = -47.2 DEGREES
REMARK 500 4 PHE A 84 CE1 - CZ - CE2 ANGL. DEV. = -68.6 DEGREES
REMARK 500 4 PHE A 84 CZ - CE2 - CD2 ANGL. DEV. = -50.3 DEGREES
REMARK 500 4 TYR A 123 CB - CG - CD2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 4 TYR A 123 CD1 - CG - CD2 ANGL. DEV. = -65.2 DEGREES
REMARK 500 4 TYR A 123 CB - CG - CD1 ANGL. DEV. = 18.4 DEGREES
REMARK 500 4 TYR A 123 CG - CD1 - CE1 ANGL. DEV. = -48.2 DEGREES
REMARK 500 4 TYR A 123 CG - CD2 - CE2 ANGL. DEV. = -51.2 DEGREES
REMARK 500 4 TYR A 123 CD1 - CE1 - CZ ANGL. DEV. = -49.9 DEGREES
REMARK 500 4 TYR A 123 OH - CZ - CE2 ANGL. DEV. = 19.0 DEGREES
REMARK 500 4 TYR A 123 CE1 - CZ - CE2 ANGL. DEV. = -68.3 DEGREES
REMARK 500 4 TYR A 123 CZ - CE2 - CD2 ANGL. DEV. = -47.0 DEGREES
REMARK 500 5 PHE A 84 CB - CG - CD2 ANGL. DEV. = 11.0 DEGREES
REMARK 500 5 PHE A 84 CD1 - CG - CD2 ANGL. DEV. = -48.5 DEGREES
REMARK 500 5 PHE A 84 CG - CD1 - CE1 ANGL. DEV. = -47.3 DEGREES
REMARK 500 5 PHE A 84 CG - CD2 - CE2 ANGL. DEV. = -68.0 DEGREES
REMARK 500 5 PHE A 84 CD1 - CE1 - CZ ANGL. DEV. = -68.5 DEGREES
REMARK 500 5 PHE A 84 CE1 - CZ - CE2 ANGL. DEV. = -50.3 DEGREES
REMARK 500 5 PHE A 84 CZ - CE2 - CD2 ANGL. DEV. = -48.1 DEGREES
REMARK 500 5 TYR A 123 CB - CG - CD2 ANGL. DEV. = -10.9 DEGREES
REMARK 500 5 TYR A 123 CD1 - CG - CD2 ANGL. DEV. = -65.0 DEGREES
REMARK 500 5 TYR A 123 CB - CG - CD1 ANGL. DEV. = 18.7 DEGREES
REMARK 500 5 TYR A 123 CG - CD1 - CE1 ANGL. DEV. = -48.1 DEGREES
REMARK 500 5 TYR A 123 CG - CD2 - CE2 ANGL. DEV. = -51.3 DEGREES
REMARK 500 5 TYR A 123 CD1 - CE1 - CZ ANGL. DEV. = -49.8 DEGREES
REMARK 500 5 TYR A 123 OH - CZ - CE2 ANGL. DEV. = 18.9 DEGREES
REMARK 500 5 TYR A 123 CE1 - CZ - CE2 ANGL. DEV. = -68.6 DEGREES
REMARK 500 5 TYR A 123 CZ - CE2 - CD2 ANGL. DEV. = -47.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 HIS A 0 108.21 40.52
REMARK 500 1 MET A 1 -163.19 55.21
REMARK 500 1 LEU A 2 -55.23 -159.16
REMARK 500 1 SER A 5 -167.10 -120.69
REMARK 500 1 LEU A 26 -68.82 -95.34
REMARK 500 1 ALA A 34 79.30 -69.36
REMARK 500 1 LEU A 35 158.58 -49.50
REMARK 500 1 ARG A 41 177.27 51.89
REMARK 500 1 MET A 47 -2.39 67.86
REMARK 500 1 ALA A 62 -166.04 -60.16
REMARK 500 1 CYS A 66 172.96 -58.58
REMARK 500 1 THR A 71 27.15 -155.03
REMARK 500 1 ASP A 99 44.73 -170.06
REMARK 500 1 ASP A 102 73.91 -69.37
REMARK 500 1 ALA A 103 -69.07 66.83
REMARK 500 1 TRP A 104 35.50 -140.88
REMARK 500 1 ARG A 106 -73.16 59.52
REMARK 500 1 ALA A 112 -75.33 -67.71
REMARK 500 1 GLN A 115 -76.65 -78.02
REMARK 500 2 SER A -4 152.49 62.24
REMARK 500 2 HIS A 0 97.53 54.91
REMARK 500 2 MET A 1 119.30 58.25
REMARK 500 2 SER A 5 41.30 -105.81
REMARK 500 2 SER A 6 -84.52 -62.41
REMARK 500 2 ASP A 7 14.69 54.89
REMARK 500 2 ARG A 41 175.63 53.73
REMARK 500 2 ALA A 62 -147.29 -65.09
REMARK 500 2 THR A 71 24.70 -146.63
REMARK 500 2 LEU A 98 48.59 -148.40
REMARK 500 2 ASP A 99 50.13 -159.31
REMARK 500 2 ALA A 103 -79.63 60.84
REMARK 500 2 LEU A 124 -71.65 -71.15
REMARK 500 2 THR A 128 -43.68 -131.64
REMARK 500 3 SER A -4 71.52 51.93
REMARK 500 3 MET A 1 -149.82 -93.55
REMARK 500 3 LEU A 2 -155.90 -78.08
REMARK 500 3 SER A 5 -68.40 -166.61
REMARK 500 3 SER A 6 -80.64 -61.57
REMARK 500 3 ASP A 7 -81.28 54.38
REMARK 500 3 GLN A 18 74.85 -112.39
REMARK 500 3 ALA A 34 93.46 -65.32
REMARK 500 3 LEU A 35 172.36 -51.90
REMARK 500 3 ASN A 36 -163.00 -103.02
REMARK 500 3 PHE A 38 33.30 -95.72
REMARK 500 3 MET A 46 32.07 -95.73
REMARK 500 3 MET A 47 -7.40 68.41
REMARK 500 3 MET A 48 27.28 46.90
REMARK 500 3 GLU A 63 76.80 -119.12
REMARK 500 3 THR A 71 38.88 -143.76
REMARK 500 3 LEU A 72 61.83 25.45
REMARK 500
REMARK 500 THIS ENTRY HAS 155 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 16 0.20 SIDE CHAIN
REMARK 500 1 ARG A 23 0.32 SIDE CHAIN
REMARK 500 1 ARG A 37 0.21 SIDE CHAIN
REMARK 500 1 ARG A 40 0.21 SIDE CHAIN
REMARK 500 1 ARG A 41 0.15 SIDE CHAIN
REMARK 500 1 ARG A 74 0.20 SIDE CHAIN
REMARK 500 1 ARG A 81 0.23 SIDE CHAIN
REMARK 500 1 PHE A 84 0.44 SIDE CHAIN
REMARK 500 1 ARG A 93 0.20 SIDE CHAIN
REMARK 500 1 ARG A 97 0.25 SIDE CHAIN
REMARK 500 1 ARG A 106 0.23 SIDE CHAIN
REMARK 500 1 ARG A 118 0.26 SIDE CHAIN
REMARK 500 1 ARG A 122 0.23 SIDE CHAIN
REMARK 500 2 ARG A 16 0.27 SIDE CHAIN
REMARK 500 2 ARG A 23 0.24 SIDE CHAIN
REMARK 500 2 ARG A 37 0.21 SIDE CHAIN
REMARK 500 2 ARG A 40 0.23 SIDE CHAIN
REMARK 500 2 ARG A 41 0.27 SIDE CHAIN
REMARK 500 2 ARG A 74 0.31 SIDE CHAIN
REMARK 500 2 ARG A 81 0.21 SIDE CHAIN
REMARK 500 2 ARG A 93 0.20 SIDE CHAIN
REMARK 500 2 ARG A 97 0.26 SIDE CHAIN
REMARK 500 2 ARG A 106 0.30 SIDE CHAIN
REMARK 500 2 ARG A 118 0.21 SIDE CHAIN
REMARK 500 2 ARG A 122 0.26 SIDE CHAIN
REMARK 500 2 TYR A 123 0.46 SIDE CHAIN
REMARK 500 3 ARG A 16 0.09 SIDE CHAIN
REMARK 500 3 ARG A 23 0.23 SIDE CHAIN
REMARK 500 3 ARG A 37 0.26 SIDE CHAIN
REMARK 500 3 ARG A 40 0.16 SIDE CHAIN
REMARK 500 3 ARG A 41 0.29 SIDE CHAIN
REMARK 500 3 ARG A 74 0.31 SIDE CHAIN
REMARK 500 3 ARG A 81 0.21 SIDE CHAIN
REMARK 500 3 ARG A 93 0.26 SIDE CHAIN
REMARK 500 3 ARG A 97 0.31 SIDE CHAIN
REMARK 500 3 ARG A 106 0.22 SIDE CHAIN
REMARK 500 3 ARG A 118 0.23 SIDE CHAIN
REMARK 500 3 ARG A 122 0.24 SIDE CHAIN
REMARK 500 4 ARG A 16 0.21 SIDE CHAIN
REMARK 500 4 ARG A 23 0.22 SIDE CHAIN
REMARK 500 4 ARG A 37 0.23 SIDE CHAIN
REMARK 500 4 ARG A 40 0.21 SIDE CHAIN
REMARK 500 4 ARG A 41 0.26 SIDE CHAIN
REMARK 500 4 ARG A 74 0.27 SIDE CHAIN
REMARK 500 4 ARG A 81 0.21 SIDE CHAIN
REMARK 500 4 PHE A 84 0.44 SIDE CHAIN
REMARK 500 4 ARG A 93 0.21 SIDE CHAIN
REMARK 500 4 ARG A 97 0.20 SIDE CHAIN
REMARK 500 4 ARG A 106 0.22 SIDE CHAIN
REMARK 500 4 ARG A 118 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 128 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1D9S A -5 130 UNP P55271 CDN2B_MOUSE 1 130
SEQADV 1D9S GLY A -5 UNP P55271 SEE REMARK 999
SEQADV 1D9S SER A -4 UNP P55271 SEE REMARK 999
SEQADV 1D9S PRO A -3 UNP P55271 SEE REMARK 999
SEQADV 1D9S GLY A -2 UNP P55271 SEE REMARK 999
SEQADV 1D9S ILE A -1 UNP P55271 SEE REMARK 999
SEQADV 1D9S HIS A 0 UNP P55271 SEE REMARK 999
SEQRES 1 A 136 GLY SER PRO GLY ILE HIS MET LEU GLY GLY SER SER ASP
SEQRES 2 A 136 ALA GLY LEU ALA THR ALA ALA ALA ARG GLY GLN VAL GLU
SEQRES 3 A 136 THR VAL ARG GLN LEU LEU GLU ALA GLY ALA ASP PRO ASN
SEQRES 4 A 136 ALA LEU ASN ARG PHE GLY ARG ARG PRO ILE GLN VAL MET
SEQRES 5 A 136 MET MET GLY SER ALA GLN VAL ALA GLU LEU LEU LEU LEU
SEQRES 6 A 136 HIS GLY ALA GLU PRO ASN CYS ALA ASP PRO ALA THR LEU
SEQRES 7 A 136 THR ARG PRO VAL HIS ASP ALA ALA ARG GLU GLY PHE LEU
SEQRES 8 A 136 ASP THR LEU VAL VAL LEU HIS ARG ALA GLY ALA ARG LEU
SEQRES 9 A 136 ASP VAL CYS ASP ALA TRP GLY ARG LEU PRO VAL ASP LEU
SEQRES 10 A 136 ALA GLU GLU GLN GLY HIS ARG ASP ILE ALA ARG TYR LEU
SEQRES 11 A 136 HIS ALA ALA THR GLY ASP
HELIX 1 1 ALA A 8 ARG A 16 1 9
HELIX 2 2 GLN A 18 ALA A 28 1 11
HELIX 3 3 SER A 50 GLY A 61 1 12
HELIX 4 4 ARG A 74 GLY A 83 1 10
HELIX 5 5 PHE A 84 ALA A 94 1 11
HELIX 6 6 LEU A 107 GLY A 116 1 10
HELIX 7 7 HIS A 117 GLY A 129 1 13
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 16 2 Bytes