HEADER APOPTOSIS 19-OCT-12 2M03
TITLE SOLUTION STRUCTURE OF BCL-XL DETERMINED WITH SELECTIVE ISOTOPE
TITLE 2 LABELLING OF I,L,V SIDECHAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BCL-2-LIKE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BCL2-L-1, APOPTOSIS REGULATOR BCL-X;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCL2-LIKE 1, BCL2L, BCL2L1, BCLX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET28
KEYWDS BCL-XL, PUMA, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.VIACAVA FOLLIS,G.ROYAPPA,R.W.KRIWACKI
REVDAT 4 14-JUN-23 2M03 1 REMARK SEQADV
REVDAT 3 06-MAR-13 2M03 1 JRNL
REVDAT 2 06-FEB-13 2M03 1 JRNL
REVDAT 1 30-JAN-13 2M03 0
JRNL AUTH A.V.FOLLIS,J.E.CHIPUK,J.C.FISHER,M.K.YUN,C.R.GRACE,A.NOURSE,
JRNL AUTH 2 K.BARAN,L.OU,L.MIN,S.W.WHITE,D.R.GREEN,R.W.KRIWACKI
JRNL TITL PUMA BINDING INDUCES PARTIAL UNFOLDING WITHIN BCL-XL TO
JRNL TITL 2 DISRUPT P53 BINDING AND PROMOTE APOPTOSIS.
JRNL REF NAT.CHEM.BIOL. V. 9 163 2013
JRNL REFN ISSN 1552-4450
JRNL PMID 23340338
JRNL DOI 10.1038/NCHEMBIO.1166
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN, AMBER
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), CASE, DARDEN, CHEATHAM,
REMARK 3 III, SIMMERLING, WANG, DUKE, LUO, ... AND KOLLM
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2M03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000103039.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.1
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.9 MM [U-100% 13C; U-100% 15N;
REMARK 210 U-95% 2H; ILE,LEU,VAL C1H3] BCL-
REMARK 210 XL, 92% H2O/8% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D HNCA; 3D HN(CO)CA; 3D HNCACB;
REMARK 210 3D CBCA(CO)NH; 3D HNCO; 3D HN(CA)
REMARK 210 CO; 3D HCCH-TOCSY; 3D 1H-15N
REMARK 210 NOESY; 3D 1H-13C NOESY ALIPHATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN, CARA, CYANA
REMARK 210 METHOD USED : TORSION ANGLE SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 178
REMARK 465 HIS A 179
REMARK 465 HIS A 180
REMARK 465 HIS A 181
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 7 GLU A 43 CD GLU A 43 OE1 -0.124
REMARK 500 7 GLU A 43 CD GLU A 43 OE2 0.120
REMARK 500 10 GLU A 117 CD GLU A 117 OE2 0.073
REMARK 500 15 GLU A 93 CD GLU A 93 OE1 0.082
REMARK 500 15 GLU A 93 CD GLU A 93 OE2 -0.072
REMARK 500 20 GLU A 43 CD GLU A 43 OE1 -0.117
REMARK 500 20 GLU A 43 CD GLU A 43 OE2 0.115
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 7 ASP A 59 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 12 ASP A 15 CB - CG - OD2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 14 ASP A 15 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 14 ASP A 120 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 17 ASP A 59 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 18 ASP A 15 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 19 ASP A 15 CB - CG - OD2 ANGL. DEV. = -5.7 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 SER A 2 130.58 -174.36
REMARK 500 1 MET A 3 168.26 61.77
REMARK 500 1 SER A 32 91.04 -58.42
REMARK 500 1 ASP A 33 43.15 70.11
REMARK 500 1 GLU A 36 -50.87 -146.05
REMARK 500 1 ASN A 37 105.18 57.25
REMARK 500 1 THR A 39 92.39 -176.16
REMARK 500 1 ALA A 41 155.78 -46.21
REMARK 500 1 PRO A 42 -172.19 -63.10
REMARK 500 1 GLU A 43 62.39 68.85
REMARK 500 1 THR A 45 -69.97 -155.88
REMARK 500 1 GLU A 46 -72.08 -121.00
REMARK 500 1 SER A 47 15.18 56.64
REMARK 500 1 TYR A 65 49.66 -144.33
REMARK 500 1 LEU A 76 57.62 -141.63
REMARK 500 1 ILE A 78 135.83 -178.44
REMARK 500 1 THR A 82 166.37 -47.64
REMARK 500 1 ASP A 97 25.75 -166.73
REMARK 500 1 ASN A 100 -72.45 71.07
REMARK 500 1 ILE A 146 -30.26 -138.56
REMARK 500 1 ARG A 173 -164.62 52.67
REMARK 500 1 LEU A 174 85.23 55.55
REMARK 500 2 GLN A 30 -36.91 -131.22
REMARK 500 2 GLU A 35 93.90 60.85
REMARK 500 2 GLU A 36 43.34 -145.03
REMARK 500 2 ASN A 37 84.31 -164.93
REMARK 500 2 THR A 39 90.08 178.25
REMARK 500 2 ALA A 41 162.48 59.76
REMARK 500 2 GLU A 43 -60.27 -172.48
REMARK 500 2 SER A 47 16.40 59.03
REMARK 500 2 TYR A 65 -69.85 -95.71
REMARK 500 2 ARG A 66 -61.78 64.14
REMARK 500 2 THR A 79 159.33 62.80
REMARK 500 2 VAL A 99 -28.24 -172.83
REMARK 500 2 ASN A 100 -54.36 -133.41
REMARK 500 2 LEU A 138 -70.48 -66.65
REMARK 500 2 ILE A 146 -30.47 -136.37
REMARK 500 2 ASN A 162 96.49 -160.46
REMARK 500 2 GLN A 171 87.64 55.26
REMARK 500 3 SER A 2 -52.53 -178.12
REMARK 500 3 SER A 32 166.64 -49.96
REMARK 500 3 VAL A 34 -38.82 -147.19
REMARK 500 3 GLU A 35 171.65 58.10
REMARK 500 3 GLU A 36 -34.71 -169.22
REMARK 500 3 ASN A 37 161.51 59.38
REMARK 500 3 PRO A 42 -169.62 -64.45
REMARK 500 3 GLU A 43 63.51 62.05
REMARK 500 3 GLU A 46 31.26 -89.36
REMARK 500 3 SER A 47 12.36 -150.67
REMARK 500 3 TYR A 65 -71.94 -112.62
REMARK 500
REMARK 500 THIS ENTRY HAS 397 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 GLU A 60 0.12 SIDE CHAIN
REMARK 500 2 GLU A 36 0.07 SIDE CHAIN
REMARK 500 2 GLU A 40 0.08 SIDE CHAIN
REMARK 500 2 GLU A 56 0.08 SIDE CHAIN
REMARK 500 2 GLU A 60 0.10 SIDE CHAIN
REMARK 500 2 GLU A 62 0.09 SIDE CHAIN
REMARK 500 3 ASP A 15 0.10 SIDE CHAIN
REMARK 500 3 GLU A 62 0.08 SIDE CHAIN
REMARK 500 3 GLU A 166 0.10 SIDE CHAIN
REMARK 500 4 GLU A 35 0.07 SIDE CHAIN
REMARK 500 4 GLU A 60 0.07 SIDE CHAIN
REMARK 500 4 GLU A 62 0.08 SIDE CHAIN
REMARK 500 4 ASP A 120 0.08 SIDE CHAIN
REMARK 500 4 ASP A 140 0.08 SIDE CHAIN
REMARK 500 5 ASP A 15 0.10 SIDE CHAIN
REMARK 500 5 ASP A 33 0.10 SIDE CHAIN
REMARK 500 5 GLU A 62 0.10 SIDE CHAIN
REMARK 500 5 ASP A 71 0.07 SIDE CHAIN
REMARK 500 5 TYR A 159 0.07 SIDE CHAIN
REMARK 500 6 ASP A 15 0.10 SIDE CHAIN
REMARK 500 6 GLU A 35 0.07 SIDE CHAIN
REMARK 500 6 GLU A 43 0.07 SIDE CHAIN
REMARK 500 6 GLU A 60 0.08 SIDE CHAIN
REMARK 500 6 GLU A 62 0.10 SIDE CHAIN
REMARK 500 7 GLU A 11 0.11 SIDE CHAIN
REMARK 500 7 GLU A 35 0.09 SIDE CHAIN
REMARK 500 7 GLU A 36 0.09 SIDE CHAIN
REMARK 500 7 ASP A 59 0.12 SIDE CHAIN
REMARK 500 7 GLU A 166 0.14 SIDE CHAIN
REMARK 500 8 GLU A 11 0.08 SIDE CHAIN
REMARK 500 8 TYR A 26 0.07 SIDE CHAIN
REMARK 500 8 GLU A 60 0.07 SIDE CHAIN
REMARK 500 8 GLU A 62 0.09 SIDE CHAIN
REMARK 500 9 GLU A 11 0.08 SIDE CHAIN
REMARK 500 9 ASP A 59 0.07 SIDE CHAIN
REMARK 500 9 TYR A 65 0.08 SIDE CHAIN
REMARK 500 9 GLU A 172 0.08 SIDE CHAIN
REMARK 500 10 GLU A 36 0.10 SIDE CHAIN
REMARK 500 10 GLU A 40 0.07 SIDE CHAIN
REMARK 500 10 GLU A 43 0.07 SIDE CHAIN
REMARK 500 10 GLU A 48 0.07 SIDE CHAIN
REMARK 500 10 GLU A 56 0.09 SIDE CHAIN
REMARK 500 10 ASP A 59 0.10 SIDE CHAIN
REMARK 500 10 GLU A 172 0.08 SIDE CHAIN
REMARK 500 11 ASP A 33 0.07 SIDE CHAIN
REMARK 500 11 GLU A 36 0.08 SIDE CHAIN
REMARK 500 11 GLU A 122 0.09 SIDE CHAIN
REMARK 500 11 GLN A 147 0.07 SIDE CHAIN
REMARK 500 12 ASP A 15 0.08 SIDE CHAIN
REMARK 500 12 GLU A 48 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 101 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 GLU A 11 -11.40
REMARK 500 1 ARG A 64 -13.39
REMARK 500 1 TYR A 65 -10.98
REMARK 500 1 ASN A 100 -13.33
REMARK 500 1 GLN A 124 -10.13
REMARK 500 1 ASP A 153 -10.22
REMARK 500 2 GLY A 25 11.59
REMARK 500 2 GLU A 40 -12.76
REMARK 500 2 ASN A 100 -10.41
REMARK 500 3 GLU A 11 -12.96
REMARK 500 3 ALA A 165 -13.99
REMARK 500 4 ASN A 100 -12.42
REMARK 500 5 GLU A 11 -12.74
REMARK 500 5 PRO A 42 -10.45
REMARK 500 5 ASN A 100 -10.96
REMARK 500 5 ASP A 153 -10.35
REMARK 500 5 ARG A 173 -12.07
REMARK 500 5 GLU A 175 11.00
REMARK 500 6 ASP A 59 -10.48
REMARK 500 6 ASN A 100 -12.17
REMARK 500 6 GLU A 175 -12.91
REMARK 500 7 GLU A 11 -13.31
REMARK 500 7 GLN A 52 -10.43
REMARK 500 7 GLU A 56 -12.29
REMARK 500 7 ASN A 100 -11.83
REMARK 500 7 ALA A 165 -10.72
REMARK 500 7 GLY A 170 -10.50
REMARK 500 8 SER A 18 -10.22
REMARK 500 9 ARG A 66 -12.22
REMARK 500 9 ARG A 173 -12.38
REMARK 500 10 LEU A 21 -11.47
REMARK 500 10 TYR A 26 10.24
REMARK 500 10 TYR A 84 -10.01
REMARK 500 10 ASN A 100 -10.90
REMARK 500 10 ARG A 173 -12.22
REMARK 500 11 ARG A 66 10.49
REMARK 500 12 MET A 1 11.55
REMARK 500 12 GLN A 7 -10.39
REMARK 500 12 GLU A 11 -11.03
REMARK 500 12 SER A 27 -10.52
REMARK 500 12 ASN A 100 -12.16
REMARK 500 12 ASN A 161 -10.48
REMARK 500 13 THR A 82 10.16
REMARK 500 13 ASN A 100 -10.37
REMARK 500 14 GLU A 11 -11.28
REMARK 500 14 ASN A 100 -10.99
REMARK 500 15 GLU A 11 -11.35
REMARK 500 15 ARG A 38 -14.27
REMARK 500 15 ARG A 67 -12.75
REMARK 500 15 GLY A 160 -11.81
REMARK 500
REMARK 500 THIS ENTRY HAS 74 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2M04 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF BCL-XL IN COMPLEX WITH PUMA BH3 PEPTIDE
REMARK 900 RELATED ID: 4HNJ RELATED DB: PDB
REMARK 900 CRYSTALLOGRAPHIC STRUCTURE OF BCL-XL DOMAIN-SWAPPED DIMER IN
REMARK 900 COMPLEX WITH PUMA BH3 PEPTIDE AT 2.9A RESOLUTION
REMARK 900 RELATED ID: 18792 RELATED DB: BMRB
DBREF 2M03 A 5 173 UNP Q07817 B2CL1_HUMAN 1 209
SEQADV 2M03 MET A 1 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 SER A 2 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 MET A 3 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 ALA A 4 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 A UNP Q07817 MET 45 DELETION
SEQADV 2M03 A UNP Q07817 GLU 46 DELETION
SEQADV 2M03 A UNP Q07817 THR 47 DELETION
SEQADV 2M03 A UNP Q07817 PRO 48 DELETION
SEQADV 2M03 A UNP Q07817 SER 49 DELETION
SEQADV 2M03 A UNP Q07817 ALA 50 DELETION
SEQADV 2M03 A UNP Q07817 ILE 51 DELETION
SEQADV 2M03 A UNP Q07817 ASN 52 DELETION
SEQADV 2M03 A UNP Q07817 GLY 53 DELETION
SEQADV 2M03 A UNP Q07817 ASN 54 DELETION
SEQADV 2M03 A UNP Q07817 PRO 55 DELETION
SEQADV 2M03 A UNP Q07817 SER 56 DELETION
SEQADV 2M03 A UNP Q07817 TRP 57 DELETION
SEQADV 2M03 A UNP Q07817 HIS 58 DELETION
SEQADV 2M03 A UNP Q07817 LEU 59 DELETION
SEQADV 2M03 A UNP Q07817 ALA 60 DELETION
SEQADV 2M03 A UNP Q07817 ASP 61 DELETION
SEQADV 2M03 A UNP Q07817 SER 62 DELETION
SEQADV 2M03 A UNP Q07817 PRO 63 DELETION
SEQADV 2M03 A UNP Q07817 ALA 64 DELETION
SEQADV 2M03 A UNP Q07817 VAL 65 DELETION
SEQADV 2M03 A UNP Q07817 ASN 66 DELETION
SEQADV 2M03 A UNP Q07817 GLY 67 DELETION
SEQADV 2M03 A UNP Q07817 ALA 68 DELETION
SEQADV 2M03 A UNP Q07817 THR 69 DELETION
SEQADV 2M03 A UNP Q07817 GLY 70 DELETION
SEQADV 2M03 A UNP Q07817 HIS 71 DELETION
SEQADV 2M03 A UNP Q07817 SER 72 DELETION
SEQADV 2M03 A UNP Q07817 SER 73 DELETION
SEQADV 2M03 A UNP Q07817 SER 74 DELETION
SEQADV 2M03 A UNP Q07817 LEU 75 DELETION
SEQADV 2M03 A UNP Q07817 ASP 76 DELETION
SEQADV 2M03 A UNP Q07817 ALA 77 DELETION
SEQADV 2M03 A UNP Q07817 ARG 78 DELETION
SEQADV 2M03 A UNP Q07817 GLU 79 DELETION
SEQADV 2M03 A UNP Q07817 VAL 80 DELETION
SEQADV 2M03 A UNP Q07817 ILE 81 DELETION
SEQADV 2M03 A UNP Q07817 PRO 82 DELETION
SEQADV 2M03 A UNP Q07817 MET 83 DELETION
SEQADV 2M03 A UNP Q07817 ALA 84 DELETION
SEQADV 2M03 LEU A 174 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 GLU A 175 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 HIS A 176 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 HIS A 177 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 HIS A 178 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 HIS A 179 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 HIS A 180 UNP Q07817 EXPRESSION TAG
SEQADV 2M03 HIS A 181 UNP Q07817 EXPRESSION TAG
SEQRES 1 A 181 MET SER MET ALA MET SER GLN SER ASN ARG GLU LEU VAL
SEQRES 2 A 181 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR
SEQRES 3 A 181 SER TRP SER GLN PHE SER ASP VAL GLU GLU ASN ARG THR
SEQRES 4 A 181 GLU ALA PRO GLU GLY THR GLU SER GLU ALA VAL LYS GLN
SEQRES 5 A 181 ALA LEU ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR
SEQRES 6 A 181 ARG ARG ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE
SEQRES 7 A 181 THR PRO GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL
SEQRES 8 A 181 ASN GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE
SEQRES 9 A 181 VAL ALA PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU
SEQRES 10 A 181 SER VAL ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE
SEQRES 11 A 181 ALA ALA TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU
SEQRES 12 A 181 PRO TRP ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL
SEQRES 13 A 181 GLU LEU TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS
SEQRES 14 A 181 GLY GLN GLU ARG LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 MET A 5 LYS A 24 1 20
HELIX 2 2 SER A 27 PHE A 31 5 5
HELIX 3 3 SER A 47 TYR A 65 1 19
HELIX 4 4 TYR A 65 LEU A 76 1 12
HELIX 5 5 ALA A 83 PHE A 95 1 13
HELIX 6 6 GLY A 102 LYS A 121 1 20
HELIX 7 7 MET A 123 GLY A 151 1 29
HELIX 8 8 GLY A 151 LEU A 158 1 8
HELIX 9 9 ALA A 163 ARG A 168 1 6
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
(ATOM LINES ARE NOT SHOWN.)
END