Header list of 1d2l.pdb file
Complete list - c 21 2 Bytes
HEADER SIGNALING PROTEIN 24-SEP-99 1D2L
TITLE NMR SOLUTION STRUCTURE OF COMPLEMENT-LIKE REPEAT CR3 FROM THE LOW
TITLE 2 DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN (LRP). EVIDENCE FOR
TITLE 3 SPECIFIC BINDING TO THE RECEPTOR BINDING DOMAIN OF HUMAN ALPHA-2
TITLE 4 MACROGLOBULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN RECEPTOR RELATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COMPLEMENT-LIKE REPEAT 3 (CR3);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS LIGAND BINDING, CALCIUM BINDING, COMPLEMENT-LIKE REPEAT, RECEPTOR,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.DOLMER,W.HUANG,P.G.W.GETTINS
REVDAT 6 21-DEC-22 1D2L 1 SEQADV
REVDAT 5 16-FEB-22 1D2L 1 REMARK LINK
REVDAT 4 24-FEB-09 1D2L 1 VERSN
REVDAT 3 01-APR-03 1D2L 1 JRNL
REVDAT 2 21-FEB-00 1D2L 1 JRNL
REVDAT 1 14-JAN-00 1D2L 0
JRNL AUTH K.DOLMER,W.HUANG,P.G.GETTINS
JRNL TITL NMR SOLUTION STRUCTURE OF COMPLEMENT-LIKE REPEAT CR3 FROM
JRNL TITL 2 THE LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN.
JRNL TITL 3 EVIDENCE FOR SPECIFIC BINDING TO THE RECEPTOR BINDING DOMAIN
JRNL TITL 4 OF HUMAN ALPHA(2)-MACROGLOBULIN.
JRNL REF J.BIOL.CHEM. V. 275 3264 2000
JRNL REFN ISSN 0021-9258
JRNL PMID 10652313
JRNL DOI 10.1074/JBC.275.5.3264
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SYBYL 6.3, AMBER 5.0
REMARK 3 AUTHORS : TRIPOS INC. (SYBYL), CASE, D. A., ET AL. (1997)
REMARK 3 AMBER 5, UNIV. OF CALIFORNIA, SAN FRANCISCO,
REMARK 3 UNPUBLISHED (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 602 NOE
REMARK 3 CONSTRAINTS, 9 DISTANCE CONSTRAINTS FOR THE CALCIUM BINDING SITE,
REMARK 3 3 DISULFIDE BRIDGES, 10 HYDROGEN BONDS AND FIVE DIHEDRAL ANGLE
REMARK 3 CONSTRAINTS.
REMARK 4
REMARK 4 1D2L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009736.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 20 MM NA-D3-ACETATE, 10 MM CACL2
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM CR3 U-15N,13C 20 MM NA-D3
REMARK 210 -ACETATE PH 5.5 10 MM CACL 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED TOCSY; 3D_13C
REMARK 210 -SEPARATED TOCSY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; HBHA(CO)NH;
REMARK 210 CBCA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, PROFIT 1.8
REMARK 210 METHOD USED : MOLECULAR DYNAMICS ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. 20 STRUCTURES IN THE DEPOSITION WERE FITTED BY
REMARK 210 FITTING STRUCTURES 2-20 TO THE FIRST, USING PROFIT V1.8
REMARK 210 (MCLACHLAN, A. D., 1982 ACTA. CRYST.A38, 871-3) AS IMPLEMENTED
REMARK 210 IN THE PROGRAM PROFIT (MARTIN, A. C. R.,HTTP://
REMARK 210 WWW.BIOCHEM.UCL.AC.UK/~MARTIN/PROGRAMS/#PROFIT)
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 OD1 ASP A 33 HG SER A 35 1.31
REMARK 500 O TRP A 23 OD2 ASP A 36 1.85
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 CYS A 18 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 CYS A 25 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 1 ASP A 30 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 1 CYS A 31 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 1 ASP A 36 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 CYS A 18 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 4 CYS A 18 CA - CB - SG ANGL. DEV. = 7.2 DEGREES
REMARK 500 4 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 CYS A 18 CA - CB - SG ANGL. DEV. = 8.0 DEGREES
REMARK 500 5 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 CYS A 25 CA - CB - SG ANGL. DEV. = 7.9 DEGREES
REMARK 500 6 CYS A 18 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 6 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 CYS A 18 CA - CB - SG ANGL. DEV. = 8.2 DEGREES
REMARK 500 8 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 8 ASP A 36 CB - CG - OD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 9 CYS A 18 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 9 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 9 CYS A 25 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 10 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 11 CYS A 18 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 11 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 11 CYS A 25 CA - CB - SG ANGL. DEV. = 7.7 DEGREES
REMARK 500 12 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 CYS A 18 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 13 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 13 CYS A 18 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 13 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ASP A 30 C - N - CA ANGL. DEV. = 17.0 DEGREES
REMARK 500 13 ASP A 36 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 14 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 15 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 15 ASP A 30 C - N - CA ANGL. DEV. = 17.4 DEGREES
REMARK 500 16 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 16 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 16 CYS A 25 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 16 ASP A 30 C - N - CA ANGL. DEV. = 17.1 DEGREES
REMARK 500 16 ASP A 36 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 17 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 CYS A 18 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 17 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 17 ASP A 30 C - N - CA ANGL. DEV. = 17.9 DEGREES
REMARK 500 18 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 18 CYS A 31 CA - CB - SG ANGL. DEV. = 6.9 DEGREES
REMARK 500 19 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 19 CYS A 18 CA - CB - SG ANGL. DEV. = 7.3 DEGREES
REMARK 500 19 ARG A 22 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 19 ASP A 30 C - N - CA ANGL. DEV. = 17.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 56 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 GLN A 5 -11.48 81.48
REMARK 500 1 CYS A 6 -50.05 -162.94
REMARK 500 1 GLU A 10 -158.90 -133.29
REMARK 500 1 SER A 16 45.42 126.55
REMARK 500 1 ASP A 30 -60.89 59.61
REMARK 500 1 LEU A 32 -34.03 71.15
REMARK 500 1 PRO A 39 20.99 -69.89
REMARK 500 1 LEU A 41 -74.39 -120.61
REMARK 500 1 CYS A 42 -70.12 -139.92
REMARK 500 1 HIS A 43 86.19 63.87
REMARK 500 2 SER A 2 -36.27 105.66
REMARK 500 2 CYS A 6 -55.50 -120.93
REMARK 500 2 SER A 16 50.75 126.28
REMARK 500 2 LEU A 32 -36.55 62.37
REMARK 500 2 ASN A 34 74.56 59.70
REMARK 500 2 ASP A 36 -67.65 -28.60
REMARK 500 2 PRO A 39 21.66 -68.31
REMARK 500 2 LEU A 41 -80.50 -120.15
REMARK 500 2 CYS A 42 -54.36 -141.74
REMARK 500 2 HIS A 43 99.25 57.15
REMARK 500 3 SER A 2 -58.47 110.55
REMARK 500 3 SER A 16 53.78 128.03
REMARK 500 3 ASN A 29 -13.81 -29.29
REMARK 500 3 LEU A 32 -29.77 69.66
REMARK 500 3 PRO A 39 20.72 -69.12
REMARK 500 3 LEU A 41 -76.07 -123.66
REMARK 500 3 CYS A 42 -67.12 -139.74
REMARK 500 3 HIS A 43 -59.41 56.95
REMARK 500 3 GLN A 44 -65.59 59.45
REMARK 500 4 SER A 2 -56.17 -167.27
REMARK 500 4 SER A 16 48.49 128.36
REMARK 500 4 ASN A 29 52.83 -65.23
REMARK 500 4 LEU A 32 -34.51 63.60
REMARK 500 4 ASN A 34 86.41 56.97
REMARK 500 4 SER A 35 -61.77 -105.05
REMARK 500 4 ASP A 36 -67.46 -29.97
REMARK 500 4 PRO A 39 20.69 -68.09
REMARK 500 4 LEU A 41 -76.62 -125.76
REMARK 500 4 CYS A 42 -71.23 -138.53
REMARK 500 4 HIS A 43 96.07 58.19
REMARK 500 4 GLN A 44 68.57 -153.58
REMARK 500 5 GLN A 5 -27.38 85.41
REMARK 500 5 CYS A 6 -52.52 -152.93
REMARK 500 5 SER A 16 53.45 106.91
REMARK 500 5 ASN A 29 56.93 -67.77
REMARK 500 5 LEU A 32 -35.75 64.16
REMARK 500 5 ASN A 34 80.75 54.58
REMARK 500 5 SER A 35 -76.45 -86.12
REMARK 500 5 ASP A 36 -70.68 -22.49
REMARK 500 5 LEU A 41 -77.09 -125.57
REMARK 500
REMARK 500 THIS ENTRY HAS 234 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 CYS A 25 ASP A 26 2 145.55
REMARK 500 CYS A 25 ASP A 26 3 137.42
REMARK 500 ASN A 29 ASP A 30 3 -85.44
REMARK 500 CYS A 25 ASP A 26 4 133.09
REMARK 500 CYS A 25 ASP A 26 7 145.45
REMARK 500 ASN A 29 ASP A 30 7 -91.61
REMARK 500 ASN A 29 ASP A 30 8 146.95
REMARK 500 CYS A 25 ASP A 26 14 145.12
REMARK 500 ASN A 29 ASP A 30 14 -120.75
REMARK 500 CYS A 25 ASP A 26 15 140.46
REMARK 500 CYS A 25 ASP A 26 17 143.32
REMARK 500 GLU A 37 ALA A 38 17 148.31
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 5 ARG A 22 0.15 SIDE CHAIN
REMARK 500 9 ARG A 22 0.09 SIDE CHAIN
REMARK 500 16 ARG A 22 0.12 SIDE CHAIN
REMARK 500 19 ARG A 22 0.10 SIDE CHAIN
REMARK 500 20 ARG A 22 0.11 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 CA A 46 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A 23 O
REMARK 620 2 ASP A 26 OD1 113.5
REMARK 620 3 ASP A 28 O 154.5 92.0
REMARK 620 4 ASP A 30 OD2 93.4 59.0 101.0
REMARK 620 5 ASP A 36 OD2 45.7 158.0 108.9 120.8
REMARK 620 6 GLU A 37 OE2 66.2 110.9 104.9 152.7 58.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 46
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CR8 RELATED DB: PDB
REMARK 900 CR3 AND CR8 ARE FROM THE SAME CLUSTER OF COMPLEMENT-LIKE REPEATS
REMARK 900 FROM LRP
DBREF 1D2L A 3 45 UNP Q07954 LRP1_HUMAN 851 893
SEQADV 1D2L GLY A 1 UNP Q07954 CLONING ARTIFACT
SEQADV 1D2L SER A 2 UNP Q07954 CLONING ARTIFACT
SEQRES 1 A 45 GLY SER PRO PRO GLN CYS GLN PRO GLY GLU PHE ALA CYS
SEQRES 2 A 45 ALA ASN SER ARG CYS ILE GLN GLU ARG TRP LYS CYS ASP
SEQRES 3 A 45 GLY ASP ASN ASP CYS LEU ASP ASN SER ASP GLU ALA PRO
SEQRES 4 A 45 ALA LEU CYS HIS GLN HIS
HET CA A 46 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 GLN A 20 LYS A 24 5 5
SHEET 1 A 2 PHE A 11 CYS A 13 0
SHEET 2 A 2 ARG A 17 ILE A 19 -1 N ARG A 17 O CYS A 13
SSBOND 1 CYS A 6 CYS A 18 1555 1555 2.05
SSBOND 2 CYS A 13 CYS A 31 1555 1555 2.02
SSBOND 3 CYS A 25 CYS A 42 1555 1555 2.02
LINK O TRP A 23 CA CA A 46 1555 1555 2.41
LINK OD1 ASP A 26 CA CA A 46 1555 1555 2.37
LINK O ASP A 28 CA CA A 46 1555 1555 2.44
LINK OD2 ASP A 30 CA CA A 46 1555 1555 2.41
LINK OD2 ASP A 36 CA CA A 46 1555 1555 2.36
LINK OE2 GLU A 37 CA CA A 46 1555 1555 2.38
SITE 1 AC1 7 TRP A 23 ASP A 26 GLY A 27 ASP A 28
SITE 2 AC1 7 ASP A 30 ASP A 36 GLU A 37
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 - c 21 2 Bytes