Header list of 1cr8.pdb file
Complete list - 16 20 Bytes
HEADER LIPID BINDING PROTEIN 14-DEC-98 1CR8
TITLE LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN COMPLEMENT REPEAT 8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COMPLEMENT REPEAT 8;
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 ORGAN: LIVER, PLACENTA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: BL21;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS RECEPTOR, LIGAND BINDING, CALCIUM BINDING, LDLR, LRP, LIPID BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.HUANG,K.DOLMER,P.G.W.GETTINS
REVDAT 6 16-FEB-22 1CR8 1 REMARK LINK
REVDAT 5 24-FEB-09 1CR8 1 VERSN
REVDAT 4 01-APR-03 1CR8 1 JRNL
REVDAT 3 29-DEC-99 1CR8 4 HEADER COMPND REMARK JRNL
REVDAT 3 2 4 ATOM SOURCE SEQRES
REVDAT 2 06-JAN-99 1CR8 3 HET REMARK HETATM SEQRES
REVDAT 2 2 3 FORMUL EXPDTA SSBOND HETNAM
REVDAT 1 23-DEC-98 1CR8 0
JRNL AUTH W.HUANG,K.DOLMER,P.G.GETTINS
JRNL TITL NMR SOLUTION STRUCTURE OF COMPLEMENT-LIKE REPEAT CR8 FROM
JRNL TITL 2 THE LOW DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN.
JRNL REF J.BIOL.CHEM. V. 274 14130 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10318830
JRNL DOI 10.1074/JBC.274.20.14130
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ENERGY MINIMIZATION
REMARK 4
REMARK 4 1CR8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-98.
REMARK 100 THE DEPOSITION ID IS D_1000000276.
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 : 0.05
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY-HSQC; TOCSY-HSQC; HCCH-
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : DYNAMICS ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 FIRST. N-15 EDITED TOCSY-HSQC, NOESY-HSQC, HNHA C-13 EDITED HCCH-
REMARK 210 TOCSY, HCCH-
REMARK 210 NOESY, TRIPLE RESONANCE HNCA, HBHA(CO)NH
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 34 HG SER A 35 1.35
REMARK 500 OD2 ASP A 34 HG SER A 36 1.36
REMARK 500 HG1 THR A 8 OD1 ASP A 9 1.48
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 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -18.9 DEGREES
REMARK 500 1 ASP A 31 CB - CG - OD1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 1 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 2 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -20.4 DEGREES
REMARK 500 2 ASP A 31 CB - CG - OD1 ANGL. DEV. = 16.0 DEGREES
REMARK 500 2 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -19.8 DEGREES
REMARK 500 2 GLU A 38 CG - CD - OE2 ANGL. DEV. = 14.4 DEGREES
REMARK 500 3 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 3 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -21.1 DEGREES
REMARK 500 3 ASP A 31 CB - CG - OD1 ANGL. DEV. = 16.3 DEGREES
REMARK 500 3 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -11.0 DEGREES
REMARK 500 4 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -18.9 DEGREES
REMARK 500 4 ASP A 31 CB - CG - OD1 ANGL. DEV. = 14.9 DEGREES
REMARK 500 4 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -20.0 DEGREES
REMARK 500 4 GLU A 38 CG - CD - OE2 ANGL. DEV. = 13.6 DEGREES
REMARK 500 5 ASP A 27 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -19.2 DEGREES
REMARK 500 5 ASP A 31 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 5 ASP A 31 CB - CG - OD2 ANGL. DEV. = 12.9 DEGREES
REMARK 500 5 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 6 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -19.1 DEGREES
REMARK 500 6 ASP A 31 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 6 ASP A 31 CB - CG - OD2 ANGL. DEV. = 13.0 DEGREES
REMARK 500 6 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -12.7 DEGREES
REMARK 500 7 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -19.6 DEGREES
REMARK 500 7 ASP A 31 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 7 ASP A 31 CB - CG - OD2 ANGL. DEV. = 13.4 DEGREES
REMARK 500 7 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -13.4 DEGREES
REMARK 500 8 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 8 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -21.4 DEGREES
REMARK 500 8 ASP A 31 CB - CG - OD1 ANGL. DEV. = 17.1 DEGREES
REMARK 500 8 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 9 ARG A 14 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -19.1 DEGREES
REMARK 500 9 ASP A 31 CB - CG - OD1 ANGL. DEV. = 13.8 DEGREES
REMARK 500 9 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 10 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -19.8 DEGREES
REMARK 500 10 ASP A 31 CB - CG - OD1 ANGL. DEV. = 14.7 DEGREES
REMARK 500 10 CYS A 32 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 10 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -9.4 DEGREES
REMARK 500 11 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 11 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -21.4 DEGREES
REMARK 500 11 ASP A 31 CB - CG - OD1 ANGL. DEV. = 17.1 DEGREES
REMARK 500 11 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 12 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -18.4 DEGREES
REMARK 500 12 ASP A 31 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 12 ASP A 31 CB - CG - OD2 ANGL. DEV. = 12.6 DEGREES
REMARK 500 12 GLU A 38 OE1 - CD - OE2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 13 ASP A 31 OD1 - CG - OD2 ANGL. DEV. = -21.1 DEGREES
REMARK 500 13 ASP A 31 CB - CG - OD1 ANGL. DEV. = 16.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 83 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 CYS A 6 -73.24 -114.09
REMARK 500 1 THR A 8 104.21 -46.05
REMARK 500 1 ASP A 9 12.82 54.06
REMARK 500 1 ASP A 16 -42.66 -151.13
REMARK 500 1 CYS A 26 57.02 -170.49
REMARK 500 1 MET A 33 1.71 -55.23
REMARK 500 1 ASP A 34 -69.26 -139.91
REMARK 500 1 SER A 35 -16.49 163.11
REMARK 500 1 GLU A 38 -0.34 -149.55
REMARK 500 1 LYS A 39 10.88 -57.12
REMARK 500 1 SER A 40 20.46 -151.81
REMARK 500 2 HIS A 7 -163.84 -166.87
REMARK 500 2 THR A 8 47.21 -62.11
REMARK 500 2 ASP A 9 -0.73 123.73
REMARK 500 2 LEU A 15 -71.62 -113.09
REMARK 500 2 CYS A 26 79.43 -169.98
REMARK 500 2 ASP A 27 -48.78 -146.75
REMARK 500 2 ASP A 34 -105.06 -83.46
REMARK 500 2 SER A 35 6.96 -168.54
REMARK 500 2 LYS A 39 26.27 -61.57
REMARK 500 2 SER A 40 33.69 -160.60
REMARK 500 3 CYS A 6 -65.61 -125.89
REMARK 500 3 THR A 8 105.59 -48.24
REMARK 500 3 ASP A 9 11.20 53.32
REMARK 500 3 ARG A 23 -13.03 -46.98
REMARK 500 3 CYS A 26 70.50 -177.72
REMARK 500 3 ASP A 27 -36.06 -131.22
REMARK 500 3 MET A 33 -19.10 -49.47
REMARK 500 3 ASP A 34 -93.76 -100.83
REMARK 500 3 SER A 35 -0.59 -171.34
REMARK 500 3 GLU A 38 5.83 -151.54
REMARK 500 3 LYS A 39 19.12 -59.88
REMARK 500 3 SER A 40 20.54 -143.73
REMARK 500 4 CYS A 6 -71.86 -109.57
REMARK 500 4 THR A 8 101.32 -43.68
REMARK 500 4 ASP A 9 12.22 51.97
REMARK 500 4 ASP A 16 -72.33 -143.45
REMARK 500 4 ARG A 25 44.75 -83.37
REMARK 500 4 CYS A 26 22.15 -175.12
REMARK 500 4 MET A 33 12.91 -53.84
REMARK 500 4 ASP A 34 -99.86 -142.96
REMARK 500 4 SER A 35 -8.69 -172.32
REMARK 500 4 LYS A 39 2.50 -50.80
REMARK 500 4 SER A 40 10.41 -146.65
REMARK 500 4 CYS A 41 48.13 -88.92
REMARK 500 4 GLU A 42 77.45 48.19
REMARK 500 5 CYS A 6 -71.67 -124.49
REMARK 500 5 THR A 8 104.54 -48.20
REMARK 500 5 ASP A 9 14.21 52.74
REMARK 500 5 ARG A 23 -15.14 -48.34
REMARK 500
REMARK 500 THIS ENTRY HAS 213 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 ASP A 29 THR A 30 1 -141.45
REMARK 500 ASP A 29 THR A 30 2 -140.82
REMARK 500 SER A 36 ASP A 37 2 139.50
REMARK 500 ASP A 37 GLU A 38 2 -146.43
REMARK 500 SER A 36 ASP A 37 3 146.10
REMARK 500 SER A 36 ASP A 37 4 142.30
REMARK 500 ASP A 31 CYS A 32 5 144.51
REMARK 500 TRP A 24 ARG A 25 6 148.17
REMARK 500 ASP A 31 CYS A 32 6 148.14
REMARK 500 LEU A 22 ARG A 23 7 148.25
REMARK 500 ASP A 31 CYS A 32 7 145.95
REMARK 500 SER A 36 ASP A 37 8 147.58
REMARK 500 ASP A 29 THR A 30 9 -146.24
REMARK 500 SER A 36 ASP A 37 9 149.58
REMARK 500 LEU A 22 ARG A 23 10 149.22
REMARK 500 ASP A 29 THR A 30 10 -140.73
REMARK 500 SER A 36 ASP A 37 11 149.23
REMARK 500 SER A 36 ASP A 37 12 144.40
REMARK 500 SER A 36 ASP A 37 13 146.25
REMARK 500 ASP A 31 CYS A 32 14 148.14
REMARK 500 SER A 36 ASP A 37 14 148.57
REMARK 500 GLY A 28 ASP A 29 15 149.50
REMARK 500 ASP A 29 THR A 30 15 -141.66
REMARK 500 SER A 36 ASP A 37 16 149.61
REMARK 500 ASP A 37 GLU A 38 17 -147.89
REMARK 500 GLU A 10 PHE A 11 18 -149.93
REMARK 500 ASP A 29 THR A 30 18 -128.16
REMARK 500 SER A 36 ASP A 37 18 139.01
REMARK 500 SER A 36 ASP A 37 19 147.96
REMARK 500 LEU A 22 ARG A 23 20 149.93
REMARK 500 SER A 36 ASP A 37 20 143.14
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 8 ARG A 23 0.08 SIDE CHAIN
REMARK 500 16 ARG A 25 0.11 SIDE CHAIN
REMARK 500 20 ARG A 23 0.09 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 45 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TRP A 24 O
REMARK 620 2 ASP A 27 OD2 89.8
REMARK 620 3 ASP A 29 O 139.9 64.0
REMARK 620 4 ASP A 31 OD1 110.0 101.2 104.7
REMARK 620 5 ASP A 37 OD2 80.6 167.9 119.9 89.0
REMARK 620 6 GLU A 38 OE2 89.0 88.7 62.4 158.4 83.9
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 45
DBREF 1CR8 A 3 44 UNP Q07954 LRP1_HUMAN 1059 1100
SEQRES 1 A 42 PRO GLY GLY CYS HIS THR ASP GLU PHE GLN CYS ARG LEU
SEQRES 2 A 42 ASP GLY LEU CYS ILE PRO LEU ARG TRP ARG CYS ASP GLY
SEQRES 3 A 42 ASP THR ASP CYS MET ASP SER SER ASP GLU LYS SER CYS
SEQRES 4 A 42 GLU GLY VAL
HET CA A 45 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 H1 LEU A 22 ARG A 25 1 4
SHEET 1 S1 1 PHE A 11 CYS A 13 0
SHEET 1 S2 1 LEU A 18 ILE A 20 0
SSBOND 1 CYS A 6 CYS A 19 1555 1555 2.03
SSBOND 2 CYS A 13 CYS A 32 1555 1555 2.01
SSBOND 3 CYS A 26 CYS A 41 1555 1555 2.05
LINK O TRP A 24 CA CA A 45 1555 1555 2.38
LINK OD2 ASP A 27 CA CA A 45 1555 1555 2.40
LINK O ASP A 29 CA CA A 45 1555 1555 2.38
LINK OD1 ASP A 31 CA CA A 45 1555 1555 2.41
LINK OD2 ASP A 37 CA CA A 45 1555 1555 2.40
LINK OE2 GLU A 38 CA CA A 45 1555 1555 2.39
SITE 1 AC1 6 TRP A 24 ASP A 27 ASP A 29 ASP A 31
SITE 2 AC1 6 ASP A 37 GLU A 38
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 - 16 20 Bytes