Header list of 1mux.pdb file
Complete list - b 23 2 Bytes
HEADER CALCIUM-BINDING 06-SEP-97 1MUX
TITLE SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF
TITLE 2 DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PAS
KEYWDS COMPLEX (CALMODULIN-INHIBITOR), CALMODULIN, W-7,
KEYWDS 2 NAPHTHALENESULFONAMIDE, CALCIUM-BINDING
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR M.OSAWA,M.B.SWINDELLS,J.TANIKAWA,T.TANAKA,T.MASE,T.FURUYA,M.IKURA
REVDAT 4 23-FEB-22 1MUX 1 REMARK LINK
REVDAT 3 24-FEB-09 1MUX 1 VERSN
REVDAT 2 25-NOV-98 1MUX 1 COMPND REMARK TITLE HEADER
REVDAT 2 2 1 SOURCE FORMUL KEYWDS SHEET
REVDAT 1 14-OCT-98 1MUX 0
JRNL AUTH M.OSAWA,M.B.SWINDELLS,J.TANIKAWA,T.TANAKA,T.MASE,T.FURUYA,
JRNL AUTH 2 M.IKURA
JRNL TITL SOLUTION STRUCTURE OF CALMODULIN-W-7 COMPLEX: THE BASIS OF
JRNL TITL 2 DIVERSITY IN MOLECULAR RECOGNITION.
JRNL REF J.MOL.BIOL. V. 276 165 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9514729
JRNL DOI 10.1006/JMBI.1997.1524
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MUX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175172.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : KCL, 100MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: DUE TO THE LACK OF NOE'S BETWEEN THE N- AND C- TERMINAL
REMARK 210 DOMAINS, IT IS IMPOSSIBLE TO SUPERIMPOSE BOTH DOMAINS OF THE 30
REMARK 210 NMR-DERIVED STRUCTURES SIMULTANEOOUSLY. HENCE, THE BACKBONE
REMARK 210 ATOMS OF THE C-TERMINAL DOMAIN HAVE HAVE BEEN SUPERIMPOSED.
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 H GLY A 132 CA CA A 152 1.42
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 LYS A 21 47.61 -109.60
REMARK 500 1 ASP A 22 22.22 -162.44
REMARK 500 1 ASP A 24 -36.83 -134.91
REMARK 500 1 LEU A 39 -78.35 -89.16
REMARK 500 1 ASN A 42 48.60 -143.04
REMARK 500 1 PRO A 43 -159.25 -68.80
REMARK 500 1 ASP A 58 -34.12 -141.54
REMARK 500 1 ASP A 64 -162.97 -112.58
REMARK 500 1 ARG A 74 -81.56 -84.14
REMARK 500 1 LYS A 75 -87.11 -107.43
REMARK 500 1 MET A 76 -40.48 80.14
REMARK 500 1 GLU A 114 -156.20 -116.19
REMARK 500 1 LYS A 115 84.05 -161.03
REMARK 500 1 ASP A 133 100.49 59.96
REMARK 500 1 ASN A 137 -168.77 -129.95
REMARK 500 1 ALA A 147 128.40 -175.16
REMARK 500 2 LEU A 4 32.02 -97.02
REMARK 500 2 THR A 28 -162.82 -108.80
REMARK 500 2 ASN A 42 -64.93 -159.85
REMARK 500 2 THR A 44 -137.79 -90.33
REMARK 500 2 ALA A 57 46.53 -93.41
REMARK 500 2 ASP A 58 -66.49 -132.02
REMARK 500 2 ASN A 60 -46.41 -142.06
REMARK 500 2 ARG A 74 45.96 -108.82
REMARK 500 2 LYS A 75 45.77 -146.06
REMARK 500 2 SER A 81 59.99 -155.15
REMARK 500 2 GLU A 83 85.34 46.13
REMARK 500 2 ASP A 93 67.63 -108.67
REMARK 500 2 ASN A 97 -75.87 -80.78
REMARK 500 2 LYS A 115 106.99 55.74
REMARK 500 3 LEU A 4 -162.54 -57.12
REMARK 500 3 ASP A 24 -46.30 -158.01
REMARK 500 3 LEU A 39 -69.72 -95.39
REMARK 500 3 GLN A 41 -56.50 -175.82
REMARK 500 3 PRO A 43 -163.04 -74.85
REMARK 500 3 VAL A 55 -72.72 -74.35
REMARK 500 3 ASP A 56 98.62 -52.03
REMARK 500 3 ASN A 60 -60.68 -169.39
REMARK 500 3 ASP A 64 -162.79 -109.02
REMARK 500 3 LYS A 75 132.29 60.79
REMARK 500 3 ASP A 78 75.46 -150.36
REMARK 500 3 ASP A 80 115.38 57.11
REMARK 500 3 SER A 81 74.12 -104.50
REMARK 500 3 GLU A 83 101.02 -177.11
REMARK 500 3 LYS A 115 47.60 -149.15
REMARK 500 3 ASP A 129 93.58 -68.29
REMARK 500 3 GLN A 135 137.36 -170.96
REMARK 500 4 THR A 5 -66.39 -156.64
REMARK 500 4 PHE A 19 -67.98 -92.74
REMARK 500 4 LYS A 21 42.54 -109.39
REMARK 500
REMARK 500 THIS ENTRY HAS 430 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 37 0.11 SIDE CHAIN
REMARK 500 1 ARG A 74 0.32 SIDE CHAIN
REMARK 500 1 ARG A 86 0.21 SIDE CHAIN
REMARK 500 1 ARG A 90 0.31 SIDE CHAIN
REMARK 500 1 ARG A 106 0.31 SIDE CHAIN
REMARK 500 1 ARG A 126 0.32 SIDE CHAIN
REMARK 500 2 ARG A 37 0.28 SIDE CHAIN
REMARK 500 2 ARG A 74 0.11 SIDE CHAIN
REMARK 500 2 ARG A 86 0.29 SIDE CHAIN
REMARK 500 2 ARG A 90 0.27 SIDE CHAIN
REMARK 500 2 ARG A 106 0.24 SIDE CHAIN
REMARK 500 2 ARG A 126 0.32 SIDE CHAIN
REMARK 500 3 ARG A 37 0.21 SIDE CHAIN
REMARK 500 3 ARG A 74 0.30 SIDE CHAIN
REMARK 500 3 ARG A 86 0.32 SIDE CHAIN
REMARK 500 3 ARG A 90 0.26 SIDE CHAIN
REMARK 500 3 ARG A 106 0.29 SIDE CHAIN
REMARK 500 3 ARG A 126 0.20 SIDE CHAIN
REMARK 500 4 ARG A 37 0.32 SIDE CHAIN
REMARK 500 4 ARG A 74 0.12 SIDE CHAIN
REMARK 500 4 ARG A 86 0.32 SIDE CHAIN
REMARK 500 4 ARG A 90 0.17 SIDE CHAIN
REMARK 500 4 ARG A 106 0.30 SIDE CHAIN
REMARK 500 4 ARG A 126 0.32 SIDE CHAIN
REMARK 500 5 ARG A 37 0.22 SIDE CHAIN
REMARK 500 5 ARG A 74 0.17 SIDE CHAIN
REMARK 500 5 ARG A 86 0.32 SIDE CHAIN
REMARK 500 5 ARG A 90 0.26 SIDE CHAIN
REMARK 500 5 ARG A 106 0.28 SIDE CHAIN
REMARK 500 5 ARG A 126 0.26 SIDE CHAIN
REMARK 500 6 ARG A 37 0.32 SIDE CHAIN
REMARK 500 6 ARG A 74 0.16 SIDE CHAIN
REMARK 500 6 ARG A 86 0.22 SIDE CHAIN
REMARK 500 6 ARG A 90 0.32 SIDE CHAIN
REMARK 500 6 ARG A 126 0.27 SIDE CHAIN
REMARK 500 7 ARG A 37 0.27 SIDE CHAIN
REMARK 500 7 ARG A 74 0.22 SIDE CHAIN
REMARK 500 7 ARG A 86 0.31 SIDE CHAIN
REMARK 500 7 ARG A 90 0.32 SIDE CHAIN
REMARK 500 7 ARG A 106 0.20 SIDE CHAIN
REMARK 500 7 ARG A 126 0.17 SIDE CHAIN
REMARK 500 8 ARG A 37 0.26 SIDE CHAIN
REMARK 500 8 ARG A 74 0.30 SIDE CHAIN
REMARK 500 8 ARG A 86 0.15 SIDE CHAIN
REMARK 500 8 ARG A 90 0.25 SIDE CHAIN
REMARK 500 8 ARG A 106 0.32 SIDE CHAIN
REMARK 500 8 ARG A 126 0.29 SIDE CHAIN
REMARK 500 9 ARG A 37 0.32 SIDE CHAIN
REMARK 500 9 ARG A 74 0.22 SIDE CHAIN
REMARK 500 9 ARG A 86 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 176 PLANE DEVIATIONS.
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 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD2
REMARK 620 2 ASP A 22 OD1 75.7
REMARK 620 3 ASP A 22 OD2 112.2 46.0
REMARK 620 4 ASP A 24 CB 82.0 104.9 83.1
REMARK 620 5 ASP A 24 OD2 127.1 139.5 94.0 55.6
REMARK 620 6 THR A 26 O 72.8 126.1 164.4 112.4 94.1
REMARK 620 7 GLU A 31 OE2 116.6 56.9 62.5 144.8 116.2 101.9
REMARK 620 8 GLU A 31 OE1 77.9 71.2 105.5 159.8 139.5 60.3 50.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD2 61.9
REMARK 620 3 ASN A 60 OD1 62.5 81.6
REMARK 620 4 ASN A 60 ND2 103.2 93.9 41.3
REMARK 620 5 THR A 62 O 100.2 145.0 63.4 59.2
REMARK 620 6 ASP A 64 OD1 172.5 113.3 112.0 70.8 80.7
REMARK 620 7 GLU A 67 OE1 142.0 113.3 154.8 114.9 99.2 44.3
REMARK 620 8 GLU A 67 OE2 99.4 78.9 158.2 149.5 135.8 84.8 45.8
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 74.3
REMARK 620 3 ASN A 97 OD1 77.2 60.1
REMARK 620 4 TYR A 99 O 120.0 137.4 82.9
REMARK 620 5 GLU A 104 OE1 143.1 122.6 139.4 72.0
REMARK 620 6 GLU A 104 OE2 135.5 76.7 115.3 104.2 46.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 GLY A 132 N 177.5
REMARK 620 3 GLY A 132 CA 137.3 45.1
REMARK 620 4 ASP A 133 N 93.0 88.9 67.6
REMARK 620 5 GLU A 140 OE1 56.7 121.9 123.5 146.6
REMARK 620 6 GLU A 140 OE2 83.6 94.0 130.4 153.1 47.2
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 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WW7 A 153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WW7 A 154
DBREF 1MUX A 1 148 UNP P62155 CALM_XENLA 1 148
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HET CA A 152 1
HET WW7 A 153 43
HET WW7 A 154 43
HETNAM CA CALCIUM ION
HETNAM WW7 N-(6-AMINOHEXYL)-5-CHLORO-1-NAPHTHALENESULFONAMIDE
FORMUL 2 CA 4(CA 2+)
FORMUL 6 WW7 2(C16 H21 CL N2 O2 S)
HELIX 1 1 GLU A 6 PHE A 19 1 14
HELIX 2 2 THR A 29 SER A 38 1 10
HELIX 3 3 GLU A 45 ASN A 53 1 9
HELIX 4 4 PHE A 65 ARG A 74 1 10
HELIX 5 5 ILE A 85 PHE A 92 1 8
HELIX 6 6 ALA A 102 ASN A 111 1 10
HELIX 7 7 ASP A 118 GLU A 127 1 10
HELIX 8 8 TYR A 138 MET A 145 1 8
SHEET 1 1 4 THR A 26 THR A 28 0
SHEET 2 1 4 THR A 62 ASP A 64 -1
SHEET 3 1 4 TYR A 99 SER A 101 -1
SHEET 4 1 4 GLN A 135 ASN A 137 -1
LINK OD2 ASP A 20 CA CA A 149 1555 1555 2.82
LINK OD1 ASP A 22 CA CA A 149 1555 1555 2.84
LINK OD2 ASP A 22 CA CA A 149 1555 1555 2.66
LINK CB ASP A 24 CA CA A 149 1555 1555 2.00
LINK OD2 ASP A 24 CA CA A 149 1555 1555 2.82
LINK O THR A 26 CA CA A 149 1555 1555 2.83
LINK OE2 GLU A 31 CA CA A 149 1555 1555 1.82
LINK OE1 GLU A 31 CA CA A 149 1555 1555 2.81
LINK OD1 ASP A 56 CA CA A 150 1555 1555 2.74
LINK OD2 ASP A 58 CA CA A 150 1555 1555 1.87
LINK OD1 ASN A 60 CA CA A 150 1555 1555 2.79
LINK ND2 ASN A 60 CA CA A 150 1555 1555 3.26
LINK O THR A 62 CA CA A 150 1555 1555 2.64
LINK OD1 ASP A 64 CA CA A 150 1555 1555 3.36
LINK OE1 GLU A 67 CA CA A 150 1555 1555 2.68
LINK OE2 GLU A 67 CA CA A 150 1555 1555 2.83
LINK OD1 ASP A 93 CA CA A 151 1555 1555 2.82
LINK OD1 ASP A 95 CA CA A 151 1555 1555 2.21
LINK OD1 ASN A 97 CA CA A 151 1555 1555 2.60
LINK O TYR A 99 CA CA A 151 1555 1555 2.65
LINK OE1 GLU A 104 CA CA A 151 1555 1555 2.82
LINK OE2 GLU A 104 CA CA A 151 1555 1555 2.69
LINK OD1 ASP A 129 CA CA A 152 1555 1555 2.87
LINK N GLY A 132 CA CA A 152 1555 1555 1.87
LINK CA GLY A 132 CA CA A 152 1555 1555 2.00
LINK N ASP A 133 CA CA A 152 1555 1555 2.30
LINK OE1 GLU A 140 CA CA A 152 1555 1555 2.84
LINK OE2 GLU A 140 CA CA A 152 1555 1555 2.43
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 ASP A 64 GLU A 67
SITE 1 AC3 6 PHE A 92 ASP A 93 ASP A 95 ASN A 97
SITE 2 AC3 6 TYR A 99 GLU A 104
SITE 1 AC4 6 ASP A 129 ASP A 131 GLY A 132 ASP A 133
SITE 2 AC4 6 GLN A 135 GLU A 140
SITE 1 AC5 8 PHE A 19 LEU A 32 LEU A 39 MET A 51
SITE 2 AC5 8 ILE A 52 ILE A 63 PHE A 68 MET A 72
SITE 1 AC6 10 GLU A 83 GLU A 84 GLU A 87 PHE A 92
SITE 2 AC6 10 LEU A 105 ILE A 125 ALA A 128 PHE A 141
SITE 3 AC6 10 MET A 144 MET A 145
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