Header list of 1cff.pdb file
Complete list - g 29 2 Bytes
HEADER CALMODULIN 18-MAR-99 1CFF
TITLE NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING
TITLE 2 PEPTIDE OF THE CA2+-PUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CALCIUM PUMP;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: CAM-BINDING DOMAIN;
COMPND 10 EC: 3.6.1.38;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: 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 STRAIN: 71;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: AR58;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PTNCO12;
SOURCE 11 EXPRESSION_SYSTEM_GENE: CALMODULIN;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS CALMODULIN, C20W, PLASMA MEMBRANE CALCIUM PUMP
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR B.ELSHORST,M.HENNIG,H.FOERSTERLING,A.DIENER,M.MAURER,P.SCHULTE,
AUTHOR 2 H.SCHWALBE,J.KREBS,H.SCHMID,T.VORHERR,E.CARAFOLI,C.GRIESINGER
REVDAT 7 29-AUG-18 1CFF 1 COMPND SOURCE REMARK
REVDAT 6 14-MAR-18 1CFF 1 REMARK SEQADV
REVDAT 5 24-FEB-09 1CFF 1 VERSN
REVDAT 4 01-APR-03 1CFF 1 JRNL
REVDAT 3 10-NOV-99 1CFF 1 SEQADV REMARK JRNL
REVDAT 2 21-OCT-99 1CFF 1 REVDAT
REVDAT 1 24-SEP-99 1CFF 0
JRNL AUTH B.ELSHORST,M.HENNIG,H.FORSTERLING,A.DIENER,M.MAURER,
JRNL AUTH 2 P.SCHULTE,H.SCHWALBE,C.GRIESINGER,J.KREBS,H.SCHMID,
JRNL AUTH 3 T.VORHERR,E.CARAFOLI
JRNL TITL NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A
JRNL TITL 2 BINDING PEPTIDE OF THE CA2+ PUMP.
JRNL REF BIOCHEMISTRY V. 38 12320 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10493800
JRNL DOI 10.1021/BI9908235
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE. IT IS IMPOSSIBLE TO SUPERIMPOSE THE N- AND
REMARK 3 C-TERMINAL DOMAIN OF CAM SIMULTANEOUSLY DUE TO THE LACK OF NOES
REMARK 3 BETWEEN BOTH DOMAINS. THEREFOR THE 26 STRUCTURES ARE
REMARK 3 SUPERIMPOSED ONLY OVER THE BACKBONE ATOMS OF THE C-TERMINAL
REMARK 3 DOMAIN OF CAM AND THE PEPTIDE C20W. RMSD VALUES OF THE N-
REMARK 3 TERMINAL DOMAIN OF CAM (LEU A 4 - ALA A 73) ARE 0.85 (BACKBONE)
REMARK 3 AND 1.27 (HEAVY ATOMS) ANGSTROMS. RMSD VALUE FOR THE C- TERMINAL
REMARK 3 DOMAIN OF CAM AND THE PEPTIDE C20W (ILE A 85 - MET A 145, GLY B
REMARK 3 4 - GLN B 16) ARE 0.57 (BACKBONE) AND 1.08 (HEAVY ATOMS)
REMARK 3 ANGSTROMS. RESIDUES ALA A 1 - GLN A 3, ARG A 74 - GLU A 84, THR
REMARK 3 A 146 - LYS A 148 OF CAM AND RESIDUES LEU B 1 - ARG B 3, THR B
REMARK 3 17 - LYS B 20 OF THE PEPTIDE C20W ARE DISORDERED.
REMARK 4
REMARK 4 1CFF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000682.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 0.115
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCO; HNCA; CBCACONH; CBCANH;
REMARK 210 HCCCONH; HCCH-TOCSY; NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX600; DRX800
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE UNLABELED PEPTIDE C20W WAS ASSIGNED USING A 12C,14N
REMARK 210 -FILTERED NOESY- EXPERIMENT. INTERMOLECULAR NOES BETWEEN 13C,15N-
REMARK 210 LABELED CALMODULIN AND THE PEPTIDE WERE MEASURED USING A 12C,14N-
REMARK 210 F2-FILTERED NOESY-HSQC EXPERIMENT
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 15 H PHE A 19 1.47
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 ASP A 2 113.09 66.09
REMARK 500 1 ASP A 22 -36.32 -162.39
REMARK 500 1 LEU A 39 -63.19 -121.64
REMARK 500 1 GLN A 41 70.40 19.41
REMARK 500 1 ASN A 42 -60.27 -175.06
REMARK 500 1 PRO A 43 113.99 -35.56
REMARK 500 1 ASP A 56 59.27 -68.65
REMARK 500 1 LYS A 75 38.11 -147.62
REMARK 500 1 LYS A 77 70.84 -150.54
REMARK 500 1 THR A 79 126.72 -173.81
REMARK 500 1 SER A 81 -51.00 -168.73
REMARK 500 1 GLU A 82 95.31 -56.75
REMARK 500 1 LYS A 94 -79.74 25.47
REMARK 500 1 ASN A 97 -56.64 -120.07
REMARK 500 1 ALA A 102 -44.11 176.80
REMARK 500 1 ASP A 129 83.27 -59.60
REMARK 500 1 TYR A 138 -36.61 -37.27
REMARK 500 1 ARG B 3 119.09 69.24
REMARK 500 1 ILE B 6 19.44 57.74
REMARK 500 1 LEU B 7 -60.42 -106.64
REMARK 500 1 ILE B 15 -71.97 -51.17
REMARK 500 1 ILE B 19 -39.27 -36.83
REMARK 500 2 ASP A 2 -78.36 -59.54
REMARK 500 2 LEU A 4 150.61 58.76
REMARK 500 2 ASP A 22 -36.87 -167.37
REMARK 500 2 LEU A 39 -63.93 -129.05
REMARK 500 2 GLN A 41 96.70 34.11
REMARK 500 2 ASN A 42 58.35 79.07
REMARK 500 2 ASP A 56 43.21 -92.75
REMARK 500 2 MET A 76 -35.78 -134.96
REMARK 500 2 LYS A 77 43.20 74.40
REMARK 500 2 THR A 79 44.41 78.57
REMARK 500 2 SER A 81 -44.45 -140.06
REMARK 500 2 GLU A 82 153.80 -46.68
REMARK 500 2 GLU A 83 -72.28 -153.74
REMARK 500 2 LYS A 94 32.81 32.91
REMARK 500 2 ASP A 95 -43.31 178.08
REMARK 500 2 ALA A 102 -36.66 171.69
REMARK 500 2 GLU A 114 -158.91 -78.48
REMARK 500 2 ASP A 129 104.59 -56.95
REMARK 500 2 ILE A 130 -85.78 -64.05
REMARK 500 2 TYR A 138 -31.25 -39.37
REMARK 500 2 ALA A 147 -178.10 65.66
REMARK 500 2 ARG B 2 71.73 -165.59
REMARK 500 2 ARG B 3 101.43 -179.15
REMARK 500 2 LEU B 7 -61.33 -101.12
REMARK 500 2 ILE B 15 -76.75 -52.92
REMARK 500 2 ILE B 19 145.09 -34.73
REMARK 500 3 ASP A 22 -33.52 -176.67
REMARK 500 3 LEU A 39 -65.23 -126.22
REMARK 500
REMARK 500 THIS ENTRY HAS 603 RAMACHANDRAN OUTLIERS.
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 OD2 67.2
REMARK 620 3 ASP A 24 OD2 112.0 106.2
REMARK 620 4 THR A 26 O 65.5 131.1 102.1
REMARK 620 5 GLU A 31 OE1 81.1 65.7 161.5 95.2
REMARK 620 6 GLU A 31 OE2 94.8 116.6 135.8 57.1 51.3
REMARK 620 N 1 2 3 4 5
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 OD1 123.9
REMARK 620 3 ASN A 60 OD1 135.4 64.8
REMARK 620 4 THR A 62 O 98.7 136.8 91.0
REMARK 620 5 GLU A 67 OE1 132.3 83.1 90.2 60.5
REMARK 620 6 GLU A 67 OE2 85.0 98.1 139.5 76.9 50.1
REMARK 620 N 1 2 3 4 5
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 O
REMARK 620 2 ASP A 93 OD1 54.6
REMARK 620 3 ASP A 95 OD2 76.6 125.9
REMARK 620 4 ASN A 97 OD1 97.8 95.4 67.2
REMARK 620 5 TYR A 99 O 145.1 117.4 115.9 117.1
REMARK 620 6 GLU A 104 OE1 80.4 96.8 96.5 163.4 66.4
REMARK 620 7 GLU A 104 OE2 100.7 143.3 59.2 116.3 65.3 48.8
REMARK 620 N 1 2 3 4 5 6
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 ASP A 131 OD2 107.2
REMARK 620 3 ASP A 133 OD1 104.3 86.9
REMARK 620 4 GLN A 135 O 67.7 173.5 98.1
REMARK 620 5 GLU A 140 OE1 112.7 57.0 133.9 120.4
REMARK 620 6 GLU A 140 OE2 61.7 77.7 154.0 96.1 51.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA4
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CALCIUM BINDING SITE
REMARK 800
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
DBREF 1CFF A 1 148 UNP P62155 CALM_XENLA 2 149
DBREF 1CFF B 1 20 UNP P23634 AT2B4_HUMAN 1100 1119
SEQADV 1CFF LYS B 20 UNP P62155 ARG 1119 ENGINEERED MUTATION
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
SEQRES 1 B 20 LEU ARG ARG GLY GLN ILE LEU TRP PHE ARG GLY LEU ASN
SEQRES 2 B 20 ARG ILE GLN THR GLN ILE LYS
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HET CA A 152 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
HELIX 1 A GLU A 7 LEU A 18 1 12
HELIX 2 B THR A 29 SER A 38 1 10
HELIX 3 C GLU A 47 GLU A 54 1 8
HELIX 4 D PHE A 65 ALA A 73 1 9
HELIX 5 E ILE A 85 PHE A 92 1 8
HELIX 6 F ALA A 103 LEU A 112 1 10
HELIX 7 G ASP A 118 ALA A 128 1 11
HELIX 8 H TYR A 138 MET A 145 1 8
SHEET 1 S1 1 THR A 26 THR A 28 0
SHEET 1 S2 1 THR A 62 ASP A 64 0
SHEET 1 S3 1 TYR A 99 SER A 101 0
SHEET 1 S4 1 GLN A 135 ASN A 137 0
LINK OD2 ASP A 20 CA CA A 149 1555 1555 2.54
LINK OD2 ASP A 22 CA CA A 149 1555 1555 2.54
LINK OD2 ASP A 24 CA CA A 149 1555 1555 2.56
LINK O THR A 26 CA CA A 149 1555 1555 2.54
LINK OE1 GLU A 31 CA CA A 149 1555 1555 2.54
LINK OE2 GLU A 31 CA CA A 149 1555 1555 2.54
LINK OD1 ASP A 56 CA CA A 150 1555 1555 2.53
LINK OD1 ASP A 58 CA CA A 150 1555 1555 2.53
LINK OD1 ASN A 60 CA CA A 150 1555 1555 2.53
LINK O THR A 62 CA CA A 150 1555 1555 2.53
LINK OE1 GLU A 67 CA CA A 150 1555 1555 2.66
LINK OE2 GLU A 67 CA CA A 150 1555 1555 2.53
LINK O ASP A 93 CA CA A 151 1555 1555 2.92
LINK OD1 ASP A 93 CA CA A 151 1555 1555 2.56
LINK OD2 ASP A 95 CA CA A 151 1555 1555 2.54
LINK OD1 ASN A 97 CA CA A 151 1555 1555 2.54
LINK O TYR A 99 CA CA A 151 1555 1555 2.53
LINK OE1 GLU A 104 CA CA A 151 1555 1555 2.64
LINK OE2 GLU A 104 CA CA A 151 1555 1555 2.66
LINK OD1 ASP A 129 CA CA A 152 1555 1555 2.53
LINK OD2 ASP A 131 CA CA A 152 1555 1555 2.55
LINK OD1 ASP A 133 CA CA A 152 1555 1555 2.55
LINK O GLN A 135 CA CA A 152 1555 1555 2.57
LINK OE1 GLU A 140 CA CA A 152 1555 1555 2.54
LINK OE2 GLU A 140 CA CA A 152 1555 1555 2.54
SITE 1 CA1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 CA1 5 GLU A 31
SITE 1 CA2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 CA2 5 GLU A 67
SITE 1 CA3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 CA3 5 GLU A 104
SITE 1 CA4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 CA4 5 GLU A 140
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 GLY A 59 ASN A 60
SITE 2 AC2 6 THR A 62 GLU A 67
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 ASN A 137 GLU A 140
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 - g 29 2 Bytes