Header list of 1mwn.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 30-SEP-02 1MWN
TITLE SOLUTION NMR STRUCTURE OF S100B BOUND TO THE HIGH-AFFINITY TARGET
TITLE 2 PEPTIDE TRTK-12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-100 PROTEIN, BETA CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: F-ACTIN CAPPING PROTEIN ALPHA-1 SUBUNIT;
COMPND 8 CHAIN: X, Y;
COMPND 9 FRAGMENT: RESIDUES 265-276;
COMPND 10 SYNONYM: CAPZ ALPHA-1, CAPZA1, TRTK-12;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: S100B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 14 OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS S100B, TRTK-12, CALCIUM-BINDING, EF-HAND, S100 PROTEIN, FOUR HELIX
KEYWDS 2 BUNDLE, HELIX LOOP HELIX, PROTEIN-PEPTIDE COMPLEX, 20 STRUCTURES,
KEYWDS 3 STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.G.INMAN,R.YANG,R.R.RUSTANDI,K.E.MILLER,D.M.BALDISSERI,D.J.WEBER
REVDAT 3 23-FEB-22 1MWN 1 REMARK LINK
REVDAT 2 24-FEB-09 1MWN 1 VERSN
REVDAT 1 18-DEC-02 1MWN 0
JRNL AUTH K.G.INMAN,R.YANG,R.R.RUSTANDI,K.E.MILLER,D.M.BALDISSERI,
JRNL AUTH 2 D.J.WEBER
JRNL TITL SOLUTION NMR STRUCTURE OF S100B BOUND TO THE HIGH-AFFINITY
JRNL TITL 2 TARGET PEPTIDE TRTK-12
JRNL REF J.MOL.BIOL. V. 324 1003 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12470955
JRNL DOI 10.1016/S0022-2836(02)01152-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.R.RUSTANDI,D.M.BALDISSERI,D.J.WEBER
REMARK 1 TITL STRUCTURE OF THE NEGATIVE REGULATORY DOMAIN OF P53 BOUND TO
REMARK 1 TITL 2 S100B(BETABETA)
REMARK 1 REF NAT.STRUCT.BIOL. V. 7 570 2000
REMARK 1 REFN ISSN 1072-8368
REMARK 1 DOI 10.1038/76797
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.C.DROHAT,D.M.BALDISSERI,R.R.RUSTANDI,D.J.WEBER
REMARK 1 TITL SOLUTION STRUCTURE OF CALCIUM-BOUND RAT S100B(BETABETA) AS
REMARK 1 TITL 2 DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 37 2729 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI972635P
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.C.DROHAT,J.C.AMBURGEY,F.ABILDGAARD,M.R.STARICH,
REMARK 1 AUTH 2 D.M.BALDISSERI,D.J.WEBER
REMARK 1 TITL SOLUTION STRUCTURE OF RAT APO-S100B(BETABETA) AS DETERMINED
REMARK 1 TITL 2 BY NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 35 11577 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI9612226
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MWN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017253.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 25 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2.2 MM S100B (SUBUNIT
REMARK 210 CONCENTRATION), 5.2 MM CACL2,
REMARK 210 2.6 MM TRTK-12 PEPTIDE, 10 MM
REMARK 210 TRIS-D11, 15 MM NACL, 0.1 MM
REMARK 210 EDTA, 5 MM DTT, 0.35 MM NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_NOESY; 3D_
REMARK 210 15N-SEPARATED_NOESY; 2D NOESY;
REMARK 210 3D 13C-FILTER NOESY; 2D TOCSY;
REMARK 210 HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 : 2
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X, Y
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 MET A 0
REMARK 465 MET B 0
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 HE2 HIS A 85 HE2 HIS B 15 1.26
REMARK 500 HE2 HIS A 15 HE2 HIS B 85 1.27
REMARK 500 O GLN B 50 H ASP B 54 1.50
REMARK 500 O GLN A 50 H ASP A 54 1.51
REMARK 500 O LEU A 60 H GLU A 62 1.53
REMARK 500 O LEU B 60 H GLU B 62 1.54
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 41 -80.71 -43.63
REMARK 500 1 LEU A 44 -35.37 -156.48
REMARK 500 1 ASP A 61 56.84 -69.51
REMARK 500 1 GLU A 62 6.18 -66.54
REMARK 500 1 SER B 41 -80.12 -44.05
REMARK 500 1 LEU B 44 -35.54 -155.81
REMARK 500 1 ASP B 61 56.80 -69.42
REMARK 500 1 GLU B 62 6.75 -66.68
REMARK 500 1 ILE X 5 -134.42 -61.13
REMARK 500 1 ILE Y 5 -134.54 -61.56
REMARK 500 2 LYS A 29 -38.53 -39.44
REMARK 500 2 LEU A 40 51.40 -114.66
REMARK 500 2 LEU A 44 -98.83 -127.91
REMARK 500 2 GLU A 62 0.64 -65.35
REMARK 500 2 GLU A 89 98.86 -64.06
REMARK 500 2 LYS B 29 -38.41 -39.81
REMARK 500 2 LEU B 40 52.08 -114.69
REMARK 500 2 LEU B 44 -98.19 -128.00
REMARK 500 2 GLU B 62 0.73 -65.02
REMARK 500 2 GLU B 89 98.86 -63.89
REMARK 500 2 ASP X 6 38.07 165.95
REMARK 500 2 ASP Y 6 38.46 166.65
REMARK 500 3 LEU A 40 67.26 -108.92
REMARK 500 3 LEU A 44 -153.66 -130.02
REMARK 500 3 GLU A 62 2.09 -68.79
REMARK 500 3 PHE A 87 -13.51 -47.23
REMARK 500 3 LEU B 40 67.39 -109.30
REMARK 500 3 LEU B 44 -153.70 -129.97
REMARK 500 3 GLU B 62 2.12 -68.82
REMARK 500 3 PHE B 87 -13.60 -47.12
REMARK 500 3 ASP X 6 43.54 -70.97
REMARK 500 3 ASP Y 6 43.71 -70.69
REMARK 500 4 GLU A 21 97.28 -167.63
REMARK 500 4 LEU A 40 71.41 -117.53
REMARK 500 4 SER A 41 -89.68 -52.74
REMARK 500 4 LEU A 44 -67.81 -150.28
REMARK 500 4 GLU A 62 2.67 -68.43
REMARK 500 4 GLU B 21 97.50 -167.61
REMARK 500 4 LEU B 40 71.37 -117.21
REMARK 500 4 SER B 41 -89.67 -52.84
REMARK 500 4 LEU B 44 -67.88 -150.13
REMARK 500 4 GLU B 62 2.51 -68.42
REMARK 500 4 THR X 3 -161.45 44.35
REMARK 500 4 LYS X 4 176.89 50.56
REMARK 500 4 ASP X 6 79.62 162.07
REMARK 500 4 THR Y 3 -161.74 44.54
REMARK 500 4 LYS Y 4 176.73 50.81
REMARK 500 4 ASP Y 6 79.81 162.08
REMARK 500 5 LEU A 40 64.35 -161.98
REMARK 500 5 LEU A 44 -98.88 -129.04
REMARK 500
REMARK 500 THIS ENTRY HAS 228 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 100 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 18 O
REMARK 620 2 ASP A 23 O 110.5
REMARK 620 3 LYS A 26 O 174.0 63.8
REMARK 620 4 GLU A 31 OE1 87.5 108.3 92.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD1
REMARK 620 2 ASP A 63 OD2 112.1
REMARK 620 3 ASP A 65 OD1 46.9 106.7
REMARK 620 4 ASP A 65 OD2 85.5 83.9 39.8
REMARK 620 5 GLU A 67 O 69.5 168.7 65.7 85.1
REMARK 620 6 GLU A 72 OE1 107.8 112.0 140.3 151.9 77.1
REMARK 620 7 GLU A 72 OE2 135.8 68.3 174.7 136.0 119.0 45.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 18 O
REMARK 620 2 ASP B 23 O 102.6
REMARK 620 3 LYS B 24 O 92.0 77.8
REMARK 620 4 LYS B 26 O 159.2 62.2 98.0
REMARK 620 5 GLU B 31 OE1 80.6 95.7 168.9 86.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 103 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 61 OD1
REMARK 620 2 ASP B 63 OD2 112.5
REMARK 620 3 ASP B 65 OD1 46.6 107.1
REMARK 620 4 ASP B 65 OD2 85.0 84.4 39.6
REMARK 620 5 GLU B 67 O 69.0 168.5 65.0 84.4
REMARK 620 6 GLU B 72 OE1 107.4 112.8 139.1 151.2 76.6
REMARK 620 7 GLU B 72 OE2 136.0 68.9 175.7 136.8 118.6 45.2
REMARK 620 N 1 2 3 4 5 6
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 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 103
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DT7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH P53 PEPTIDE.
DBREF 1MWN A 0 91 UNP P04631 S100B_RAT 0 91
DBREF 1MWN B 0 91 UNP P04631 S100B_RAT 0 91
DBREF 1MWN X 1 12 UNP P52907 CAZA1_HUMAN 265 276
DBREF 1MWN Y 1 12 UNP P52907 CAZA1_HUMAN 265 276
SEQRES 1 A 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP
SEQRES 2 A 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 A 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 A 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 A 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY
SEQRES 6 A 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 A 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 A 92 GLU
SEQRES 1 B 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP
SEQRES 2 B 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 B 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 B 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 B 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY
SEQRES 6 B 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 B 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 B 92 GLU
SEQRES 1 X 12 THR ARG THR LYS ILE ASP TRP ASN LYS ILE LEU SER
SEQRES 1 Y 12 THR ARG THR LYS ILE ASP TRP ASN LYS ILE LEU SER
HET CA A 100 1
HET CA A 101 1
HET CA B 102 1
HET CA B 103 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 4(CA 2+)
HELIX 1 1 SER A 1 GLY A 19 1 19
HELIX 2 2 LYS A 29 LEU A 40 1 12
HELIX 3 3 GLU A 49 ASP A 61 1 13
HELIX 4 4 ASP A 69 PHE A 88 1 20
HELIX 5 5 SER B 1 GLY B 19 1 19
HELIX 6 6 LYS B 29 LEU B 40 1 12
HELIX 7 7 GLU B 49 ASP B 61 1 13
HELIX 8 8 ASP B 69 PHE B 88 1 20
HELIX 9 9 ASP X 6 SER X 12 1 7
HELIX 10 10 ASP Y 6 SER Y 12 1 7
SHEET 1 A 2 LEU A 27 LYS A 29 0
SHEET 2 A 2 GLU A 67 CYS A 68 -1 O CYS A 68 N LEU A 27
SHEET 1 B 2 LEU B 27 LYS B 28 0
SHEET 2 B 2 GLU B 67 CYS B 68 -1 O CYS B 68 N LEU B 27
LINK O SER A 18 CA CA A 100 1555 1555 2.65
LINK O ASP A 23 CA CA A 100 1555 1555 2.19
LINK O LYS A 26 CA CA A 100 1555 1555 2.56
LINK OE1 GLU A 31 CA CA A 100 1555 1555 2.54
LINK OD1 ASP A 61 CA CA A 101 1555 1555 2.86
LINK OD2 ASP A 63 CA CA A 101 1555 1555 2.83
LINK OD1 ASP A 65 CA CA A 101 1555 1555 3.07
LINK OD2 ASP A 65 CA CA A 101 1555 1555 3.24
LINK O GLU A 67 CA CA A 101 1555 1555 2.74
LINK OE1 GLU A 72 CA CA A 101 1555 1555 2.79
LINK OE2 GLU A 72 CA CA A 101 1555 1555 2.83
LINK O SER B 18 CA CA B 102 1555 1555 2.75
LINK O ASP B 23 CA CA B 102 1555 1555 2.34
LINK O LYS B 24 CA CA B 102 1555 1555 3.40
LINK O LYS B 26 CA CA B 102 1555 1555 2.54
LINK OE1 GLU B 31 CA CA B 102 1555 1555 2.82
LINK OD1 ASP B 61 CA CA B 103 1555 1555 2.86
LINK OD2 ASP B 63 CA CA B 103 1555 1555 2.80
LINK OD1 ASP B 65 CA CA B 103 1555 1555 3.09
LINK OD2 ASP B 65 CA CA B 103 1555 1555 3.26
LINK O GLU B 67 CA CA B 103 1555 1555 2.77
LINK OE1 GLU B 72 CA CA B 103 1555 1555 2.79
LINK OE2 GLU B 72 CA CA B 103 1555 1555 2.82
SITE 1 AC1 6 SER A 18 ASP A 23 LYS A 24 LYS A 26
SITE 2 AC1 6 LEU A 27 GLU A 31
SITE 1 AC2 5 ASP A 61 ASP A 63 ASP A 65 GLU A 67
SITE 2 AC2 5 GLU A 72
SITE 1 AC3 6 SER B 18 ASP B 23 LYS B 24 LYS B 26
SITE 2 AC3 6 LEU B 27 GLU B 31
SITE 1 AC4 5 ASP B 61 ASP B 63 ASP B 65 GLU B 67
SITE 2 AC4 5 GLU B 72
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