Header list of 1awz.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 07-OCT-97 1AWZ
TITLE 3D SOLUTION STRUCTURE OF HUMAN ANGIOGENIN DETERMINED BY 1H, 15N NMR
TITLE 2 SPECTROSCOPY, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANGIOGENIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.27.-;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: PANCREATIC RIBONUCLEASE SUPERFAMILY
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: PLASMA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PXL694
KEYWDS HYDROLASE, ENDORIBONUCLEASE, ANGIOGENESIS
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR O.LEQUIN,H.THURING,M.ROBIN,J.-Y.LALLEMAND
REVDAT 4 16-FEB-22 1AWZ 1 REMARK
REVDAT 3 24-FEB-09 1AWZ 1 VERSN
REVDAT 2 01-APR-03 1AWZ 1 JRNL
REVDAT 1 25-FEB-98 1AWZ 0
JRNL AUTH O.LEQUIN,H.THURING,M.ROBIN,J.Y.LALLEMAND
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF HUMAN ANGIOGENIN
JRNL TITL 2 DETERMINED BY 1H,15N-NMR SPECTROSCOPY--CHARACTERIZATION OF
JRNL TITL 3 HISTIDINE PROTONATION STATES AND PKA VALUES.
JRNL REF EUR.J.BIOCHEM. V. 250 712 1997
JRNL REFN ISSN 0014-2956
JRNL PMID 9461294
JRNL DOI 10.1111/J.1432-1033.1997.00712.X
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: CHARMM22 PARAMETER FILE RMS DEVIATION
REMARK 3 FROM EXPERIMENTAL DATA: NOE (A) : 0.0179 DIHEDRAL ANGLES
REMARK 3 (DEGREES) : 0.99
REMARK 4
REMARK 4 1AWZ 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_1000171358.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 150 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY-HSQC; TOCSY-HMQC; HNHA;
REMARK 210 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA, X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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
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 TYR A 6 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 TYR A 14 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 2 LEU A 10 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 3 TYR A 6 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 3 LEU A 10 CB - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 3 PHE A 120 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 4 TYR A 6 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 LEU A 115 CB - CG - CD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 5 TYR A 6 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 5 TYR A 14 CB - CG - CD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 5 TYR A 14 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 6 TYR A 6 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 6 TYR A 14 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 6 MET A 30 CG - SD - CE ANGL. DEV. = -9.9 DEGREES
REMARK 500 7 TYR A 6 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 8 TYR A 14 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 TYR A 14 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 9 TYR A 6 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 9 TYR A 14 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 10 TYR A 14 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 11 TYR A 6 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 11 LEU A 10 CB - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 12 TYR A 14 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 12 LEU A 115 CB - CG - CD1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 12 PHE A 120 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 13 LEU A 10 CB - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 13 TYR A 14 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 14 TYR A 6 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 15 LEU A 10 CB - CA - C ANGL. DEV. = 11.9 DEGREES
REMARK 500 16 TYR A 6 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 16 TYR A 14 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 17 LEU A 10 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 17 TYR A 14 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 18 TYR A 6 CB - CG - CD2 ANGL. DEV. = -6.9 DEGREES
REMARK 500 18 TYR A 6 CB - CG - CD1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 18 TYR A 14 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 19 TYR A 6 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 19 PHE A 120 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 20 TYR A 6 CB - CG - CD1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 20 TYR A 14 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 20 LEU A 115 CB - CG - CD1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 22 TYR A 6 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 22 PHE A 120 CB - CG - CD2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 22 PHE A 120 CB - CG - CD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 23 TYR A 6 CB - CG - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 23 TYR A 6 CB - CG - CD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 23 PHE A 120 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 23 PHE A 120 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 24 TYR A 6 CB - CG - CD2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 24 TYR A 6 CB - CG - CD1 ANGL. DEV. = -6.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 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 ASP A 2 71.83 59.34
REMARK 500 1 ASN A 3 -28.84 93.15
REMARK 500 1 ARG A 21 73.46 -106.84
REMARK 500 1 ARG A 66 -109.59 46.31
REMARK 500 1 GLU A 67 77.47 -107.33
REMARK 500 1 GLN A 117 41.84 -100.86
REMARK 500 1 PHE A 120 43.40 -105.06
REMARK 500 2 ASN A 3 -26.04 109.36
REMARK 500 2 GLN A 19 -74.99 -74.64
REMARK 500 2 ARG A 21 72.56 -118.16
REMARK 500 2 LYS A 60 -49.08 -159.77
REMARK 500 2 ASN A 61 47.24 -144.34
REMARK 500 2 ARG A 66 -108.72 65.66
REMARK 500 2 SER A 74 74.02 -109.54
REMARK 500 3 ASP A 2 68.01 -102.74
REMARK 500 3 HIS A 13 -62.94 -127.29
REMARK 500 3 ARG A 21 68.28 -109.53
REMARK 500 3 ARG A 66 -109.81 60.50
REMARK 500 3 GLN A 117 59.53 -114.20
REMARK 500 4 ASN A 3 -35.32 111.67
REMARK 500 4 GLN A 19 -76.65 -70.10
REMARK 500 4 ARG A 21 74.47 -112.63
REMARK 500 4 ARG A 66 -102.49 65.51
REMARK 500 4 GLN A 117 51.04 -106.59
REMARK 500 5 ASN A 3 5.78 81.71
REMARK 500 5 ARG A 66 -103.21 66.29
REMARK 500 5 GLU A 67 113.75 -163.36
REMARK 500 5 HIS A 84 46.85 -142.10
REMARK 500 5 PHE A 100 101.61 -162.28
REMARK 500 5 GLN A 117 37.44 -96.18
REMARK 500 6 ASP A 2 59.99 -116.50
REMARK 500 6 GLN A 19 -73.05 -73.21
REMARK 500 6 ARG A 21 72.81 -115.16
REMARK 500 6 ASN A 59 -3.46 -159.88
REMARK 500 6 ARG A 66 -103.59 66.39
REMARK 500 6 ASN A 68 -12.70 90.93
REMARK 500 6 ASN A 109 68.55 31.95
REMARK 500 7 ASP A 2 60.69 -108.31
REMARK 500 7 GLN A 19 -77.97 -70.08
REMARK 500 7 ARG A 21 74.67 -110.15
REMARK 500 7 LYS A 60 -46.51 -141.06
REMARK 500 7 ARG A 66 -103.91 70.81
REMARK 500 7 SER A 87 110.74 -163.51
REMARK 500 7 GLN A 117 41.06 -106.06
REMARK 500 8 HIS A 13 -55.59 -123.64
REMARK 500 8 ARG A 21 75.53 -109.38
REMARK 500 8 ARG A 66 -97.13 69.85
REMARK 500 8 GLN A 117 42.11 -105.41
REMARK 500 9 ASP A 2 62.96 -111.34
REMARK 500 9 ASN A 61 36.14 73.64
REMARK 500
REMARK 500 THIS ENTRY HAS 177 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 TYR A 6 0.09 SIDE CHAIN
REMARK 500 6 TYR A 6 0.08 SIDE CHAIN
REMARK 500 7 TYR A 6 0.09 SIDE CHAIN
REMARK 500 8 TYR A 6 0.07 SIDE CHAIN
REMARK 500 9 TYR A 6 0.07 SIDE CHAIN
REMARK 500 10 TYR A 6 0.07 SIDE CHAIN
REMARK 500 12 TYR A 6 0.07 SIDE CHAIN
REMARK 500 13 TYR A 6 0.08 SIDE CHAIN
REMARK 500 14 TYR A 6 0.11 SIDE CHAIN
REMARK 500 15 TYR A 6 0.10 SIDE CHAIN
REMARK 500 16 TYR A 6 0.10 SIDE CHAIN
REMARK 500 18 TYR A 6 0.09 SIDE CHAIN
REMARK 500 18 TYR A 94 0.07 SIDE CHAIN
REMARK 500 21 TYR A 6 0.06 SIDE CHAIN
REMARK 500 23 TYR A 6 0.08 SIDE CHAIN
REMARK 500 25 TYR A 6 0.07 SIDE CHAIN
REMARK 500 26 TYR A 6 0.10 SIDE CHAIN
REMARK 500 27 TYR A 6 0.07 SIDE CHAIN
REMARK 500 28 TYR A 6 0.07 SIDE CHAIN
REMARK 500 30 TYR A 6 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: RIB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: RIBONUCLEOLYTIC ACTIVE SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: RBS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PUTATIVE CELL RECEPTOR BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: NLS
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NUCLEOLAR LOCALIZATION SIGNAL.
DBREF 1AWZ A 1 123 UNP P03950 ANGI_HUMAN 25 147
SEQRES 1 A 123 GLN ASP ASN SER ARG TYR THR HIS PHE LEU THR GLN HIS
SEQRES 2 A 123 TYR ASP ALA LYS PRO GLN GLY ARG ASP ASP ARG TYR CYS
SEQRES 3 A 123 GLU SER ILE MET ARG ARG ARG GLY LEU THR SER PRO CYS
SEQRES 4 A 123 LYS ASP ILE ASN THR PHE ILE HIS GLY ASN LYS ARG SER
SEQRES 5 A 123 ILE LYS ALA ILE CYS GLU ASN LYS ASN GLY ASN PRO HIS
SEQRES 6 A 123 ARG GLU ASN LEU ARG ILE SER LYS SER SER PHE GLN VAL
SEQRES 7 A 123 THR THR CYS LYS LEU HIS GLY GLY SER PRO TRP PRO PRO
SEQRES 8 A 123 CYS GLN TYR ARG ALA THR ALA GLY PHE ARG ASN VAL VAL
SEQRES 9 A 123 VAL ALA CYS GLU ASN GLY LEU PRO VAL HIS LEU ASP GLN
SEQRES 10 A 123 SER ILE PHE ARG ARG PRO
HELIX 1 1 SER A 4 GLN A 12 1 9
HELIX 2 2 ASP A 23 ARG A 33 1 11
HELIX 3 3 LYS A 50 ILE A 56 1 7
SHEET 1 A 3 ILE A 42 HIS A 47 0
SHEET 2 A 3 PHE A 76 LEU A 83 -1 N CYS A 81 O ASN A 43
SHEET 3 A 3 TYR A 94 ARG A 101 -1 N ARG A 101 O PHE A 76
SHEET 1 B 4 GLY A 62 HIS A 65 0
SHEET 2 B 4 LEU A 69 SER A 72 -1 N ILE A 71 O ASN A 63
SHEET 3 B 4 VAL A 104 GLU A 108 -1 N VAL A 105 O ARG A 70
SHEET 4 B 4 LEU A 111 LEU A 115 -1 N HIS A 114 O ALA A 106
SSBOND 1 CYS A 26 CYS A 81 1555 1555 2.00
SSBOND 2 CYS A 39 CYS A 92 1555 1555 2.02
SSBOND 3 CYS A 57 CYS A 107 1555 1555 2.02
CISPEP 1 SER A 37 PRO A 38 1 -18.48
CISPEP 2 PRO A 90 PRO A 91 1 15.85
CISPEP 3 SER A 37 PRO A 38 2 -20.25
CISPEP 4 PRO A 90 PRO A 91 2 -1.76
CISPEP 5 SER A 37 PRO A 38 3 -21.87
CISPEP 6 PRO A 90 PRO A 91 3 7.37
CISPEP 7 SER A 37 PRO A 38 4 -22.02
CISPEP 8 PRO A 90 PRO A 91 4 9.41
CISPEP 9 SER A 37 PRO A 38 5 -20.63
CISPEP 10 PRO A 90 PRO A 91 5 1.88
CISPEP 11 SER A 37 PRO A 38 6 -24.60
CISPEP 12 PRO A 90 PRO A 91 6 10.81
CISPEP 13 SER A 37 PRO A 38 7 -22.45
CISPEP 14 PRO A 90 PRO A 91 7 -4.44
CISPEP 15 SER A 37 PRO A 38 8 -22.19
CISPEP 16 PRO A 90 PRO A 91 8 12.33
CISPEP 17 SER A 37 PRO A 38 9 -27.48
CISPEP 18 PRO A 90 PRO A 91 9 5.47
CISPEP 19 SER A 37 PRO A 38 10 -19.22
CISPEP 20 PRO A 90 PRO A 91 10 19.08
CISPEP 21 SER A 37 PRO A 38 11 -24.78
CISPEP 22 PRO A 90 PRO A 91 11 10.92
CISPEP 23 SER A 37 PRO A 38 12 -23.72
CISPEP 24 PRO A 90 PRO A 91 12 9.80
CISPEP 25 SER A 37 PRO A 38 13 -19.75
CISPEP 26 PRO A 90 PRO A 91 13 3.11
CISPEP 27 SER A 37 PRO A 38 14 -16.15
CISPEP 28 PRO A 90 PRO A 91 14 7.88
CISPEP 29 SER A 37 PRO A 38 15 -22.37
CISPEP 30 PRO A 90 PRO A 91 15 13.11
CISPEP 31 SER A 37 PRO A 38 16 -20.92
CISPEP 32 PRO A 90 PRO A 91 16 4.11
CISPEP 33 SER A 37 PRO A 38 17 -22.42
CISPEP 34 PRO A 90 PRO A 91 17 7.62
CISPEP 35 SER A 37 PRO A 38 18 -25.01
CISPEP 36 PRO A 90 PRO A 91 18 -1.10
CISPEP 37 SER A 37 PRO A 38 19 -18.68
CISPEP 38 PRO A 90 PRO A 91 19 7.82
CISPEP 39 SER A 37 PRO A 38 20 -22.13
CISPEP 40 PRO A 90 PRO A 91 20 5.84
CISPEP 41 SER A 37 PRO A 38 21 -23.27
CISPEP 42 PRO A 90 PRO A 91 21 10.26
CISPEP 43 SER A 37 PRO A 38 22 -19.80
CISPEP 44 PRO A 90 PRO A 91 22 4.86
CISPEP 45 SER A 37 PRO A 38 23 -23.36
CISPEP 46 PRO A 90 PRO A 91 23 -4.78
CISPEP 47 SER A 37 PRO A 38 24 -23.41
CISPEP 48 PRO A 90 PRO A 91 24 13.08
CISPEP 49 SER A 37 PRO A 38 25 -21.04
CISPEP 50 PRO A 90 PRO A 91 25 12.97
CISPEP 51 SER A 37 PRO A 38 26 -21.10
CISPEP 52 PRO A 90 PRO A 91 26 8.59
CISPEP 53 SER A 37 PRO A 38 27 -21.59
CISPEP 54 PRO A 90 PRO A 91 27 -1.78
CISPEP 55 SER A 37 PRO A 38 28 -24.62
CISPEP 56 PRO A 90 PRO A 91 28 10.71
CISPEP 57 SER A 37 PRO A 38 29 -22.25
CISPEP 58 PRO A 90 PRO A 91 29 8.88
CISPEP 59 SER A 37 PRO A 38 30 -22.03
CISPEP 60 PRO A 90 PRO A 91 30 -1.09
SITE 1 RIB 8 GLN A 12 HIS A 13 LYS A 40 THR A 44
SITE 2 RIB 8 HIS A 114 LEU A 115 ASP A 116 GLN A 117
SITE 1 RBS 6 LYS A 60 ASN A 61 ARG A 66 GLU A 67
SITE 2 RBS 6 ASN A 68 ASN A 109
SITE 1 NLS 3 ARG A 31 ARG A 32 ARG A 33
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 16 2 Bytes