Header list of 1de3.pdb file
Complete list - b 16 2 Bytes
HEADER HYDROLASE 12-NOV-99 1DE3
TITLE SOLUTION STRUCTURE OF THE CYTOTOXIC RIBONUCLEASE ALPHA-SARCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBONUCLEASE ALPHA-SARCIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.27.10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS GIGANTEUS;
SOURCE 3 ORGANISM_TAXID: 5060;
SOURCE 4 STRAIN: MDH 18894;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PINPGAS
KEYWDS ALPHA-BETA PROTEIN, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.M.PEREZ-CANADILLAS,R.CAMPOS-OLIVAS,J.SANTORO,J.LACADENA,A.MARTINEZ
AUTHOR 2 DEL POZO,J.G.GAVILANES,M.RICO,M.BRUIX
REVDAT 3 16-FEB-22 1DE3 1 REMARK
REVDAT 2 24-FEB-09 1DE3 1 VERSN
REVDAT 1 21-JUN-00 1DE3 0
JRNL AUTH J.M.PEREZ-CANADILLAS,J.SANTORO,R.CAMPOS-OLIVAS,J.LACADENA,
JRNL AUTH 2 A.MARTINEZ DEL POZO,J.G.GAVILANES,M.RICO,M.BRUIX
JRNL TITL THE HIGHLY REFINED SOLUTION STRUCTURE OF THE CYTOTOXIC
JRNL TITL 2 RIBONUCLEASE ALPHA-SARCIN REVEALS THE STRUCTURAL
JRNL TITL 3 REQUIREMENTS FOR SUBSTRATE RECOGNITION AND RIBONUCLEOLYTIC
JRNL TITL 4 ACTIVITY.
JRNL REF J.MOL.BIOL. V. 299 1061 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10843858
JRNL DOI 10.1006/JMBI.2000.3813
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.M.PEREZ-CANADILLAS,R.CAMPOS-OLIVAS,J.LACADENA,
REMARK 1 AUTH 2 A.MARTINEZ DEL POZO,J.G.GAVILANES,J.SANTORO,M.RICO,M.BRUIX
REMARK 1 TITL CHARACTERIZATION OF PKA VALUES AND TITRATION SHIFTS IN THE
REMARK 1 TITL 2 CYTOTOXIC RIBONUCLEASE ALPHA-SARCIN BY NMR. RELATIONSHIP
REMARK 1 TITL 3 BETWEEN ELECTROSTATIC INTERACTIONS, STRUCTURE, AND CATALYTIC
REMARK 1 TITL 4 FUNCTION.
REMARK 1 REF BIOCHEMISTRY V. 37 15865 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI981672T
REMARK 1 REFERENCE 2
REMARK 1 AUTH R.CAMPOS-OLIVAS,M.BRUIX,J.SANTORO,A.MARTINEZ DEL POZO,
REMARK 1 AUTH 2 J.LACADENA,J.G.GAVILANES,M.RICO
REMARK 1 TITL STRUCTURAL BASIS FOR THE CATALYTIC MECHANISM AND SUBSTRATE
REMARK 1 TITL 2 SPECIFICITY OF THE RIBONUCLEASE ALPHA-SARCIN.
REMARK 1 REF FEBS LETT. V. 399 163 1996
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(96)01320-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.1, GROMOS 97
REMARK 3 AUTHORS : VAN GUNSTEREN (GROMOS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2777 RESTRAINTS, 2658 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND 119 DIHEDRAL PHI ANGLE RESTRAINTS. THE
REMARK 3 STRUCTURES
REMARK 3 WERE ENERGY MINIMISED WITH THE GROMOS FORCE FIELD.
REMARK 4
REMARK 4 1DE3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-NOV-99.
REMARK 100 THE DEPOSITION ID IS D_1000010008.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 313
REMARK 210 PH : 6.0; 4.0
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : NA; NA; U-15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 1H-15N 3JHNHA
REMARK 210 MODULATED HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3, DYANA 1.5, GROMOS 97
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 47
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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 25 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 1 TYR A 126 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 TYR A 25 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 2 TYR A 48 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 2 TYR A 93 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 TYR A 106 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 2 TYR A 126 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 3 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 3 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 3 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 3 TYR A 126 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 4 TYR A 25 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 4 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 4 TYR A 126 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 5 TYR A 56 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 5 TYR A 106 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 6 TYR A 25 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 6 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 6 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 7 TYR A 25 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 7 TYR A 56 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 7 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 7 TYR A 124 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 8 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 8 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 8 TYR A 126 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 9 TYR A 48 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 9 TYR A 93 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 9 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 9 TYR A 126 CB - CG - CD1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 10 TYR A 25 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 10 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 10 TYR A 106 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 10 TYR A 126 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 11 TYR A 25 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 11 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 11 TYR A 126 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 12 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 12 TYR A 56 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 12 TYR A 106 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 12 TYR A 124 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 12 TYR A 126 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 13 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 13 TYR A 106 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 13 TYR A 126 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 14 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 14 TYR A 93 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 14 TYR A 106 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 69 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 ASN A 16 29.01 44.79
REMARK 500 1 HIS A 36 -44.79 -131.04
REMARK 500 1 SER A 40 117.31 -161.84
REMARK 500 1 LYS A 43 29.10 -150.91
REMARK 500 1 SER A 47 -36.56 88.59
REMARK 500 1 ASP A 59 -46.30 -153.78
REMARK 500 1 PRO A 63 -163.37 -71.64
REMARK 500 1 SER A 83 -149.81 -85.93
REMARK 500 1 ASN A 87 76.08 -156.04
REMARK 500 1 THR A 90 32.35 -154.82
REMARK 500 1 TYR A 106 143.71 -35.31
REMARK 500 1 PRO A 117 -165.01 -70.78
REMARK 500 1 THR A 125 -162.49 -70.70
REMARK 500 1 VAL A 130 87.15 -65.69
REMARK 500 1 PHE A 131 109.13 -39.12
REMARK 500 1 GLU A 140 -95.90 61.40
REMARK 500 1 ASN A 141 34.89 -147.20
REMARK 500 1 GLN A 142 -46.92 -141.25
REMARK 500 1 LEU A 147 105.35 -49.15
REMARK 500 2 ASN A 16 28.45 44.18
REMARK 500 2 HIS A 36 -68.36 -94.14
REMARK 500 2 LYS A 43 30.86 -149.00
REMARK 500 2 SER A 47 13.70 82.62
REMARK 500 2 THR A 53 -38.77 -37.82
REMARK 500 2 ASP A 59 -84.39 -94.72
REMARK 500 2 PRO A 63 -161.55 -71.83
REMARK 500 2 ARG A 66 106.15 -57.58
REMARK 500 2 SER A 74 -53.48 -121.78
REMARK 500 2 SER A 83 -147.94 -85.62
REMARK 500 2 ASN A 87 78.66 -158.86
REMARK 500 2 THR A 90 24.50 -155.21
REMARK 500 2 HIS A 92 67.57 -112.12
REMARK 500 2 TYR A 106 135.93 -33.82
REMARK 500 2 LYS A 107 75.97 -63.15
REMARK 500 2 PRO A 117 -164.57 -71.59
REMARK 500 2 TYR A 124 139.25 -171.72
REMARK 500 2 THR A 125 -165.41 -63.76
REMARK 500 2 VAL A 130 87.18 -65.54
REMARK 500 2 PHE A 131 109.82 -44.85
REMARK 500 2 THR A 138 45.37 -80.57
REMARK 500 2 LYS A 139 80.95 -179.92
REMARK 500 2 GLU A 140 -84.86 65.62
REMARK 500 2 ASN A 141 23.44 -153.07
REMARK 500 2 LEU A 147 100.63 -52.27
REMARK 500 2 CYS A 148 159.13 -48.52
REMARK 500 3 LYS A 43 35.67 -150.27
REMARK 500 3 SER A 47 -26.52 87.63
REMARK 500 3 THR A 53 -39.39 -39.44
REMARK 500 3 ASP A 59 -86.59 -96.61
REMARK 500 3 PRO A 63 -169.56 -70.64
REMARK 500
REMARK 500 THIS ENTRY HAS 450 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 3 TYR A 93 0.07 SIDE CHAIN
REMARK 500 5 TYR A 93 0.07 SIDE CHAIN
REMARK 500 6 TYR A 56 0.08 SIDE CHAIN
REMARK 500 6 TYR A 93 0.06 SIDE CHAIN
REMARK 500 6 PHE A 131 0.09 SIDE CHAIN
REMARK 500 9 TYR A 93 0.07 SIDE CHAIN
REMARK 500 13 TYR A 124 0.07 SIDE CHAIN
REMARK 500 14 TYR A 93 0.08 SIDE CHAIN
REMARK 500 15 TYR A 56 0.10 SIDE CHAIN
REMARK 500 15 TYR A 93 0.09 SIDE CHAIN
REMARK 500 16 TYR A 25 0.06 SIDE CHAIN
REMARK 500 18 TYR A 25 0.08 SIDE CHAIN
REMARK 500 19 TYR A 56 0.06 SIDE CHAIN
REMARK 500 20 TYR A 93 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 SER A 34 -10.39
REMARK 500 2 LYS A 29 -10.90
REMARK 500 2 PRO A 49 11.12
REMARK 500 4 SER A 34 -10.91
REMARK 500 5 ASN A 28 -12.02
REMARK 500 6 SER A 34 -11.02
REMARK 500 7 PRO A 49 10.49
REMARK 500 8 PRO A 49 12.28
REMARK 500 9 SER A 34 -11.47
REMARK 500 10 PRO A 49 11.55
REMARK 500 11 SER A 34 -11.06
REMARK 500 13 LYS A 81 10.24
REMARK 500 14 ASN A 28 -10.12
REMARK 500 14 PRO A 49 10.37
REMARK 500 15 SER A 34 -10.53
REMARK 500 15 PRO A 49 10.01
REMARK 500 16 SER A 34 -12.29
REMARK 500 17 ASN A 28 -10.11
REMARK 500 17 SER A 34 -12.55
REMARK 500 19 ASN A 28 -11.20
REMARK 500 20 LYS A 29 -11.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4158 RELATED DB: BMRB
REMARK 900 15N AND 1H CHEMICAL SHIFTS
DBREF 1DE3 A 1 150 UNP P00655 RNAS_ASPGI 28 177
SEQRES 1 A 150 ALA VAL THR TRP THR CYS LEU ASN ASP GLN LYS ASN PRO
SEQRES 2 A 150 LYS THR ASN LYS TYR GLU THR LYS ARG LEU LEU TYR ASN
SEQRES 3 A 150 GLN ASN LYS ALA GLU SER ASN SER HIS HIS ALA PRO LEU
SEQRES 4 A 150 SER ASP GLY LYS THR GLY SER SER TYR PRO HIS TRP PHE
SEQRES 5 A 150 THR ASN GLY TYR ASP GLY ASP GLY LYS LEU PRO LYS GLY
SEQRES 6 A 150 ARG THR PRO ILE LYS PHE GLY LYS SER ASP CYS ASP ARG
SEQRES 7 A 150 PRO PRO LYS HIS SER LYS ASP GLY ASN GLY LYS THR ASP
SEQRES 8 A 150 HIS TYR LEU LEU GLU PHE PRO THR PHE PRO ASP GLY HIS
SEQRES 9 A 150 ASP TYR LYS PHE ASP SER LYS LYS PRO LYS GLU ASN PRO
SEQRES 10 A 150 GLY PRO ALA ARG VAL ILE TYR THR TYR PRO ASN LYS VAL
SEQRES 11 A 150 PHE CYS GLY ILE ILE ALA HIS THR LYS GLU ASN GLN GLY
SEQRES 12 A 150 GLU LEU LYS LEU CYS SER HIS
HELIX 1 1 GLN A 27 SER A 34 1 8
SHEET 1 A 2 THR A 3 ASN A 12 0
SHEET 2 A 2 LYS A 17 ASN A 26 -1 O LYS A 17 N ASN A 12
SHEET 1 B 5 HIS A 50 TRP A 51 0
SHEET 2 B 5 LEU A 95 PHE A 97 -1 N GLU A 96 O HIS A 50
SHEET 3 B 5 ARG A 121 TYR A 124 -1 N VAL A 122 O PHE A 97
SHEET 4 B 5 PHE A 131 HIS A 137 -1 N CYS A 132 O ILE A 123
SHEET 5 B 5 LEU A 145 LEU A 147 -1 N LYS A 146 O ALA A 136
SSBOND 1 CYS A 6 CYS A 148 1555 1555 2.04
SSBOND 2 CYS A 76 CYS A 132 1555 1555 2.04
CISPEP 1 TYR A 48 PRO A 49 1 0.97
CISPEP 2 LYS A 112 PRO A 113 1 -1.64
CISPEP 3 TYR A 126 PRO A 127 1 -5.92
CISPEP 4 TYR A 48 PRO A 49 2 2.39
CISPEP 5 LYS A 112 PRO A 113 2 -1.67
CISPEP 6 TYR A 126 PRO A 127 2 -6.59
CISPEP 7 TYR A 48 PRO A 49 3 1.09
CISPEP 8 LYS A 112 PRO A 113 3 -5.41
CISPEP 9 TYR A 126 PRO A 127 3 -6.63
CISPEP 10 TYR A 48 PRO A 49 4 0.92
CISPEP 11 LYS A 112 PRO A 113 4 -2.62
CISPEP 12 TYR A 126 PRO A 127 4 -6.31
CISPEP 13 TYR A 48 PRO A 49 5 -0.11
CISPEP 14 LYS A 112 PRO A 113 5 -2.74
CISPEP 15 TYR A 126 PRO A 127 5 -7.47
CISPEP 16 TYR A 48 PRO A 49 6 1.18
CISPEP 17 LYS A 112 PRO A 113 6 -4.36
CISPEP 18 TYR A 126 PRO A 127 6 -8.91
CISPEP 19 TYR A 48 PRO A 49 7 1.17
CISPEP 20 LYS A 112 PRO A 113 7 -1.70
CISPEP 21 TYR A 126 PRO A 127 7 -6.62
CISPEP 22 TYR A 48 PRO A 49 8 2.72
CISPEP 23 LYS A 112 PRO A 113 8 -1.92
CISPEP 24 TYR A 126 PRO A 127 8 -9.18
CISPEP 25 TYR A 48 PRO A 49 9 -0.20
CISPEP 26 LYS A 112 PRO A 113 9 -0.63
CISPEP 27 TYR A 126 PRO A 127 9 -7.47
CISPEP 28 TYR A 48 PRO A 49 10 1.27
CISPEP 29 LYS A 112 PRO A 113 10 -3.96
CISPEP 30 TYR A 126 PRO A 127 10 -6.44
CISPEP 31 TYR A 48 PRO A 49 11 -0.37
CISPEP 32 LYS A 112 PRO A 113 11 -1.86
CISPEP 33 TYR A 126 PRO A 127 11 -6.87
CISPEP 34 TYR A 48 PRO A 49 12 -0.38
CISPEP 35 LYS A 112 PRO A 113 12 -1.18
CISPEP 36 TYR A 126 PRO A 127 12 -6.19
CISPEP 37 TYR A 48 PRO A 49 13 -0.95
CISPEP 38 LYS A 112 PRO A 113 13 -4.06
CISPEP 39 TYR A 126 PRO A 127 13 -7.91
CISPEP 40 TYR A 48 PRO A 49 14 1.88
CISPEP 41 LYS A 112 PRO A 113 14 -3.12
CISPEP 42 TYR A 126 PRO A 127 14 -8.50
CISPEP 43 TYR A 48 PRO A 49 15 0.41
CISPEP 44 LYS A 112 PRO A 113 15 -1.76
CISPEP 45 TYR A 126 PRO A 127 15 -6.38
CISPEP 46 TYR A 48 PRO A 49 16 0.31
CISPEP 47 LYS A 112 PRO A 113 16 -1.52
CISPEP 48 TYR A 126 PRO A 127 16 -5.34
CISPEP 49 TYR A 48 PRO A 49 17 1.57
CISPEP 50 LYS A 112 PRO A 113 17 -1.44
CISPEP 51 TYR A 126 PRO A 127 17 -8.73
CISPEP 52 TYR A 48 PRO A 49 18 1.40
CISPEP 53 LYS A 112 PRO A 113 18 -2.24
CISPEP 54 TYR A 126 PRO A 127 18 -6.83
CISPEP 55 TYR A 48 PRO A 49 19 1.52
CISPEP 56 LYS A 112 PRO A 113 19 -0.18
CISPEP 57 TYR A 126 PRO A 127 19 -5.38
CISPEP 58 TYR A 48 PRO A 49 20 3.23
CISPEP 59 LYS A 112 PRO A 113 20 -1.94
CISPEP 60 TYR A 126 PRO A 127 20 -6.43
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