Header list of 1e8l.pdb file
Complete list - n 24 2 Bytes
HEADER HYDROLASE 27-SEP-00 1E8L
TITLE NMR SOLUTION STRUCTURE OF HEN LYSOZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.17;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 CELLULAR_LOCATION: EGG WHITE;
SOURCE 6 EXPRESSION_SYSTEM: ASPERGILLUS NIGER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 5061;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TRANSFORMANT B1
KEYWDS HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 50
AUTHOR H.SCHWALBE,S.B.GRIMSHAW,A.SPENCER,M.BUCK,J.BOYD,C.M.DOBSON,
AUTHOR 2 C.REDFIELD,L.J.SMITH
REVDAT 5 24-JAN-18 1E8L 1 JRNL REMARK
REVDAT 4 24-FEB-09 1E8L 1 VERSN
REVDAT 3 31-MAR-01 1E8L 1 JRNL
REVDAT 2 23-OCT-00 1E8L 1 ENDMDL
REVDAT 1 09-OCT-00 1E8L 0
SPRSDE 09-OCT-00 1E8L 1HWA
JRNL AUTH H.SCHWALBE,S.B.GRIMSHAW,A.SPENCER,M.BUCK,J.BOYD,C.M.DOBSON,
JRNL AUTH 2 C.REDFIELD,L.J.SMITH
JRNL TITL A REFINED SOLUTION STRUCTURE OF HEN LYSOZYME DETERMINED
JRNL TITL 2 USING RESIDUAL DIPOLAR COUPLING DATA.
JRNL REF PROTEIN SCI. V. 10 677 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11274458
JRNL DOI 10.1110/PS.43301
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DETAILS OF THE NMR DATA USED IN THE
REMARK 3 STRUCTURE CALCULATIONS ARE AS FOLLOWS NUMBER OF RESTRAINTS NOE
REMARK 3 DISTANCE RESTRAINTS 1632 HYDROGEN BOND RESTRAINTS 60 DIHEDRAL
REMARK 3 ANGLE PHI RESTRAINTS 51 DIHEDRAL ANGLE CHI 1 RESTRAINTS 59
REMARK 3 RESIDUAL DIPOLAR COUPLING RESTRAINTS 209 RMS DEVIATIONS FROM
REMARK 3 EXPERIMENTAL RESTRAINTS NOE RESTRAINTS (ANGSTROMS) 0.0439
REMARK 3 DIHEDRAL RESTRAINTS (DEGREES) 0.655 DIPOLAR COUPLING RESTRAINTS
REMARK 3 (HZ) 1.159 RMS DEVIATIONS FROM IDEAL COVALENT GEOMETRY BONDS
REMARK 3 (ANGSTROMS) 0.00333 ANGLES (DEGREES) 0.492 IMPROPERS (DEGREES)
REMARK 3 0.384
REMARK 4
REMARK 4 1E8L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1290005391.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 3.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCA; HNCO; HCCH-TOCSY; 13C
REMARK 210 NOESY-HMQC; HCCH-COSY; 15N NOESY-
REMARK 210 HMQC; HMQCJ; HCCH-E.COSY; 15N
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : HOMEBUILT; DMX
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT; 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 : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 50
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 49
REMARK 210
REMARK 210 REMARK: NOE DATA FROM EXPERIMENTS ON 13C,15N-LABELED SAMPLE.
REMARK 210 STRUCTURES REFINED USING 209 RESIDUAL 1H-15N DIPOLAR COUPLING
REMARK 210 RESTRAINTS FROM MEASUREMENTS MADE IN TWO DIFFERENT LIQUID
REMARK 210 CRYSTALLINE PHASES.
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 ASN A 19 HA SER A 24 1.24
REMARK 500 O VAL A 92 H LYS A 96 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 ARG A 21 -39.86 -24.89
REMARK 500 1 GLN A 57 74.69 71.90
REMARK 500 1 ASN A 59 97.19 -67.29
REMARK 500 1 TRP A 62 -12.78 -160.76
REMARK 500 1 TRP A 63 -71.22 -131.66
REMARK 500 1 ASN A 103 93.95 -58.45
REMARK 500 1 MET A 105 5.07 82.09
REMARK 500 1 ARG A 112 45.43 -93.23
REMARK 500 1 ASN A 113 -62.40 -155.00
REMARK 500 1 LYS A 116 95.45 -54.51
REMARK 500 1 THR A 118 -149.34 -117.19
REMARK 500 1 CYS A 127 -168.35 -65.19
REMARK 500 2 ARG A 21 -39.72 -24.62
REMARK 500 2 GLN A 57 74.41 71.63
REMARK 500 2 ASN A 59 97.90 -67.28
REMARK 500 2 TRP A 62 -9.47 -161.47
REMARK 500 2 TRP A 63 -70.94 -130.87
REMARK 500 2 SER A 72 -138.66 -65.58
REMARK 500 2 ARG A 73 -38.49 -173.31
REMARK 500 2 ASN A 103 -147.57 -70.05
REMARK 500 2 MET A 105 4.69 80.59
REMARK 500 2 ARG A 112 45.08 -93.24
REMARK 500 2 ASN A 113 -63.99 -153.08
REMARK 500 2 LYS A 116 96.04 -54.35
REMARK 500 2 THR A 118 -150.14 -117.15
REMARK 500 2 ARG A 125 91.48 -65.88
REMARK 500 2 CYS A 127 -173.71 -64.03
REMARK 500 3 ARG A 21 -39.12 -24.90
REMARK 500 3 GLN A 57 74.66 69.98
REMARK 500 3 ASN A 59 99.15 -63.55
REMARK 500 3 TRP A 62 -12.02 -161.28
REMARK 500 3 SER A 72 108.16 -54.02
REMARK 500 3 ASN A 103 -148.68 -68.91
REMARK 500 3 MET A 105 5.20 81.05
REMARK 500 3 ARG A 112 44.92 -93.39
REMARK 500 3 ASN A 113 -64.14 -153.32
REMARK 500 3 LYS A 116 95.11 -55.68
REMARK 500 3 THR A 118 -148.39 -116.67
REMARK 500 3 ARG A 125 93.00 -65.64
REMARK 500 4 ARG A 21 -40.38 -25.45
REMARK 500 4 TYR A 53 79.33 -100.17
REMARK 500 4 GLN A 57 73.55 68.19
REMARK 500 4 ASN A 59 96.37 -69.31
REMARK 500 4 TRP A 62 -13.71 -161.08
REMARK 500 4 TRP A 63 -74.47 -129.32
REMARK 500 4 SER A 72 -136.64 -67.02
REMARK 500 4 ARG A 73 -44.18 -169.76
REMARK 500 4 ASN A 103 93.62 -57.96
REMARK 500 4 MET A 105 5.59 84.51
REMARK 500 4 ARG A 112 44.53 -93.33
REMARK 500
REMARK 500 THIS ENTRY HAS 611 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 193L RELATED DB: PDB
REMARK 900 THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 194L RELATED DB: PDB
REMARK 900 THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1A2Y RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME, D18A MUTANT, IN COMPLEX WITH MOUSE
REMARK 900 MONOCLONAL ANTIBODY D1.3
REMARK 900 RELATED ID: 1AKI RELATED DB: PDB
REMARK 900 THE STRUCTURE OF THE ORTHORHOMBIC FORM OF HEN EGG-WHITE LYSOZYME AT
REMARK 900 1.5 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 1AT5 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE
REMARK 900 RELATED ID: 1AT6 RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE
REMARK 900 RELATED ID: 1AZF RELATED DB: PDB
REMARK 900 CHICKEN EGG WHITE LYSOZYME CRYSTAL GROWN IN BROMIDE SOLUTION
REMARK 900 RELATED ID: 1B0D RELATED DB: PDB
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME
REMARK 900 CRYSTALS
REMARK 900 RELATED ID: 1BVX RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GEL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWH RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG
REMARK 900 WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWI RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG
REMARK 900 WHITE LYSOZYME
REMARK 900 RELATED ID: 1BWJ RELATED DB: PDB
REMARK 900 THE 1.8 A STRUCTURE OF MICROGRAVITY GROWN TETRAGONAL HEN EGG WHITE
REMARK 900 LYSOZYME
REMARK 900 RELATED ID: 1C08 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX
REMARK 900 RELATED ID: 1C10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF XENON (8 BAR)
REMARK 900 RELATED ID: 1DPW RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPD
REMARK 900 RELATED ID: 1DPX RELATED DB: PDB
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1DQJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ANTI-LYSOZYME ANTIBODY HYHEL-63 COMPLEXED
REMARK 900 WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1F0W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5
REMARK 900 RELATED ID: 1F10 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5 AT 88%
REMARK 900 RELATIVE HUMIDITY
REMARK 900 RELATED ID: 1JPO RELATED DB: PDB
REMARK 900 LOW TEMPERATURE ORTHORHOMBIC LYSOZYME
REMARK 900 RELATED ID: 1KIP RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 32)A (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIQ RELATED DB: PDB
REMARK 900 FV MUTANT Y(B 101)F (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KIR RELATED DB: PDB
REMARK 900 FV MUTANT Y(A 50)S (VL DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME
REMARK 900 RELATED ID: 1KXW RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1KXX RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1KXY RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1LCN RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME, THIOCYANATE COMPLEX
REMARK 900 RELATED ID: 1LKR RELATED DB: PDB
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE
REMARK 900 RELATED ID: 1LKS RELATED DB: PDB
REMARK 900 HEN EGG WHITE LYSOZYME NITRATE
REMARK 900 RELATED ID: 1LPI RELATED DB: PDB
REMARK 900 HEW LYSOZYME: TRP...NA CATION-PI INTERACTION
REMARK 900 RELATED ID: 1LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER
REMARK 900 RELATED ID: 1LZ8 RELATED DB: PDB
REMARK 900 LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES
REMARK 900 RELATED ID: 1LZN RELATED DB: PDB
REMARK 900 NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME
REMARK 900 RELATED ID: 1MEL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN
REMARK 900 COMPLEX WITH LYSOZYME
REMARK 900 RELATED ID: 1QTK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF KRYPTON (55 BAR)
REMARK 900 RELATED ID: 1RFP RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UCO RELATED DB: PDB
REMARK 900 HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM
REMARK 900 RELATED ID: 1UIA RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIB RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIC RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UID RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIE RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIF RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIG RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1UIH RELATED DB: PDB
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE
REMARK 900 AND CHARGED SIDE CHAINS
REMARK 900 RELATED ID: 1XEI RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEJ RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 1XEK RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION
REMARK 900 RELATED ID: 2LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 90% ACETONITRILE-WATER
REMARK 900 RELATED ID: 3LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 95% ACETONITRILE-WATER
REMARK 900 RELATED ID: 3LZT RELATED DB: PDB
REMARK 900 REFINEMENT OF TRICLINIC LYSOZYME AT ATOMIC RESOLUTION
REMARK 900 RELATED ID: 4LYO RELATED DB: PDB
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN NEAT ACETONITRILE, THEN
REMARK 900 BACK-SOAKED IN WATER
REMARK 900 RELATED ID: 4LZT RELATED DB: PDB
REMARK 900 ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K
DBREF 1E8L A 1 129 UNP P00698 LYC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
HELIX 1 1 ARG A 5 GLY A 16 1 12
HELIX 2 2 SER A 24 ASN A 37 1 14
HELIX 3 3 CYS A 80 LEU A 84 5 5
HELIX 4 4 ILE A 88 ASP A 101 1 14
HELIX 5 5 ALA A 110 CYS A 115 1 6
HELIX 6 6 ASP A 119 ILE A 124 1 6
SHEET 1 A 2 THR A 43 ARG A 45 0
SHEET 2 A 2 THR A 51 TYR A 53 -1 N ASP A 52 O ASN A 44
SSBOND 1 CYS A 6 CYS A 127 1555 1555 2.03
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.03
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.03
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.03
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 - n 24 2 Bytes