Header list of 1cj5.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSPORT PROTEIN 22-APR-99 1CJ5
TITLE BOVINE BETA-LACTOGLOBULIN A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTOGLOBULIN A;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 VARIANT: A;
SOURCE 6 GENE: BLG CDNA;
SOURCE 7 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PTTQ18BLG;
SOURCE 12 EXPRESSION_SYSTEM_GENE: BLG CDNA
KEYWDS BETA-LACTOGLOBULIN A, DYNAMICS, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR K.KUWATA,M.HOSHINO,V.FORGE,S.ERA,C.A.BATT,Y.GOTO
REVDAT 3 16-FEB-22 1CJ5 1 REMARK SEQADV SSBOND
REVDAT 2 24-FEB-09 1CJ5 1 VERSN
REVDAT 1 26-APR-00 1CJ5 0
JRNL AUTH K.KUWATA,M.HOSHINO,V.FORGE,S.ERA,C.A.BATT,Y.GOTO
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF BOVINE BETA-LACTOGLOBULIN
JRNL TITL 2 A.
JRNL REF PROTEIN SCI. V. 8 2541 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10595563
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: NULL
REMARK 4
REMARK 4 1CJ5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000912.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 2.0
REMARK 210 IONIC STRENGTH : 0.02
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 5% WATER/95% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA 500; DMA600; DMX750
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINTS VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NONE. 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-10
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ILE A 162 O
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 ASP A 137 HA ALA A 142 1.31
REMARK 500 O LYS A 75 H ILE A 78 1.32
REMARK 500 HG1 THR A 49 O ASP A 53 1.42
REMARK 500 O PHE A 105 H GLN A 120 1.43
REMARK 500 O ASP A 11 H LYS A 14 1.45
REMARK 500 O PRO A 113 H SER A 116 1.49
REMARK 500 H LEU A 95 O LEU A 104 1.51
REMARK 500 O GLU A 127 H ASP A 129 1.56
REMARK 500 O SER A 27 HD1 HIS A 146 1.56
REMARK 500 O TYR A 20 H VAL A 123 1.58
REMARK 500 O ASN A 109 H ALA A 111 1.60
REMARK 500 O TRP A 19 O VAL A 43 2.02
REMARK 500 O LYS A 75 N ILE A 78 2.16
REMARK 500 O ILE A 84 O GLU A 89 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 4 LYS A 141 N LYS A 141 CA -0.161
REMARK 500 6 LYS A 138 C LYS A 138 O -0.120
REMARK 500 8 LYS A 141 N LYS A 141 CA -0.150
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 ILE A 29 N - CA - CB ANGL. DEV. = -14.6 DEGREES
REMARK 500 1 ALA A 73 N - CA - CB ANGL. DEV. = -8.8 DEGREES
REMARK 500 1 ILE A 84 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 1 ASP A 85 N - CA - CB ANGL. DEV. = -11.8 DEGREES
REMARK 500 2 THR A 6 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 2 ILE A 29 N - CA - CB ANGL. DEV. = -14.8 DEGREES
REMARK 500 2 ILE A 84 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 2 ALA A 139 C - N - CA ANGL. DEV. = -16.3 DEGREES
REMARK 500 3 THR A 6 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 3 ILE A 29 N - CA - CB ANGL. DEV. = -14.3 DEGREES
REMARK 500 3 ALA A 73 N - CA - CB ANGL. DEV. = -8.7 DEGREES
REMARK 500 3 ILE A 84 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 3 ASP A 85 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 3 ALA A 142 CB - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 4 ILE A 29 N - CA - CB ANGL. DEV. = -16.6 DEGREES
REMARK 500 4 ALA A 73 N - CA - CB ANGL. DEV. = -8.5 DEGREES
REMARK 500 4 ILE A 84 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 4 ASP A 85 N - CA - CB ANGL. DEV. = -10.8 DEGREES
REMARK 500 4 LEU A 140 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 4 LYS A 141 N - CA - CB ANGL. DEV. = -15.0 DEGREES
REMARK 500 5 THR A 6 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 5 ILE A 29 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 5 ILE A 84 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 5 ASP A 85 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 5 CYS A 106 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 5 ALA A 139 C - N - CA ANGL. DEV. = -16.4 DEGREES
REMARK 500 6 THR A 6 N - CA - C ANGL. DEV. = -18.6 DEGREES
REMARK 500 6 ILE A 29 N - CA - CB ANGL. DEV. = -14.8 DEGREES
REMARK 500 6 ALA A 73 N - CA - CB ANGL. DEV. = -9.1 DEGREES
REMARK 500 6 ASP A 85 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 6 ALA A 142 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 7 ILE A 29 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 7 ALA A 73 N - CA - CB ANGL. DEV. = -8.5 DEGREES
REMARK 500 7 ASP A 85 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 7 ALA A 139 C - N - CA ANGL. DEV. = -16.9 DEGREES
REMARK 500 8 ILE A 29 N - CA - CB ANGL. DEV. = -14.7 DEGREES
REMARK 500 8 ALA A 73 N - CA - CB ANGL. DEV. = -8.6 DEGREES
REMARK 500 8 ASP A 85 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 8 CYS A 106 N - CA - CB ANGL. DEV. = -14.9 DEGREES
REMARK 500 8 LEU A 140 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 8 LYS A 141 N - CA - CB ANGL. DEV. = -15.7 DEGREES
REMARK 500 9 ILE A 29 N - CA - CB ANGL. DEV. = -15.5 DEGREES
REMARK 500 9 ALA A 73 N - CA - CB ANGL. DEV. = -8.9 DEGREES
REMARK 500 9 ILE A 84 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 10 ILE A 29 N - CA - CB ANGL. DEV. = -15.1 DEGREES
REMARK 500 10 ALA A 73 N - CA - CB ANGL. DEV. = -8.6 DEGREES
REMARK 500 10 ASP A 85 N - CA - CB ANGL. DEV. = -11.0 DEGREES
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 TYR A 2 47.31 -100.03
REMARK 500 1 VAL A 3 175.49 52.04
REMARK 500 1 THR A 4 39.83 -171.98
REMARK 500 1 GLN A 5 -129.24 -144.50
REMARK 500 1 ILE A 29 -10.00 -37.21
REMARK 500 1 ALA A 34 135.12 110.98
REMARK 500 1 ALA A 37 147.44 58.97
REMARK 500 1 ARG A 40 70.70 -117.35
REMARK 500 1 THR A 49 174.46 -48.64
REMARK 500 1 PRO A 50 -15.09 -49.53
REMARK 500 1 GLU A 51 -5.75 149.64
REMARK 500 1 ASN A 63 -37.59 -23.29
REMARK 500 1 ASP A 64 -17.96 -149.27
REMARK 500 1 THR A 76 -128.19 33.89
REMARK 500 1 ILE A 78 93.06 80.07
REMARK 500 1 ALA A 80 5.75 -154.35
REMARK 500 1 ASN A 90 -10.74 -156.05
REMARK 500 1 THR A 97 113.70 170.07
REMARK 500 1 ASP A 98 -1.56 57.28
REMARK 500 1 LYS A 101 -25.98 136.95
REMARK 500 1 SER A 110 -40.91 26.39
REMARK 500 1 GLU A 112 60.32 -171.26
REMARK 500 1 LEU A 117 109.66 -55.00
REMARK 500 1 ARG A 124 -36.45 -177.95
REMARK 500 1 THR A 125 167.75 14.53
REMARK 500 1 ASP A 130 -3.03 -43.86
REMARK 500 1 PRO A 144 50.55 -90.80
REMARK 500 1 MET A 145 150.77 -28.86
REMARK 500 1 CYS A 160 -122.96 51.93
REMARK 500 2 THR A 4 18.16 -165.52
REMARK 500 2 GLN A 5 -124.87 -155.01
REMARK 500 2 ILE A 29 -8.37 -35.86
REMARK 500 2 ALA A 34 130.19 71.49
REMARK 500 2 ALA A 37 138.87 -31.53
REMARK 500 2 LEU A 39 32.08 -89.53
REMARK 500 2 ARG A 40 67.67 -115.47
REMARK 500 2 THR A 49 175.99 -49.52
REMARK 500 2 PRO A 50 -15.85 -47.28
REMARK 500 2 GLU A 51 -9.57 149.31
REMARK 500 2 ASN A 63 -36.84 -24.28
REMARK 500 2 ASP A 64 -18.50 -147.53
REMARK 500 2 THR A 76 -128.63 36.55
REMARK 500 2 ILE A 78 95.54 82.20
REMARK 500 2 ALA A 80 4.67 -156.41
REMARK 500 2 ASN A 88 30.10 82.06
REMARK 500 2 ASN A 90 -7.89 -156.96
REMARK 500 2 THR A 97 112.01 171.16
REMARK 500 2 ASP A 98 -0.68 62.23
REMARK 500 2 LYS A 101 -25.10 139.45
REMARK 500 2 SER A 110 -44.99 33.82
REMARK 500
REMARK 500 THIS ENTRY HAS 296 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 ARG A 40 0.32 SIDE CHAIN
REMARK 500 1 ARG A 124 0.23 SIDE CHAIN
REMARK 500 1 ARG A 148 0.30 SIDE CHAIN
REMARK 500 2 ARG A 40 0.23 SIDE CHAIN
REMARK 500 2 ARG A 124 0.09 SIDE CHAIN
REMARK 500 2 ARG A 148 0.29 SIDE CHAIN
REMARK 500 3 ARG A 40 0.30 SIDE CHAIN
REMARK 500 3 ARG A 124 0.31 SIDE CHAIN
REMARK 500 3 ARG A 148 0.30 SIDE CHAIN
REMARK 500 4 ARG A 40 0.15 SIDE CHAIN
REMARK 500 4 ARG A 124 0.20 SIDE CHAIN
REMARK 500 4 ARG A 148 0.18 SIDE CHAIN
REMARK 500 5 ARG A 40 0.18 SIDE CHAIN
REMARK 500 5 ARG A 124 0.15 SIDE CHAIN
REMARK 500 5 ARG A 148 0.10 SIDE CHAIN
REMARK 500 6 ARG A 40 0.14 SIDE CHAIN
REMARK 500 6 ARG A 124 0.20 SIDE CHAIN
REMARK 500 6 ARG A 148 0.25 SIDE CHAIN
REMARK 500 7 ARG A 40 0.31 SIDE CHAIN
REMARK 500 7 ARG A 124 0.27 SIDE CHAIN
REMARK 500 7 ARG A 148 0.29 SIDE CHAIN
REMARK 500 8 ARG A 40 0.19 SIDE CHAIN
REMARK 500 8 ARG A 124 0.24 SIDE CHAIN
REMARK 500 9 ARG A 40 0.15 SIDE CHAIN
REMARK 500 9 ARG A 148 0.27 SIDE CHAIN
REMARK 500 10 ARG A 40 0.15 SIDE CHAIN
REMARK 500 10 ARG A 124 0.26 SIDE CHAIN
REMARK 500 10 ARG A 148 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CJ5 A 3 162 UNP P02754 LACB_BOVIN 19 178
SEQADV 1CJ5 ALA A 1 UNP P02754 INSERTION
SEQADV 1CJ5 TYR A 2 UNP P02754 INSERTION
SEQADV 1CJ5 PHE A 105 UNP P02754 VAL 121 CONFLICT
SEQRES 1 A 162 ALA TYR VAL THR GLN THR MET LYS GLY LEU ASP ILE GLN
SEQRES 2 A 162 LYS VAL ALA GLY THR TRP TYR SER LEU ALA MET ALA ALA
SEQRES 3 A 162 SER ASP ILE SER LEU LEU ASP ALA GLN SER ALA PRO LEU
SEQRES 4 A 162 ARG VAL TYR VAL GLU GLU LEU LYS PRO THR PRO GLU GLY
SEQRES 5 A 162 ASP LEU GLU ILE LEU LEU GLN LYS TRP GLU ASN ASP GLU
SEQRES 6 A 162 CYS ALA GLN LYS LYS ILE ILE ALA GLU LYS THR LYS ILE
SEQRES 7 A 162 PRO ALA VAL PHE LYS ILE ASP ALA LEU ASN GLU ASN LYS
SEQRES 8 A 162 VAL LEU VAL LEU ASP THR ASP TYR LYS LYS TYR LEU LEU
SEQRES 9 A 162 PHE CYS MET GLU ASN SER ALA GLU PRO GLU GLN SER LEU
SEQRES 10 A 162 VAL CYS GLN CYS LEU VAL ARG THR PRO GLU VAL ASP ASP
SEQRES 11 A 162 GLU ALA LEU GLU LYS PHE ASP LYS ALA LEU LYS ALA LEU
SEQRES 12 A 162 PRO MET HIS ILE ARG LEU SER PHE ASN PRO THR GLN LEU
SEQRES 13 A 162 GLU GLU GLN CYS HIS ILE
HELIX 1 H ASP A 130 ALA A 139 1 10
SHEET 1 B0 1 THR A 4 THR A 6 0
SHEET 1 BA 1 THR A 18 SER A 27 0
SHEET 1 BB 1 GLU A 44 PRO A 48 0
SHEET 1 BC 1 GLU A 55 GLU A 62 0
SHEET 1 BD 1 CYS A 66 LYS A 75 0
SHEET 1 BE 1 VAL A 81 ILE A 84 0
SHEET 1 BF 1 GLU A 89 LEU A 95 0
SHEET 1 BG 1 LYS A 101 ASN A 109 0
SHEET 1 BH 1 LEU A 117 THR A 125 0
SHEET 1 BI 1 HIS A 146 ASN A 152 0
SSBOND 1 CYS A 66 CYS A 160 1555 1555 2.93
SSBOND 2 CYS A 106 CYS A 119 1555 1555 2.92
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