Header list of 1yx6.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 19-FEB-05 1YX6
TITLE SOLUTION STRUCTURE OF S5A UIM-2/UBIQUITIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: POLYUBIQUITIN BINDING REGION OF S5A;
COMPND 5 SYNONYM: 26S PROTEASOME REGULATORY SUBUNIT S5A, RPN10, MULTIUBIQUITIN
COMPND 6 CHAIN BINDING PROTEIN, ANTISECRETORY FACTOR-1, AF, ASF;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UBIQUITIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: SEQUENCE DATABASE RESIDUES 1-76;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PSMD4, MCB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYUBIQUITIN, PROTEASOME, S5A, UIM, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR Q.WANG,P.YOUNG,K.J.WALTERS
REVDAT 3 02-MAR-22 1YX6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1YX6 1 VERSN
REVDAT 1 19-APR-05 1YX6 0
JRNL AUTH Q.WANG,P.YOUNG,K.J.WALTERS
JRNL TITL STRUCTURE OF S5A BOUND TO MONOUBIQUITIN PROVIDES A MODEL FOR
JRNL TITL 2 POLYUBIQUITIN RECOGNITION
JRNL REF J.MOL.BIOL. V. 348 727 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15826667
JRNL DOI 10.1016/J.JMB.2005.03.007
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851, X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YX6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032024.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5 MM S5A U-15N, 2H; 2.0 MM
REMARK 210 UBIQUITIN UNLABELED; 0.5 MM S5A
REMARK 210 U-15N, 2H; 2.0 MM UBIQUITIN U-
REMARK 210 13C; 0.5 MM S5A U-13C; 2.0 MM
REMARK 210 UBIQUITIN UNLABELED
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY;
REMARK 210 4D_13C/15N-SEPARATED_NOESY; 3D
REMARK 210 HALF-FILTERED 13C-SEPARATED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 1-18
REMARK 465 RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 SER A -7
REMARK 465 SER A -6
REMARK 465 GLY A -5
REMARK 465 HIS A -4
REMARK 465 ILE A -3
REMARK 465 GLU A -2
REMARK 465 GLY A -1
REMARK 465 ARG A 0
REMARK 465 ARG B 77
REMARK 465 ASP B 78
REMARK 465 PRO B 79
REMARK 465 ASN B 80
REMARK 465 SER B 81
REMARK 465 SER B 82
REMARK 465 SER B 83
REMARK 465 VAL B 84
REMARK 465 ASP B 85
REMARK 465 LYS B 86
REMARK 465 LEU B 87
REMARK 465 ALA B 88
REMARK 465 ALA B 89
REMARK 465 ALA B 90
REMARK 465 LEU B 91
REMARK 465 GLU B 92
REMARK 465 HIS B 93
REMARK 465 HIS B 94
REMARK 465 HIS B 95
REMARK 465 HIS B 96
REMARK 465 HIS B 97
REMARK 465 HIS B 98
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 PHE B 45 H LYS B 48 1.55
REMARK 500 H1 MET B 1 O VAL B 17 1.56
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 LEU A 5 33.81 -148.87
REMARK 500 1 GLU A 11 90.39 -59.91
REMARK 500 1 ALA A 55 -173.16 -56.73
REMARK 500 1 THR A 57 -58.24 -152.71
REMARK 500 1 PHE A 76 36.57 -95.62
REMARK 500 1 ARG A 78 94.99 52.66
REMARK 500 1 PRO A 82 31.45 -77.78
REMARK 500 1 ASP A 83 149.29 60.14
REMARK 500 1 LEU A 84 -72.63 -135.66
REMARK 500 1 MET A 87 -142.50 -108.43
REMARK 500 1 PHE A 106 64.27 -112.88
REMARK 500 1 ALA A 109 -139.95 -112.15
REMARK 500 1 GLU A 110 59.66 -111.70
REMARK 500 1 ALA B 46 28.62 45.24
REMARK 500 1 LYS B 63 154.40 -46.62
REMARK 500 1 ARG B 74 32.77 -154.82
REMARK 500 2 SER A 8 -37.32 -166.13
REMARK 500 2 GLU A 11 72.06 -101.76
REMARK 500 2 VAL A 14 -66.73 -135.48
REMARK 500 2 ASP A 19 113.71 -160.22
REMARK 500 2 GLU A 60 76.16 -114.16
REMARK 500 2 ASP A 61 -41.17 -166.62
REMARK 500 2 SER A 62 67.68 -110.90
REMARK 500 2 THR A 79 45.48 -154.12
REMARK 500 2 LEU A 81 147.71 -172.66
REMARK 500 2 ASP A 83 99.58 -59.48
REMARK 500 2 GLN A 102 -70.40 -105.36
REMARK 500 2 ALA A 104 73.93 -109.14
REMARK 500 2 PHE A 106 -76.13 -133.62
REMARK 500 2 ALA A 109 52.85 -169.19
REMARK 500 2 GLU A 110 29.97 -151.53
REMARK 500 2 LYS B 63 154.39 -46.59
REMARK 500 2 ARG B 74 73.55 -150.46
REMARK 500 3 SER A 8 -43.96 -166.89
REMARK 500 3 GLU A 11 43.81 -159.65
REMARK 500 3 ASP A 19 117.43 -169.48
REMARK 500 3 ALA A 52 -52.74 -166.13
REMARK 500 3 THR A 56 58.83 -153.64
REMARK 500 3 LEU A 81 41.84 -161.47
REMARK 500 3 ASP A 83 101.56 56.70
REMARK 500 3 THR A 88 -165.45 -78.23
REMARK 500 3 PHE A 106 -48.21 -133.89
REMARK 500 3 GLN A 108 54.51 -116.19
REMARK 500 3 ALA A 109 79.02 52.82
REMARK 500 3 GLU A 110 50.68 -106.79
REMARK 500 3 ALA B 46 28.56 45.78
REMARK 500 3 LYS B 63 154.03 -46.50
REMARK 500 3 ARG B 74 95.90 -164.60
REMARK 500 4 MET A 2 -178.42 -60.86
REMARK 500 4 PHE A 10 119.55 -160.80
REMARK 500
REMARK 500 THIS ENTRY HAS 295 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 27 0.24 SIDE CHAIN
REMARK 500 1 ARG A 34 0.27 SIDE CHAIN
REMARK 500 1 ARG A 36 0.26 SIDE CHAIN
REMARK 500 1 ARG A 42 0.25 SIDE CHAIN
REMARK 500 1 ARG A 43 0.32 SIDE CHAIN
REMARK 500 1 ARG A 78 0.27 SIDE CHAIN
REMARK 500 1 ARG B 42 0.24 SIDE CHAIN
REMARK 500 1 ARG B 54 0.25 SIDE CHAIN
REMARK 500 1 ARG B 72 0.20 SIDE CHAIN
REMARK 500 1 ARG B 74 0.32 SIDE CHAIN
REMARK 500 2 ARG A 27 0.21 SIDE CHAIN
REMARK 500 2 ARG A 34 0.32 SIDE CHAIN
REMARK 500 2 ARG A 36 0.31 SIDE CHAIN
REMARK 500 2 ARG A 42 0.24 SIDE CHAIN
REMARK 500 2 ARG A 43 0.30 SIDE CHAIN
REMARK 500 2 ARG A 78 0.31 SIDE CHAIN
REMARK 500 2 ARG B 42 0.31 SIDE CHAIN
REMARK 500 2 ARG B 54 0.27 SIDE CHAIN
REMARK 500 2 ARG B 72 0.28 SIDE CHAIN
REMARK 500 2 ARG B 74 0.21 SIDE CHAIN
REMARK 500 3 ARG A 27 0.28 SIDE CHAIN
REMARK 500 3 ARG A 34 0.26 SIDE CHAIN
REMARK 500 3 ARG A 36 0.29 SIDE CHAIN
REMARK 500 3 ARG A 42 0.31 SIDE CHAIN
REMARK 500 3 ARG A 43 0.32 SIDE CHAIN
REMARK 500 3 ARG A 78 0.32 SIDE CHAIN
REMARK 500 3 ARG B 42 0.20 SIDE CHAIN
REMARK 500 3 ARG B 54 0.30 SIDE CHAIN
REMARK 500 3 ARG B 72 0.21 SIDE CHAIN
REMARK 500 3 ARG B 74 0.32 SIDE CHAIN
REMARK 500 4 ARG A 27 0.27 SIDE CHAIN
REMARK 500 4 ARG A 34 0.31 SIDE CHAIN
REMARK 500 4 ARG A 36 0.31 SIDE CHAIN
REMARK 500 4 ARG A 42 0.31 SIDE CHAIN
REMARK 500 4 ARG A 43 0.31 SIDE CHAIN
REMARK 500 4 ARG A 78 0.31 SIDE CHAIN
REMARK 500 4 ARG B 42 0.29 SIDE CHAIN
REMARK 500 4 ARG B 54 0.32 SIDE CHAIN
REMARK 500 4 ARG B 72 0.28 SIDE CHAIN
REMARK 500 4 ARG B 74 0.23 SIDE CHAIN
REMARK 500 5 ARG A 27 0.31 SIDE CHAIN
REMARK 500 5 ARG A 34 0.31 SIDE CHAIN
REMARK 500 5 ARG A 36 0.23 SIDE CHAIN
REMARK 500 5 ARG A 42 0.22 SIDE CHAIN
REMARK 500 5 ARG A 43 0.31 SIDE CHAIN
REMARK 500 5 ARG A 78 0.31 SIDE CHAIN
REMARK 500 5 ARG B 42 0.32 SIDE CHAIN
REMARK 500 5 ARG B 54 0.22 SIDE CHAIN
REMARK 500 5 ARG B 72 0.25 SIDE CHAIN
REMARK 500 5 ARG B 74 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 180 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D3Z RELATED DB: PDB
REMARK 900 UBIQUITIN
REMARK 900 RELATED ID: 1TBE RELATED DB: PDB
REMARK 900 TETRA-UBIQUITIN
REMARK 900 RELATED ID: 1YX4 RELATED DB: PDB
REMARK 900 RELATED ID: 1YX5 RELATED DB: PDB
DBREF 1YX6 A 2 112 UNP P55036 PSD4_HUMAN 196 306
DBREF 1YX6 B 1 76 UNP P62988 UBIQ_HUMAN 1 76
SEQADV 1YX6 MET A -19 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 GLY A -18 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 HIS A -17 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -16 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -15 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -14 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -13 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -12 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -11 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -10 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -9 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 HIS A -8 UNP P55036 EXPRESSION TAG
SEQADV 1YX6 SER A -7 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 SER A -6 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 GLY A -5 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 HIS A -4 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 ILE A -3 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 GLU A -2 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 GLY A -1 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 ARG A 0 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 HIS A 1 UNP P55036 CLONING ARTIFACT
SEQADV 1YX6 ARG B 77 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 ASP B 78 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 PRO B 79 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 ASN B 80 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 SER B 81 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 SER B 82 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 SER B 83 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 VAL B 84 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 ASP B 85 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 LYS B 86 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 LEU B 87 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 ALA B 88 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 ALA B 89 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 ALA B 90 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 LEU B 91 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 GLU B 92 UNP P62988 CLONING ARTIFACT
SEQADV 1YX6 HIS B 93 UNP P62988 EXPRESSION TAG
SEQADV 1YX6 HIS B 94 UNP P62988 EXPRESSION TAG
SEQADV 1YX6 HIS B 95 UNP P62988 EXPRESSION TAG
SEQADV 1YX6 HIS B 96 UNP P62988 EXPRESSION TAG
SEQADV 1YX6 HIS B 97 UNP P62988 EXPRESSION TAG
SEQADV 1YX6 HIS B 98 UNP P62988 EXPRESSION TAG
SEQRES 1 A 132 MET GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS SER
SEQRES 2 A 132 SER GLY HIS ILE GLU GLY ARG HIS MET LEU GLY LEU GLY
SEQRES 3 A 132 ALA SER ASP PHE GLU PHE GLY VAL ASP PRO SER ALA ASP
SEQRES 4 A 132 PRO GLU LEU ALA LEU ALA LEU ARG VAL SER MET GLU GLU
SEQRES 5 A 132 GLN ARG GLN ARG GLN GLU GLU GLU ALA ARG ARG ALA ALA
SEQRES 6 A 132 ALA ALA SER ALA ALA GLU ALA GLY ILE ALA THR THR GLY
SEQRES 7 A 132 THR GLU ASP SER ASP ASP ALA LEU LEU LYS MET THR ILE
SEQRES 8 A 132 SER GLN GLN GLU PHE GLY ARG THR GLY LEU PRO ASP LEU
SEQRES 9 A 132 SER SER MET THR GLU GLU GLU GLN ILE ALA TYR ALA MET
SEQRES 10 A 132 GLN MET SER LEU GLN GLY ALA GLU PHE GLY GLN ALA GLU
SEQRES 11 A 132 SER ALA
SEQRES 1 B 98 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 B 98 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 B 98 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 B 98 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 B 98 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 B 98 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY ARG ASP
SEQRES 7 B 98 PRO ASN SER SER SER VAL ASP LYS LEU ALA ALA ALA LEU
SEQRES 8 B 98 GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 ASP A 15 ALA A 18 5 4
HELIX 2 2 ASP A 19 ALA A 50 1 32
HELIX 3 3 SER A 62 PHE A 76 1 15
HELIX 4 4 THR A 88 LEU A 101 1 14
HELIX 5 5 THR B 22 GLU B 34 1 13
HELIX 6 6 PRO B 37 ASP B 39 5 3
HELIX 7 7 THR B 55 ASN B 60 5 6
SHEET 1 A 5 THR B 12 GLU B 16 0
SHEET 2 A 5 GLN B 2 LYS B 6 -1 N ILE B 3 O LEU B 15
SHEET 3 A 5 THR B 66 LEU B 71 1 O LEU B 67 N PHE B 4
SHEET 4 A 5 GLN B 41 PHE B 45 -1 N ILE B 44 O HIS B 68
SHEET 5 A 5 LYS B 48 GLN B 49 -1 O LYS B 48 N PHE B 45
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 - r 2 2 Bytes