{"feature_sets":[{"about":"Physico-chemical properties of a protein sequence (ProtParam-compatible) and its composition","features":[{"name":"length","group":"size","unit":"residues","description":"Number of residues"},{"name":"molecular_weight","group":"size","unit":"Da","description":"Average molecular weight (average residue masses plus one water)","reference":"Gasteiger et al. (2005) Protein identification and analysis tools on the ExPASy server"},{"name":"isoelectric_point","group":"charge","unit":"pH","description":"Theoretical pI: the pH at which the net charge is zero (Bjellqvist pK values with terminal-dependent values)","reference":"Bjellqvist et al. (1993) Electrophoresis 14:1023; (1994) 15:529"},{"name":"net_charge_ph7","group":"charge","unit":"e","description":"Net charge at pH 7.0 with the same pK values","reference":"Henderson–Hasselbalch"},{"name":"charge_density_ph7","group":"charge","unit":"e/residue","description":"Net charge at pH 7.0 per residue"},{"name":"extinction_280_reduced","group":"optics","unit":"M^-1 cm^-1","description":"Molar extinction coefficient at 280 nm with every cysteine reduced: 5500·W + 1490·Y","reference":"Pace et al. (1995) Protein Sci 4:2411"},{"name":"extinction_280_cystines","group":"optics","unit":"M^-1 cm^-1","description":"Molar extinction coefficient at 280 nm with every cysteine pair forming a cystine: + 125 per cystine","reference":"Pace et al. (1995) Protein Sci 4:2411"},{"name":"absorbance_280_1mgml","group":"optics","unit":"AU","description":"Absorbance at 280 nm of a 1 mg/mL solution (1 cm, cysteines reduced)"},{"name":"instability_index","group":"stability","description":"Instability index; above 40 suggests a protein unstable in vitro","reference":"Guruprasad et al. (1990) Protein Eng 4:155"},{"name":"aliphatic_index","group":"stability","description":"Relative volume of aliphatic side chains: X(Ala) + 2.9·X(Val) + 3.9·(X(Ile) + X(Leu)), mole percent","reference":"Ikai (1980) J Biochem 88:1895"},{"name":"gravy","group":"hydropathy","description":"Grand average of hydropathy (Kyte–Doolittle)","reference":"Kyte & Doolittle (1982) J Mol Biol 157:105"},{"name":"aromaticity","group":"hydropathy","unit":"fraction","description":"Fraction of F, W and Y","reference":"Lobry & Gautier (1994) Nucleic Acids Res 22:3174"},{"name":"frac_tiny","group":"classes","unit":"fraction","description":"Fraction of tiny residues (ACGST)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_small","group":"classes","unit":"fraction","description":"Fraction of small residues (ABCDGNPSTV)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_aliphatic","group":"classes","unit":"fraction","description":"Fraction of aliphatic residues (AILV)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_aromatic","group":"classes","unit":"fraction","description":"Fraction of aromatic residues (FHWY)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_nonpolar","group":"classes","unit":"fraction","description":"Fraction of nonpolar residues (ACFGILMPVWY)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_polar","group":"classes","unit":"fraction","description":"Fraction of polar residues (DEHKNQRSTZ)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_charged","group":"classes","unit":"fraction","description":"Fraction of charged residues (BDEHKRZ)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_basic","group":"classes","unit":"fraction","description":"Fraction of basic residues (HKR)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"frac_acidic","group":"classes","unit":"fraction","description":"Fraction of acidic residues (BDEZ)","reference":"EMBOSS pepstats residue classes (Rice et al. 2000)"},{"name":"cysteine_count","group":"composition","unit":"residues","description":"Number of cysteines (disulfide capacity)"},{"name":"entropy_bits","group":"complexity","unit":"bits","description":"Shannon entropy of the amino-acid composition"},{"name":"entropy_normalized","group":"complexity","unit":"fraction","description":"Shannon entropy divided by its maximum, log2(20)"},{"name":"low_complexity_fraction","group":"complexity","unit":"fraction","description":"Fraction of residues SEG masks as low complexity (window 12, 2.2, 2.5, as BLAST)","reference":"Wootton & Federhen (1993) Comput Chem 17:149"},{"name":"ambiguous_fraction","group":"complexity","unit":"fraction","description":"Fraction of letters outside the 20 standard amino acids (X, B, Z, J, U, O)"},{"name":"aa_A","group":"composition","unit":"fraction","description":"Fraction of alanine"},{"name":"aa_C","group":"composition","unit":"fraction","description":"Fraction of cysteine"},{"name":"aa_D","group":"composition","unit":"fraction","description":"Fraction of aspartate"},{"name":"aa_E","group":"composition","unit":"fraction","description":"Fraction of glutamate"},{"name":"aa_F","group":"composition","unit":"fraction","description":"Fraction of phenylalanine"},{"name":"aa_G","group":"composition","unit":"fraction","description":"Fraction of glycine"},{"name":"aa_H","group":"composition","unit":"fraction","description":"Fraction of histidine"},{"name":"aa_I","group":"composition","unit":"fraction","description":"Fraction of isoleucine"},{"name":"aa_K","group":"composition","unit":"fraction","description":"Fraction of lysine"},{"name":"aa_L","group":"composition","unit":"fraction","description":"Fraction of leucine"},{"name":"aa_M","group":"composition","unit":"fraction","description":"Fraction of methionine"},{"name":"aa_N","group":"composition","unit":"fraction","description":"Fraction of asparagine"},{"name":"aa_P","group":"composition","unit":"fraction","description":"Fraction of proline"},{"name":"aa_Q","group":"composition","unit":"fraction","description":"Fraction of glutamine"},{"name":"aa_R","group":"composition","unit":"fraction","description":"Fraction of arginine"},{"name":"aa_S","group":"composition","unit":"fraction","description":"Fraction of serine"},{"name":"aa_T","group":"composition","unit":"fraction","description":"Fraction of threonine"},{"name":"aa_V","group":"composition","unit":"fraction","description":"Fraction of valine"},{"name":"aa_W","group":"composition","unit":"fraction","description":"Fraction of tryptophan"},{"name":"aa_Y","group":"composition","unit":"fraction","description":"Fraction of tyrosine"}],"kind":"protein","name":"gl1x-protein-1","prefix":"p_"},{"about":"Size, shape, secondary structure, contacts, confidence and GSA composition of a protein chain with coordinates","features":[{"name":"residues","group":"size","unit":"residues","description":"Residues with CA coordinates"},{"name":"radius_of_gyration","group":"shape","unit":"Å","description":"Radius of gyration of the CA atoms"},{"name":"rg_relative","group":"shape","unit":"ratio","description":"Radius of gyration over that of a compact chain of the same length, 2.2·N^0.38 Å; near 1 for a compact globule, larger for extended or multi-domain chains","reference":"Skolnick, Kolinski & Ortiz (1997) J Mol Biol 265:217"},{"name":"asphericity","group":"shape","description":"Relative shape anisotropy κ² of the CA gyration tensor: 0 for a sphere, 1 for a rod","reference":"Theodorou & Suter (1985) Macromolecules 18:1206"},{"name":"max_dimension","group":"shape","unit":"Å","description":"Largest distance between two CA atoms"},{"name":"end_to_end_distance","group":"shape","unit":"Å","description":"Distance between the first and the last CA atom"},{"name":"helix_fraction","group":"secondary","unit":"fraction","description":"Fraction of residues TM-align assigns to a helix (H)","reference":"Zhang & Skolnick (2005) Nucleic Acids Res 33:2302 (TM-align secondary structure from CA distances)"},{"name":"strand_fraction","group":"secondary","unit":"fraction","description":"Fraction of residues TM-align assigns to a strand (E)","reference":"Zhang & Skolnick (2005) Nucleic Acids Res 33:2302 (TM-align secondary structure from CA distances)"},{"name":"turn_fraction","group":"secondary","unit":"fraction","description":"Fraction of residues TM-align assigns to a turn (T)","reference":"Zhang & Skolnick (2005) Nucleic Acids Res 33:2302 (TM-align secondary structure from CA distances)"},{"name":"coil_fraction","group":"secondary","unit":"fraction","description":"Fraction of residues TM-align assigns to coil (C)","reference":"Zhang & Skolnick (2005) Nucleic Acids Res 33:2302 (TM-align secondary structure from CA distances)"},{"name":"helix_segments","group":"secondary","unit":"count","description":"Helices: runs of 3 or more H residues (helices of about 7 residues and more)","reference":"Zhang & Skolnick (2005) Nucleic Acids Res 33:2302 (TM-align secondary structure from CA distances)"},{"name":"strand_segments","group":"secondary","unit":"count","description":"Strands: runs of 2 or more E residues (strands of about 6 residues and more)","reference":"Zhang & Skolnick (2005) Nucleic Acids Res 33:2302 (TM-align secondary structure from CA distances)"},{"name":"contacts_per_residue","group":"contacts","unit":"contacts/residue","description":"CA–CA contacts per residue","reference":"CA–CA distance below 8 Å, sequence separation 6 or more (CASP ranges: medium 12–23, long 24+)"},{"name":"medium_range_contact_fraction","group":"contacts","unit":"fraction","description":"Fraction of contacts at a sequence separation of 12 to 23","reference":"CA–CA distance below 8 Å, sequence separation 6 or more (CASP ranges: medium 12–23, long 24+)"},{"name":"long_range_contact_fraction","group":"contacts","unit":"fraction","description":"Fraction of contacts at a sequence separation of 24 or more","reference":"CA–CA distance below 8 Å, sequence separation 6 or more (CASP ranges: medium 12–23, long 24+)"},{"name":"relative_contact_order","group":"contacts","unit":"fraction","description":"Relative contact order: mean sequence separation of the contacts over the chain length (CA contacts as defined here)","reference":"Plaxco, Simons & Baker (1998) J Mol Biol 277:985"},{"name":"absolute_contact_order","group":"contacts","unit":"residues","description":"Absolute contact order: mean sequence separation of the contacts","reference":"Ivankov et al. (2003) Protein Sci 12:2057"},{"name":"chain_breaks","group":"quality","unit":"count","description":"Consecutive CA atoms more than 4.3 Å apart (missing residues)"},{"name":"mean_b","group":"quality","unit":"Ų or pLDDT","description":"Mean B-factor of the CA atoms; for predicted models, the mean pLDDT"},{"name":"std_b","group":"quality","unit":"Ų or pLDDT","description":"Standard deviation of the CA B-factors (pLDDT for predicted models)"},{"name":"predicted","group":"quality","unit":"flag","description":"1 when the structure is a computed model (B-factors are then pLDDT)"},{"name":"low_confidence_fraction","group":"quality","unit":"fraction","description":"Predicted models: fraction of residues with pLDDT below 70; 0 for experimental structures","reference":"AlphaFold DB confidence bands"},{"name":"gsa_entropy_bits","group":"gsa","unit":"bits","description":"Shannon entropy of the chain's GSA state composition"},{"name":"gsa_a","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state a","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_b","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state b","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_c","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state c","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_d","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state d","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_e","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state e","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_f","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state f","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_g","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state g","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_h","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state h","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_i","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state i","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_j","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state j","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_k","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state k","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_l","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state l","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_m","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state m","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_n","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state n","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_o","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state o","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_p","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state p","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_q","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state q","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_r","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state r","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_s","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state s","reference":"GL1X structural alphabet (internal/fold/gsa.go)"},{"name":"gsa_t","group":"gsa","unit":"fraction","description":"Fraction of residues in GSA state t","reference":"GL1X structural alphabet (internal/fold/gsa.go)"}],"kind":"structure","name":"gl1x-structure-1","prefix":"s_"}],"gl1f":{"default_scale_q":1000,"features_text":"the GL1F NFT features string: one feature name per line, in input order, as a model NFT stores its inputs","note":"a model trained on a dataset's feature columns takes them in the dataset's column order; quantize new inputs with the model's own scale_q","packing":"one little-endian int32 per input in feature order: the bytes the GL1F runtime's predict functions take","quantization":"q = clamp(round(x · scale_q)) to the int32 range, the GL1F Forest input rule (half rounds away from zero for positive x, toward +∞ as JavaScript's Math.round)"},"molnft_paths":{"0xd58b01f6c18086e5202cdc5d7ad3e41790360102:224162":"/molnft/8WKI"},"record":{"accession":null,"collection_name":"MolNFT v2 / PDB Bank","contract_address":"0xd58b01f6c18086e5202cdc5d7ad3e41790360102","molecular_id":"8WKI","molnft_version":"v2","pdb_id":"8WKI","structure_available":true,"title":"Cryo-EM structure of the distal rod-hook within the flagellar motor-hook complex in the CW state.","token_id":"224162","url":"/molnft/8WKI"},"sequences":[{"ambiguous":0,"chain_id":"ZF","chains":["ZF","ZG","ZH","ZI","ZJ","ZK","ZL","ZM","ZN","ZO","ZP","ZQ","ZR","ZS","ZT","ZU","ZV","ZW","ZX","ZY","ZZ","Za","Zb","Zc","Zd","Ze","Zf","Zg","Zh"],"is_primary":true,"length":403,"notes":["403 residues, 42,210.5 Da (42.2 kDa) average mass","Theoretical pI 4.77; net charge -8.3 at pH 7 (acidic)","Extinction at 280 nm: 27,390 M⁻¹cm⁻¹ with every cysteine pair a cystine, 27,390 reduced; A280 of 1 mg/mL ≈ 0.649","Instability index 13.50: classified stable in vitro (below 40)","GRAVY -0.275: hydrophilic on average; aliphatic index 73.6 (higher suggests more thermostable)","SEG masks 13.2% of the residues as low complexity"],"sequence":"MSFSQAVSGLNAAATNLDVIGNNIANSATYGFKSGTASFADMFAGSKVGLGVKVAGITQDFTDGTTTNTGRGLDVAISQNGFFRLVDSNGSVFYSRNGQFKLDENRNLVNMQGMQLTGYPATGTPPTIQQGANPAPITIPNTLMAAKSTTTASMQINLNSTDPVPSKTPFSVSDADSYNKKGTVTVYDSQGNAHDMNVYFVKTKDNEWAVYTHDSSDPAATAPTTASTTLKFNENGILESGGTVNITTGTINGATAATFSLSFLNSMQQNTGANNIVATNQNGYKPGDLVSYQINNDGTVVGNYSNEQEQVLGQIVLANFANNEGLASQGDNVWAATQASGVALLGTAGSGNFGKLTNGALEASNVDLSKELVNMIVAQRNYQSNAQTIKTQDQILNTLVNLR","sequence_key":"pdb-chain:ZF","sequence_keys":["pdb-chain:ZF","pdb-chain:ZG","pdb-chain:ZH","pdb-chain:ZI","pdb-chain:ZJ","pdb-chain:ZK","pdb-chain:ZL","pdb-chain:ZM","pdb-chain:ZN","pdb-chain:ZO","pdb-chain:ZP","pdb-chain:ZQ","pdb-chain:ZR","pdb-chain:ZS","pdb-chain:ZT","pdb-chain:ZU","pdb-chain:ZV","pdb-chain:ZW","pdb-chain:ZX","pdb-chain:ZY","pdb-chain:ZZ","pdb-chain:Za","pdb-chain:Zb","pdb-chain:Zc","pdb-chain:Zd","pdb-chain:Ze","pdb-chain:Zf","pdb-chain:Zg","pdb-chain:Zh"],"sequence_type":"protein","set":"gl1x-protein-1","sha256":"7c0f2a912fac46f10adcb15f4cc5e5839909e0fe4d7562a646f06419c0ab7e2f","values":[403,42210.48,4.7744,-8.3036,-0.020605,27390,27390,0.6489,13.4956,73.6228,-0.2747,0.07196,0.39206,0.657568,0.282878,0.076923,0.503722,0.496278,0.129032,0.057072,0.07196,0,3.918815,0.906728,0.131514,0,0.101737,0,0.049628,0.022333,0.039702,0.096774,0.004963,0.042184,0.037221,0.066998,0.022333,0.114144,0.029777,0.059553,0.014888,0.084367,0.109181,0.07196,0.004963,0.027295]},{"ambiguous":0,"chain_id":"0","chains":["0","1","2","3","4","5","6","7","8","9","ZA","ZB","ZC","ZD","ZE","r","s","t","u","v","w","x","y","z"],"is_primary":false,"length":260,"notes":["260 residues, 27,770.0 Da (27.8 kDa) average mass","Theoretical pI 4.68; net charge -7.4 at pH 7 (acidic)","Extinction at 280 nm: 14,440 M⁻¹cm⁻¹ with every cysteine pair a cystine, 14,440 reduced; A280 of 1 mg/mL ≈ 0.520","Instability index 28.59: classified stable in vitro (below 40)","GRAVY -0.248: hydrophilic on average; aliphatic index 86.6 (higher suggests more thermostable)","SEG masks 4.6% of the residues as low complexity"],"sequence":"MISSLWIAKTGLDAQQTNMDVIANNLANVSTNGFKRQRAVFEDLLYQTIRQPGAQSSEQTTLPSGLQIGTGVRPVATERLHSQGNLSQTNNSKDVAIKGQGFFQVMLPDGTSAYTRDGSFQVDQNGQLVTAGGFQVQPAITIPANALSITIGRDGVVSVTQQGQAAPVQVGQLNLTTFMNDTGLESIGENLYIETQSSGAPNESTPGLNGAGLLYQGYVETSNVNVAEELVNMIQVQRAYEINSKAVSTTDQMLQKLTQL","sequence_key":"pdb-chain:0","sequence_keys":["pdb-chain:0","pdb-chain:1","pdb-chain:2","pdb-chain:3","pdb-chain:4","pdb-chain:5","pdb-chain:6","pdb-chain:7","pdb-chain:8","pdb-chain:9","pdb-chain:ZA","pdb-chain:ZB","pdb-chain:ZC","pdb-chain:ZD","pdb-chain:ZE","pdb-chain:r","pdb-chain:s","pdb-chain:t","pdb-chain:u","pdb-chain:v","pdb-chain:w","pdb-chain:x","pdb-chain:y","pdb-chain:z"],"sequence_type":"protein","set":"gl1x-protein-1","sha256":"eebedefbc2c8fe931af5cac557fa777c9caabee24f70a790ade8f91a8b2b5f0d","values":[260,27769.97,4.6792,-7.3824,-0.028394,14440,14440,0.52,28.5938,86.6154,-0.2477,0.053846,0.342308,0.569231,0.3,0.057692,0.507692,0.492308,0.138462,0.057692,0.080769,0,3.944785,0.912737,0.046154,0,0.076923,0,0.038462,0.042308,0.026923,0.096154,0.003846,0.053846,0.023077,0.088462,0.023077,0.073077,0.034615,0.111538,0.030769,0.076923,0.092308,0.080769,0.003846,0.023077]}],"sequences_truncated":false,"structure":{"chains":[{"accessions":["P0A1J1"],"chain_id":"ZF","chains":["ZF","ZG","ZH","ZI","ZJ","ZK","ZL","ZM","ZN","ZO","ZP","ZQ","ZR","ZS","ZT","ZU","ZV","ZW","ZX","ZY","ZZ","Za","Zb","Zc","Zd","Ze","Zf","Zg","Zh"],"kind":"protein","notes":["Radius of gyration 35.88 Å, 1.67× that of a compact chain of 401 residues: extended or made of several domains","Secondary structure (TM-align): 15.2% helix in 2 helices, 37.9% strand in 35 strands","2.26 CA contacts per residue, 57.9% long-range; relative contact order 0.236","Mean B-factor 71.0 Ų (sd 41.2)"],"residues":401,"secondary":"CCHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEEEECCTCCECCEECCCEEECCCCCCEEECCCCCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCEECTTCCEEECCEEECTTCEECCCCCCCCEEECCCEEEEECCCCEEEEEEEECCCEEECCCCCCCHCCHHCCCEEEEEEECTTCEEEEEEEEEEECTTTCEEEEEECCHCCCCCCCCCCCCEEEECTTCCCCTCCCEEEEEEECHTCCCEEEEEEECCCEECCCCCCEECCEEECCECCEEECCEEECTTCCEEEECTTCCEEECCEEEEEECCCCHCCEECTTTCEEECTHTCCCEEECTTCTTCEEEECCCEEEECCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[401,35.8803,1.672,0.716,137.284,20.23,0.15212,0.379052,0.0798,0.389027,2,35,2.2594,0.246137,0.57947,0.235881,94.5883,0,71.008,41.199,0,0,4.041024,0.122195,0.052369,0.004988,0.0399,0.054863,0.042394,0.007481,0.072319,0.0399,0.032419,0.104738,0.102244,0.044888,0.042394,0.032419,0.022444,0.044888,0.087282,0.027431,0.022444]},{"accessions":["P0A1J3"],"chain_id":"2","chains":["2","3","4","5","6","7","8","9","ZA","ZB","ZC","ZD","ZE"],"kind":"protein","notes":["Radius of gyration 26.84 Å, 1.47× that of a compact chain of 260 residues: extended or made of several domains","Secondary structure (TM-align): 22.7% helix in 2 helices, 32.7% strand in 20 strands","2.02 CA contacts per residue, 62.9% long-range; relative contact order 0.247","Mean B-factor 56.3 Ų (sd 12.8)"],"residues":260,"secondary":"CCTHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEECCEECCCETCCCCTTTCEECCCCEEEEEEEECCEEEEECCCCEEECCCCCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCCECTTCCECTTCEEECTCCCCEEECTTCCEEEEETCCCCEEECCEEEEEECTCCHCCEECTTTCEEECTHTCCCEEECTCCHCCEEEECCCEEECCCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[260,26.8377,1.4745,0.5319,100.47,16.365,0.226923,0.326923,0.096154,0.35,2,20,2.0192,0.2,0.628571,0.246637,64.1257,0,56.283,12.845,0,0,4.148922,0.1,0.053846,0.007692,0.046154,0.057692,0.053846,0.011538,0.096154,0.030769,0.053846,0.080769,0.076923,0.05,0.042308,0.034615,0.034615,0.053846,0.053846,0.030769,0.030769]},{"accessions":["P0A1J3"],"chain_id":"0","chains":["0","x","y","z"],"kind":"protein","notes":["Radius of gyration 25.33 Å, 1.42× that of a compact chain of 248 residues: extended or made of several domains","Secondary structure (TM-align): 23.8% helix in 2 helices, 35.1% strand in 21 strands","2.05 CA contacts per residue, 64.2% long-range; relative contact order 0.254","Mean B-factor 58.7 Ų (sd 12.1)","1 chain breaks (residues missing from the coordinates)"],"residues":248,"secondary":"CCCCHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEECCEEEEETTCCEEECCEEECCEEEEECCEEEEECCCCCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCEECTTCCECTHCEEECTCCCCEEECTTCCEEEECTCCCCEEECCEEEEEECTCCHCCEECTTTCEEECTHCCCEEEECTTCHTCEEEECCCEEEECCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[248,25.3274,1.4167,0.5683,98.046,16.95,0.237903,0.350806,0.08871,0.322581,2,21,2.0524,0.204322,0.642436,0.253854,66.002,1,58.705,12.132,0,0,4.163419,0.108871,0.044355,0.020161,0.040323,0.052419,0.052419,0.016129,0.084677,0.040323,0.060484,0.072581,0.076613,0.048387,0.044355,0.016129,0.03629,0.052419,0.072581,0.03629,0.024194]},{"accessions":["P0A1J3"],"chain_id":"1","chains":["1"],"kind":"protein","notes":["Radius of gyration 25.78 Å, 1.43× that of a compact chain of 252 residues: extended or made of several domains","Secondary structure (TM-align): 23.4% helix in 2 helices, 33.7% strand in 21 strands","1.98 CA contacts per residue, 64.3% long-range; relative contact order 0.254","Mean B-factor 66.4 Ų (sd 14.0)","1 chain breaks (residues missing from the coordinates)"],"residues":252,"secondary":"CCCCHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEECCEEEEECCCCCCCCEEECCEEECCEEECCCCEEEEECCCCCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCEECTTCCECTTCEEECTCCCCEEECTTCCEEEEETCCCCEEECCEEEEEEECCCHCCEECTHCCEEECTHCCCEEEECTTCHTCEEEECCCEECCCCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[252,25.7798,1.4333,0.5526,97.344,17.072,0.234127,0.337302,0.071429,0.357143,2,21,1.9802,0.200401,0.643287,0.254185,66.0882,1,66.391,14.042,0,0,4.154157,0.095238,0.047619,0.019841,0.039683,0.059524,0.051587,0.015873,0.087302,0.043651,0.055556,0.09127,0.09127,0.043651,0.027778,0.019841,0.035714,0.059524,0.051587,0.039683,0.02381]},{"accessions":["P0A1J3"],"chain_id":"r","chains":["r","u"],"kind":"protein","notes":["Radius of gyration 26.17 Å, 1.45× that of a compact chain of 254 residues: extended or made of several domains","Secondary structure (TM-align): 23.2% helix in 2 helices, 34.3% strand in 19 strands","2.01 CA contacts per residue, 63.0% long-range; relative contact order 0.250","Mean B-factor 57.1 Ų (sd 14.1)","1 chain breaks (residues missing from the coordinates)"],"residues":254,"secondary":"CCHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEECCEEECCCCCCCCTCCECEEEEEEEEECCEEEEECCEEEEECCCCCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCEECTTCCECTTCEEECTCCCCEEECTHCCEEEEETCCCCEEECCEEEEEECCCCHCCECCTTTCEEECTHCCCEEEECTTTHTCEEEECCCEECCCCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[254,26.1712,1.4507,0.5518,97.559,19.507,0.232283,0.34252,0.082677,0.34252,2,19,2.0118,0.209393,0.630137,0.250284,64.5734,1,57.143,14.142,0,0,4.13309,0.098425,0.047244,0.015748,0.051181,0.051181,0.051181,0.007874,0.090551,0.035433,0.059055,0.074803,0.086614,0.043307,0.03937,0.015748,0.031496,0.062992,0.070866,0.043307,0.023622]},{"accessions":["P0A1J3"],"chain_id":"s","chains":["s","v"],"kind":"protein","notes":["Radius of gyration 26.22 Å, 1.45× that of a compact chain of 255 residues: extended or made of several domains","Secondary structure (TM-align): 23.5% helix in 2 helices, 34.9% strand in 20 strands","2.01 CA contacts per residue, 62.9% long-range; relative contact order 0.246","Mean B-factor 49.5 Ų (sd 12.3)","1 chain breaks (residues missing from the coordinates)"],"residues":255,"secondary":"CCHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEECCEEECCCCCCCCTEEEEEEEECCEEECCEEEEECCEEEEECCCCCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCEECTTCCECTTCEEECTCCCCEEECTHCCEEEEETCCCCEEECCEEEEEEECCCHCCECCTTTCEEECTHCCCEEEECTCTHTCEEEECCCEECCCCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[255,26.2196,1.4512,0.5545,98.048,17.621,0.235294,0.34902,0.078431,0.337255,2,20,2.0078,0.210938,0.628906,0.245898,63.6875,1,49.526,12.324,0,0,4.117287,0.086275,0.043137,0.015686,0.047059,0.054902,0.05098,0.007843,0.098039,0.043137,0.066667,0.086275,0.101961,0.047059,0.023529,0.019608,0.035294,0.05098,0.058824,0.039216,0.023529]},{"accessions":["P0A1J3"],"chain_id":"t","chains":["t"],"kind":"protein","notes":["Radius of gyration 26.24 Å, 1.45× that of a compact chain of 256 residues: extended or made of several domains","Secondary structure (TM-align): 24.2% helix in 2 helices, 34.0% strand in 21 strands","1.97 CA contacts per residue, 63.6% long-range; relative contact order 0.251","Mean B-factor 46.7 Ų (sd 11.5)","1 chain breaks (residues missing from the coordinates)"],"residues":256,"secondary":"CCHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEECCEEECCEECCCCCCCECEEEECCEEECCEEEEECCEEEEECCCTCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCEECTTCCECTTCEEECTCCCCEEECTHCCEEEEETCCCCEEECCEEEEEECCCCHCCECCTHTCEEECTHCCCEEEECTTCHTCEEEECCCEECCCCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[256,26.2429,1.4503,0.5555,98.009,20.02,0.242188,0.339844,0.074219,0.34375,2,21,1.9727,0.205941,0.635644,0.251424,65.3703,1,46.735,11.505,0,0,4.151928,0.078125,0.039063,0.015625,0.050781,0.0625,0.050781,0.007813,0.082031,0.039063,0.058594,0.082031,0.097656,0.050781,0.035156,0.019531,0.035156,0.054688,0.070313,0.042969,0.027344]},{"accessions":["P0A1J3"],"chain_id":"w","chains":["w"],"kind":"protein","notes":["Radius of gyration 24.66 Å, 1.39× that of a compact chain of 243 residues: somewhat extended","Secondary structure (TM-align): 25.1% helix in 2 helices, 35.4% strand in 19 strands","2.05 CA contacts per residue, 64.3% long-range; relative contact order 0.248","Mean B-factor 57.0 Ų (sd 11.7)","1 chain breaks (residues missing from the coordinates)"],"residues":243,"secondary":"CCHHHHHHHHHHHHHHHHHHHHHHHCCCCCCEEEEEEEEEECCEECCHCEEEEEEEECCEEEEECCEEEEECCCCCCEEECTCEEEEEECTTCCEEEECCCCEEECTTCCEECTTCCECTTCEEECTCCCCEEECTHCCEEEEETCCCCEEEEEEEEEEECCCCHCCEECTHTCEEECTHCCCEEECCTTCHTCEEEECCCEECCCCECHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHCC","set":"gl1x-structure-1","values":[243,24.6614,1.3902,0.5598,98.084,18.098,0.251029,0.353909,0.074074,0.320988,2,19,2.0494,0.200803,0.64257,0.248334,64.0703,1,56.966,11.712,0,0,4.101312,0.090535,0.041152,0.020576,0.037037,0.053498,0.049383,0.00823,0.078189,0.045267,0.061728,0.111111,0.106996,0.037037,0.028807,0.016461,0.037037,0.065844,0.049383,0.041152,0.020576]}],"entry_id":"8WKI","method":"ELECTRON MICROSCOPY","predicted":false,"skipped":[],"status":"complete"}}