cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5281/zenodo.18768952
title: GOWIRES v1.0: Global dataset of onshore wind turbines

description: GOWIRES (Global Onshore Wind Infrastructure and Resource Estimates) is a comprehensive global dataset of 416,417 horizontal-axis wind turbines (HAWT) across 89 countries. The dataset provides harmonized geographic coordinates, key technical specifications (rated power, rotor diameter, hub height, specific rating), and site-specific environmental characteristics for each turbine. In addition, GOWIRES includes historical (1989–2018) and future (2030–2059) wind resource metrics at the turbine scale. Wind resources are described by mean wind speed, mean wind power density, air density, power law exponents, and Weibull scale and shape parameters. Future wind resource estimates are derived from 13 statistically downscaled CMIP6 global climate models under the SSP2‑4.5 and SSP5‑8.5 scenarios. The dataset is designed to support (among others) wind energy assessment, climate impact analysis, infrastructure planning, and energy system modeling at local to global scales.

A detailed description of the dataset methodology and validation is provided in the associated Data Descriptor: 

A global dataset of onshore wind turbines with site-specific historical (1989–2018) and future (2030–2059) wind resources across 89 countries (under review at Scientific Data).
DOI: 10.13018/bmr18326
title: 1H, 13C, and 15N resonance assignments of Ni(II)-NmtR
DOI: 10.13018/bmr18327
title: Solution structure of the atypical SH3 domain of DOCK180
DOI: 10.13018/bmr18328
title: Solution structure of CHCHD7
DOI: 10.13018/bmr18329
title: Structure of decorbin-binding protein A from Borrelia burgdorferi
DOI: 10.13018/bmr18331
title: 1H, 13C and 15N assignments of the holo-acyl carrier protein of Pseudomonas aeruginosa
DOI: 10.13018/bmr18332
title: E. coli Protein
DOI: 10.13018/bmr18333
title: Solution structure of phosphorylated CRKL
DOI: 10.13018/bmr18334
title: NMR spatial structure of the trypsin inhibitor BWI-2c from the buckwheat seeds
DOI: 10.13018/bmr18335
title: Structure and orientation of the gH625-644 membrane interacting region of herpes simplex virus type 1 in a membrane mimetic system.
DOI: 10.13018/bmr18336
title: Structure of the RNA claw of the DNA packaging motor of bacteriophage 29
DOI: 10.13018/bmr18337
title: SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR136
DOI: 10.13018/bmr18338
title: C-terminal propeptide (PPc) region of vibrio extracellular metalloprotease
DOI: 10.13018/bmr18339
title: 1H, 15N and 13C backbone resonance assignments of FTSA
DOI: 10.13018/bmr18340
title: Structural Mechanism for Bax Inhibition by Cytomegalovirus Protein vMIA
DOI: 10.13018/bmr18341
title: Sgt2_NT
DOI: 10.13018/bmr18342
title: Backbone and sidechain assignments for Get5_UBL domain
DOI: 10.13018/bmr18344
title: Gal-GalNac-Interferon Alpha-2a
DOI: 10.13018/bmr18345
title: Solution structure of the anti-fungal defensin DEF4 (MTR_8g070770) from Medicago truncatula (barrel clover)
DOI: 10.13018/bmr18346
title: NMR structure of the protein NP_390037.1 from Bacillus subtilis.
DOI: 10.13018/bmr18347
title: 1H chemical shift assignments for micasin
DOI: 10.13018/bmr18348
title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 CH domain
DOI: 10.13018/bmr18349
title: NMR structure of a LINE-1 type transposase domain-containing protein 1 (L1TD1) from HOMO SAPINES
DOI: 10.13018/bmr18350
title: cathelicidin-PY
DOI: 10.13018/bmr18351
title: Solution structure of the Class II hydrophobin NC2
DOI: 10.13018/bmr18352
title: Solution NMR Structure of CASP8-associated protein 2 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8150A
DOI: 10.13018/bmr18353
title: 1H, 15N and 13C backbone resonance assignments of the Kelch domain of mouse Keap1
DOI: 10.13018/bmr18354
title: High-resolution solution NMR structure of the rho-conotoxin TIA.
DOI: 10.13018/bmr18355
title: NMR Structure of Signal Sequence Deleted (SSD) Rv0603 Protein from Mycobacterium tuberculosis without N-terminal His-tag
DOI: 10.13018/bmr18356
title: Solution Structure of ADF like UNC-60A Protein of Caenorhabditis elegans
DOI: 10.13018/bmr18357
title: The solution structure of the monomeric Acanthaporin
DOI: 10.13018/bmr18358
title: The solution structure of the dimeric Acanthaporin
DOI: 10.13018/bmr18359
title: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(D39V)
DOI: 10.13018/bmr18360
title: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(E111A)
DOI: 10.13018/bmr18361
title: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(N90A)
DOI: 10.13018/bmr18362
title: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(S107A)
DOI: 10.13018/bmr18363
title: 'Backbone Chemical Shift Assignments for Scylla Serrata anti lipopolysaccharide Factor-24 (SsALF-24) peptide'
DOI: 10.13018/bmr18364
title: NMR structure of the protein YP_001300941.1 from Bacteroides vulgatus
DOI: 10.13018/bmr18365
title: Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant WT-ALA
DOI: 10.13018/bmr18366
title: Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W28G.
DOI: 10.13018/bmr18367
title: Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W62G.
DOI: 10.13018/bmr18368
title: Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W108G.
DOI: 10.13018/bmr18369
title: Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W111G.
DOI: 10.13018/bmr18370
title: Backbone 1H and 15N Chemical Shift Assignments for Hen Egg White Lysozyme mutant W123G.
DOI: 10.13018/bmr18371
title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 C-terminal domain
DOI: 10.13018/bmr18372
title: SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR137
DOI: 10.13018/bmr18373
title: bLac - Oceanobacillus iheyensis
DOI: 10.13018/bmr18374
title: NMR structure of the second PHD finger of AIRE (AIRE-PHD2)
DOI: 10.13018/bmr18375
title: NMR solution structure of staphyloxanthin biosynthesis protein
DOI: 10.13018/bmr18376
title: Free MTIP(61-204) from Plasmodium falciparum
DOI: 10.13018/bmr18377
title: MTIP(61-204) from Plasmodium falciparum bound to peptide MyoA(799-818)
DOI: 10.13018/bmr18378
title: Liraglutide
DOI: 10.13018/bmr18379
title: Solution Structures of the IIA(Chitobiose)-HPr complex of the N,N'-Diacetylchitobiose Branch of the Escherichia coli Phosphotransferase System
DOI: 10.13018/bmr18380
title: Backbone 1H, 13C, and 15N Chemical Shift Assignments and Complete 15N Relaxation Analysis of the Soluble C-terminal Domain of CcmE Heme Chaperone from Desulfovibrio vulgaris, dvCcmE(44-137). Northeast Structural Genomics Target DvR115.
DOI: 10.13018/bmr18381
title: The backbone chemical shifts of IscU complexed with HscA
DOI: 10.13018/bmr18385
title: Characterization of the chromoshadow domain-mediated binding of heterochromatin protein 1 alpha (HP1 alpha) to histone H3: Backbone 1H, 15N chemical shift assignments for histone H3 (1-59)
DOI: 10.13018/bmr18386
title: Characterization of the chromoshadow domain-mediated binding of heterochromatin protein 1 alpha (HP1 alpha) to histone H3: Backbone 1H, 15N chemical shift assignments for HP1 CSDalpha(109-185)
DOI: 10.13018/bmr18387
title: Solution structure of a thiol:disulfide interchange protein from Bacteroides sp.
DOI: 10.15468/dl.7kx7jp
title: Occurrence Download

description: A dataset containing 216693 records in GBIF matching the query:
SELECT
 kingdom,
 kingdomkey,
 phylum,
 phylumkey,
 class,
 classkey,
 "order",
 orderkey,
 family,
 familykey,
 genus,
 genuskey,
 species,
 specieskey,
 "year",
 IF(ISNULL(kingdomkey), NULL, SUM(COUNT(*)) OVER (
 PARTITION BY kingdomkey, "year")) kingdomcount,
 IF(ISNULL(phylumkey), NULL, SUM(COUNT(*)) OVER (
 PARTITION BY phylumkey, "year")) phylumcount,
 IF(ISNULL(classkey), NULL, SUM(COUNT(*)) OVER (
 PARTITION BY classkey, "year")) classcount,
 IF(ISNULL(orderkey), NULL, SUM(COUNT(*)) OVER (
 PARTITION BY orderkey, "year")) ordercount,
 IF(ISNULL(familykey), NULL, SUM(COUNT(*)) OVER (
 PARTITION BY familykey, "year")) familycount,
 IF(ISNULL(genuskey), NULL, SUM(COUNT(*)) OVER (
 PARTITION BY genuskey, "year")) genuscount,
 COUNT(*) occurrences,
 MIN(GBIF_TEMPORALUNCERTAINTY(eventdate, eventtime)) mintemporaluncertainty,
 MIN(COALESCE(coordinateuncertaintyinmeters, 1000)) mincoordinateuncertaintyinmeters
FROM
 occurrence
WHERE
 occurrence.countrycode = 'NZ'
 AND occurrence.occurrencestatus = 'PRESENT'
 AND (occurrence."year" &gt;= 1999 AND occurrence."year" &lt;= 2026)
 AND occurrence.hasgeospatialissues = FALSE
 AND NOT GBIF_STRINGARRAYCONTAINS(occurrence.issue, 'TAXON_MATCH_FUZZY', TRUE)
 AND (occurrence.distancefromcentroidinmeters &gt;= 2000.0 OR occurrence.distancefromcentroidinmeters IS NULL)
 AND NOT occurrence.basisofrecord IN ('FOSSIL_SPECIMEN', 'LIVING_SPECIMEN')
 AND (occurrence.classificationdetails['d7dddbf4-2cf0-4f39-9b2a-bb099caae36c']['specieskey'] &lt;&gt; '' AND occurrence."year" IS NOT NULL)
GROUP BY
 occurrence.kingdom,
 occurrence.kingdomkey,
 occurrence.phylum,
 occurrence.phylumkey,
 occurrence.class,
 occurrence.classkey,
 occurrence."order",
 occurrence.orderkey,
 occurrence.family,
 occurrence.familykey,
 occurrence.genus,
 occurrence.genuskey,
 occurrence.species,
 occurrence.specieskey,
 occurrence."year"

 The dataset's 216693 records were derived from 638 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0003149-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr18388
title: Solution structure, dynamics and binding studies of CtCBM11
DOI: 10.13018/bmr18389
title: Solution structure, dynamics and binding studies of CtCBM11
DOI: 10.13018/bmr18390
title: Chemical Shift Assignment and Solution Structure of ChR145 from Drosophila melanogaster. Northeast Structural Genomics Consortium Target Fr822A
DOI: 10.13018/bmr18391
title: Solution structure of the R3H domain from human Smubp-2 in complex with 2'-deoxyguanosine-5'-monophosphate
DOI: 10.13018/bmr18392
title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the C-terminal Domain of E. coli Enzyme I
DOI: 10.13018/bmr18393
title: The second dsRBD domain from A. thaliana DICER-LIKE 1
DOI: 10.13018/bmr18394
title: Solution structure of the uncharacterized thioredoxin-like protein BVU_1432 from Bacteroides vulgatus
DOI: 10.13018/bmr18395
title: Chemical shift assignments of deuterated DsbB by 1H-detected solid-state NMR
DOI: 10.57707/fmi-b2share.g1k4j-9wa81
title: Test Record
DOI: 10.13018/bmr18396
title: nanocrystalline DsbA 1H, 13C, 15N chemical shifts
DOI: 10.13018/bmr18397
title: nanocrystalline GB1 1H, 13C, 15N assignments
DOI: 10.13018/bmr18398
title: Solution Structure of the WNK1 Autoinhibitory Domain
DOI: 10.13018/bmr18399
title: Solution structure of a ubiquitin-like protein from Trypanosoma brucei
DOI: 10.13018/bmr18400
title: RNA structural dynamics are modulated through anti-folding by chaperones
DOI: 10.13018/bmr18403
title: 1H,13C and 15N resonance assignment of the UIM-SH3 construct of the STAM2 protein
DOI: 10.13018/bmr18404
title: Solution Structure of the Target Recognition Domain of Zoocin A
DOI: 10.13018/bmr18405
title: Structure of Sviceucin, an type I lasso peptide from Streptomyces sviceus
DOI: 10.13018/bmr18406
title: Solid-state NMR sequential assignments of Sup35NM
DOI: 10.13018/bmr18407
title: Solid-state NMR sequential assignments of full-length Sup35p
DOI: 10.13018/bmr18408
title: 1H Chemical Shift Assignments for the first transmembrane domain from human copper transport 1
DOI: 10.13018/bmr18409
title: 1H Chemical Shift Assignments for the second transmembrane domain from human copper transport 1
DOI: 10.13018/bmr18410
title: 1H Chemical Shift Assignments for the third transmembrane domain from the human copper transport 1
DOI: 10.6084/m9.figshare.31422047
title: Managing architecture in fragmented markets: survey insights from Croatia

description: Architectural management is a relatively underexplored discipline in Croatia, where it is often confused with design management and insufficiently integrated into professional practice and continuing professional development (CPD) frameworks. This study investigates the state of architectural management among Croatian architectural firms through an online survey of members of the Croatian Chamber of Architects (CCA), comprising 216 respondents, of whom 142 employers form the analytically relevant sample. The survey examined firm demographics, use of professional standards, fee-determination practices, management skill self-assessment and perceived challenges. Results reveal that 89.4% of surveyed firms are micro-enterprises with fewer than five employees, underscoring the dominance of SMEs in the sector. Most architects rely on simplified fee-determination methods – such as cost per square metre or percentages of construction costs – rather than structured scope-of-services standards, while over 70% identify low fees and unclear regulation as key challenges. Although respondents report relatively high self-assessed management skills, correlation analysis shows that demand for management education is not suppressed by confidence in existing abilities, suggesting that the underdevelopment of architectural management is structural rather than individual. This study provides the first systematic, survey-based assessment of architectural management in Croatia and positions its findings within broader European debates on professional fragmentation, fee formation, and firm resilience. While recent CCA reforms represent progress, the results highlight the need for deeper integration of management principles into professional standards and CPD frameworks to support the long-term sustainability of architectural practice.
DOI: 10.6084/m9.figshare.31422047.v1
title: Managing architecture in fragmented markets: survey insights from Croatia

description: Architectural management is a relatively underexplored discipline in Croatia, where it is often confused with design management and insufficiently integrated into professional practice and continuing professional development (CPD) frameworks. This study investigates the state of architectural management among Croatian architectural firms through an online survey of members of the Croatian Chamber of Architects (CCA), comprising 216 respondents, of whom 142 employers form the analytically relevant sample. The survey examined firm demographics, use of professional standards, fee-determination practices, management skill self-assessment and perceived challenges. Results reveal that 89.4% of surveyed firms are micro-enterprises with fewer than five employees, underscoring the dominance of SMEs in the sector. Most architects rely on simplified fee-determination methods – such as cost per square metre or percentages of construction costs – rather than structured scope-of-services standards, while over 70% identify low fees and unclear regulation as key challenges. Although respondents report relatively high self-assessed management skills, correlation analysis shows that demand for management education is not suppressed by confidence in existing abilities, suggesting that the underdevelopment of architectural management is structural rather than individual. This study provides the first systematic, survey-based assessment of architectural management in Croatia and positions its findings within broader European debates on professional fragmentation, fee formation, and firm resilience. While recent CCA reforms represent progress, the results highlight the need for deeper integration of management principles into professional standards and CPD frameworks to support the long-term sustainability of architectural practice.
DOI: 10.13018/bmr18411
title: Solution structure of a putative protein disulfide isomerase from Bacteroides thetaiotaomicron
DOI: 10.13018/bmr18412
title: High Definition Solution Structure of PED/PEA-15 Death Effector Domain
DOI: 10.13018/bmr18413
title: Apo-AdcR
DOI: 10.13018/bmr18414
title: Zn(II)-AdcR
DOI: 10.13018/bmr18415
title: Solution structure of human C-type lectin domain family 4 member D
DOI: 10.13018/bmr18416
title: 1H,15N and 13C backbone and side chain chemical shifts of the ubiquitin homology domain of mouse BAG-1
DOI: 10.13018/bmr18417
title: 1H, 13C and 15N resonance assignments of human BASP1
DOI: 10.13018/bmr18418
title: Pleurocidin-NH2
DOI: 10.13018/bmr18419
title: B2 domain of Neisseria meningitidis Pilus assembly protein PilQ
DOI: 10.6084/m9.figshare.31422056
title: Female reproductive factors, genetic susceptibility and incident osteoporosis risk

description: Osteoporosis risk is shaped by both reproductive factors and genetic predisposition, yet their combined effects remain insufficiently studied. A total of 49,885 women from the UK Biobank were analyzed, excluding those with baseline osteoporosis or missing reproductive data. Reproductive factors included age at menarche, menopause time/status, history of stillbirth, hysterectomy, oophorectomy and oral contraceptive (OC) use. Genetic susceptibility was assessed using the polygenic risk score (PRS). Cox models estimated associations, with restricted cubic splines testing non-linear trends. Kaplan–Meier curves and sensitivity analyses were performed. Late menarche, premature ovarian insufficiency, menopausal status, stillbirth, hysterectomy and oophorectomy were linked to higher osteoporosis risk, while OC use was protective. Women with high PRS combined with adverse reproductive histories had the greatest risk. Additive interactions were evident between genetic risk and menopause, stillbirth, hysterectomy and oophorectomy, whereas other factors acted largely independently. Sensitivity analyses supported robustness. Both reproductive history and genetic susceptibility contribute to osteoporosis risk in women. Joint assessment of these factors may enhance risk stratification and inform personalized prevention. Osteoporosis is a condition that weakens bones and increases fracture risk, especially in women, and both life-long hormonal factors and genetics may contribute to its development. Hormonal milestones such as the timing of first menstruation and menopause, along with reproductive events including stillbirth or surgeries involving the uterus or ovaries, can influence bone strength, but how these factors interact with genetic susceptibility has been unclear. We studied nearly 50,000 women from the UK Biobank over an average follow-up of 12 years and found that women with later first menstruation, premature ovarian insufficiency, or a history of stillbirth, hysterectomy, or ovary removal had a higher risk of developing osteoporosis, whereas use of oral contraceptives was associated with a slightly lower risk. Importantly, women who had both high genetic risk and adverse reproductive factors showed the greatest likelihood of osteoporosis, indicating that genes and reproductive history can reinforce each other. These findings suggest that considering both genetic background and reproductive history may improve osteoporosis risk assessment in women, support earlier identification of high-risk individuals, and help guide personalized prevention strategies such as targeted screening, lifestyle modification, or preventive treatment to protect bone health later in life.
DOI: 10.6084/m9.figshare.31422056.v1
title: Female reproductive factors, genetic susceptibility and incident osteoporosis risk

description: Osteoporosis risk is shaped by both reproductive factors and genetic predisposition, yet their combined effects remain insufficiently studied. A total of 49,885 women from the UK Biobank were analyzed, excluding those with baseline osteoporosis or missing reproductive data. Reproductive factors included age at menarche, menopause time/status, history of stillbirth, hysterectomy, oophorectomy and oral contraceptive (OC) use. Genetic susceptibility was assessed using the polygenic risk score (PRS). Cox models estimated associations, with restricted cubic splines testing non-linear trends. Kaplan–Meier curves and sensitivity analyses were performed. Late menarche, premature ovarian insufficiency, menopausal status, stillbirth, hysterectomy and oophorectomy were linked to higher osteoporosis risk, while OC use was protective. Women with high PRS combined with adverse reproductive histories had the greatest risk. Additive interactions were evident between genetic risk and menopause, stillbirth, hysterectomy and oophorectomy, whereas other factors acted largely independently. Sensitivity analyses supported robustness. Both reproductive history and genetic susceptibility contribute to osteoporosis risk in women. Joint assessment of these factors may enhance risk stratification and inform personalized prevention. Osteoporosis is a condition that weakens bones and increases fracture risk, especially in women, and both life-long hormonal factors and genetics may contribute to its development. Hormonal milestones such as the timing of first menstruation and menopause, along with reproductive events including stillbirth or surgeries involving the uterus or ovaries, can influence bone strength, but how these factors interact with genetic susceptibility has been unclear. We studied nearly 50,000 women from the UK Biobank over an average follow-up of 12 years and found that women with later first menstruation, premature ovarian insufficiency, or a history of stillbirth, hysterectomy, or ovary removal had a higher risk of developing osteoporosis, whereas use of oral contraceptives was associated with a slightly lower risk. Importantly, women who had both high genetic risk and adverse reproductive factors showed the greatest likelihood of osteoporosis, indicating that genes and reproductive history can reinforce each other. These findings suggest that considering both genetic background and reproductive history may improve osteoporosis risk assessment in women, support earlier identification of high-risk individuals, and help guide personalized prevention strategies such as targeted screening, lifestyle modification, or preventive treatment to protect bone health later in life.
DOI: 10.13018/bmr18420
title: magainin
DOI: 10.13018/bmr18421
title: Capsid protein from Equine Infectious Anemia Virus
DOI: 10.13018/bmr18422
title: Backbone dynamics of the truncated (2/2) hemoglobin from Synechococcus sp. PCC 7002 (ferrous form with heme PTM, carbonmonoxy complex)
DOI: 10.13018/bmr18423
title: Backbone dynamics of the truncated (2/2) hemoglobin from Synechococcus sp. PCC 7002 (ferric form with heme PTM, cyanide complex)
DOI: 10.13018/bmr18424
title: Backbone dynamics of the truncated (2/2) hemoglobin from Synechococcus sp. PCC 7002 (ferric form without heme PTM, cyanide complex)
DOI: 10.13018/bmr18425
title: Resonance Assignments of Ca2+-bound human S100A11
DOI: 10.13018/bmr18426
title: Solution-state NMR structure of the human prion protein
DOI: 10.13018/bmr18427
title: Solution structure of 2'F-ANA and ANA self-complementary duplex
DOI: 10.13018/bmr18428
title: N0N1 domains of Neisseria meningitidis Pilus assembly protein PilQ
DOI: 10.13018/bmr18429
title: Solution NMR Structure of De Novo Designed Four Helix Bundle Protein, Northeast Structural Genomics Consortium (NESG) Target OR188
DOI: 10.13018/bmr18430
title: Structure and Stability of Duplex DNA Containing (5 S) 5 ,8-Cyclo-2 -Deoxyadenosine: An Oxidative Lesion Repair by NER.
DOI: 10.13018/bmr18431
title: Solution structure of the mouse Rev1 C-terminal domain
DOI: 10.13018/bmr18432
title: Solution structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase kappa
DOI: 10.13018/bmr18433
title: Solution structure of the mouse Rev1 CTD in complex with the Rev1-interacting Region (RIR)of Pol Kappa
DOI: 10.13018/bmr18434
title: C-terminal domain of human REV1 in complex with DNA-polymerase H (eta)
DOI: 10.13018/bmr18435
title: Solution structure of the C-terminal domain of Tetrahymena telomerase protein p65