BLASTP 2.2.1 [Apr-13-2001]
Reference:
Altschul, Stephen F., Thomas L. Madden, Alejandro A. Schäffer,
Jinghui Zhang, Zheng Zhang, Webb Miller, and David J. Lipman (1997),
"Gapped BLAST and PSI-BLAST: a new generation of protein database search
programs", Nucleic Acids Res. 25:3389-3402.
Query= gi|15645894|ref|NP_208073.1| anthranilate synthase
component II (trpD) [Helicobacter pylori 26695]
(194 letters)
Database: /var/www/html/HP/blast_new/blast/db/pdbaa
13,198 sequences; 2,899,336 total letters
Searching...........................done
Score E
Sequences producing significant alignments: (bits) Value
pdb|1I1Q|B Chain B, Structure Of The Cooperative Allosteric... 159 2e-40
pdb|1I7Q|B Chain B, Anthranilate Synthase From S. Marcescen... 157 8e-40
pdb|1QDL|B Chain B, The Crystal Structure Of Anthranilate S... 106 2e-24
pdb|1GPM|A Chain A, Escherichia Coli Gmp Synthetase Complex... 59 4e-10
pdb|1M6V|B Chain B, Crystal Structure Of The G359f (Small S... 45 5e-06
pdb|1JDB|F Chain F, Carbamoyl Phosphate Synthetase From Esc... 45 5e-06
pdb|1C30|B Chain B, Crystal Structure Of Carbamoyl Phosphat... 41 8e-05
pdb|1CS0|B Chain B, Crystal Structure Of Carbamoyl Phosphat... 41 1e-04
pdb|1A9X|B Chain B, Carbamoyl Phosphate Synthetase: Caught ... 38 7e-04
pdb|1KXJ|A Chain A, The Crystal Structure Of Glutamine Amid... 35 0.006
pdb|1GPW|B Chain B, Structural Evidence For Ammonia Tunneli... 35 0.006
pdb|1EQJ|A Chain A, Crystal Structure Of Phosphoglycerate M... 27 1.5
pdb|1M1B|A Chain A, Crystal Structure Of Phosphoenolpyruvat... 25 4.5
pdb|1MVO|A Chain A, Crystal Structure Of The Phop Receiver ... 25 5.9
pdb|1LSH|B Chain B, Lipid-Protein Interactions In Lipovitellin 25 7.7
>pdb|1I1Q|B Chain B, Structure Of The Cooperative Allosteric Anthranilate
Synthase From Salmonella Typhimurium
Length = 192
Score = 159 bits (403), Expect = 2e-40
Identities = 77/189 (40%), Positives = 122/189 (63%), Gaps = 1/189 (0%)
Query: 3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMDLMNEESKTPLLFISPGPGNPN 62
I +DN DSF++NL +L G+ V +Y+N I L+D + K P+L +SPGPG P+
Sbjct: 3 ILLLDNIDSFTWNLADQLRTNGHNVVIYRNHIPAQTLIDRL-ATMKNPVLMLSPGPGVPS 61
Query: 63 SSGNLLKIIAMAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKATAIALKKHAVFKG 122
+G + +++ + K PI+GICLG QA+ ++YG + ++ EI+HGKAT+I A+F G
Sbjct: 62 EAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKATSIEHDGQAMFAG 121
Query: 123 LGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMAIVNEEDKILAYQFHPESIMTLQGRAL 182
L + V RYHSL+ S +P L + A + + MA+ ++ D++ +QFHPESI+T QG L
Sbjct: 122 LANPLPVARYHSLVGSNVPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARL 181
Query: 183 LEQSVGFLE 191
LEQ++ + +
Sbjct: 182 LEQTLAWAQ 190
>pdb|1I7Q|B Chain B, Anthranilate Synthase From S. Marcescens
pdb|1I7Q|D Chain D, Anthranilate Synthase From S. Marcescens
pdb|1I7S|B Chain B, Anthranilate Synthase From Serratia Marcescens In Complex
With Its End Product Inhibitor L-Tryptophan
pdb|1I7S|D Chain D, Anthranilate Synthase From Serratia Marcescens In Complex
With Its End Product Inhibitor L-Tryptophan
Length = 193
Score = 157 bits (397), Expect = 8e-40
Identities = 73/187 (39%), Positives = 123/187 (65%), Gaps = 1/187 (0%)
Query: 3 IFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMDLMNEESKTPLLFISPGPGNPN 62
I +DN DSF+YNLV +L G++V +Y+N I +++ + + + P+L +SPGPG P+
Sbjct: 4 ILLLDNVDSFTYNLVDQLRASGHQVVIYRNQIGAEVIIERL-QHMEQPVLMLSPGPGTPS 62
Query: 63 SSGNLLKIIAMAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKATAIALKKHAVFKG 122
+G + +++ + + PI+GICLG QA+ ++YG ++ ++ EI+HGKA+AIA +F G
Sbjct: 63 EAGCMPELLQRLRGQLPIIGICLGHQAIVEAYGGQVGQAGEILHGKASAIAHDGEGMFAG 122
Query: 123 LGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMAIVNEEDKILAYQFHPESIMTLQGRAL 182
+ + V RYHSL+ S +P +L V A + MA+ ++ ++ +QFHPESI+T G L
Sbjct: 123 MANPLPVARYHSLVGSNIPADLTVNARFGEMVMAVRDDRRRVCGFQFHPESILTTHGARL 182
Query: 183 LEQSVGF 189
LEQ++ +
Sbjct: 183 LEQTLAW 189
>pdb|1QDL|B Chain B, The Crystal Structure Of Anthranilate Synthase From
Sulfolobus Solfataricus
Length = 195
Score = 106 bits (265), Expect = 2e-24
Identities = 68/187 (36%), Positives = 103/187 (54%), Gaps = 14/187 (7%)
Query: 6 IDNFDSFSYNLVYELECLG-YEVAVYQNDIDPSYLMDLMNEESKTPLLFISPGPGNPNSS 64
IDN+DSF YN+ + LG Y + + ++I + E L ISPGPG P
Sbjct: 7 IDNYDSFVYNIAQIVGELGSYPIVIRNDEISIKGI-----ERIDPDRLIISPGPGTPEKR 61
Query: 65 GNL---LKIIAMAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKATAIALKKH---A 118
++ L +I K+ PILG+CLG QA+ ++GAKI R++++ HGK + I L + +
Sbjct: 62 EDIGVSLDVIKYLGKRTPILGVCLGHQAIGYAFGAKIRRARKVFHGKISNIILVNNSPLS 121
Query: 119 VFKGLGESMVVGRYHSLMASGL--PKNLEVIAEHDNIPMAIVNEEDKILAYQFHPESIMT 176
++ G+ + RYHSL+ + P ++ I+ DN MAI +EE I QFHPES+ T
Sbjct: 122 LYYGIAKEFKATRYHSLVVDEVHRPLIVDAISAEDNEIMAIHHEEYPIYGVQFHPESVGT 181
Query: 177 LQGRALL 183
G +L
Sbjct: 182 SLGYKIL 188
>pdb|1GPM|A Chain A, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
pdb|1GPM|C Chain C, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
pdb|1GPM|B Chain B, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
pdb|1GPM|D Chain D, Escherichia Coli Gmp Synthetase Complexed With Amp And
Pyrophosphate
Length = 525
Score = 58.9 bits (141), Expect = 4e-10
Identities = 34/118 (28%), Positives = 56/118 (46%), Gaps = 9/118 (7%)
Query: 79 PILGICLGLQALAQSYGAKIIRSKEIVHGKATAIALKKHAVFKGLGESMV--------VG 130
P+ G+C G+Q +A G + S E G A + A+ +G+ +++ V
Sbjct: 81 PVFGVCYGMQTMAMQLGGHVEASNEREFGYAQVEVVNDSALVRGIEDALTADGKPLLDVW 140
Query: 131 RYHSLMASGLPKNLEVIAEHDNIPMAIV-NEEDKILAYQFHPESIMTLQGRALLEQSV 187
H + +P + +A ++ P AI+ NEE + QFHPE T QG +LE+ V
Sbjct: 141 MSHGDKVTAIPSDFITVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFV 198
>pdb|1M6V|B Chain B, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
pdb|1M6V|D Chain D, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
pdb|1M6V|F Chain F, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
pdb|1M6V|H Chain H, Crystal Structure Of The G359f (Small Subunit) Point
Mutant Of Carbamoyl Phosphate Synthetase
Length = 382
Score = 45.1 bits (105), Expect = 5e-06
Identities = 37/128 (28%), Positives = 58/128 (44%), Gaps = 13/128 (10%)
Query: 52 LFISPGPGNPNSSGNLLKIIA-MAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKAT 110
+F+S GPG+P + I + P+ GICLG Q LA + GAK ++ K HG
Sbjct: 236 IFLSNGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNH 295
Query: 111 AIA-LKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE--HDNIPMAIVNEEDKIL 165
+ ++K+ V M+ + H + LP NL V + D I +
Sbjct: 296 PVKDVEKNVV-------MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAF 348
Query: 166 AYQFHPES 173
++Q HPE+
Sbjct: 349 SFQGHPEA 356
>pdb|1JDB|F Chain F, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1JDB|C Chain C, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1JDB|I Chain I, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1JDB|L Chain L, Carbamoyl Phosphate Synthetase From Escherichia Coli
pdb|1CE8|B Chain B, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1CE8|D Chain D, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1CE8|F Chain F, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1CE8|H Chain H, Carbamoyl Phosphate Synthetase From Escherichis Coli With
Complexed With The Allosteric Ligand Imp
pdb|1BXR|B Chain B, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
pdb|1BXR|D Chain D, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
pdb|1BXR|F Chain F, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
pdb|1BXR|H Chain H, Structure Of Carbamoyl Phosphate Synthetase Complexed With
The Atp Analog Amppnp
Length = 382
Score = 45.1 bits (105), Expect = 5e-06
Identities = 37/128 (28%), Positives = 58/128 (44%), Gaps = 13/128 (10%)
Query: 52 LFISPGPGNPNSSGNLLKIIA-MAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKAT 110
+F+S GPG+P + I + P+ GICLG Q LA + GAK ++ K HG
Sbjct: 236 IFLSNGPGDPAPCDYAITAIQKFLETDIPVFGICLGHQLLALASGAKTVKMKFGHHGGNH 295
Query: 111 AIA-LKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE--HDNIPMAIVNEEDKIL 165
+ ++K+ V M+ + H + LP NL V + D I +
Sbjct: 296 PVKDVEKNVV-------MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAF 348
Query: 166 AYQFHPES 173
++Q HPE+
Sbjct: 349 SFQGHPEA 356
>pdb|1C30|B Chain B, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C30|D Chain D, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C30|F Chain F, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C30|H Chain H, Crystal Structure Of Carbamoyl Phosphate Synthetase: Small
Subunit Mutation C269s
pdb|1C3O|B Chain B, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
pdb|1C3O|D Chain D, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
pdb|1C3O|F Chain F, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
pdb|1C3O|H Chain H, Crystal Structure Of The Carbamoyl Phosphate Synthetase:
Small Subunit Mutant C269s With Bound Glutamine
Length = 382
Score = 41.2 bits (95), Expect = 8e-05
Identities = 36/128 (28%), Positives = 57/128 (44%), Gaps = 13/128 (10%)
Query: 52 LFISPGPGNPNSSGNLLKIIA-MAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKAT 110
+F+S GPG+P + I + P+ GI LG Q LA + GAK ++ K HG
Sbjct: 236 IFLSNGPGDPAPCDYAITAIQKFLETDIPVFGISLGHQLLALASGAKTVKMKFGHHGGNH 295
Query: 111 AIA-LKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE--HDNIPMAIVNEEDKIL 165
+ ++K+ V M+ + H + LP NL V + D I +
Sbjct: 296 PVKDVEKNVV-------MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAF 348
Query: 166 AYQFHPES 173
++Q HPE+
Sbjct: 349 SFQGHPEA 356
>pdb|1CS0|B Chain B, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1CS0|D Chain D, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1CS0|F Chain F, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1CS0|H Chain H, Crystal Structure Of Carbamoyl Phosphate Synthetase
Complexed At Cys269 In The Small Subunit With The
Tetrahedral Mimic L-Glutamate Gamma-Semialdehyde
pdb|1KEE|B Chain B, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
pdb|1KEE|D Chain D, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
pdb|1KEE|F Chain F, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
pdb|1KEE|H Chain H, Inactivation Of The Amidotransferase Activity Of Carbamoyl
Phosphate Synthetase By The Antibiotic Acivicin
Length = 382
Score = 40.8 bits (94), Expect = 1e-04
Identities = 36/128 (28%), Positives = 57/128 (44%), Gaps = 13/128 (10%)
Query: 52 LFISPGPGNPNSSGNLLKIIA-MAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKAT 110
+F+S GPG+P + I + P+ GI LG Q LA + GAK ++ K HG
Sbjct: 236 IFLSNGPGDPAPCDYAITAIQKFLETDIPVFGIXLGHQLLALASGAKTVKMKFGHHGGNH 295
Query: 111 AIA-LKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE--HDNIPMAIVNEEDKIL 165
+ ++K+ V M+ + H + LP NL V + D I +
Sbjct: 296 PVKDVEKNVV-------MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAF 348
Query: 166 AYQFHPES 173
++Q HPE+
Sbjct: 349 SFQGHPEA 356
>pdb|1A9X|B Chain B, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
pdb|1A9X|D Chain D, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
pdb|1A9X|F Chain F, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
pdb|1A9X|H Chain H, Carbamoyl Phosphate Synthetase: Caught In The Act Of
Glutamine Hydrolysis
Length = 379
Score = 38.1 bits (87), Expect = 7e-04
Identities = 35/128 (27%), Positives = 57/128 (44%), Gaps = 13/128 (10%)
Query: 52 LFISPGPGNPNSSGNLLKIIA-MAKKKFPILGICLGLQALAQSYGAKIIRSKEIVHGKAT 110
+F+S GPG+P + I + P+ GI LG Q LA + GAK ++ K HG
Sbjct: 235 IFLSNGPGDPAPCDYAITAIQKFLETDIPVFGIXLGHQLLALASGAKTVKMKFGHHGGNH 294
Query: 111 AIA-LKKHAVFKGLGESMVVGRYHSLMA--SGLPKNLEVIAE--HDNIPMAIVNEEDKIL 165
+ ++K+ V M+ + H + LP NL V + D I +
Sbjct: 295 PVKDVEKNVV-------MITAQNHGFAVDEATLPANLRVTHKSLFDGTLQGIHRTDKPAF 347
Query: 166 AYQFHPES 173
++Q +PE+
Sbjct: 348 SFQGNPEA 355
>pdb|1KXJ|A Chain A, The Crystal Structure Of Glutamine Amidotransferase From
Thermotoga Maritima
pdb|1KXJ|B Chain B, The Crystal Structure Of Glutamine Amidotransferase From
Thermotoga Maritima
Length = 205
Score = 35.0 bits (79), Expect = 0.006
Identities = 27/116 (23%), Positives = 52/116 (44%), Gaps = 9/116 (7%)
Query: 80 ILGICLGLQAL-AQSYGAKIIRSKEIVHGKATAIALKK-------HAVFKGLGESMVVGR 131
++G+CLG+Q L +S A ++ ++ G + ++ +FK +
Sbjct: 82 VVGVCLGMQLLFEESEEAPGVKGLSLIEGNVVKLRSRRLPHMGWNEVIFKDTFPNGYYYF 141
Query: 132 YHSLMASGLPKNLEVIAEHDNIPMAIVNEEDKILAYQFHPESIMTLQGRALLEQSV 187
H+ A +++ E+D + +IL +QFHPE + GR LLE+ +
Sbjct: 142 VHTYRAVCEEEHVLGTTEYDGEIFPSAVRKGRILGFQFHPEKSSKI-GRKLLEKVI 196
>pdb|1GPW|B Chain B, Structural Evidence For Ammonia Tunneling Across The
(BetaALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE
Synthase Bienzyme Complex.
pdb|1GPW|D Chain D, Structural Evidence For Ammonia Tunneling Across The
(BetaALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE
Synthase Bienzyme Complex.
pdb|1GPW|F Chain F, Structural Evidence For Ammonia Tunneling Across The
(BetaALPHA)8 BARREL OF THE IMIDAZOLE GLYCEROL PHOSPHATE
Synthase Bienzyme Complex.
pdb|1K9V|F Chain F, Structural Evidence For Ammonia Tunelling Across The
(Beta- Alpha)8-Barrel Of The Imidazole Glycerol
Phosphate Synthase Bienzyme Complex
Length = 201
Score = 35.0 bits (79), Expect = 0.006
Identities = 27/116 (23%), Positives = 52/116 (44%), Gaps = 9/116 (7%)
Query: 80 ILGICLGLQAL-AQSYGAKIIRSKEIVHGKATAIALKK-------HAVFKGLGESMVVGR 131
++G+CLG+Q L +S A ++ ++ G + ++ +FK +
Sbjct: 80 VVGVCLGMQLLFEESEEAPGVKGLSLIEGNVVKLRSRRLPHMGWNEVIFKDTFPNGYYYF 139
Query: 132 YHSLMASGLPKNLEVIAEHDNIPMAIVNEEDKILAYQFHPESIMTLQGRALLEQSV 187
H+ A +++ E+D + +IL +QFHPE + GR LLE+ +
Sbjct: 140 VHTYRAVCEEEHVLGTTEYDGEIFPSAVRKGRILGFQFHPEKSSKI-GRKLLEKVI 194
>pdb|1EQJ|A Chain A, Crystal Structure Of Phosphoglycerate Mutase From Bacillus
Stearothermophilus Complexed With 2-Phosphoglycerate
pdb|1EJJ|A Chain A, Crystal Structural Analysis Of Phosphoglycerate Mutase
Cocrystallized With 3-Phosphoglycerate
Length = 511
Score = 26.9 bits (58), Expect = 1.5
Identities = 10/27 (37%), Positives = 15/27 (55%)
Query: 146 VIAEHDNIPMAIVNEEDKILAYQFHPE 172
VI D P+A + + D I+ Y F P+
Sbjct: 237 VIVREDGRPVATIQDNDAIIFYNFRPD 263
>pdb|1M1B|A Chain A, Crystal Structure Of Phosphoenolpyruvate Mutase Complexed
With Sulfopyruvate
pdb|1M1B|B Chain B, Crystal Structure Of Phosphoenolpyruvate Mutase Complexed
With Sulfopyruvate
Length = 295
Score = 25.4 bits (54), Expect = 4.5
Identities = 16/47 (34%), Positives = 26/47 (55%), Gaps = 2/47 (4%)
Query: 120 FKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMAIVNEEDKILA 166
F+ +G SMV+ H+L AS +D+ ++VN EDKI++
Sbjct: 227 FRDMGVSMVIWANHNLRASVSAIQQTTKQIYDD--QSLVNVEDKIVS 271
>pdb|1MVO|A Chain A, Crystal Structure Of The Phop Receiver Domain From
Bacillus Subtilis
Length = 136
Score = 25.0 bits (53), Expect = 5.9
Identities = 28/112 (25%), Positives = 43/112 (38%), Gaps = 14/112 (12%)
Query: 2 KIFFIDNFDSFSYNLVYELECLGYEVAVYQNDIDPSYLMDLMNEESKTPLLFISPGPGNP 61
KI +D+ +S L Y LE GY+V + + L E++ P L +
Sbjct: 5 KILVVDDEESIVTLLQYNLERSGYDVITASDGEEA-----LKKAETEKPDLIVLDVMLPK 59
Query: 62 NSSGNLLKIIAMAKKKFPILGI---------CLGLQALAQSYGAKIIRSKEI 104
+ K + K FPIL + LGL+ A Y K +E+
Sbjct: 60 LDGIEVCKQLRQQKLMFPILMLTAKDEEFDKVLGLELGADDYMTKPFSPREV 111
>pdb|1LSH|B Chain B, Lipid-Protein Interactions In Lipovitellin
Length = 319
Score = 24.6 bits (52), Expect = 7.7
Identities = 21/90 (23%), Positives = 40/90 (44%), Gaps = 4/90 (4%)
Query: 106 HGKATAIALKKHAVFKGLGESMVVGRYHSLMASGLPKNLEVIAEHDNIPMAIVNEEDKIL 165
H K + + + G + + Y+ L ++GLPK V E ++ + + + ++
Sbjct: 50 HSKPKVVIVLRAVRADGKQQGLQTTLYYGLTSNGLPKAKIVAVELSDLSVWKLCAKFRLS 109
Query: 166 AYQFHPESI----MTLQGRALLEQSVGFLE 191
A+ +I Q RA+LE S G L+
Sbjct: 110 AHMKAKAAIGWGKNCQQYRAMLEASTGNLQ 139
Database: /var/www/html/HP/blast_new/blast/db/pdbaa
Posted date: Dec 20, 2002 11:08 AM
Number of letters in database: 2,899,336
Number of sequences in database: 13,198
Lambda K H
0.320 0.139 0.395
Gapped
Lambda K H
0.267 0.0410 0.140
Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 1,090,248
Number of Sequences: 13198
Number of extensions: 41782
Number of successful extensions: 106
Number of sequences better than 10.0: 15
Number of HSP's better than 10.0 without gapping: 10
Number of HSP's successfully gapped in prelim test: 5
Number of HSP's that attempted gapping in prelim test: 86
Number of HSP's gapped (non-prelim): 15
length of query: 194
length of database: 2,899,336
effective HSP length: 83
effective length of query: 111
effective length of database: 1,803,902
effective search space: 200233122
effective search space used: 200233122
T: 11
A: 40
X1: 16 ( 7.4 bits)
X2: 38 (14.6 bits)
X3: 64 (24.7 bits)
S1: 41 (21.8 bits)
S2: 52 (24.6 bits)