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|15645323|ref|NP_207494.1| diacylglycerol kinase
(dgkA) [Helicobacter pylori 26695]
(128 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|1FXO|B Chain B, The Structural Basis Of The Catalytic M... 25 2.7
pdb|1G23|A Chain A, The Structural Basis Of The Catalytic M... 25 2.7
pdb|1IIN|A Chain A, Thymidylyltransferase Complexed With Ud... 25 2.7
pdb|1MTY|D Chain D, Methane Monooxygenase Hydroxylase From ... 25 2.7
pdb|1KHO|A Chain A, Crystal Structure Analysis Of Clostridi... 25 2.7
pdb|1FZI|A Chain A, Methane Monooxygenase Hydroxylase, Form... 25 2.7
pdb|1MP3|A Chain A, L89t Variant Of S. Enterica Rmla >gi|24... 25 2.7
pdb|1MP4|A Chain A, W224h Variant Of S. Enterica Rmla >gi|2... 25 2.7
pdb|1MP5|A Chain A, Y177f Variant Of S. Enterica Rmla >gi|2... 25 2.7
pdb|1MHY|D Chain D, Methane Monooxygenase Hydroxylase >gi|2... 25 3.6
pdb|4CLA| Type III Chloramphenicol Acetyltransferase (CAT... 23 8.0
pdb|1CIA| Chloramphenicol Acetyltransferase (Type Iii) (E... 23 8.0
pdb|2CLA| Chloramphenicol Acetyltransferase (E.C.2.3.1.28... 23 8.0
pdb|1QCA| Quadruple Mutant Q92c, N146f, Y168f, I172v Type... 23 8.0
pdb|1CLA| Type III Chloramphenicol Acetyltransferase (CAT... 23 8.0
pdb|3CLA| Type III Chloramphenicol Acetyltransferase (CAT... 23 8.0
>pdb|1FXO|B Chain B, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1FXO|E Chain E, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1FXO|F Chain F, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1FXO|G Chain G, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1G1L|B Chain B, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G1L|F Chain F, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G0R|F Chain F, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1FZW|C Chain C, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1FZW|F Chain F, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1G3L|D Chain D, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-L-Rhamnose Complex.
pdb|1FXO|A Chain A, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1FXO|C Chain C, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1FXO|D Chain D, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1FXO|H Chain H, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tmp Complex.
pdb|1G1L|A Chain A, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G1L|C Chain C, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G1L|D Chain D, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G1L|E Chain E, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G1L|G Chain G, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G1L|H Chain H, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-Glucose Complex.
pdb|1G0R|A Chain A, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1G0R|B Chain B, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1G0R|C Chain C, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1G0R|D Chain D, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1G0R|E Chain E, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1G0R|G Chain G, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1G0R|H Chain H, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). ThymidineGLUCOSE-1-Phosphate Complex.
pdb|1FZW|A Chain A, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1FZW|B Chain B, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1FZW|D Chain D, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1FZW|E Chain E, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1FZW|G Chain G, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1FZW|H Chain H, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Apo Enzyme.
pdb|1G2V|A Chain A, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G2V|B Chain B, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G2V|C Chain C, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G2V|D Chain D, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G2V|E Chain E, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G2V|F Chain F, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G2V|G Chain G, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G2V|H Chain H, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Ttp Complex.
pdb|1G3L|A Chain A, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-L-Rhamnose Complex.
pdb|1G3L|B Chain B, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-L-Rhamnose Complex.
pdb|1G3L|C Chain C, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Tdp-L-Rhamnose Complex
Length = 293
Score = 25.0 bits (53), Expect = 2.7
Identities = 18/41 (43%), Positives = 23/41 (55%)
Query: 17 FKALFYSKDGLKCAWIEESAFRQIVILALFCIVLASYLAKD 57
F A ++ GLK A EE A+RQ I A LA+ LAK+
Sbjct: 238 FIATLENRQGLKVACPEEIAYRQKWIDAAQLEKLAAPLAKN 278
>pdb|1G23|A Chain A, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex.
pdb|1G23|B Chain B, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex.
pdb|1G23|C Chain C, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex.
pdb|1G23|D Chain D, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex.
pdb|1G23|E Chain E, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex.
pdb|1G23|F Chain F, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex.
pdb|1G23|G Chain G, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex.
pdb|1G23|H Chain H, The Structural Basis Of The Catalytic Mechanism And
Regulation Of Glucose-1-Phosphate Thymidylyltransferase
(Rmla). Glucose-1-Phosphate Complex
Length = 293
Score = 25.0 bits (53), Expect = 2.7
Identities = 18/41 (43%), Positives = 23/41 (55%)
Query: 17 FKALFYSKDGLKCAWIEESAFRQIVILALFCIVLASYLAKD 57
F A ++ GLK A EE A+RQ I A LA+ LAK+
Sbjct: 238 FIATLENRQGLKVACPEEIAYRQKWIDAAQLEKLAAPLAKN 278
>pdb|1IIN|A Chain A, Thymidylyltransferase Complexed With Udp-Glucose
pdb|1IIN|B Chain B, Thymidylyltransferase Complexed With Udp-Glucose
pdb|1IIN|C Chain C, Thymidylyltransferase Complexed With Udp-Glucose
pdb|1IIN|D Chain D, Thymidylyltransferase Complexed With Udp-Glucose
pdb|1IIM|A Chain A, Thymidylyltransferase Complexed With Ttp
pdb|1IIM|B Chain B, Thymidylyltransferase Complexed With Ttp
Length = 292
Score = 25.0 bits (53), Expect = 2.7
Identities = 17/41 (41%), Positives = 22/41 (53%)
Query: 17 FKALFYSKDGLKCAWIEESAFRQIVILALFCIVLASYLAKD 57
F A + GLK + EE AFR+ I A I LA L+K+
Sbjct: 239 FIATIEERQGLKVSCPEEIAFRKNFINAQQVIELAGPLSKN 279
>pdb|1MTY|D Chain D, Methane Monooxygenase Hydroxylase From Methylococcus
Capsulatus (Bath)
pdb|1MTY|E Chain E, Methane Monooxygenase Hydroxylase From Methylococcus
Capsulatus (Bath)
pdb|1MMO|D Chain D, Methane Monooxygenase Hydrolase (E.C.1.14.13.25) (Methane
Hydroxylase)
pdb|1MMO|E Chain E, Methane Monooxygenase Hydrolase (E.C.1.14.13.25) (Methane
Hydroxylase)
Length = 512
Score = 25.0 bits (53), Expect = 2.7
Identities = 14/44 (31%), Positives = 24/44 (53%), Gaps = 4/44 (9%)
Query: 6 VPPKAKGFKRLFKALFYSKDGLKCA----WIEESAFRQIVILAL 45
+ P KG KR+F F S D ++C+ + E+ F +I+A+
Sbjct: 163 IGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPLIVAV 206
>pdb|1KHO|A Chain A, Crystal Structure Analysis Of Clostridium Perfringens
Alpha- Toxin Isolated From Avian Strain Swcp
pdb|1KHO|B Chain B, Crystal Structure Analysis Of Clostridium Perfringens
Alpha- Toxin Isolated From Avian Strain Swcp
Length = 370
Score = 25.0 bits (53), Expect = 2.7
Identities = 9/24 (37%), Positives = 14/24 (57%)
Query: 10 AKGFKRLFKALFYSKDGLKCAWIE 33
A+ F + K L+YS + C+W E
Sbjct: 193 ARSFAKTAKDLYYSHANMSCSWDE 216
>pdb|1FZI|A Chain A, Methane Monooxygenase Hydroxylase, Form I Pressurized With
Xenon Gas
pdb|1FZI|B Chain B, Methane Monooxygenase Hydroxylase, Form I Pressurized With
Xenon Gas
pdb|1FZ1|A Chain A, Methane Monooxygenase Hydroxylase, Form Iii Oxidized
pdb|1FZ1|B Chain B, Methane Monooxygenase Hydroxylase, Form Iii Oxidized
pdb|1FZ3|A Chain A, Methane Monooxygenase Hydroxylase, Form Iii Soak At Ph 6.2
(0.1 M Pipes)
pdb|1FZ3|B Chain B, Methane Monooxygenase Hydroxylase, Form Iii Soak At Ph 6.2
(0.1 M Pipes)
pdb|1FZ0|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Mixed-Valent
Grown Anaerobically
pdb|1FZ0|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Mixed-Valent
Grown Anaerobically
pdb|1FZ8|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Cocrystallized
With Dibromomethane
pdb|1FZ2|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Mixed-Valent
Generated By Crystal Soaking
pdb|1FYZ|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Reduced By
Soaking
pdb|1FYZ|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Reduced By
Soaking
pdb|1FZ9|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Cocrystallized
With Iodoethane
pdb|1FZ4|A Chain A, Methane Monooxygenase Hydroxylase, Form Iii Soaked At Ph
8.5 (0.1 M Tris)
pdb|1FZH|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Pressurized
With Xenon Gas
pdb|1FZ5|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Crystallized
Anaerobically From Reduced Enzyme
pdb|1FZ7|A Chain A, Methane Monooxygenase Hydroxylase, Form Iii Soaked In 0.9
M Ethanol
pdb|1FZ7|B Chain B, Methane Monooxygenase Hydroxylase, Form Iii Soaked In 0.9
M Ethanol
pdb|1FZ6|A Chain A, Methane Monooxygenase Hydroxylase, Form Ii Soaked In 1 M
Methanol
pdb|1FZ8|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Cocrystallized
With Dibromomethane
pdb|1FZ2|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Mixed-Valent
Generated By Crystal Soaking
pdb|1FZ9|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Cocrystallized
With Iodoethane
pdb|1FZ4|B Chain B, Methane Monooxygenase Hydroxylase, Form Iii Soaked At Ph
8.5 (0.1 M Tris)
pdb|1FZ5|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Crystallized
Anaerobically From Reduced Enzyme
pdb|1FZH|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Pressurized
With Xenon Gas
pdb|1FZ6|B Chain B, Methane Monooxygenase Hydroxylase, Form Ii Soaked In 1 M
Methanol
Length = 527
Score = 25.0 bits (53), Expect = 2.7
Identities = 14/44 (31%), Positives = 24/44 (53%), Gaps = 4/44 (9%)
Query: 6 VPPKAKGFKRLFKALFYSKDGLKCA----WIEESAFRQIVILAL 45
+ P KG KR+F F S D ++C+ + E+ F +I+A+
Sbjct: 177 IGPLWKGMKRVFSDGFISGDAVECSLNLQLVGEACFTNPLIVAV 220
>pdb|1MP3|A Chain A, L89t Variant Of S. Enterica Rmla
pdb|1MP3|B Chain B, L89t Variant Of S. Enterica Rmla
Length = 292
Score = 25.0 bits (53), Expect = 2.7
Identities = 17/41 (41%), Positives = 22/41 (53%)
Query: 17 FKALFYSKDGLKCAWIEESAFRQIVILALFCIVLASYLAKD 57
F A + GLK + EE AFR+ I A I LA L+K+
Sbjct: 239 FIATIEERQGLKVSCPEEIAFRKNFINAQQVIELAGPLSKN 279
>pdb|1MP4|A Chain A, W224h Variant Of S. Enterica Rmla
pdb|1MP4|B Chain B, W224h Variant Of S. Enterica Rmla
Length = 292
Score = 25.0 bits (53), Expect = 2.7
Identities = 17/41 (41%), Positives = 22/41 (53%)
Query: 17 FKALFYSKDGLKCAWIEESAFRQIVILALFCIVLASYLAKD 57
F A + GLK + EE AFR+ I A I LA L+K+
Sbjct: 239 FIATIEERQGLKVSCPEEIAFRKNFINAQQVIELAGPLSKN 279
>pdb|1MP5|A Chain A, Y177f Variant Of S. Enterica Rmla
pdb|1MP5|B Chain B, Y177f Variant Of S. Enterica Rmla
pdb|1MP5|C Chain C, Y177f Variant Of S. Enterica Rmla
pdb|1MP5|D Chain D, Y177f Variant Of S. Enterica Rmla
Length = 292
Score = 25.0 bits (53), Expect = 2.7
Identities = 17/41 (41%), Positives = 22/41 (53%)
Query: 17 FKALFYSKDGLKCAWIEESAFRQIVILALFCIVLASYLAKD 57
F A + GLK + EE AFR+ I A I LA L+K+
Sbjct: 239 FIATIEERQGLKVSCPEEIAFRKNFINAQQVIELAGPLSKN 279
>pdb|1MHY|D Chain D, Methane Monooxygenase Hydroxylase
pdb|1MHZ|D Chain D, Methane Monooxygenase Hydroxylase
Length = 521
Score = 24.6 bits (52), Expect = 3.6
Identities = 14/44 (31%), Positives = 24/44 (53%), Gaps = 4/44 (9%)
Query: 6 VPPKAKGFKRLFKALFYSKDGLKCA----WIEESAFRQIVILAL 45
+ P KG KR+F F S D ++C+ + E+ F +I+A+
Sbjct: 172 IGPLWKGMKRVFADGFISGDAVECSVNLQLVGEACFTNPLIVAV 215
>pdb|4CLA| Type III Chloramphenicol Acetyltransferase (CATIII)
(E.C.2.3.1.28) (Mutant With Leu 160 Replaced By Phe)
(L160F) Complex With Chloramphenicol
Length = 213
Score = 23.5 bits (49), Expect = 8.0
Identities = 9/44 (20%), Positives = 28/44 (63%)
Query: 52 SYLAKDFLEWGLLILPCFLSVVVELINSSIEKAVDFTGTEFHPL 95
+++ ++ E+ LPC S+ ++ ++++K++D + +F+P+
Sbjct: 10 NWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPV 53
>pdb|1CIA| Chloramphenicol Acetyltransferase (Type Iii) (E.C.2.3.1.28)
Mutant With His 195 Replaced By Gln (H195q)
(Engineered)
Length = 213
Score = 23.5 bits (49), Expect = 8.0
Identities = 9/44 (20%), Positives = 28/44 (63%)
Query: 52 SYLAKDFLEWGLLILPCFLSVVVELINSSIEKAVDFTGTEFHPL 95
+++ ++ E+ LPC S+ ++ ++++K++D + +F+P+
Sbjct: 10 NWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPV 53
>pdb|2CLA| Chloramphenicol Acetyltransferase (E.C.2.3.1.28) (CATIII) (D199N
Mutant)
Length = 213
Score = 23.5 bits (49), Expect = 8.0
Identities = 9/44 (20%), Positives = 28/44 (63%)
Query: 52 SYLAKDFLEWGLLILPCFLSVVVELINSSIEKAVDFTGTEFHPL 95
+++ ++ E+ LPC S+ ++ ++++K++D + +F+P+
Sbjct: 10 NWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPV 53
>pdb|1QCA| Quadruple Mutant Q92c, N146f, Y168f, I172v Type Iii Cat
Complexed With Fusidic Acid. Crystals Grown At Ph 6.3.
X-Ray Data Collected At Room Temperature
Length = 213
Score = 23.5 bits (49), Expect = 8.0
Identities = 9/44 (20%), Positives = 28/44 (63%)
Query: 52 SYLAKDFLEWGLLILPCFLSVVVELINSSIEKAVDFTGTEFHPL 95
+++ ++ E+ LPC S+ ++ ++++K++D + +F+P+
Sbjct: 10 NWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPV 53
>pdb|1CLA| Type III Chloramphenicol Acetyltransferase (CATIII)
(E.C.2.3.1.28) (S148A Mutant) - Chloramphenicol Complex
Length = 213
Score = 23.5 bits (49), Expect = 8.0
Identities = 9/44 (20%), Positives = 28/44 (63%)
Query: 52 SYLAKDFLEWGLLILPCFLSVVVELINSSIEKAVDFTGTEFHPL 95
+++ ++ E+ LPC S+ ++ ++++K++D + +F+P+
Sbjct: 10 NWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPV 53
>pdb|3CLA| Type III Chloramphenicol Acetyltransferase (CATIII)
(E.C.2.3.1.28) Complex With Chloramphenicol
Length = 213
Score = 23.5 bits (49), Expect = 8.0
Identities = 9/44 (20%), Positives = 28/44 (63%)
Query: 52 SYLAKDFLEWGLLILPCFLSVVVELINSSIEKAVDFTGTEFHPL 95
+++ ++ E+ LPC S+ ++ ++++K++D + +F+P+
Sbjct: 10 NWVRREHFEFYRHRLPCGFSLTSKIDITTLKKSLDDSAYKFYPV 53
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
0.329 0.143 0.446
Gapped
Lambda K H
0.267 0.0410 0.140
Matrix: BLOSUM62
Gap Penalties: Existence: 11, Extension: 1
Number of Hits to DB: 686,864
Number of Sequences: 13198
Number of extensions: 22772
Number of successful extensions: 52
Number of sequences better than 10.0: 16
Number of HSP's better than 10.0 without gapping: 16
Number of HSP's successfully gapped in prelim test: 0
Number of HSP's that attempted gapping in prelim test: 36
Number of HSP's gapped (non-prelim): 16
length of query: 128
length of database: 2,899,336
effective HSP length: 78
effective length of query: 50
effective length of database: 1,869,892
effective search space: 93494600
effective search space used: 93494600
T: 11
A: 40
X1: 15 ( 7.1 bits)
X2: 38 (14.6 bits)
X3: 64 (24.7 bits)
S1: 40 (21.8 bits)
S2: 49 (23.5 bits)