HEADER HYDROLASE/RNA 23-APR-14 4PEH
TITLE DBR1 IN COMPLEX WITH SYNTHETIC LINEAR RNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA LARIAT DEBRANCHING ENZYME, PUTATIVE;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RNA (5'-R(*CP*UP*AP*(A2P)P*AP*CP*AP*A)-3');
COMPND 8 CHAIN: V, W, X, Y, Z;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA;
SOURCE 3 ORGANISM_TAXID: 5759;
SOURCE 4 GENE: EHI_062730;
SOURCE 5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4932;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: YEP351;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630
KEYWDS NUCLEASE, PHOSPHODIESTERASE, METALLOHYDROLASE,
KEYWDS 2 METALLOPHOSPHOESTERASE, LARIAT RNA, HYDROLASE, METALLOENZYME,
KEYWDS 3 HYDROLASE-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.J.MONTEMAYOR,A.KATOLIK,N.E.CLARK,A.B.TAYLOR,J.P.SCHUERMANN,
AUTHOR 2 D.J.COMBS,R.JOHNSSON,S.P.HOLLOWAY,S.W.STEVENS,M.J.DAMHA,P.J.HART
REVDAT 4 27-DEC-23 4PEH 1 REMARK LINK
REVDAT 3 27-SEP-17 4PEH 1 SOURCE JRNL REMARK
REVDAT 2 01-OCT-14 4PEH 1 JRNL
REVDAT 1 27-AUG-14 4PEH 0
JRNL AUTH E.J.MONTEMAYOR,A.KATOLIK,N.E.CLARK,A.B.TAYLOR,
JRNL AUTH 2 J.P.SCHUERMANN,D.J.COMBS,R.JOHNSSON,S.P.HOLLOWAY,
JRNL AUTH 3 S.W.STEVENS,M.J.DAMHA,P.J.HART
JRNL TITL STRUCTURAL BASIS OF LARIAT RNA RECOGNITION BY THE INTRON
JRNL TITL 2 DEBRANCHING ENZYME DBR1.
JRNL REF NUCLEIC ACIDS RES. V. 42 10845 2014
JRNL REFN ESSN 1362-4962
JRNL PMID 25123664
JRNL DOI 10.1093/NAR/GKU725
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 129111
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 6446
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.0401 - 6.4953 0.99 4390 235 0.1792 0.2020
REMARK 3 2 6.4953 - 5.1593 0.99 4258 201 0.1868 0.2347
REMARK 3 3 5.1593 - 4.5082 0.98 4154 219 0.1583 0.2011
REMARK 3 4 4.5082 - 4.0965 0.98 4114 226 0.1645 0.1776
REMARK 3 5 4.0965 - 3.8032 0.99 4117 234 0.1738 0.2098
REMARK 3 6 3.8032 - 3.5791 0.99 4148 213 0.1901 0.2141
REMARK 3 7 3.5791 - 3.4000 0.99 4121 208 0.2004 0.2595
REMARK 3 8 3.4000 - 3.2520 0.99 4139 209 0.1982 0.2570
REMARK 3 9 3.2520 - 3.1269 0.99 4101 215 0.2069 0.2346
REMARK 3 10 3.1269 - 3.0190 0.99 4124 208 0.2122 0.2491
REMARK 3 11 3.0190 - 2.9247 0.99 4111 207 0.2159 0.2813
REMARK 3 12 2.9247 - 2.8411 1.00 4103 227 0.2226 0.2731
REMARK 3 13 2.8411 - 2.7663 0.99 4096 244 0.2310 0.2852
REMARK 3 14 2.7663 - 2.6989 1.00 4100 208 0.2306 0.2933
REMARK 3 15 2.6989 - 2.6375 1.00 4112 209 0.2259 0.2820
REMARK 3 16 2.6375 - 2.5814 1.00 4118 209 0.2214 0.2905
REMARK 3 17 2.5814 - 2.5298 0.99 4061 227 0.2285 0.2836
REMARK 3 18 2.5298 - 2.4820 1.00 4129 188 0.2395 0.2800
REMARK 3 19 2.4820 - 2.4377 1.00 4065 232 0.2448 0.3118
REMARK 3 20 2.4377 - 2.3964 0.99 4072 228 0.2485 0.3259
REMARK 3 21 2.3964 - 2.3578 0.99 4080 209 0.2438 0.3292
REMARK 3 22 2.3578 - 2.3215 0.99 4120 223 0.2430 0.3167
REMARK 3 23 2.3215 - 2.2873 1.00 4015 227 0.2489 0.3048
REMARK 3 24 2.2873 - 2.2551 0.99 4133 203 0.2516 0.2920
REMARK 3 25 2.2551 - 2.2247 0.99 4071 207 0.2577 0.2939
REMARK 3 26 2.2247 - 2.1958 0.99 4036 235 0.2489 0.3023
REMARK 3 27 2.1958 - 2.1683 0.99 4107 187 0.2532 0.2999
REMARK 3 28 2.1683 - 2.1422 0.99 4063 215 0.2614 0.3213
REMARK 3 29 2.1422 - 2.1173 0.99 4069 213 0.2773 0.3330
REMARK 3 30 2.1173 - 2.1000 0.82 3338 180 0.2841 0.3416
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 15176
REMARK 3 ANGLE : 0.907 20605
REMARK 3 CHIRALITY : 0.064 2176
REMARK 3 PLANARITY : 0.004 2516
REMARK 3 DIHEDRAL : 14.116 5656
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201214.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129196
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 47.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.52100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE, 0.1 M BIS-TRIS,
REMARK 280 25% PEG 3350, 8.5 % GLYCEROL, 3.0 MM MANGANESE SULFATE, 1.45 MM
REMARK 280 AK65, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.51050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.47100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.96800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 106.47100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.51050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 70.96800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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, V
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, W
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, X
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, Y
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, Z
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 ASN A 354
REMARK 465 C V 498
REMARK 465 U V 499
REMARK 465 A V 504
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 GLU B 4
REMARK 465 ASN B 354
REMARK 465 C W 498
REMARK 465 U W 499
REMARK 465 GLY C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 GLU C 4
REMARK 465 ASN C 354
REMARK 465 C X 498
REMARK 465 GLY D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 THR D 3
REMARK 465 GLU D 4
REMARK 465 ASN D 354
REMARK 465 C Y 498
REMARK 465 U Y 499
REMARK 465 GLY E -1
REMARK 465 ALA E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 THR E 3
REMARK 465 GLU E 4
REMARK 465 ASN E 354
REMARK 465 C Z 498
REMARK 465 U Z 499
REMARK 465 A Z 504
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 A V 500 P OP1 OP2
REMARK 470 A V 503 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A V 503 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A V 503 N1 C2 N3 C4
REMARK 470 A W 504 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A W 504 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A W 504 N1 C2 N3 C4
REMARK 470 U X 499 P OP1 OP2 O5' C5' C4' O4'
REMARK 470 U X 499 C3' C2' O2' C1' N1 C2 O2
REMARK 470 U X 499 N3 C4 O4 C5 C6
REMARK 470 A X 504 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A X 504 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A X 504 N1 C2 N3 C4
REMARK 470 A Y 500 P OP1 OP2
REMARK 470 A Y 504 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A Y 504 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A Y 504 N1 C2 N3 C4
REMARK 470 A Z 500 P OP1 OP2
REMARK 470 A Z 503 C5' C4' O4' C3' O3' C2' O2'
REMARK 470 A Z 503 C1' N9 C8 N7 C5 C6 N6
REMARK 470 A Z 503 N1 C2 N3 C4
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 LYS A 18 62.44 -102.79
REMARK 500 LYS A 65 73.92 -66.74
REMARK 500 HIS A 230 -41.50 91.04
REMARK 500 ASN A 352 80.38 63.48
REMARK 500 LEU B 100 33.47 -99.24
REMARK 500 HIS B 180 -73.00 -84.56
REMARK 500 LYS B 222 62.60 35.90
REMARK 500 HIS B 230 -32.78 64.24
REMARK 500 ASN B 254 3.14 -68.76
REMARK 500 PRO C 148 -7.77 -58.88
REMARK 500 HIS C 230 -39.59 22.44
REMARK 500 HIS C 230 -39.59 -29.79
REMARK 500 ASN C 352 84.06 49.39
REMARK 500 LYS D 18 58.93 -94.34
REMARK 500 GLU D 28 0.65 -63.11
REMARK 500 LEU D 100 33.10 -98.49
REMARK 500 HIS D 180 -68.74 -90.25
REMARK 500 ASN D 191 74.70 -59.02
REMARK 500 LYS D 222 62.73 39.04
REMARK 500 HIS D 230 -36.84 59.07
REMARK 500 ASN D 254 25.07 -70.54
REMARK 500 ASP D 260 74.67 -102.80
REMARK 500 LYS D 264 -70.67 -69.96
REMARK 500 CYS E 107 -175.37 -170.50
REMARK 500 ASN E 191 69.40 -69.07
REMARK 500 LYS E 222 57.04 39.10
REMARK 500 HIS E 230 -47.50 67.55
REMARK 500 GLN E 291 108.84 -161.32
REMARK 500 LYS E 305 0.24 -68.69
REMARK 500 ASN E 352 93.08 82.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 45 OD2
REMARK 620 2 ASN A 90 OD1 109.4
REMARK 620 3 HIS A 180 NE2 87.3 84.0
REMARK 620 4 HIS A 230 ND1 163.0 84.6 84.7
REMARK 620 5 A2P V 501 O1P 101.3 84.5 167.5 89.2
REMARK 620 6 HOH V 701 O 78.6 171.0 100.8 88.2 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 45 OD2
REMARK 620 2 ASN B 90 OD1 106.1
REMARK 620 3 HIS B 180 NE2 90.9 76.9
REMARK 620 4 HIS B 230 ND1 162.9 90.3 88.1
REMARK 620 5 A2P W 501 O2P 88.4 82.9 158.7 98.6
REMARK 620 6 HOH W 701 O 74.8 175.8 107.3 89.3 93.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN C 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 45 OD2
REMARK 620 2 ASN C 90 OD1 107.9
REMARK 620 3 HIS C 180 NE2 89.3 80.8
REMARK 620 4 HIS C 230 ND1 163.1 87.5 86.3
REMARK 620 5 HOH C 725 O 75.8 174.1 103.9 89.4
REMARK 620 6 A2P X 501 O2P 97.8 84.9 165.4 90.3 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN D 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 45 OD2
REMARK 620 2 ASN D 90 OD1 121.3
REMARK 620 3 HIS D 180 NE2 82.8 84.9
REMARK 620 4 HIS D 230 ND1 154.7 80.0 86.3
REMARK 620 5 HOH D 691 O 64.9 173.7 96.1 93.8
REMARK 620 6 A2P Y 501 O1P 103.8 86.7 171.2 89.8 91.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN E 401 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 45 OD2
REMARK 620 2 ASN E 90 OD1 111.1
REMARK 620 3 HIS E 180 NE2 86.6 83.5
REMARK 620 4 HIS E 230 ND1 158.5 88.6 87.2
REMARK 620 5 A2P Z 501 O2P 95.2 87.7 171.1 94.1
REMARK 620 6 HOH Z 703 O 72.8 172.1 103.8 88.7 85.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MN E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PEF RELATED DB: PDB
REMARK 900 RELATED ID: 4PEG RELATED DB: PDB
REMARK 900 RELATED ID: 4PEI RELATED DB: PDB
DBREF 4PEH A 1 354 UNP C4M1P9 C4M1P9_ENTHI 1 354
DBREF 4PEH V 498 504 PDB 4PEH 4PEH 498 504
DBREF 4PEH B 1 354 UNP C4M1P9 C4M1P9_ENTHI 1 354
DBREF 4PEH W 498 504 PDB 4PEH 4PEH 498 504
DBREF 4PEH C 1 354 UNP C4M1P9 C4M1P9_ENTHI 1 354
DBREF 4PEH X 498 504 PDB 4PEH 4PEH 498 504
DBREF 4PEH D 1 354 UNP C4M1P9 C4M1P9_ENTHI 1 354
DBREF 4PEH Y 498 504 PDB 4PEH 4PEH 498 504
DBREF 4PEH E 1 354 UNP C4M1P9 C4M1P9_ENTHI 1 354
DBREF 4PEH Z 498 504 PDB 4PEH 4PEH 498 504
SEQADV 4PEH GLY A -1 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH ALA A 0 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH SER A 14 UNP C4M1P9 CYS 14 ENGINEERED MUTATION
SEQADV 4PEH GLY B -1 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH ALA B 0 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH SER B 14 UNP C4M1P9 CYS 14 ENGINEERED MUTATION
SEQADV 4PEH GLY C -1 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH ALA C 0 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH SER C 14 UNP C4M1P9 CYS 14 ENGINEERED MUTATION
SEQADV 4PEH GLY D -1 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH ALA D 0 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH SER D 14 UNP C4M1P9 CYS 14 ENGINEERED MUTATION
SEQADV 4PEH GLY E -1 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH ALA E 0 UNP C4M1P9 EXPRESSION TAG
SEQADV 4PEH SER E 14 UNP C4M1P9 CYS 14 ENGINEERED MUTATION
SEQRES 1 A 356 GLY ALA MET ALA THR GLU GLN ILE GLN HIS ILE ALA ILE
SEQRES 2 A 356 VAL GLY SER VAL HIS GLY LYS TYR ARG GLU MET TYR ARG
SEQRES 3 A 356 GLN LEU SER GLU TYR GLU LYS SER THR GLY LYS GLU ILE
SEQRES 4 A 356 SER PHE VAL ILE CYS THR GLY ASP MET GLN THR LEU ARG
SEQRES 5 A 356 TYR GLU ALA ASP LEU VAL TYR LEU LYS VAL PRO PRO LYS
SEQRES 6 A 356 TYR LYS GLN MET GLY ASP PHE HIS LEU TYR TYR GLU GLY
SEQRES 7 A 356 LYS GLU LYS ALA PRO TYR LEU THR LEU PHE ILE GLY GLY
SEQRES 8 A 356 ASN HIS GLU SER SER ASN VAL LEU LEU HIS LEU TYR ASN
SEQRES 9 A 356 GLY GLY PHE VAL CYS PHE ASN MET TYR TYR LEU GLY VAL
SEQRES 10 A 356 CYS SER CYS ILE ASN ILE ASN GLY LEU ARG ILE VAL GLY
SEQRES 11 A 356 VAL SER GLY ILE TYR LYS SER PHE ASP GLU LYS LYS PRO
SEQRES 12 A 356 TYR THR TYR PRO PRO SER PRO ASN ASP VAL VAL SER LEU
SEQRES 13 A 356 PHE HIS THR ARG ASN TYR VAL ILE GLN MET LEU SER ASN
SEQRES 14 A 356 LEU SER GLN SER SER GLN ILE ASP ILE SER LEU SER HIS
SEQRES 15 A 356 ASP TRP PRO GLN GLY ILE VAL MET LYS GLY ASN TYR LYS
SEQRES 16 A 356 GLN LEU TYR ARG PHE GLN PRO GLY PHE LYS LYS ASP GLY
SEQRES 17 A 356 ALA SER LEU GLY SER PRO ILE ASN LYS VAL ILE LEU ASN
SEQRES 18 A 356 THR LEU LYS PRO LYS TYR TRP ILE SER GLY HIS MET HIS
SEQRES 19 A 356 CYS GLU TYR HIS ALA GLU GLU GLY PRO THR HIS PHE ILE
SEQRES 20 A 356 ALA LEU GLY LYS ILE GLY TYR LYS ASN ALA ILE SER TYR
SEQRES 21 A 356 LEU ASP LEU PRO LEU LYS GLN LYS THR ASP LEU GLU TYR
SEQRES 22 A 356 ASP LYS ASP TRP VAL CYS ASN LEU ILE MET THR TRP PRO
SEQRES 23 A 356 ALA PHE SER ASN LYS ALA GLN PHE PRO ASP LEU SER TYR
SEQRES 24 A 356 SER ILE SER GLU LEU LEU SER LYS ARG THR LYS GLU LEU
SEQRES 25 A 356 ASP LYS LYS ILE ILE GLU LEU TRP GLU LYS TYR ILE GLY
SEQRES 26 A 356 LEU LYS ILE ILE TYR ASP SER ASP THR PHE ASP ILE GLN
SEQRES 27 A 356 PHE THR SER ARG ARG PHE TYR ILE GLU LYS ILE TYR ASN
SEQRES 28 A 356 GLU LEU ASN ILE ASN
SEQRES 1 V 7 C U A A2P C A A
SEQRES 1 B 356 GLY ALA MET ALA THR GLU GLN ILE GLN HIS ILE ALA ILE
SEQRES 2 B 356 VAL GLY SER VAL HIS GLY LYS TYR ARG GLU MET TYR ARG
SEQRES 3 B 356 GLN LEU SER GLU TYR GLU LYS SER THR GLY LYS GLU ILE
SEQRES 4 B 356 SER PHE VAL ILE CYS THR GLY ASP MET GLN THR LEU ARG
SEQRES 5 B 356 TYR GLU ALA ASP LEU VAL TYR LEU LYS VAL PRO PRO LYS
SEQRES 6 B 356 TYR LYS GLN MET GLY ASP PHE HIS LEU TYR TYR GLU GLY
SEQRES 7 B 356 LYS GLU LYS ALA PRO TYR LEU THR LEU PHE ILE GLY GLY
SEQRES 8 B 356 ASN HIS GLU SER SER ASN VAL LEU LEU HIS LEU TYR ASN
SEQRES 9 B 356 GLY GLY PHE VAL CYS PHE ASN MET TYR TYR LEU GLY VAL
SEQRES 10 B 356 CYS SER CYS ILE ASN ILE ASN GLY LEU ARG ILE VAL GLY
SEQRES 11 B 356 VAL SER GLY ILE TYR LYS SER PHE ASP GLU LYS LYS PRO
SEQRES 12 B 356 TYR THR TYR PRO PRO SER PRO ASN ASP VAL VAL SER LEU
SEQRES 13 B 356 PHE HIS THR ARG ASN TYR VAL ILE GLN MET LEU SER ASN
SEQRES 14 B 356 LEU SER GLN SER SER GLN ILE ASP ILE SER LEU SER HIS
SEQRES 15 B 356 ASP TRP PRO GLN GLY ILE VAL MET LYS GLY ASN TYR LYS
SEQRES 16 B 356 GLN LEU TYR ARG PHE GLN PRO GLY PHE LYS LYS ASP GLY
SEQRES 17 B 356 ALA SER LEU GLY SER PRO ILE ASN LYS VAL ILE LEU ASN
SEQRES 18 B 356 THR LEU LYS PRO LYS TYR TRP ILE SER GLY HIS MET HIS
SEQRES 19 B 356 CYS GLU TYR HIS ALA GLU GLU GLY PRO THR HIS PHE ILE
SEQRES 20 B 356 ALA LEU GLY LYS ILE GLY TYR LYS ASN ALA ILE SER TYR
SEQRES 21 B 356 LEU ASP LEU PRO LEU LYS GLN LYS THR ASP LEU GLU TYR
SEQRES 22 B 356 ASP LYS ASP TRP VAL CYS ASN LEU ILE MET THR TRP PRO
SEQRES 23 B 356 ALA PHE SER ASN LYS ALA GLN PHE PRO ASP LEU SER TYR
SEQRES 24 B 356 SER ILE SER GLU LEU LEU SER LYS ARG THR LYS GLU LEU
SEQRES 25 B 356 ASP LYS LYS ILE ILE GLU LEU TRP GLU LYS TYR ILE GLY
SEQRES 26 B 356 LEU LYS ILE ILE TYR ASP SER ASP THR PHE ASP ILE GLN
SEQRES 27 B 356 PHE THR SER ARG ARG PHE TYR ILE GLU LYS ILE TYR ASN
SEQRES 28 B 356 GLU LEU ASN ILE ASN
SEQRES 1 W 7 C U A A2P C A A
SEQRES 1 C 356 GLY ALA MET ALA THR GLU GLN ILE GLN HIS ILE ALA ILE
SEQRES 2 C 356 VAL GLY SER VAL HIS GLY LYS TYR ARG GLU MET TYR ARG
SEQRES 3 C 356 GLN LEU SER GLU TYR GLU LYS SER THR GLY LYS GLU ILE
SEQRES 4 C 356 SER PHE VAL ILE CYS THR GLY ASP MET GLN THR LEU ARG
SEQRES 5 C 356 TYR GLU ALA ASP LEU VAL TYR LEU LYS VAL PRO PRO LYS
SEQRES 6 C 356 TYR LYS GLN MET GLY ASP PHE HIS LEU TYR TYR GLU GLY
SEQRES 7 C 356 LYS GLU LYS ALA PRO TYR LEU THR LEU PHE ILE GLY GLY
SEQRES 8 C 356 ASN HIS GLU SER SER ASN VAL LEU LEU HIS LEU TYR ASN
SEQRES 9 C 356 GLY GLY PHE VAL CYS PHE ASN MET TYR TYR LEU GLY VAL
SEQRES 10 C 356 CYS SER CYS ILE ASN ILE ASN GLY LEU ARG ILE VAL GLY
SEQRES 11 C 356 VAL SER GLY ILE TYR LYS SER PHE ASP GLU LYS LYS PRO
SEQRES 12 C 356 TYR THR TYR PRO PRO SER PRO ASN ASP VAL VAL SER LEU
SEQRES 13 C 356 PHE HIS THR ARG ASN TYR VAL ILE GLN MET LEU SER ASN
SEQRES 14 C 356 LEU SER GLN SER SER GLN ILE ASP ILE SER LEU SER HIS
SEQRES 15 C 356 ASP TRP PRO GLN GLY ILE VAL MET LYS GLY ASN TYR LYS
SEQRES 16 C 356 GLN LEU TYR ARG PHE GLN PRO GLY PHE LYS LYS ASP GLY
SEQRES 17 C 356 ALA SER LEU GLY SER PRO ILE ASN LYS VAL ILE LEU ASN
SEQRES 18 C 356 THR LEU LYS PRO LYS TYR TRP ILE SER GLY HIS MET HIS
SEQRES 19 C 356 CYS GLU TYR HIS ALA GLU GLU GLY PRO THR HIS PHE ILE
SEQRES 20 C 356 ALA LEU GLY LYS ILE GLY TYR LYS ASN ALA ILE SER TYR
SEQRES 21 C 356 LEU ASP LEU PRO LEU LYS GLN LYS THR ASP LEU GLU TYR
SEQRES 22 C 356 ASP LYS ASP TRP VAL CYS ASN LEU ILE MET THR TRP PRO
SEQRES 23 C 356 ALA PHE SER ASN LYS ALA GLN PHE PRO ASP LEU SER TYR
SEQRES 24 C 356 SER ILE SER GLU LEU LEU SER LYS ARG THR LYS GLU LEU
SEQRES 25 C 356 ASP LYS LYS ILE ILE GLU LEU TRP GLU LYS TYR ILE GLY
SEQRES 26 C 356 LEU LYS ILE ILE TYR ASP SER ASP THR PHE ASP ILE GLN
SEQRES 27 C 356 PHE THR SER ARG ARG PHE TYR ILE GLU LYS ILE TYR ASN
SEQRES 28 C 356 GLU LEU ASN ILE ASN
SEQRES 1 X 7 C U A A2P C A A
SEQRES 1 D 356 GLY ALA MET ALA THR GLU GLN ILE GLN HIS ILE ALA ILE
SEQRES 2 D 356 VAL GLY SER VAL HIS GLY LYS TYR ARG GLU MET TYR ARG
SEQRES 3 D 356 GLN LEU SER GLU TYR GLU LYS SER THR GLY LYS GLU ILE
SEQRES 4 D 356 SER PHE VAL ILE CYS THR GLY ASP MET GLN THR LEU ARG
SEQRES 5 D 356 TYR GLU ALA ASP LEU VAL TYR LEU LYS VAL PRO PRO LYS
SEQRES 6 D 356 TYR LYS GLN MET GLY ASP PHE HIS LEU TYR TYR GLU GLY
SEQRES 7 D 356 LYS GLU LYS ALA PRO TYR LEU THR LEU PHE ILE GLY GLY
SEQRES 8 D 356 ASN HIS GLU SER SER ASN VAL LEU LEU HIS LEU TYR ASN
SEQRES 9 D 356 GLY GLY PHE VAL CYS PHE ASN MET TYR TYR LEU GLY VAL
SEQRES 10 D 356 CYS SER CYS ILE ASN ILE ASN GLY LEU ARG ILE VAL GLY
SEQRES 11 D 356 VAL SER GLY ILE TYR LYS SER PHE ASP GLU LYS LYS PRO
SEQRES 12 D 356 TYR THR TYR PRO PRO SER PRO ASN ASP VAL VAL SER LEU
SEQRES 13 D 356 PHE HIS THR ARG ASN TYR VAL ILE GLN MET LEU SER ASN
SEQRES 14 D 356 LEU SER GLN SER SER GLN ILE ASP ILE SER LEU SER HIS
SEQRES 15 D 356 ASP TRP PRO GLN GLY ILE VAL MET LYS GLY ASN TYR LYS
SEQRES 16 D 356 GLN LEU TYR ARG PHE GLN PRO GLY PHE LYS LYS ASP GLY
SEQRES 17 D 356 ALA SER LEU GLY SER PRO ILE ASN LYS VAL ILE LEU ASN
SEQRES 18 D 356 THR LEU LYS PRO LYS TYR TRP ILE SER GLY HIS MET HIS
SEQRES 19 D 356 CYS GLU TYR HIS ALA GLU GLU GLY PRO THR HIS PHE ILE
SEQRES 20 D 356 ALA LEU GLY LYS ILE GLY TYR LYS ASN ALA ILE SER TYR
SEQRES 21 D 356 LEU ASP LEU PRO LEU LYS GLN LYS THR ASP LEU GLU TYR
SEQRES 22 D 356 ASP LYS ASP TRP VAL CYS ASN LEU ILE MET THR TRP PRO
SEQRES 23 D 356 ALA PHE SER ASN LYS ALA GLN PHE PRO ASP LEU SER TYR
SEQRES 24 D 356 SER ILE SER GLU LEU LEU SER LYS ARG THR LYS GLU LEU
SEQRES 25 D 356 ASP LYS LYS ILE ILE GLU LEU TRP GLU LYS TYR ILE GLY
SEQRES 26 D 356 LEU LYS ILE ILE TYR ASP SER ASP THR PHE ASP ILE GLN
SEQRES 27 D 356 PHE THR SER ARG ARG PHE TYR ILE GLU LYS ILE TYR ASN
SEQRES 28 D 356 GLU LEU ASN ILE ASN
SEQRES 1 Y 7 C U A A2P C A A
SEQRES 1 E 356 GLY ALA MET ALA THR GLU GLN ILE GLN HIS ILE ALA ILE
SEQRES 2 E 356 VAL GLY SER VAL HIS GLY LYS TYR ARG GLU MET TYR ARG
SEQRES 3 E 356 GLN LEU SER GLU TYR GLU LYS SER THR GLY LYS GLU ILE
SEQRES 4 E 356 SER PHE VAL ILE CYS THR GLY ASP MET GLN THR LEU ARG
SEQRES 5 E 356 TYR GLU ALA ASP LEU VAL TYR LEU LYS VAL PRO PRO LYS
SEQRES 6 E 356 TYR LYS GLN MET GLY ASP PHE HIS LEU TYR TYR GLU GLY
SEQRES 7 E 356 LYS GLU LYS ALA PRO TYR LEU THR LEU PHE ILE GLY GLY
SEQRES 8 E 356 ASN HIS GLU SER SER ASN VAL LEU LEU HIS LEU TYR ASN
SEQRES 9 E 356 GLY GLY PHE VAL CYS PHE ASN MET TYR TYR LEU GLY VAL
SEQRES 10 E 356 CYS SER CYS ILE ASN ILE ASN GLY LEU ARG ILE VAL GLY
SEQRES 11 E 356 VAL SER GLY ILE TYR LYS SER PHE ASP GLU LYS LYS PRO
SEQRES 12 E 356 TYR THR TYR PRO PRO SER PRO ASN ASP VAL VAL SER LEU
SEQRES 13 E 356 PHE HIS THR ARG ASN TYR VAL ILE GLN MET LEU SER ASN
SEQRES 14 E 356 LEU SER GLN SER SER GLN ILE ASP ILE SER LEU SER HIS
SEQRES 15 E 356 ASP TRP PRO GLN GLY ILE VAL MET LYS GLY ASN TYR LYS
SEQRES 16 E 356 GLN LEU TYR ARG PHE GLN PRO GLY PHE LYS LYS ASP GLY
SEQRES 17 E 356 ALA SER LEU GLY SER PRO ILE ASN LYS VAL ILE LEU ASN
SEQRES 18 E 356 THR LEU LYS PRO LYS TYR TRP ILE SER GLY HIS MET HIS
SEQRES 19 E 356 CYS GLU TYR HIS ALA GLU GLU GLY PRO THR HIS PHE ILE
SEQRES 20 E 356 ALA LEU GLY LYS ILE GLY TYR LYS ASN ALA ILE SER TYR
SEQRES 21 E 356 LEU ASP LEU PRO LEU LYS GLN LYS THR ASP LEU GLU TYR
SEQRES 22 E 356 ASP LYS ASP TRP VAL CYS ASN LEU ILE MET THR TRP PRO
SEQRES 23 E 356 ALA PHE SER ASN LYS ALA GLN PHE PRO ASP LEU SER TYR
SEQRES 24 E 356 SER ILE SER GLU LEU LEU SER LYS ARG THR LYS GLU LEU
SEQRES 25 E 356 ASP LYS LYS ILE ILE GLU LEU TRP GLU LYS TYR ILE GLY
SEQRES 26 E 356 LEU LYS ILE ILE TYR ASP SER ASP THR PHE ASP ILE GLN
SEQRES 27 E 356 PHE THR SER ARG ARG PHE TYR ILE GLU LYS ILE TYR ASN
SEQRES 28 E 356 GLU LEU ASN ILE ASN
SEQRES 1 Z 7 C U A A2P C A A
HET A2P V 501 26
HET A2P W 501 26
HET A2P X 501 26
HET A2P Y 501 26
HET A2P Z 501 26
HET MN A 401 1
HET SO4 A 402 5
HET GOL A 403 6
HET MN B 401 1
HET SO4 B 402 5
HET SO4 B 403 5
HET MN C 401 1
HET SO4 C 402 5
HET SO4 C 403 5
HET SO4 C 404 5
HET MN D 401 1
HET SO4 D 402 5
HET MN E 401 1
HET SO4 E 402 5
HETNAM A2P ADENOSINE-2'-5'-DIPHOSPHATE
HETNAM MN MANGANESE (II) ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 A2P 5(C10 H15 N5 O10 P2)
FORMUL 11 MN 5(MN 2+)
FORMUL 12 SO4 8(O4 S 2-)
FORMUL 13 GOL C3 H8 O3
FORMUL 25 HOH *1007(H2 O)
HELIX 1 AA1 LYS A 18 LYS A 31 1 14
HELIX 2 AA2 TYR A 51 LEU A 58 5 8
HELIX 3 AA3 PRO A 61 LYS A 65 5 5
HELIX 4 AA4 ASP A 69 GLU A 75 1 7
HELIX 5 AA5 SER A 93 LEU A 100 1 8
HELIX 6 AA6 LYS A 134 GLU A 138 5 5
HELIX 7 AA7 SER A 147 VAL A 151 5 5
HELIX 8 AA8 TYR A 160 SER A 166 1 7
HELIX 9 AA9 GLY A 185 GLY A 190 5 6
HELIX 10 AB1 ASN A 191 GLN A 199 1 9
HELIX 11 AB2 PRO A 200 LYS A 203 5 4
HELIX 12 AB3 ASP A 205 LEU A 209 5 5
HELIX 13 AB4 SER A 211 LYS A 222 1 12
HELIX 14 AB5 ASP A 272 THR A 282 1 11
HELIX 15 AB6 TRP A 283 SER A 287 5 5
HELIX 16 AB7 SER A 298 LYS A 305 1 8
HELIX 17 AB8 THR A 307 ILE A 322 1 16
HELIX 18 AB9 THR A 332 ASN A 352 1 21
HELIX 19 AC1 LYS B 18 GLY B 34 1 17
HELIX 20 AC2 TYR B 51 LEU B 58 5 8
HELIX 21 AC3 PRO B 61 LYS B 65 5 5
HELIX 22 AC4 ASP B 69 GLU B 75 1 7
HELIX 23 AC5 SER B 93 LEU B 100 1 8
HELIX 24 AC6 LYS B 134 GLU B 138 5 5
HELIX 25 AC7 SER B 147 SER B 153 5 7
HELIX 26 AC8 TYR B 160 SER B 166 1 7
HELIX 27 AC9 GLY B 185 GLY B 190 5 6
HELIX 28 AD1 ASN B 191 GLN B 199 1 9
HELIX 29 AD2 PRO B 200 LYS B 203 5 4
HELIX 30 AD3 ASP B 205 LEU B 209 5 5
HELIX 31 AD4 SER B 211 LYS B 222 1 12
HELIX 32 AD5 TYR B 252 ASN B 254 5 3
HELIX 33 AD6 ASP B 272 THR B 282 1 11
HELIX 34 AD7 THR B 282 SER B 287 1 6
HELIX 35 AD8 SER B 298 LYS B 305 1 8
HELIX 36 AD9 THR B 307 ILE B 322 1 16
HELIX 37 AE1 THR B 332 ASN B 352 1 21
HELIX 38 AE2 LYS C 18 GLY C 34 1 17
HELIX 39 AE3 TYR C 51 LEU C 58 5 8
HELIX 40 AE4 PRO C 61 LYS C 65 5 5
HELIX 41 AE5 ASP C 69 GLU C 75 1 7
HELIX 42 AE6 SER C 93 LEU C 100 1 8
HELIX 43 AE7 TYR C 160 SER C 166 1 7
HELIX 44 AE8 GLY C 185 GLY C 190 5 6
HELIX 45 AE9 ASN C 191 GLN C 199 1 9
HELIX 46 AF1 PRO C 200 LEU C 209 5 10
HELIX 47 AF2 SER C 211 LYS C 222 1 12
HELIX 48 AF3 ASP C 272 THR C 282 1 11
HELIX 49 AF4 TRP C 283 SER C 287 5 5
HELIX 50 AF5 SER C 298 SER C 304 1 7
HELIX 51 AF6 THR C 307 ILE C 322 1 16
HELIX 52 AF7 THR C 332 LEU C 351 1 20
HELIX 53 AF8 LYS D 18 LYS D 31 1 14
HELIX 54 AF9 TYR D 51 LEU D 58 5 8
HELIX 55 AG1 PRO D 61 LYS D 65 5 5
HELIX 56 AG2 ASP D 69 GLU D 75 1 7
HELIX 57 AG3 SER D 93 LEU D 100 1 8
HELIX 58 AG4 LYS D 134 GLU D 138 5 5
HELIX 59 AG5 SER D 147 VAL D 151 5 5
HELIX 60 AG6 TYR D 160 SER D 166 1 7
HELIX 61 AG7 GLY D 185 GLY D 190 5 6
HELIX 62 AG8 ASN D 191 GLN D 199 1 9
HELIX 63 AG9 PRO D 200 LYS D 203 5 4
HELIX 64 AH1 ASP D 205 LEU D 209 5 5
HELIX 65 AH2 SER D 211 LYS D 222 1 12
HELIX 66 AH3 TYR D 252 ASN D 254 5 3
HELIX 67 AH4 ASP D 272 THR D 282 1 11
HELIX 68 AH5 THR D 282 SER D 287 1 6
HELIX 69 AH6 SER D 298 SER D 304 1 7
HELIX 70 AH7 THR D 307 ILE D 322 1 16
HELIX 71 AH8 THR D 332 ASN D 352 1 21
HELIX 72 AH9 LYS E 18 GLY E 34 1 17
HELIX 73 AI1 TYR E 51 LEU E 58 5 8
HELIX 74 AI2 PRO E 61 LYS E 65 5 5
HELIX 75 AI3 ASP E 69 GLU E 75 1 7
HELIX 76 AI4 SER E 93 LEU E 100 1 8
HELIX 77 AI5 LYS E 134 GLU E 138 5 5
HELIX 78 AI6 SER E 147 VAL E 151 5 5
HELIX 79 AI7 ASN E 159 SER E 166 1 8
HELIX 80 AI8 ASN E 167 GLN E 170 5 4
HELIX 81 AI9 GLY E 185 GLY E 190 5 6
HELIX 82 AJ1 ASN E 191 GLN E 199 1 9
HELIX 83 AJ2 PRO E 200 LYS E 203 5 4
HELIX 84 AJ3 ASP E 205 LEU E 209 5 5
HELIX 85 AJ4 SER E 211 LYS E 222 1 12
HELIX 86 AJ5 ASP E 272 THR E 282 1 11
HELIX 87 AJ6 TRP E 283 SER E 287 5 5
HELIX 88 AJ7 SER E 298 LYS E 305 1 8
HELIX 89 AJ8 THR E 307 ILE E 322 1 16
HELIX 90 AJ9 THR E 332 ASN E 349 1 18
SHEET 1 AA1 6 GLY A 104 CYS A 107 0
SHEET 2 AA1 6 MET A 110 TYR A 112 -1 O TYR A 112 N GLY A 104
SHEET 3 AA1 6 THR A 84 PHE A 86 1 N THR A 84 O TYR A 111
SHEET 4 AA1 6 ILE A 37 CYS A 42 1 N VAL A 40 O LEU A 85
SHEET 5 AA1 6 ILE A 6 VAL A 12 1 N ALA A 10 O ILE A 41
SHEET 6 AA1 6 ILE A 256 PRO A 262 -1 O LEU A 259 N ILE A 9
SHEET 1 AA2 7 TYR A 235 GLU A 239 0
SHEET 2 AA2 7 THR A 242 ALA A 246 -1 O ALA A 246 N TYR A 235
SHEET 3 AA2 7 TYR A 225 SER A 228 1 N TRP A 226 O ILE A 245
SHEET 4 AA2 7 ILE A 176 SER A 179 1 N SER A 177 O ILE A 227
SHEET 5 AA2 7 LEU A 124 VAL A 129 1 N VAL A 127 O ILE A 176
SHEET 6 AA2 7 CYS A 116 ILE A 121 -1 N ILE A 119 O ILE A 126
SHEET 7 AA2 7 GLU A 270 TYR A 271 -1 O GLU A 270 N ASN A 120
SHEET 1 AA3 2 TYR A 142 THR A 143 0
SHEET 2 AA3 2 GLN A 291 PHE A 292 -1 O PHE A 292 N TYR A 142
SHEET 1 AA4 6 GLY B 104 CYS B 107 0
SHEET 2 AA4 6 MET B 110 TYR B 112 -1 O TYR B 112 N GLY B 104
SHEET 3 AA4 6 THR B 84 PHE B 86 1 N THR B 84 O TYR B 111
SHEET 4 AA4 6 ILE B 37 CYS B 42 1 N CYS B 42 O LEU B 85
SHEET 5 AA4 6 ILE B 6 VAL B 12 1 N ALA B 10 O ILE B 41
SHEET 6 AA4 6 ILE B 256 PRO B 262 -1 O LEU B 259 N ILE B 9
SHEET 1 AA5 7 TYR B 235 GLU B 239 0
SHEET 2 AA5 7 THR B 242 ALA B 246 -1 O PHE B 244 N ALA B 237
SHEET 3 AA5 7 TYR B 225 SER B 228 1 N TRP B 226 O ILE B 245
SHEET 4 AA5 7 ILE B 176 SER B 179 1 N SER B 177 O ILE B 227
SHEET 5 AA5 7 LEU B 124 VAL B 129 1 N VAL B 129 O LEU B 178
SHEET 6 AA5 7 CYS B 116 ILE B 121 -1 N ILE B 119 O ILE B 126
SHEET 7 AA5 7 GLU B 270 TYR B 271 -1 O GLU B 270 N ASN B 120
SHEET 1 AA6 2 TYR B 142 THR B 143 0
SHEET 2 AA6 2 GLN B 291 PHE B 292 -1 O PHE B 292 N TYR B 142
SHEET 1 AA7 6 GLY C 104 CYS C 107 0
SHEET 2 AA7 6 MET C 110 TYR C 112 -1 O TYR C 112 N GLY C 104
SHEET 3 AA7 6 THR C 84 PHE C 86 1 N THR C 84 O TYR C 111
SHEET 4 AA7 6 ILE C 37 CYS C 42 1 N VAL C 40 O LEU C 85
SHEET 5 AA7 6 ILE C 6 VAL C 12 1 N HIS C 8 O SER C 38
SHEET 6 AA7 6 ILE C 256 PRO C 262 -1 O LEU C 261 N GLN C 7
SHEET 1 AA8 7 TYR C 235 GLU C 239 0
SHEET 2 AA8 7 THR C 242 ALA C 246 -1 O PHE C 244 N ALA C 237
SHEET 3 AA8 7 TYR C 225 SER C 228 1 N TRP C 226 O ILE C 245
SHEET 4 AA8 7 ILE C 176 SER C 179 1 N SER C 177 O ILE C 227
SHEET 5 AA8 7 LEU C 124 VAL C 129 1 N VAL C 127 O ILE C 176
SHEET 6 AA8 7 CYS C 116 ILE C 121 -1 N ILE C 119 O ILE C 126
SHEET 7 AA8 7 GLU C 270 TYR C 271 -1 O GLU C 270 N ASN C 120
SHEET 1 AA9 2 TYR C 142 THR C 143 0
SHEET 2 AA9 2 GLN C 291 PHE C 292 -1 O PHE C 292 N TYR C 142
SHEET 1 AB1 6 GLY D 104 CYS D 107 0
SHEET 2 AB1 6 MET D 110 TYR D 112 -1 O TYR D 112 N GLY D 104
SHEET 3 AB1 6 THR D 84 PHE D 86 1 N THR D 84 O TYR D 111
SHEET 4 AB1 6 ILE D 37 CYS D 42 1 N VAL D 40 O LEU D 85
SHEET 5 AB1 6 ILE D 6 VAL D 12 1 N HIS D 8 O SER D 38
SHEET 6 AB1 6 ILE D 256 PRO D 262 -1 O LEU D 261 N GLN D 7
SHEET 1 AB2 7 TYR D 235 GLU D 239 0
SHEET 2 AB2 7 THR D 242 ALA D 246 -1 O PHE D 244 N ALA D 237
SHEET 3 AB2 7 TYR D 225 SER D 228 1 N TRP D 226 O ILE D 245
SHEET 4 AB2 7 ILE D 176 LEU D 178 1 N SER D 177 O TYR D 225
SHEET 5 AB2 7 LEU D 124 VAL D 129 1 N VAL D 127 O LEU D 178
SHEET 6 AB2 7 CYS D 116 ILE D 121 -1 N ILE D 121 O LEU D 124
SHEET 7 AB2 7 GLU D 270 TYR D 271 -1 O GLU D 270 N ASN D 120
SHEET 1 AB3 2 TYR D 142 THR D 143 0
SHEET 2 AB3 2 GLN D 291 PHE D 292 -1 O PHE D 292 N TYR D 142
SHEET 1 AB4 6 GLY E 104 CYS E 107 0
SHEET 2 AB4 6 MET E 110 TYR E 112 -1 O TYR E 112 N GLY E 104
SHEET 3 AB4 6 THR E 84 PHE E 86 1 N PHE E 86 O TYR E 111
SHEET 4 AB4 6 ILE E 37 CYS E 42 1 N VAL E 40 O LEU E 85
SHEET 5 AB4 6 ILE E 6 VAL E 12 1 N ALA E 10 O ILE E 41
SHEET 6 AB4 6 ILE E 256 PRO E 262 -1 O LEU E 261 N GLN E 7
SHEET 1 AB5 7 TYR E 235 GLU E 239 0
SHEET 2 AB5 7 THR E 242 ALA E 246 -1 O PHE E 244 N ALA E 237
SHEET 3 AB5 7 TYR E 225 SER E 228 1 N TRP E 226 O HIS E 243
SHEET 4 AB5 7 ILE E 176 SER E 179 1 N SER E 177 O ILE E 227
SHEET 5 AB5 7 LEU E 124 VAL E 129 1 N VAL E 127 O LEU E 178
SHEET 6 AB5 7 CYS E 116 ILE E 121 -1 N ILE E 119 O ILE E 126
SHEET 7 AB5 7 GLU E 270 TYR E 271 -1 O GLU E 270 N ASN E 120
SHEET 1 AB6 2 TYR E 142 THR E 143 0
SHEET 2 AB6 2 GLN E 291 PHE E 292 -1 O PHE E 292 N TYR E 142
LINK O3' A V 500 P2 A2P V 501 1555 1555 1.61
LINK O3' A2P V 501 P C V 502 1555 1555 1.61
LINK O3' A W 500 P2 A2P W 501 1555 1555 1.61
LINK O3' A2P W 501 P C W 502 1555 1555 1.61
LINK O3' A X 500 P2 A2P X 501 1555 1555 1.61
LINK O3' A2P X 501 P C X 502 1555 1555 1.61
LINK O3' A Y 500 P2 A2P Y 501 1555 1555 1.61
LINK O3' A2P Y 501 P C Y 502 1555 1555 1.61
LINK O3' A Z 500 P2 A2P Z 501 1555 1555 1.61
LINK O3' A2P Z 501 P C Z 502 1555 1555 1.61
LINK OD2 ASP A 45 MN MN A 401 1555 1555 2.14
LINK OD1 ASN A 90 MN MN A 401 1555 1555 2.12
LINK NE2 HIS A 180 MN MN A 401 1555 1555 2.20
LINK ND1 HIS A 230 MN MN A 401 1555 1555 2.41
LINK MN MN A 401 O1P A2P V 501 1555 1555 2.22
LINK MN MN A 401 O HOH V 701 1555 1555 2.41
LINK OD2 ASP B 45 MN MN B 401 1555 1555 2.18
LINK OD1 ASN B 90 MN MN B 401 1555 1555 2.26
LINK NE2 HIS B 180 MN MN B 401 1555 1555 2.27
LINK ND1 HIS B 230 MN MN B 401 1555 1555 2.12
LINK MN MN B 401 O2P A2P W 501 1555 1555 2.07
LINK MN MN B 401 O HOH W 701 1555 1555 2.78
LINK OD2 ASP C 45 MN MN C 401 1555 1555 2.17
LINK OD1 ASN C 90 MN MN C 401 1555 1555 2.08
LINK NE2 HIS C 180 MN MN C 401 1555 1555 2.23
LINK ND1 HIS C 230 MN MN C 401 1555 1555 2.35
LINK MN MN C 401 O HOH C 725 1555 1555 2.04
LINK MN MN C 401 O2P A2P X 501 1555 1555 2.16
LINK OD2 ASP D 45 MN MN D 401 1555 1555 2.18
LINK OD1 ASN D 90 MN MN D 401 1555 1555 2.07
LINK NE2 HIS D 180 MN MN D 401 1555 1555 2.25
LINK ND1 HIS D 230 MN MN D 401 1555 1555 2.54
LINK MN MN D 401 O HOH D 691 1555 1555 1.97
LINK MN MN D 401 O1P A2P Y 501 1555 1555 2.17
LINK OD2 ASP E 45 MN MN E 401 1555 1555 2.18
LINK OD1 ASN E 90 MN MN E 401 1555 1555 2.17
LINK NE2 HIS E 180 MN MN E 401 1555 1555 2.24
LINK ND1 HIS E 230 MN MN E 401 1555 1555 2.35
LINK MN MN E 401 O2P A2P Z 501 1555 1555 2.13
LINK MN MN E 401 O HOH Z 703 1555 1555 2.21
CISPEP 1 TYR A 144 PRO A 145 0 1.07
CISPEP 2 PHE A 292 PRO A 293 0 -2.83
CISPEP 3 TYR B 144 PRO B 145 0 3.51
CISPEP 4 PHE B 292 PRO B 293 0 -5.64
CISPEP 5 TYR C 144 PRO C 145 0 3.58
CISPEP 6 PHE C 292 PRO C 293 0 -0.14
CISPEP 7 TYR D 144 PRO D 145 0 3.89
CISPEP 8 PHE D 292 PRO D 293 0 -6.58
CISPEP 9 TYR E 144 PRO E 145 0 -0.79
CISPEP 10 PHE E 292 PRO E 293 0 -5.17
SITE 1 AC1 6 ASP A 45 ASN A 90 HIS A 180 HIS A 230
SITE 2 AC1 6 A2P V 501 HOH V 701
SITE 1 AC2 7 ARG A 50 ASN A 95 HIS A 99 PRO A 146
SITE 2 AC2 7 HOH A 502 HOH A 508 HOH A 678
SITE 1 AC3 5 GLN A 163 SER A 298 ILE A 299 SER A 300
SITE 2 AC3 5 HOH A 622
SITE 1 AC4 6 ASP B 45 ASN B 90 HIS B 180 HIS B 230
SITE 2 AC4 6 A2P W 501 HOH W 701
SITE 1 AC5 5 LYS A 320 TYR B 51 TYR B 74 HOH B 600
SITE 2 AC5 5 HOH B 656
SITE 1 AC6 7 ARG B 50 ASN B 95 HIS B 99 HOH B 536
SITE 2 AC6 7 HOH B 603 HOH B 619 HOH B 631
SITE 1 AC7 6 ASP C 45 ASN C 90 HIS C 180 HIS C 230
SITE 2 AC7 6 HOH C 725 A2P X 501
SITE 1 AC8 3 THR B 307 LYS B 308 LYS C 215
SITE 1 AC9 6 ARG C 50 ASN C 95 HIS C 99 HOH C 501
SITE 2 AC9 6 HOH C 598 HOH C 689
SITE 1 AD1 4 LYS C 18 TYR C 64 HOH C 710 A2P X 501
SITE 1 AD2 6 ASP D 45 ASN D 90 HIS D 180 HIS D 230
SITE 2 AD2 6 HOH D 691 A2P Y 501
SITE 1 AD3 8 ARG D 50 ASN D 95 HIS D 99 PRO D 146
SITE 2 AD3 8 HOH D 509 HOH D 522 HOH D 583 HOH D 677
SITE 1 AD4 6 ASP E 45 ASN E 90 HIS E 180 HIS E 230
SITE 2 AD4 6 A2P Z 501 HOH Z 703
SITE 1 AD5 6 ARG E 50 ASN E 95 HIS E 99 HOH E 555
SITE 2 AD5 6 HOH E 584 HOH E 615
CRYST1 73.021 141.936 212.942 90.00 90.00 90.00 P 21 21 21 20
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 0.013695 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007045 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004696 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
