HEADER LIGASE 21-MAY-17 5VVW
TITLE STRUCTURE OF MURC FROM PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: UNP RESIDUES 16-322;
COMPND 5 SYNONYM: UDP-N-ACETYLMURAMOYL-L-ALANINE SYNTHETASE;
COMPND 6 EC: 6.3.2.8;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 / DSM
SOURCE 3 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
SOURCE 4 ORGANISM_TAXID: 208964;
SOURCE 5 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 6 / 1C / PRS 101 / PAO1;
SOURCE 7 GENE: MURC, PA4411;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS MURC, PSEUDOMONAS AERUGINOSA, SSGCID, BERYLLIUM, STRUCTURAL GENOMICS,
KEYWDS 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 04-OCT-23 5VVW 1 REMARK
REVDAT 1 31-MAY-17 5VVW 0
JRNL AUTH P.S.HORANYI,S.J.MAYCLIN,
JRNL AUTH 2 SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 3 (SSGCID)
JRNL TITL STRUCTURE OF MURC FROM PSEUDOMONAS AERUGINOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2744: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 136319
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.470
REMARK 3 FREE R VALUE TEST SET COUNT : 2006
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 29.8146 - 5.5323 0.98 9589 143 0.1679 0.1466
REMARK 3 2 5.5323 - 4.3957 1.00 9695 145 0.1479 0.1475
REMARK 3 3 4.3957 - 3.8414 1.00 9641 145 0.1509 0.1730
REMARK 3 4 3.8414 - 3.4907 1.00 9608 143 0.1768 0.1878
REMARK 3 5 3.4907 - 3.2409 1.00 9575 142 0.1909 0.2020
REMARK 3 6 3.2409 - 3.0500 1.00 9614 144 0.2040 0.2574
REMARK 3 7 3.0500 - 2.8974 1.00 9619 143 0.2036 0.2259
REMARK 3 8 2.8974 - 2.7713 1.00 9577 144 0.2055 0.2365
REMARK 3 9 2.7713 - 2.6647 1.00 9569 149 0.2169 0.2728
REMARK 3 10 2.6647 - 2.5728 1.00 9610 142 0.2247 0.2380
REMARK 3 11 2.5728 - 2.4924 1.00 9522 136 0.2377 0.2471
REMARK 3 12 2.4924 - 2.4212 1.00 9582 140 0.2447 0.3109
REMARK 3 13 2.4212 - 2.3575 1.00 9557 145 0.2576 0.2593
REMARK 3 14 2.3575 - 2.3000 1.00 9555 145 0.2813 0.3241
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.008 18473
REMARK 3 ANGLE : 0.916 25186
REMARK 3 CHIRALITY : 0.056 2990
REMARK 3 PLANARITY : 0.006 3324
REMARK 3 DIHEDRAL : 21.346 6553
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9837 -3.0553 -37.7030
REMARK 3 T TENSOR
REMARK 3 T11: 0.2044 T22: 0.2452
REMARK 3 T33: 0.2170 T12: -0.0178
REMARK 3 T13: -0.0041 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.2001 L22: 0.2441
REMARK 3 L33: 0.1871 L12: -0.0725
REMARK 3 L13: -0.0065 L23: 0.0493
REMARK 3 S TENSOR
REMARK 3 S11: 0.0266 S12: 0.0304 S13: -0.0118
REMARK 3 S21: -0.0105 S22: -0.0119 S23: -0.0498
REMARK 3 S31: 0.0143 S32: 0.0286 S33: -0.0155
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 5VVW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1000228053.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 136319
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.812
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4HV4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS A2: 60MM DIVALENTS, (0.3M
REMARK 280 MAGNESIUM CHLORIDE HEXAHYDRATE; 0.3M CALCIUM CHLORIDE DIHYDRATE),
REMARK 280 100MM IMIDAZOLE; MES MONOHYDRATE (ACID), 20% V/V ETHYLENE
REMARK 280 GLYCOL; 10 % W/V PEG 8000., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 142.41000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.70000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 142.41000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 54.70000
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
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, G, H
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, E
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 MET A 8
REMARK 465 ALA A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 VAL A 320
REMARK 465 GLY A 321
REMARK 465 ARG A 322
REMARK 465 MET B 8
REMARK 465 ALA B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 VAL B 320
REMARK 465 GLY B 321
REMARK 465 ARG B 322
REMARK 465 MET C 8
REMARK 465 ALA C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 HIS C 13
REMARK 465 HIS C 14
REMARK 465 VAL C 320
REMARK 465 GLY C 321
REMARK 465 ARG C 322
REMARK 465 MET D 8
REMARK 465 ALA D 9
REMARK 465 HIS D 10
REMARK 465 HIS D 11
REMARK 465 HIS D 12
REMARK 465 HIS D 13
REMARK 465 HIS D 14
REMARK 465 VAL D 320
REMARK 465 GLY D 321
REMARK 465 ARG D 322
REMARK 465 MET E 8
REMARK 465 ALA E 9
REMARK 465 HIS E 10
REMARK 465 HIS E 11
REMARK 465 HIS E 12
REMARK 465 HIS E 13
REMARK 465 HIS E 14
REMARK 465 GLY E 319
REMARK 465 VAL E 320
REMARK 465 GLY E 321
REMARK 465 ARG E 322
REMARK 465 MET F 8
REMARK 465 ALA F 9
REMARK 465 HIS F 10
REMARK 465 HIS F 11
REMARK 465 HIS F 12
REMARK 465 HIS F 13
REMARK 465 HIS F 14
REMARK 465 VAL F 320
REMARK 465 GLY F 321
REMARK 465 ARG F 322
REMARK 465 MET G 8
REMARK 465 ALA G 9
REMARK 465 HIS G 10
REMARK 465 HIS G 11
REMARK 465 HIS G 12
REMARK 465 HIS G 13
REMARK 465 HIS G 14
REMARK 465 VAL G 320
REMARK 465 GLY G 321
REMARK 465 ARG G 322
REMARK 465 MET H 8
REMARK 465 ALA H 9
REMARK 465 HIS H 10
REMARK 465 HIS H 11
REMARK 465 HIS H 12
REMARK 465 HIS H 13
REMARK 465 HIS H 14
REMARK 465 VAL H 320
REMARK 465 GLY H 321
REMARK 465 ARG H 322
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 HIS A 15 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 GLN A 68 CG CD OE1 NE2
REMARK 470 SER A 82 OG
REMARK 470 ILE A 84 CG1 CG2 CD1
REMARK 470 ARG A 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 96 CG CD OE1 OE2
REMARK 470 ARG A 151 CG CD NE CZ NH1 NH2
REMARK 470 THR A 157 OG1 CG2
REMARK 470 LYS A 208 CG CD CE NZ
REMARK 470 GLU A 250 CG CD OE1 OE2
REMARK 470 MET A 264 CG SD CE
REMARK 470 GLN A 318 CG CD OE1 NE2
REMARK 470 HIS B 15 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 GLU B 54 CG CD OE1 OE2
REMARK 470 GLU B 70 CG CD OE1 OE2
REMARK 470 SER B 82 OG
REMARK 470 ILE B 84 CG1 CG2 CD1
REMARK 470 ASN B 85 CG OD1 ND2
REMARK 470 ARG B 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 96 CG CD OE1 OE2
REMARK 470 ASN B 158 CG OD1 ND2
REMARK 470 LYS B 208 CG CD CE NZ
REMARK 470 GLU B 250 CG CD OE1 OE2
REMARK 470 GLU B 262 CG CD OE1 OE2
REMARK 470 MET B 264 CG SD CE
REMARK 470 GLN B 318 CG CD OE1 NE2
REMARK 470 HIS C 15 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 48 CG CD CE NZ
REMARK 470 GLU C 70 CG CD OE1 OE2
REMARK 470 SER C 82 OG
REMARK 470 ILE C 84 CG1 CG2 CD1
REMARK 470 ARG C 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 96 CG CD OE1 OE2
REMARK 470 ARG C 151 CG CD NE CZ NH1 NH2
REMARK 470 THR C 157 OG1 CG2
REMARK 470 LYS C 208 CG CD CE NZ
REMARK 470 GLU C 250 CG CD OE1 OE2
REMARK 470 MET C 264 CG SD CE
REMARK 470 GLU C 274 CG CD OE1 OE2
REMARK 470 GLN C 318 CG CD OE1 NE2
REMARK 470 HIS D 15 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 GLN D 68 CG CD OE1 NE2
REMARK 470 GLU D 70 CG CD OE1 OE2
REMARK 470 SER D 82 OG
REMARK 470 ASN D 85 CG OD1 ND2
REMARK 470 ARG D 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 96 CG CD OE1 OE2
REMARK 470 ARG D 151 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 208 CG CD CE NZ
REMARK 470 GLU D 250 CG CD OE1 OE2
REMARK 470 MET D 264 CG SD CE
REMARK 470 GLN D 318 CG CD OE1 NE2
REMARK 470 HIS E 15 CG ND1 CD2 CE1 NE2
REMARK 470 LYS E 48 CG CD CE NZ
REMARK 470 GLU E 54 CG CD OE1 OE2
REMARK 470 SER E 82 OG
REMARK 470 ARG E 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 96 CG CD OE1 OE2
REMARK 470 ARG E 151 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 208 CG CD CE NZ
REMARK 470 GLU E 250 CG CD OE1 OE2
REMARK 470 GLU E 262 CG CD OE1 OE2
REMARK 470 MET E 264 CG SD CE
REMARK 470 HIS E 288 CG ND1 CD2 CE1 NE2
REMARK 470 GLN E 318 CG CD OE1 NE2
REMARK 470 HIS F 15 CG ND1 CD2 CE1 NE2
REMARK 470 SER F 82 OG
REMARK 470 ASN F 85 CG OD1 ND2
REMARK 470 ARG F 86 CG CD NE CZ NH1 NH2
REMARK 470 ASN F 158 CG OD1 ND2
REMARK 470 LYS F 208 CG CD CE NZ
REMARK 470 GLU F 250 CG CD OE1 OE2
REMARK 470 GLU F 262 CG CD OE1 OE2
REMARK 470 MET F 264 CG SD CE
REMARK 470 GLU F 274 CG CD OE1 OE2
REMARK 470 GLN F 318 CG CD OE1 NE2
REMARK 470 HIS G 15 CG ND1 CD2 CE1 NE2
REMARK 470 LYS G 48 CG CD CE NZ
REMARK 470 GLN G 68 CG CD OE1 NE2
REMARK 470 GLU G 70 CG CD OE1 OE2
REMARK 470 SER G 82 OG
REMARK 470 ASN G 85 CG OD1 ND2
REMARK 470 ARG G 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 96 CG CD OE1 OE2
REMARK 470 ASN G 158 CG OD1 ND2
REMARK 470 LYS G 208 CG CD CE NZ
REMARK 470 GLU G 250 CG CD OE1 OE2
REMARK 470 MET G 264 CG SD CE
REMARK 470 GLU G 274 CG CD OE1 OE2
REMARK 470 GLN G 318 CG CD OE1 NE2
REMARK 470 HIS H 15 CG ND1 CD2 CE1 NE2
REMARK 470 LYS H 48 CG CD CE NZ
REMARK 470 GLN H 68 CG CD OE1 NE2
REMARK 470 SER H 82 OG
REMARK 470 ARG H 86 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 96 CG CD OE1 OE2
REMARK 470 ARG H 151 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 208 CG CD CE NZ
REMARK 470 GLU H 250 CG CD OE1 OE2
REMARK 470 MET H 264 CG SD CE
REMARK 470 GLU H 274 CG CD OE1 OE2
REMARK 470 GLN H 318 CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU H 57 O HOH H 501 2.14
REMARK 500 OG SER C 50 O HOH C 501 2.15
REMARK 500 NZ LYS C 126 O HOH C 502 2.17
REMARK 500 O LYS F 48 O HOH F 401 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU C 248 CA - CB - CG ANGL. DEV. = -14.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 SER A 82 -108.26 -145.02
REMARK 500 ASN A 85 81.70 -56.48
REMARK 500 ASP A 143 61.89 31.30
REMARK 500 ALA A 240 56.95 -96.47
REMARK 500 ASN A 283 35.60 -89.96
REMARK 500 SER B 82 -101.97 -140.36
REMARK 500 ILE B 84 76.56 -69.32
REMARK 500 ASN B 85 92.40 -64.97
REMARK 500 ASP B 143 54.62 34.77
REMARK 500 THR B 157 -64.84 58.04
REMARK 500 ALA B 240 52.24 -90.68
REMARK 500 ASN B 283 46.17 -103.08
REMARK 500 GLN B 318 -72.20 -76.11
REMARK 500 ARG C 16 -28.05 -147.43
REMARK 500 SER C 82 -90.36 -144.31
REMARK 500 ASN C 85 87.26 -56.51
REMARK 500 ASP C 143 55.89 33.85
REMARK 500 THR C 157 -65.67 65.81
REMARK 500 ALA C 240 55.69 -94.43
REMARK 500 GLU C 262 83.83 -161.89
REMARK 500 SER D 82 -107.17 -112.81
REMARK 500 ILE D 84 98.21 -66.13
REMARK 500 ASP D 143 54.38 37.19
REMARK 500 THR D 157 -59.27 61.19
REMARK 500 ASN D 190 158.51 176.93
REMARK 500 ALA D 240 52.18 -96.29
REMARK 500 GLN D 318 -77.25 -75.13
REMARK 500 ARG E 16 -24.72 -145.80
REMARK 500 ARG E 16 -24.63 -145.76
REMARK 500 SER E 82 -133.92 -98.34
REMARK 500 ARG E 86 -25.31 62.20
REMARK 500 ASP E 143 55.45 37.83
REMARK 500 THR E 157 -46.88 59.83
REMARK 500 GLN E 182 70.54 -118.30
REMARK 500 ALA E 240 52.24 -98.83
REMARK 500 ARG F 16 -10.99 -145.83
REMARK 500 ASP F 143 58.93 35.47
REMARK 500 GLU F 262 80.37 -153.65
REMARK 500 GLN F 318 -67.54 -90.12
REMARK 500 SER G 82 -98.07 -93.96
REMARK 500 ASP G 143 54.04 38.12
REMARK 500 ALA G 240 47.06 -88.07
REMARK 500 SER H 82 -106.28 -150.57
REMARK 500 ARG H 86 -55.27 61.04
REMARK 500 ASP H 143 56.86 38.86
REMARK 500 ALA H 240 52.57 -96.20
REMARK 500 GLU H 262 89.16 -150.61
REMARK 500 ASN H 283 40.90 -98.37
REMARK 500 GLN H 318 -78.54 -73.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH F 519 DISTANCE = 6.18 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO H 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PSAEA.00137.B.B5 RELATED DB: TARGETTRACK
DBREF 5VVW A 16 322 UNP Q9HW02 MURC_PSEAE 16 322
DBREF 5VVW B 16 322 UNP Q9HW02 MURC_PSEAE 16 322
DBREF 5VVW C 16 322 UNP Q9HW02 MURC_PSEAE 16 322
DBREF 5VVW D 16 322 UNP Q9HW02 MURC_PSEAE 16 322
DBREF 5VVW E 16 322 UNP Q9HW02 MURC_PSEAE 16 322
DBREF 5VVW F 16 322 UNP Q9HW02 MURC_PSEAE 16 322
DBREF 5VVW G 16 322 UNP Q9HW02 MURC_PSEAE 16 322
DBREF 5VVW H 16 322 UNP Q9HW02 MURC_PSEAE 16 322
SEQADV 5VVW MET A 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA A 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS A 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS A 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS A 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS A 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS A 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS A 15 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW MET B 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA B 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS B 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS B 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS B 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS B 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS B 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS B 15 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW MET C 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA C 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS C 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS C 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS C 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS C 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS C 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS C 15 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW MET D 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA D 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS D 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS D 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS D 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS D 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS D 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS D 15 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW MET E 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA E 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS E 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS E 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS E 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS E 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS E 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS E 15 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW MET F 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA F 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS F 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS F 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS F 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS F 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS F 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS F 15 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW MET G 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA G 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS G 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS G 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS G 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS G 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS G 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS G 15 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW MET H 8 UNP Q9HW02 INITIATING METHIONINE
SEQADV 5VVW ALA H 9 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS H 10 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS H 11 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS H 12 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS H 13 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS H 14 UNP Q9HW02 EXPRESSION TAG
SEQADV 5VVW HIS H 15 UNP Q9HW02 EXPRESSION TAG
SEQRES 1 A 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 A 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 A 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 A 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 A 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 A 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 A 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 A 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 A 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 A 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 A 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 A 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 A 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 A 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 A 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 A 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 A 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 A 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 A 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 A 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 A 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 A 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 A 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 A 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 A 315 VAL GLY ARG
SEQRES 1 B 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 B 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 B 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 B 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 B 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 B 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 B 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 B 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 B 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 B 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 B 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 B 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 B 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 B 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 B 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 B 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 B 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 B 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 B 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 B 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 B 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 B 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 B 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 B 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 B 315 VAL GLY ARG
SEQRES 1 C 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 C 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 C 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 C 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 C 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 C 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 C 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 C 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 C 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 C 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 C 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 C 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 C 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 C 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 C 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 C 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 C 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 C 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 C 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 C 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 C 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 C 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 C 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 C 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 C 315 VAL GLY ARG
SEQRES 1 D 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 D 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 D 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 D 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 D 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 D 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 D 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 D 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 D 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 D 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 D 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 D 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 D 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 D 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 D 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 D 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 D 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 D 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 D 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 D 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 D 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 D 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 D 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 D 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 D 315 VAL GLY ARG
SEQRES 1 E 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 E 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 E 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 E 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 E 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 E 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 E 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 E 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 E 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 E 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 E 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 E 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 E 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 E 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 E 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 E 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 E 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 E 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 E 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 E 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 E 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 E 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 E 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 E 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 E 315 VAL GLY ARG
SEQRES 1 F 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 F 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 F 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 F 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 F 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 F 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 F 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 F 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 F 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 F 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 F 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 F 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 F 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 F 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 F 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 F 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 F 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 F 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 F 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 F 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 F 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 F 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 F 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 F 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 F 315 VAL GLY ARG
SEQRES 1 G 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 G 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 G 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 G 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 G 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 G 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 G 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 G 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 G 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 G 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 G 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 G 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 G 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 G 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 G 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 G 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 G 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 G 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 G 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 G 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 G 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 G 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 G 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 G 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 G 315 VAL GLY ARG
SEQRES 1 H 315 MET ALA HIS HIS HIS HIS HIS HIS ARG ARG ILE HIS PHE
SEQRES 2 H 315 VAL GLY ILE GLY GLY ALA GLY MET CYS GLY ILE ALA GLU
SEQRES 3 H 315 VAL LEU LEU ASN LEU GLY TYR GLU VAL SER GLY SER ASP
SEQRES 4 H 315 LEU LYS ALA SER ALA VAL THR GLU ARG LEU GLU LYS PHE
SEQRES 5 H 315 GLY ALA GLN ILE PHE ILE GLY HIS GLN ALA GLU ASN ALA
SEQRES 6 H 315 ASP GLY ALA ASP VAL LEU VAL VAL SER SER ALA ILE ASN
SEQRES 7 H 315 ARG ALA ASN PRO GLU VAL ALA SER ALA LEU GLU ARG ARG
SEQRES 8 H 315 ILE PRO VAL VAL PRO ARG ALA GLU MET LEU ALA GLU LEU
SEQRES 9 H 315 MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR HIS
SEQRES 10 H 315 GLY LYS THR THR THR THR SER LEU ILE ALA SER VAL PHE
SEQRES 11 H 315 ALA ALA GLY GLY LEU ASP PRO THR PHE VAL ILE GLY GLY
SEQRES 12 H 315 ARG LEU ASN ALA ALA GLY THR ASN ALA GLN LEU GLY ALA
SEQRES 13 H 315 SER ARG TYR LEU VAL ALA GLU ALA ASP GLU SER ASP ALA
SEQRES 14 H 315 SER PHE LEU HIS LEU GLN PRO MET VAL ALA VAL VAL THR
SEQRES 15 H 315 ASN ILE ASP ALA ASP HIS MET ALA THR TYR GLY GLY ASP
SEQRES 16 H 315 PHE ASN LYS LEU LYS LYS THR PHE VAL GLU PHE LEU HIS
SEQRES 17 H 315 ASN LEU PRO PHE TYR GLY LEU ALA VAL MET CYS VAL ASP
SEQRES 18 H 315 ASP PRO VAL VAL ARG GLU ILE LEU PRO GLN ILE ALA ARG
SEQRES 19 H 315 PRO THR VAL THR TYR GLY LEU SER GLU ASP ALA ASP VAL
SEQRES 20 H 315 ARG ALA ILE ASN ILE ARG GLN GLU GLY MET ARG THR TRP
SEQRES 21 H 315 PHE THR VAL LEU ARG PRO GLU ARG GLU PRO LEU ASP VAL
SEQRES 22 H 315 SER VAL ASN MET PRO GLY LEU HIS ASN VAL LEU ASN SER
SEQRES 23 H 315 LEU ALA THR ILE VAL ILE ALA THR ASP GLU GLY ILE SER
SEQRES 24 H 315 ASP GLU ALA ILE VAL GLN GLY LEU SER GLY PHE GLN GLY
SEQRES 25 H 315 VAL GLY ARG
HET EDO A 401 4
HET EDO B 401 4
HET EDO C 401 4
HET EDO G 401 4
HET EDO G 402 4
HET EDO G 403 4
HET EDO H 401 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 EDO 7(C2 H6 O2)
FORMUL 16 HOH *877(H2 O)
HELIX 1 AA1 MET A 28 LEU A 38 1 11
HELIX 2 AA2 SER A 50 PHE A 59 1 10
HELIX 3 AA3 GLN A 68 ASP A 73 5 6
HELIX 4 AA4 ASN A 88 ARG A 97 1 10
HELIX 5 AA5 ARG A 104 LEU A 111 1 8
HELIX 6 AA6 MET A 112 ARG A 115 5 4
HELIX 7 AA7 GLY A 125 GLY A 140 1 16
HELIX 8 AA8 SER A 177 LEU A 181 5 5
HELIX 9 AA9 HIS A 195 GLY A 200 5 6
HELIX 10 AB1 ASP A 202 HIS A 215 1 14
HELIX 11 AB2 ASP A 229 LEU A 236 1 8
HELIX 12 AB3 PRO A 237 ILE A 239 5 3
HELIX 13 AB4 GLY A 286 GLY A 304 1 19
HELIX 14 AB5 SER A 306 PHE A 317 1 12
HELIX 15 AB6 MET B 28 LEU B 38 1 11
HELIX 16 AB7 SER B 50 PHE B 59 1 10
HELIX 17 AB8 GLN B 68 ASP B 73 5 6
HELIX 18 AB9 ASN B 88 ARG B 97 1 10
HELIX 19 AC1 ARG B 104 LEU B 111 1 8
HELIX 20 AC2 MET B 112 ARG B 115 5 4
HELIX 21 AC3 GLY B 125 GLY B 140 1 16
HELIX 22 AC4 SER B 177 LEU B 181 5 5
HELIX 23 AC5 HIS B 195 GLY B 200 5 6
HELIX 24 AC6 ASP B 202 ASN B 216 1 15
HELIX 25 AC7 ASP B 229 LEU B 236 1 8
HELIX 26 AC8 PRO B 237 ILE B 239 5 3
HELIX 27 AC9 GLY B 286 GLY B 304 1 19
HELIX 28 AD1 SER B 306 PHE B 317 1 12
HELIX 29 AD2 GLY C 27 LEU C 38 1 12
HELIX 30 AD3 SER C 50 PHE C 59 1 10
HELIX 31 AD4 GLN C 68 ASP C 73 5 6
HELIX 32 AD5 ASN C 88 ARG C 97 1 10
HELIX 33 AD6 ARG C 104 LEU C 111 1 8
HELIX 34 AD7 MET C 112 ARG C 115 5 4
HELIX 35 AD8 GLY C 125 GLY C 140 1 16
HELIX 36 AD9 SER C 177 LEU C 181 5 5
HELIX 37 AE1 ASP C 202 ASN C 216 1 15
HELIX 38 AE2 ASP C 229 LEU C 236 1 8
HELIX 39 AE3 PRO C 237 ILE C 239 5 3
HELIX 40 AE4 GLY C 286 GLY C 304 1 19
HELIX 41 AE5 SER C 306 GLY C 316 1 11
HELIX 42 AE6 MET D 28 LEU D 38 1 11
HELIX 43 AE7 SER D 50 PHE D 59 1 10
HELIX 44 AE8 GLN D 68 ASP D 73 5 6
HELIX 45 AE9 ASN D 88 ARG D 97 1 10
HELIX 46 AF1 ARG D 104 LEU D 111 1 8
HELIX 47 AF2 MET D 112 ARG D 115 5 4
HELIX 48 AF3 GLY D 125 GLY D 140 1 16
HELIX 49 AF4 SER D 177 LEU D 181 5 5
HELIX 50 AF5 HIS D 195 GLY D 200 5 6
HELIX 51 AF6 ASP D 202 HIS D 215 1 14
HELIX 52 AF7 ASP D 229 LEU D 236 1 8
HELIX 53 AF8 PRO D 237 ILE D 239 5 3
HELIX 54 AF9 GLY D 286 GLY D 304 1 19
HELIX 55 AG1 SER D 306 PHE D 317 1 12
HELIX 56 AG2 GLY E 27 LEU E 38 1 12
HELIX 57 AG3 SER E 50 PHE E 59 1 10
HELIX 58 AG4 GLN E 68 ASP E 73 5 6
HELIX 59 AG5 ASN E 88 ARG E 97 1 10
HELIX 60 AG6 ARG E 104 LEU E 111 1 8
HELIX 61 AG7 MET E 112 ARG E 115 5 4
HELIX 62 AG8 GLY E 125 GLY E 140 1 16
HELIX 63 AG9 SER E 177 LEU E 181 5 5
HELIX 64 AH1 HIS E 195 GLY E 200 5 6
HELIX 65 AH2 ASP E 202 HIS E 215 1 14
HELIX 66 AH3 ASP E 229 LEU E 236 1 8
HELIX 67 AH4 PRO E 237 ILE E 239 5 3
HELIX 68 AH5 GLY E 286 GLY E 304 1 19
HELIX 69 AH6 SER E 306 PHE E 317 1 12
HELIX 70 AH7 GLY F 27 LEU F 38 1 12
HELIX 71 AH8 SER F 50 PHE F 59 1 10
HELIX 72 AH9 GLN F 68 ASP F 73 5 6
HELIX 73 AI1 ASN F 88 ARG F 97 1 10
HELIX 74 AI2 ARG F 104 LEU F 111 1 8
HELIX 75 AI3 MET F 112 ARG F 115 5 4
HELIX 76 AI4 GLY F 125 GLY F 140 1 16
HELIX 77 AI5 SER F 177 LEU F 181 5 5
HELIX 78 AI6 HIS F 195 GLY F 200 5 6
HELIX 79 AI7 ASP F 202 ASN F 216 1 15
HELIX 80 AI8 ASP F 229 LEU F 236 1 8
HELIX 81 AI9 PRO F 237 ILE F 239 5 3
HELIX 82 AJ1 GLY F 286 GLY F 304 1 19
HELIX 83 AJ2 SER F 306 PHE F 317 1 12
HELIX 84 AJ3 GLY G 25 LEU G 38 1 14
HELIX 85 AJ4 SER G 50 PHE G 59 1 10
HELIX 86 AJ5 GLN G 68 ASP G 73 5 6
HELIX 87 AJ6 ASN G 88 ARG G 97 1 10
HELIX 88 AJ7 ARG G 104 LEU G 111 1 8
HELIX 89 AJ8 MET G 112 ARG G 115 5 4
HELIX 90 AJ9 GLY G 125 GLY G 140 1 16
HELIX 91 AK1 SER G 177 LEU G 181 5 5
HELIX 92 AK2 HIS G 195 GLY G 200 5 6
HELIX 93 AK3 ASP G 202 ASN G 216 1 15
HELIX 94 AK4 ASP G 229 LEU G 236 1 8
HELIX 95 AK5 PRO G 237 ILE G 239 5 3
HELIX 96 AK6 GLY G 286 GLY G 304 1 19
HELIX 97 AK7 SER G 306 PHE G 317 1 12
HELIX 98 AK8 GLY H 27 LEU H 38 1 12
HELIX 99 AK9 SER H 50 PHE H 59 1 10
HELIX 100 AL1 GLN H 68 ASP H 73 5 6
HELIX 101 AL2 ASN H 88 ARG H 97 1 10
HELIX 102 AL3 ARG H 104 LEU H 111 1 8
HELIX 103 AL4 MET H 112 ARG H 115 5 4
HELIX 104 AL5 GLY H 125 GLY H 140 1 16
HELIX 105 AL6 SER H 177 LEU H 181 5 5
HELIX 106 AL7 HIS H 195 GLY H 200 5 6
HELIX 107 AL8 ASP H 202 HIS H 215 1 14
HELIX 108 AL9 ASP H 229 LEU H 236 1 8
HELIX 109 AM1 PRO H 237 ILE H 239 5 3
HELIX 110 AM2 GLY H 286 GLY H 304 1 19
HELIX 111 AM3 SER H 306 GLY H 316 1 11
SHEET 1 AA1 5 GLN A 62 ILE A 65 0
SHEET 2 AA1 5 GLU A 41 ASP A 46 1 N GLY A 44 O PHE A 64
SHEET 3 AA1 5 ARG A 17 VAL A 21 1 N ILE A 18 O SER A 43
SHEET 4 AA1 5 VAL A 77 VAL A 80 1 O VAL A 79 N VAL A 21
SHEET 5 AA1 5 VAL A 101 PRO A 103 1 O VAL A 102 N LEU A 78
SHEET 1 AA210 ARG A 151 ASN A 153 0
SHEET 2 AA210 THR A 145 ILE A 148 -1 N PHE A 146 O ASN A 153
SHEET 3 AA210 TYR A 166 ALA A 171 1 O VAL A 168 N THR A 145
SHEET 4 AA210 HIS A 116 ALA A 121 1 N VAL A 120 O ALA A 169
SHEET 5 AA210 VAL A 185 VAL A 188 1 O VAL A 187 N ALA A 119
SHEET 6 AA210 LEU A 222 CYS A 226 1 O VAL A 224 N ALA A 186
SHEET 7 AA210 THR A 243 GLY A 247 1 O VAL A 244 N ALA A 223
SHEET 8 AA210 VAL A 254 GLU A 262 1 O VAL A 254 N GLY A 247
SHEET 9 AA210 ARG A 265 LEU A 271 -1 O LEU A 271 N ARG A 255
SHEET 10 AA210 LEU A 278 VAL A 282 -1 O LEU A 278 N VAL A 270
SHEET 1 AA3 5 GLN B 62 ILE B 65 0
SHEET 2 AA3 5 GLU B 41 ASP B 46 1 N GLY B 44 O PHE B 64
SHEET 3 AA3 5 ARG B 17 VAL B 21 1 N ILE B 18 O GLU B 41
SHEET 4 AA3 5 VAL B 77 VAL B 80 1 O VAL B 79 N VAL B 21
SHEET 5 AA3 5 VAL B 101 PRO B 103 1 O VAL B 102 N LEU B 78
SHEET 1 AA410 ARG B 151 ASN B 153 0
SHEET 2 AA410 THR B 145 ILE B 148 -1 N PHE B 146 O ASN B 153
SHEET 3 AA410 TYR B 166 ALA B 171 1 O VAL B 168 N THR B 145
SHEET 4 AA410 HIS B 116 ALA B 121 1 N VAL B 120 O ALA B 169
SHEET 5 AA410 VAL B 185 VAL B 188 1 O VAL B 185 N ALA B 119
SHEET 6 AA410 LEU B 222 CYS B 226 1 O VAL B 224 N ALA B 186
SHEET 7 AA410 THR B 243 GLY B 247 1 O VAL B 244 N ALA B 223
SHEET 8 AA410 VAL B 254 GLU B 262 1 O VAL B 254 N THR B 245
SHEET 9 AA410 ARG B 265 LEU B 271 -1 O LEU B 271 N ARG B 255
SHEET 10 AA410 LEU B 278 VAL B 282 -1 O LEU B 278 N VAL B 270
SHEET 1 AA5 5 GLN C 62 ILE C 65 0
SHEET 2 AA5 5 GLU C 41 ASP C 46 1 N GLY C 44 O PHE C 64
SHEET 3 AA5 5 ARG C 17 VAL C 21 1 N ILE C 18 O GLU C 41
SHEET 4 AA5 5 VAL C 77 VAL C 80 1 O VAL C 79 N VAL C 21
SHEET 5 AA5 5 VAL C 101 PRO C 103 1 O VAL C 102 N LEU C 78
SHEET 1 AA610 ARG C 151 ASN C 153 0
SHEET 2 AA610 THR C 145 ILE C 148 -1 N PHE C 146 O ASN C 153
SHEET 3 AA610 TYR C 166 ALA C 171 1 O VAL C 168 N THR C 145
SHEET 4 AA610 HIS C 116 ALA C 121 1 N VAL C 120 O ALA C 169
SHEET 5 AA610 VAL C 185 VAL C 188 1 O VAL C 187 N ALA C 119
SHEET 6 AA610 LEU C 222 CYS C 226 1 O VAL C 224 N ALA C 186
SHEET 7 AA610 THR C 243 GLY C 247 1 O VAL C 244 N ALA C 223
SHEET 8 AA610 VAL C 254 GLU C 262 1 O VAL C 254 N GLY C 247
SHEET 9 AA610 ARG C 265 LEU C 271 -1 O TRP C 267 N ARG C 260
SHEET 10 AA610 LEU C 278 VAL C 282 -1 O LEU C 278 N VAL C 270
SHEET 1 AA7 5 GLN D 62 ILE D 65 0
SHEET 2 AA7 5 GLU D 41 ASP D 46 1 N GLY D 44 O PHE D 64
SHEET 3 AA7 5 ARG D 17 VAL D 21 1 N PHE D 20 O SER D 43
SHEET 4 AA7 5 VAL D 77 VAL D 80 1 O VAL D 79 N VAL D 21
SHEET 5 AA7 5 VAL D 101 PRO D 103 1 O VAL D 102 N LEU D 78
SHEET 1 AA810 ARG D 151 ASN D 153 0
SHEET 2 AA810 THR D 145 ILE D 148 -1 N PHE D 146 O ASN D 153
SHEET 3 AA810 TYR D 166 ALA D 171 1 O VAL D 168 N VAL D 147
SHEET 4 AA810 HIS D 116 ALA D 121 1 N VAL D 120 O ALA D 169
SHEET 5 AA810 VAL D 185 VAL D 188 1 O VAL D 187 N ALA D 121
SHEET 6 AA810 LEU D 222 CYS D 226 1 O VAL D 224 N ALA D 186
SHEET 7 AA810 THR D 243 GLY D 247 1 O VAL D 244 N ALA D 223
SHEET 8 AA810 VAL D 254 GLN D 261 1 O VAL D 254 N THR D 245
SHEET 9 AA810 THR D 266 LEU D 271 -1 O LEU D 271 N ARG D 255
SHEET 10 AA810 LEU D 278 VAL D 282 -1 O VAL D 282 N THR D 266
SHEET 1 AA9 5 GLN E 62 ILE E 65 0
SHEET 2 AA9 5 GLU E 41 ASP E 46 1 N GLY E 44 O PHE E 64
SHEET 3 AA9 5 ARG E 17 VAL E 21 1 N ILE E 18 O SER E 43
SHEET 4 AA9 5 VAL E 77 VAL E 80 1 O VAL E 79 N VAL E 21
SHEET 5 AA9 5 VAL E 101 PRO E 103 1 O VAL E 102 N LEU E 78
SHEET 1 AB110 ARG E 151 ASN E 153 0
SHEET 2 AB110 THR E 145 ILE E 148 -1 N PHE E 146 O ASN E 153
SHEET 3 AB110 TYR E 166 ALA E 171 1 O VAL E 168 N THR E 145
SHEET 4 AB110 HIS E 116 ALA E 121 1 N VAL E 120 O ALA E 169
SHEET 5 AB110 VAL E 185 VAL E 188 1 O VAL E 185 N ALA E 119
SHEET 6 AB110 LEU E 222 CYS E 226 1 O VAL E 224 N ALA E 186
SHEET 7 AB110 THR E 243 GLY E 247 1 O TYR E 246 N MET E 225
SHEET 8 AB110 VAL E 254 GLU E 262 1 O VAL E 254 N THR E 245
SHEET 9 AB110 ARG E 265 LEU E 271 -1 O TRP E 267 N ARG E 260
SHEET 10 AB110 LEU E 278 VAL E 282 -1 O LEU E 278 N VAL E 270
SHEET 1 AB2 5 GLN F 62 ILE F 65 0
SHEET 2 AB2 5 GLU F 41 ASP F 46 1 N GLY F 44 O PHE F 64
SHEET 3 AB2 5 ARG F 17 VAL F 21 1 N ILE F 18 O GLU F 41
SHEET 4 AB2 5 VAL F 77 VAL F 80 1 O VAL F 79 N VAL F 21
SHEET 5 AB2 5 VAL F 101 PRO F 103 1 O VAL F 102 N LEU F 78
SHEET 1 AB310 ARG F 151 ASN F 153 0
SHEET 2 AB310 THR F 145 ILE F 148 -1 N PHE F 146 O ASN F 153
SHEET 3 AB310 TYR F 166 ALA F 171 1 O VAL F 168 N THR F 145
SHEET 4 AB310 HIS F 116 ALA F 121 1 N VAL F 120 O ALA F 169
SHEET 5 AB310 VAL F 185 VAL F 188 1 O VAL F 187 N ALA F 119
SHEET 6 AB310 LEU F 222 CYS F 226 1 O VAL F 224 N ALA F 186
SHEET 7 AB310 THR F 243 GLY F 247 1 O VAL F 244 N ALA F 223
SHEET 8 AB310 VAL F 254 GLU F 262 1 O VAL F 254 N THR F 245
SHEET 9 AB310 ARG F 265 LEU F 271 -1 O THR F 269 N ILE F 257
SHEET 10 AB310 LEU F 278 VAL F 282 -1 O VAL F 282 N THR F 266
SHEET 1 AB4 5 GLN G 62 ILE G 65 0
SHEET 2 AB4 5 GLU G 41 ASP G 46 1 N GLY G 44 O PHE G 64
SHEET 3 AB4 5 ARG G 17 VAL G 21 1 N ILE G 18 O GLU G 41
SHEET 4 AB4 5 VAL G 77 VAL G 80 1 O VAL G 79 N VAL G 21
SHEET 5 AB4 5 VAL G 101 PRO G 103 1 O VAL G 102 N LEU G 78
SHEET 1 AB510 ARG G 151 ASN G 153 0
SHEET 2 AB510 THR G 145 ILE G 148 -1 N PHE G 146 O ASN G 153
SHEET 3 AB510 TYR G 166 ALA G 171 1 O VAL G 168 N THR G 145
SHEET 4 AB510 HIS G 116 ALA G 121 1 N VAL G 120 O ALA G 169
SHEET 5 AB510 VAL G 185 VAL G 188 1 O VAL G 187 N ALA G 121
SHEET 6 AB510 LEU G 222 CYS G 226 1 O VAL G 224 N ALA G 186
SHEET 7 AB510 THR G 243 GLY G 247 1 O VAL G 244 N ALA G 223
SHEET 8 AB510 VAL G 254 GLU G 262 1 O VAL G 254 N GLY G 247
SHEET 9 AB510 ARG G 265 LEU G 271 -1 O TRP G 267 N ARG G 260
SHEET 10 AB510 LEU G 278 VAL G 282 -1 O LEU G 278 N VAL G 270
SHEET 1 AB6 5 GLN H 62 ILE H 65 0
SHEET 2 AB6 5 GLU H 41 ASP H 46 1 N ASP H 46 O PHE H 64
SHEET 3 AB6 5 ARG H 17 VAL H 21 1 N PHE H 20 O SER H 45
SHEET 4 AB6 5 VAL H 77 VAL H 80 1 O VAL H 79 N VAL H 21
SHEET 5 AB6 5 VAL H 101 PRO H 103 1 O VAL H 102 N LEU H 78
SHEET 1 AB710 ARG H 151 ASN H 153 0
SHEET 2 AB710 THR H 145 ILE H 148 -1 N PHE H 146 O ASN H 153
SHEET 3 AB710 TYR H 166 ALA H 171 1 O VAL H 168 N THR H 145
SHEET 4 AB710 HIS H 116 ALA H 121 1 N VAL H 120 O ALA H 169
SHEET 5 AB710 VAL H 185 VAL H 188 1 O VAL H 187 N ALA H 119
SHEET 6 AB710 LEU H 222 CYS H 226 1 O VAL H 224 N ALA H 186
SHEET 7 AB710 THR H 243 GLY H 247 1 O VAL H 244 N ALA H 223
SHEET 8 AB710 VAL H 254 GLU H 262 1 O VAL H 254 N THR H 245
SHEET 9 AB710 ARG H 265 LEU H 271 -1 O THR H 269 N ILE H 257
SHEET 10 AB710 LEU H 278 VAL H 282 -1 O VAL H 280 N PHE H 268
SITE 1 AC1 3 ARG A 233 ASP A 251 ARG C 233
SITE 1 AC2 4 ALA B 26 GLY B 30 ARG B 151 LEU B 152
SITE 1 AC3 5 ALA C 26 GLY C 27 GLY C 30 LEU C 152
SITE 2 AC3 5 LEU C 161
SITE 1 AC4 9 VAL D 227 ASP D 228 ASP D 229 PRO D 230
SITE 2 AC4 9 ARG D 233 VAL G 227 ASP G 228 PRO G 230
SITE 3 AC4 9 ARG G 233
SITE 1 AC5 4 ALA G 252 ASP G 253 ARG G 255 ARG G 272
SITE 1 AC6 5 VAL G 254 PRO G 273 THR G 301 ASP G 302
SITE 2 AC6 5 HOH G 535
SITE 1 AC7 5 ALA H 26 GLY H 27 GLY H 30 ARG H 151
SITE 2 AC7 5 LEU H 152
CRYST1 284.820 109.400 108.580 90.00 112.38 90.00 C 1 2 1 32
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 0.003511 0.000000 0.001445 0.00000
SCALE2 0.000000 0.009141 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009960 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
