HEADER HYDROLASE 18-NOV-16 5MFS
TITLE THE CRYSTAL STRUCTURE OF E. COLI AMINOPEPTIDASE N IN COMPLEX WITH 7-
TITLE 2 AMINO-4-PHENYL-5,7,8,9-TETRAHYDROBENZOCYCLOHEPTEN-6-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOPEPTIDASE N;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-AMINOACYLPEPTIDE HYDROLASE;
COMPND 5 EC: 3.4.11.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: PEPN, B0932, JW0915;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS M1 AMINOPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PENG,V.OLIERIC,A.G.MCEWEN,C.SCHMITT,S.ALBRECHT,J.CAVARELLI,C.TARNUS
REVDAT 4 17-JAN-24 5MFS 1 REMARK LINK
REVDAT 3 30-AUG-17 5MFS 1 REMARK
REVDAT 2 02-AUG-17 5MFS 1
REVDAT 1 19-APR-17 5MFS 0
JRNL AUTH G.PENG,A.G.MCEWEN,V.OLIERIC,C.SCHMITT,S.ALBRECHT,
JRNL AUTH 2 J.CAVARELLI,C.TARNUS
JRNL TITL INSIGHT INTO THE REMARKABLE AFFINITY AND SELECTIVITY OF THE
JRNL TITL 2 AMINOBENZOSUBERONE SCAFFOLD FOR THE M1 AMINOPEPTIDASES
JRNL TITL 3 FAMILY BASED ON STRUCTURE ANALYSIS.
JRNL REF PROTEINS V. 85 1413 2017
JRNL REFN ESSN 1097-0134
JRNL PMID 28383176
JRNL DOI 10.1002/PROT.25301
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.210
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 200028
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.114
REMARK 3 R VALUE (WORKING SET) : 0.113
REMARK 3 FREE R VALUE : 0.139
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.870
REMARK 3 FREE R VALUE TEST SET COUNT : 3398
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 89.3457 - 4.5285 1.00 16076 144 0.1301 0.1341
REMARK 3 2 4.5285 - 3.5943 1.00 16044 141 0.0754 0.0912
REMARK 3 3 3.5943 - 3.1400 1.00 16097 142 0.0742 0.0909
REMARK 3 4 3.1400 - 2.8529 1.00 16058 138 0.0743 0.0903
REMARK 3 5 2.8529 - 2.6484 1.00 16039 148 0.0741 0.1103
REMARK 3 6 2.6484 - 2.4922 1.00 16175 138 0.0748 0.1178
REMARK 3 7 2.4922 - 2.3674 1.00 15969 142 0.0731 0.1210
REMARK 3 8 2.3674 - 2.2643 1.00 16155 146 0.0741 0.1120
REMARK 3 9 2.2643 - 2.1771 1.00 16037 150 0.0744 0.0925
REMARK 3 10 2.1771 - 2.1020 1.00 16148 134 0.0832 0.1236
REMARK 3 11 2.1020 - 2.0363 1.00 16028 132 0.0930 0.1303
REMARK 3 12 2.0363 - 1.9781 1.00 16064 144 0.1135 0.1402
REMARK 3 13 1.9781 - 1.9260 1.00 16091 146 0.1346 0.1572
REMARK 3 14 1.9260 - 1.8790 1.00 16094 142 0.1470 0.1959
REMARK 3 15 1.8790 - 1.8363 1.00 15995 144 0.1581 0.2060
REMARK 3 16 1.8363 - 1.7972 1.00 16129 134 0.1683 0.2066
REMARK 3 17 1.7972 - 1.7612 1.00 16086 144 0.1832 0.2275
REMARK 3 18 1.7612 - 1.7280 1.00 15992 149 0.1988 0.2066
REMARK 3 19 1.7280 - 1.6971 1.00 16150 140 0.2172 0.2318
REMARK 3 20 1.6971 - 1.6684 1.00 16094 136 0.2423 0.3344
REMARK 3 21 1.6684 - 1.6415 1.00 16091 144 0.2737 0.2947
REMARK 3 22 1.6415 - 1.6162 1.00 16071 137 0.2925 0.3072
REMARK 3 23 1.6162 - 1.5924 0.99 15972 139 0.3044 0.3483
REMARK 3 24 1.5924 - 1.5700 0.98 15631 144 0.3183 0.3416
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.36
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 : 0.012 8160
REMARK 3 ANGLE : 1.137 11189
REMARK 3 CHIRALITY : 0.062 1205
REMARK 3 PLANARITY : 0.008 1511
REMARK 3 DIHEDRAL : 13.846 5148
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 5MFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1200002344.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.27, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 200123
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 89.201
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 21.40
REMARK 200 R MERGE (I) : 0.18700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 13.30
REMARK 200 R MERGE FOR SHELL (I) : 2.96900
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: 3B34
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.M M SODIUM MALONATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.87600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 113.75200
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 113.75200
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 56.87600
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2139 LIES ON A SPECIAL POSITION.
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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
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 GLN A 3 CG CD OE1 NE2
REMARK 470 ASP A 30 CG OD1 OD2
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 HO1 GOL A 1030 O HOH A 1155 1.45
REMARK 500 HZ1 LYS A 144 O HOH A 1138 1.46
REMARK 500 HE21 GLN A 328 O1 GOL A 1036 1.47
REMARK 500 HH12 ARG A 204 O HOH A 1139 1.47
REMARK 500 HH12 ARG A 783 O HOH A 1104 1.51
REMARK 500 HE21 GLN A 423 O HOH A 1110 1.51
REMARK 500 HH12 ARG A 293 O HOH A 1120 1.51
REMARK 500 ZN ZN A 1001 H17 7ML A 1002 1.53
REMARK 500 HZ1 LYS A 151 O HOH A 1161 1.56
REMARK 500 HZ2 LYS A 748 O HOH A 1131 1.58
REMARK 500 O HOH A 2270 O HOH A 2517 1.75
REMARK 500 O HOH A 1740 O HOH A 2307 1.84
REMARK 500 O HOH A 1129 O HOH A 2309 1.85
REMARK 500 OE2 GLU A 459 O HOH A 1101 1.86
REMARK 500 O HOH A 1693 O HOH A 2762 1.87
REMARK 500 O HOH A 1404 O HOH A 1606 1.87
REMARK 500 OE1 GLU A 78 O HOH A 1102 1.88
REMARK 500 O HOH A 1414 O HOH A 2624 1.89
REMARK 500 O7 MLI A 1013 O HOH A 1103 1.92
REMARK 500 O HOH A 1269 O HOH A 1299 1.93
REMARK 500 NH1 ARG A 783 O HOH A 1104 1.93
REMARK 500 O HOH A 1114 O HOH A 1639 1.94
REMARK 500 O HOH A 2699 O HOH A 2833 1.96
REMARK 500 O HOH A 1131 O HOH A 1326 1.96
REMARK 500 O HOH A 2770 O HOH A 2811 1.97
REMARK 500 O HOH A 1126 O HOH A 1767 1.97
REMARK 500 O HOH A 2744 O HOH A 2817 1.98
REMARK 500 O HOH A 2232 O HOH A 2487 1.99
REMARK 500 O HOH A 2213 O HOH A 2620 1.99
REMARK 500 O HOH A 2303 O HOH A 2378 2.00
REMARK 500 O HOH A 1940 O HOH A 2094 2.00
REMARK 500 O HOH A 1684 O HOH A 2608 2.01
REMARK 500 NZ LYS A 451 O HOH A 1105 2.02
REMARK 500 O HOH A 1790 O HOH A 2600 2.02
REMARK 500 O HOH A 2429 O HOH A 2609 2.04
REMARK 500 O HOH A 2017 O HOH A 2137 2.04
REMARK 500 O HOH A 2049 O HOH A 2283 2.05
REMARK 500 O HOH A 2327 O HOH A 2409 2.05
REMARK 500 O HOH A 1138 O HOH A 1156 2.06
REMARK 500 O HOH A 1671 O HOH A 2136 2.07
REMARK 500 O HOH A 1221 O HOH A 2280 2.07
REMARK 500 O HOH A 2572 O HOH A 2747 2.07
REMARK 500 O HOH A 1676 O HOH A 1767 2.07
REMARK 500 O HOH A 2811 O HOH A 2840 2.07
REMARK 500 OE2 GLU A 535 O HOH A 1106 2.08
REMARK 500 O HOH A 2283 O HOH A 2569 2.08
REMARK 500 O HOH A 2269 O HOH A 2538 2.09
REMARK 500 O HOH A 2198 O HOH A 2347 2.09
REMARK 500 OD1 ASP A 24 O HOH A 1107 2.09
REMARK 500 O HOH A 1240 O HOH A 1422 2.10
REMARK 500
REMARK 500 THIS ENTRY HAS 89 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ALA A 581 O HOH A 1139 4455 1.60
REMARK 500 OE1 GLN A 585 O HOH A 1928 4455 1.88
REMARK 500 O HOH A 1769 O HOH A 2537 4565 1.94
REMARK 500 O HOH A 1266 O HOH A 2178 2565 1.99
REMARK 500 O HOH A 2416 O HOH A 2510 5554 2.01
REMARK 500 O HOH A 2075 O HOH A 2375 4565 2.03
REMARK 500 O HOH A 1526 O HOH A 2575 3454 2.10
REMARK 500 O HOH A 2062 O HOH A 2760 4565 2.16
REMARK 500 O HOH A 1301 O HOH A 2840 3454 2.16
REMARK 500 O HOH A 1266 O HOH A 2100 2565 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 161 CB ARG A 161 CG -0.164
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 GLN A 4 95.04 5.74
REMARK 500 GLU A 264 34.20 -85.35
REMARK 500 VAL A 276 -50.98 -127.04
REMARK 500 ASN A 306 -60.81 -99.25
REMARK 500 THR A 309 -165.26 -110.44
REMARK 500 GLN A 527 109.80 -58.07
REMARK 500 ASN A 819 79.97 -157.37
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 A2855 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A2856 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A2857 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A2858 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH A2859 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A2860 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH A2861 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A2862 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A2863 DISTANCE = 6.75 ANGSTROMS
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 2321
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 NA A1009 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 67 OD1
REMARK 620 2 THR A 91 OG1 92.3
REMARK 620 3 HOH A2262 O 170.7 83.0
REMARK 620 4 HOH A2378 O 79.4 86.7 92.3
REMARK 620 5 HOH A2400 O 96.8 157.8 84.9 75.2
REMARK 620 6 HOH A2449 O 96.2 92.9 92.1 175.5 106.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 297 NE2
REMARK 620 2 HIS A 301 NE2 99.3
REMARK 620 3 GLU A 320 OE1 112.7 103.9
REMARK 620 4 7ML A1002 O2 114.8 128.8 97.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1003 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 332 O
REMARK 620 2 ASP A 333 O 82.4
REMARK 620 3 GLY A 335 O 87.3 105.6
REMARK 620 4 HOH A1927 O 105.1 169.3 82.6
REMARK 620 5 HOH A2214 O 157.7 79.5 85.1 94.7
REMARK 620 6 HOH A2302 O 102.7 81.7 168.4 89.1 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1006 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 371 OE1
REMARK 620 2 HOH A1145 O 98.1
REMARK 620 3 HOH A1497 O 74.7 77.1
REMARK 620 4 HOH A1675 O 90.6 89.3 158.1
REMARK 620 5 HOH A1872 O 167.1 81.4 92.7 102.3
REMARK 620 6 HOH A2314 O 86.3 166.7 92.1 103.3 91.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1008 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 371 OE1
REMARK 620 2 HOH A1154 O 115.1
REMARK 620 3 HOH A1219 O 50.2 141.1
REMARK 620 4 HOH A1327 O 110.4 130.7 64.2
REMARK 620 5 HOH A1535 O 147.1 60.4 110.4 71.2
REMARK 620 6 HOH A1605 O 99.8 109.6 108.5 79.4 112.4
REMARK 620 7 HOH A2314 O 72.4 73.7 67.5 104.1 75.4 172.1
REMARK 620 8 HOH A2481 O 108.9 95.0 65.7 51.8 44.8 129.2 56.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1007 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 452 OD1
REMARK 620 2 TYR A 544 OH 76.4
REMARK 620 3 HOH A1555 O 160.2 84.2
REMARK 620 4 HOH A2295 O 79.7 93.6 97.3
REMARK 620 5 HOH A2330 O 79.6 81.3 102.0 159.4
REMARK 620 6 HOH A2508 O 98.9 160.5 100.8 104.3 79.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1011 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 452 O
REMARK 620 2 HOH A1293 O 68.5
REMARK 620 3 HOH A1843 O 81.9 86.3
REMARK 620 4 HOH A2225 O 78.8 77.1 158.1
REMARK 620 5 HOH A2265 O 85.1 153.4 87.2 101.3
REMARK 620 6 HOH A2783 O 168.6 118.6 106.8 93.7 88.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1005 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 508 OG
REMARK 620 2 HOH A1882 O 90.0
REMARK 620 3 HOH A2060 O 88.7 90.5
REMARK 620 4 HOH A2145 O 81.1 169.4 94.8
REMARK 620 5 HOH A2340 O 91.6 77.7 168.2 96.9
REMARK 620 6 HOH A2806 O 173.3 90.1 98.0 98.1 81.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1010 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 511 O
REMARK 620 2 THR A 513 OG1 93.9
REMARK 620 3 HOH A1607 O 90.0 87.2
REMARK 620 4 HOH A2249 O 87.3 177.6 94.9
REMARK 620 5 HOH A2586 O 109.1 98.4 159.6 79.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1004 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 771 O
REMARK 620 2 PHE A 774 O 86.2
REMARK 620 3 HOH A1322 O 98.7 80.2
REMARK 620 4 HOH A1559 O 98.0 90.4 160.2
REMARK 620 5 HOH A2247 O 171.4 89.7 88.0 74.4
REMARK 620 6 HOH A2291 O 87.8 173.7 102.6 88.6 96.0
REMARK 620 7 HOH A2587 O 121.0 132.5 126.1 50.8 57.4 50.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7ML A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 1014
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 1015
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 1016
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1017
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1018
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1019
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1020
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1021
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1023
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1024
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1025
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1026
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1027
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1028
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1029
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1030
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1031
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1032
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1033
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1034
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1035
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1036
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1037
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1038
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1039
DBREF 5MFS A 1 870 UNP P04825 AMPN_ECOLI 1 870
SEQADV 5MFS MET A -20 UNP P04825 INITIATING METHIONINE
SEQADV 5MFS GLY A -19 UNP P04825 EXPRESSION TAG
SEQADV 5MFS SER A -18 UNP P04825 EXPRESSION TAG
SEQADV 5MFS SER A -17 UNP P04825 EXPRESSION TAG
SEQADV 5MFS HIS A -16 UNP P04825 EXPRESSION TAG
SEQADV 5MFS HIS A -15 UNP P04825 EXPRESSION TAG
SEQADV 5MFS HIS A -14 UNP P04825 EXPRESSION TAG
SEQADV 5MFS HIS A -13 UNP P04825 EXPRESSION TAG
SEQADV 5MFS HIS A -12 UNP P04825 EXPRESSION TAG
SEQADV 5MFS HIS A -11 UNP P04825 EXPRESSION TAG
SEQADV 5MFS SER A -10 UNP P04825 EXPRESSION TAG
SEQADV 5MFS SER A -9 UNP P04825 EXPRESSION TAG
SEQADV 5MFS GLY A -8 UNP P04825 EXPRESSION TAG
SEQADV 5MFS GLU A -7 UNP P04825 EXPRESSION TAG
SEQADV 5MFS ASN A -6 UNP P04825 EXPRESSION TAG
SEQADV 5MFS LEU A -5 UNP P04825 EXPRESSION TAG
SEQADV 5MFS TYR A -4 UNP P04825 EXPRESSION TAG
SEQADV 5MFS PHE A -3 UNP P04825 EXPRESSION TAG
SEQADV 5MFS GLN A -2 UNP P04825 EXPRESSION TAG
SEQADV 5MFS GLY A -1 UNP P04825 EXPRESSION TAG
SEQADV 5MFS HIS A 0 UNP P04825 EXPRESSION TAG
SEQRES 1 A 891 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 891 GLU ASN LEU TYR PHE GLN GLY HIS MET THR GLN GLN PRO
SEQRES 3 A 891 GLN ALA LYS TYR ARG HIS ASP TYR ARG ALA PRO ASP TYR
SEQRES 4 A 891 GLN ILE THR ASP ILE ASP LEU THR PHE ASP LEU ASP ALA
SEQRES 5 A 891 GLN LYS THR VAL VAL THR ALA VAL SER GLN ALA VAL ARG
SEQRES 6 A 891 HIS GLY ALA SER ASP ALA PRO LEU ARG LEU ASN GLY GLU
SEQRES 7 A 891 ASP LEU LYS LEU VAL SER VAL HIS ILE ASN ASP GLU PRO
SEQRES 8 A 891 TRP THR ALA TRP LYS GLU GLU GLU GLY ALA LEU VAL ILE
SEQRES 9 A 891 SER ASN LEU PRO GLU ARG PHE THR LEU LYS ILE ILE ASN
SEQRES 10 A 891 GLU ILE SER PRO ALA ALA ASN THR ALA LEU GLU GLY LEU
SEQRES 11 A 891 TYR GLN SER GLY ASP ALA LEU CYS THR GLN CYS GLU ALA
SEQRES 12 A 891 GLU GLY PHE ARG HIS ILE THR TYR TYR LEU ASP ARG PRO
SEQRES 13 A 891 ASP VAL LEU ALA ARG PHE THR THR LYS ILE ILE ALA ASP
SEQRES 14 A 891 LYS ILE LYS TYR PRO PHE LEU LEU SER ASN GLY ASN ARG
SEQRES 15 A 891 VAL ALA GLN GLY GLU LEU GLU ASN GLY ARG HIS TRP VAL
SEQRES 16 A 891 GLN TRP GLN ASP PRO PHE PRO LYS PRO CYS TYR LEU PHE
SEQRES 17 A 891 ALA LEU VAL ALA GLY ASP PHE ASP VAL LEU ARG ASP THR
SEQRES 18 A 891 PHE THR THR ARG SER GLY ARG GLU VAL ALA LEU GLU LEU
SEQRES 19 A 891 TYR VAL ASP ARG GLY ASN LEU ASP ARG ALA PRO TRP ALA
SEQRES 20 A 891 MET THR SER LEU LYS ASN SER MET LYS TRP ASP GLU GLU
SEQRES 21 A 891 ARG PHE GLY LEU GLU TYR ASP LEU ASP ILE TYR MET ILE
SEQRES 22 A 891 VAL ALA VAL ASP PHE PHE ASN MET GLY ALA MET GLU ASN
SEQRES 23 A 891 LYS GLY LEU ASN ILE PHE ASN SER LYS TYR VAL LEU ALA
SEQRES 24 A 891 ARG THR ASP THR ALA THR ASP LYS ASP TYR LEU ASP ILE
SEQRES 25 A 891 GLU ARG VAL ILE GLY HIS GLU TYR PHE HIS ASN TRP THR
SEQRES 26 A 891 GLY ASN ARG VAL THR CYS ARG ASP TRP PHE GLN LEU SER
SEQRES 27 A 891 LEU LYS GLU GLY LEU THR VAL PHE ARG ASP GLN GLU PHE
SEQRES 28 A 891 SER SER ASP LEU GLY SER ARG ALA VAL ASN ARG ILE ASN
SEQRES 29 A 891 ASN VAL ARG THR MET ARG GLY LEU GLN PHE ALA GLU ASP
SEQRES 30 A 891 ALA SER PRO MET ALA HIS PRO ILE ARG PRO ASP MET VAL
SEQRES 31 A 891 ILE GLU MET ASN ASN PHE TYR THR LEU THR VAL TYR GLU
SEQRES 32 A 891 LYS GLY ALA GLU VAL ILE ARG MET ILE HIS THR LEU LEU
SEQRES 33 A 891 GLY GLU GLU ASN PHE GLN LYS GLY MET GLN LEU TYR PHE
SEQRES 34 A 891 GLU ARG HIS ASP GLY SER ALA ALA THR CYS ASP ASP PHE
SEQRES 35 A 891 VAL GLN ALA MET GLU ASP ALA SER ASN VAL ASP LEU SER
SEQRES 36 A 891 HIS PHE ARG ARG TRP TYR SER GLN SER GLY THR PRO ILE
SEQRES 37 A 891 VAL THR VAL LYS ASP ASP TYR ASN PRO GLU THR GLU GLN
SEQRES 38 A 891 TYR THR LEU THR ILE SER GLN ARG THR PRO ALA THR PRO
SEQRES 39 A 891 ASP GLN ALA GLU LYS GLN PRO LEU HIS ILE PRO PHE ALA
SEQRES 40 A 891 ILE GLU LEU TYR ASP ASN GLU GLY LYS VAL ILE PRO LEU
SEQRES 41 A 891 GLN LYS GLY GLY HIS PRO VAL ASN SER VAL LEU ASN VAL
SEQRES 42 A 891 THR GLN ALA GLU GLN THR PHE VAL PHE ASP ASN VAL TYR
SEQRES 43 A 891 PHE GLN PRO VAL PRO ALA LEU LEU CYS GLU PHE SER ALA
SEQRES 44 A 891 PRO VAL LYS LEU GLU TYR LYS TRP SER ASP GLN GLN LEU
SEQRES 45 A 891 THR PHE LEU MET ARG HIS ALA ARG ASN ASP PHE SER ARG
SEQRES 46 A 891 TRP ASP ALA ALA GLN SER LEU LEU ALA THR TYR ILE LYS
SEQRES 47 A 891 LEU ASN VAL ALA ARG HIS GLN GLN GLY GLN PRO LEU SER
SEQRES 48 A 891 LEU PRO VAL HIS VAL ALA ASP ALA PHE ARG ALA VAL LEU
SEQRES 49 A 891 LEU ASP GLU LYS ILE ASP PRO ALA LEU ALA ALA GLU ILE
SEQRES 50 A 891 LEU THR LEU PRO SER VAL ASN GLU MET ALA GLU LEU PHE
SEQRES 51 A 891 ASP ILE ILE ASP PRO ILE ALA ILE ALA GLU VAL ARG GLU
SEQRES 52 A 891 ALA LEU THR ARG THR LEU ALA THR GLU LEU ALA ASP GLU
SEQRES 53 A 891 LEU LEU ALA ILE TYR ASN ALA ASN TYR GLN SER GLU TYR
SEQRES 54 A 891 ARG VAL GLU HIS GLU ASP ILE ALA LYS ARG THR LEU ARG
SEQRES 55 A 891 ASN ALA CYS LEU ARG PHE LEU ALA PHE GLY GLU THR HIS
SEQRES 56 A 891 LEU ALA ASP VAL LEU VAL SER LYS GLN PHE HIS GLU ALA
SEQRES 57 A 891 ASN ASN MET THR ASP ALA LEU ALA ALA LEU SER ALA ALA
SEQRES 58 A 891 VAL ALA ALA GLN LEU PRO CYS ARG ASP ALA LEU MET GLN
SEQRES 59 A 891 GLU TYR ASP ASP LYS TRP HIS GLN ASN GLY LEU VAL MET
SEQRES 60 A 891 ASP LYS TRP PHE ILE LEU GLN ALA THR SER PRO ALA ALA
SEQRES 61 A 891 ASN VAL LEU GLU THR VAL ARG GLY LEU LEU GLN HIS ARG
SEQRES 62 A 891 SER PHE THR MET SER ASN PRO ASN ARG ILE ARG SER LEU
SEQRES 63 A 891 ILE GLY ALA PHE ALA GLY SER ASN PRO ALA ALA PHE HIS
SEQRES 64 A 891 ALA GLU ASP GLY SER GLY TYR LEU PHE LEU VAL GLU MET
SEQRES 65 A 891 LEU THR ASP LEU ASN SER ARG ASN PRO GLN VAL ALA SER
SEQRES 66 A 891 ARG LEU ILE GLU PRO LEU ILE ARG LEU LYS ARG TYR ASP
SEQRES 67 A 891 ALA LYS ARG GLN GLU LYS MET ARG ALA ALA LEU GLU GLN
SEQRES 68 A 891 LEU LYS GLY LEU GLU ASN LEU SER GLY ASP LEU TYR GLU
SEQRES 69 A 891 LYS ILE THR LYS ALA LEU ALA
HET ZN A1001 1
HET 7ML A1002 40
HET NA A1003 1
HET NA A1004 1
HET NA A1005 1
HET NA A1006 1
HET NA A1007 1
HET NA A1008 1
HET NA A1009 1
HET NA A1010 1
HET NA A1011 1
HET MLI A1012 9
HET MLI A1013 9
HET MLI A1014 9
HET MLI A1015 9
HET MLI A1016 9
HET DMS A1017 10
HET DMS A1018 10
HET DMS A1019 10
HET DMS A1020 10
HET DMS A1021 10
HET CL A1022 1
HET CL A1023 1
HET CL A1024 1
HET CL A1025 1
HET GOL A1026 14
HET GOL A1027 14
HET GOL A1028 14
HET GOL A1029 14
HET GOL A1030 14
HET GOL A1031 14
HET GOL A1032 14
HET GOL A1033 13
HET GOL A1034 14
HET GOL A1035 14
HET GOL A1036 14
HET GOL A1037 14
HET GOL A1038 14
HET GOL A1039 14
HETNAM ZN ZINC ION
HETNAM 7ML [(7~{S})-6,6-BIS(OXIDANYL)-4-PHENYL-5,7,8,9-
HETNAM 2 7ML TETRAHYDROBENZO[7]ANNULEN-7-YL]AZANIUM
HETNAM NA SODIUM ION
HETNAM MLI MALONATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 7ML C17 H20 N O2 1+
FORMUL 4 NA 9(NA 1+)
FORMUL 13 MLI 5(C3 H2 O4 2-)
FORMUL 18 DMS 5(C2 H6 O S)
FORMUL 23 CL 4(CL 1-)
FORMUL 27 GOL 14(C3 H8 O3)
FORMUL 41 HOH *1763(H2 O)
HELIX 1 AA1 HIS A 11 TYR A 13 5 3
HELIX 2 AA2 SER A 99 ASN A 103 5 5
HELIX 3 AA3 GLY A 124 ILE A 128 5 5
HELIX 4 AA4 PRO A 183 PHE A 187 5 5
HELIX 5 AA5 ASN A 219 ARG A 222 5 4
HELIX 6 AA6 ALA A 223 GLY A 242 1 20
HELIX 7 AA7 LYS A 274 VAL A 276 5 3
HELIX 8 AA8 THR A 284 HIS A 301 1 18
HELIX 9 AA9 ASP A 312 PHE A 314 5 3
HELIX 10 AB1 GLN A 315 GLY A 335 1 21
HELIX 11 AB2 SER A 336 LEU A 351 1 16
HELIX 12 AB3 LEU A 351 ALA A 357 1 7
HELIX 13 AB4 GLU A 371 TYR A 376 5 6
HELIX 14 AB5 THR A 377 ASP A 412 1 36
HELIX 15 AB6 THR A 417 ASN A 430 1 14
HELIX 16 AB7 ARG A 437 GLN A 442 1 6
HELIX 17 AB8 SER A 547 ALA A 558 1 12
HELIX 18 AB9 ASN A 560 GLN A 585 1 26
HELIX 19 AC1 PRO A 592 ASP A 605 1 14
HELIX 20 AC2 ASP A 609 LEU A 617 1 9
HELIX 21 AC3 SER A 621 GLU A 627 1 7
HELIX 22 AC4 ASP A 633 LEU A 652 1 20
HELIX 23 AC5 LEU A 652 ASN A 663 1 12
HELIX 24 AC6 GLU A 671 ALA A 689 1 19
HELIX 25 AC7 GLU A 692 ALA A 707 1 16
HELIX 26 AC8 ASN A 709 ALA A 723 1 15
HELIX 27 AC9 CYS A 727 HIS A 740 1 14
HELIX 28 AD1 ASN A 742 THR A 755 1 14
HELIX 29 AD2 ASN A 760 LEU A 769 1 10
HELIX 30 AD3 ASN A 778 ASN A 793 1 16
HELIX 31 AD4 ASN A 793 HIS A 798 1 6
HELIX 32 AD5 GLY A 802 ASN A 819 1 18
HELIX 33 AD6 ASN A 819 ARG A 832 1 14
HELIX 34 AD7 LEU A 833 TYR A 836 5 4
HELIX 35 AD8 ASP A 837 GLY A 853 1 17
HELIX 36 AD9 SER A 858 ALA A 870 1 13
SHEET 1 AA1 2 LYS A 8 TYR A 9 0
SHEET 2 AA1 2 MET A 368 VAL A 369 -1 O VAL A 369 N LYS A 8
SHEET 1 AA2 8 GLU A 69 PRO A 70 0
SHEET 2 AA2 8 LYS A 60 ILE A 66 -1 N ILE A 66 O GLU A 69
SHEET 3 AA2 8 ARG A 89 ILE A 98 -1 O ILE A 95 N VAL A 62
SHEET 4 AA2 8 THR A 34 ARG A 44 -1 N VAL A 36 O ASN A 96
SHEET 5 AA2 8 TYR A 18 ASP A 28 -1 N ASP A 28 O VAL A 35
SHEET 6 AA2 8 ALA A 139 ASP A 148 1 O LYS A 144 N LEU A 25
SHEET 7 AA2 8 ARG A 171 LYS A 182 -1 O TRP A 176 N THR A 143
SHEET 8 AA2 8 ASN A 160 GLU A 166 -1 N ALA A 163 O GLN A 175
SHEET 1 AA3 3 LEU A 52 ASN A 55 0
SHEET 2 AA3 3 ALA A 80 ILE A 83 -1 O LEU A 81 N LEU A 54
SHEET 3 AA3 3 TRP A 74 GLU A 77 -1 N LYS A 75 O VAL A 82
SHEET 1 AA4 4 GLY A 108 SER A 112 0
SHEET 2 AA4 4 ALA A 115 GLN A 119 -1 O CYS A 117 N TYR A 110
SHEET 3 AA4 4 LEU A 189 GLY A 192 -1 O ALA A 191 N LEU A 116
SHEET 4 AA4 4 PHE A 154 SER A 157 -1 N LEU A 156 O VAL A 190
SHEET 1 AA5 5 ASP A 195 THR A 202 0
SHEET 2 AA5 5 GLU A 208 VAL A 215 -1 O VAL A 209 N PHE A 201
SHEET 3 AA5 5 ILE A 249 VAL A 255 1 O ILE A 252 N TYR A 214
SHEET 4 AA5 5 LEU A 268 ASN A 272 1 O PHE A 271 N VAL A 253
SHEET 5 AA5 5 ALA A 262 MET A 263 -1 N MET A 263 O ILE A 270
SHEET 1 AA6 2 VAL A 308 CYS A 310 0
SHEET 2 AA6 2 SER A 414 ALA A 416 1 O SER A 414 N THR A 309
SHEET 1 AA7 4 GLU A 516 PHE A 521 0
SHEET 2 AA7 4 GLN A 460 ARG A 468 -1 N LEU A 463 O PHE A 519
SHEET 3 AA7 4 ILE A 447 ASN A 455 -1 N ILE A 447 O ARG A 468
SHEET 4 AA7 4 LYS A 541 GLU A 543 1 O LYS A 541 N VAL A 448
SHEET 1 AA8 3 VAL A 509 VAL A 512 0
SHEET 2 AA8 3 ILE A 483 TYR A 490 -1 N PHE A 485 O LEU A 510
SHEET 3 AA8 3 VAL A 529 LEU A 532 -1 O ALA A 531 N GLU A 488
SHEET 1 AA9 2 GLN A 500 LYS A 501 0
SHEET 2 AA9 2 HIS A 504 PRO A 505 -1 O HIS A 504 N LYS A 501
LINK OD1 ASN A 67 NA NA A1009 1555 1555 2.68
LINK OG1 THR A 91 NA NA A1009 1555 1555 2.59
LINK NE2 HIS A 297 ZN ZN A1001 1555 1555 2.03
LINK NE2 HIS A 301 ZN ZN A1001 1555 1555 2.04
LINK OE1 GLU A 320 ZN ZN A1001 1555 1555 2.00
LINK O SER A 332 NA NA A1003 1555 1555 2.35
LINK O ASP A 333 NA NA A1003 1555 1555 2.84
LINK O GLY A 335 NA NA A1003 1555 1555 2.30
LINK OE1 GLU A 371 NA NA A1006 1555 1555 2.49
LINK OE1 GLU A 371 NA NA A1008 1555 1555 2.68
LINK OD1 ASP A 452 NA NA A1007 1555 1555 2.87
LINK O ASP A 452 NA NA A1011 1555 1555 2.50
LINK OG SER A 508 NA NA A1005 1555 1555 2.42
LINK O ASN A 511 NA NA A1010 1555 1555 2.65
LINK OG1 THR A 513 NA NA A1010 1555 1555 2.91
LINK OH TYR A 544 NA NA A1007 1555 1555 2.83
LINK O HIS A 771 NA NA A1004 1555 1555 2.63
LINK O PHE A 774 NA NA A1004 1555 1555 2.35
LINK ZN ZN A1001 O2 7ML A1002 1555 1555 1.95
LINK NA NA A1003 O HOH A1927 1555 1555 2.48
LINK NA NA A1003 O HOH A2214 1555 1555 2.41
LINK NA NA A1003 O HOH A2302 1555 1555 2.30
LINK NA NA A1004 O HOH A1322 1555 1555 2.49
LINK NA NA A1004 O HOH A1559 1555 1555 2.23
LINK NA NA A1004 O HOH A2247 1555 1555 2.28
LINK NA NA A1004 O HOH A2291 1555 1555 2.27
LINK NA NA A1004 O HOH A2587 1555 1555 3.15
LINK NA NA A1005 O HOH A1882 1555 1555 2.37
LINK NA NA A1005 O HOH A2060 1555 1555 2.50
LINK NA NA A1005 O HOH A2145 1555 1555 2.33
LINK NA NA A1005 O HOH A2340 1555 1555 2.73
LINK NA NA A1005 O HOH A2806 1555 1555 2.39
LINK NA NA A1006 O HOH A1145 1555 1555 2.81
LINK NA NA A1006 O HOH A1497 1555 1555 2.85
LINK NA NA A1006 O HOH A1675 1555 1555 2.33
LINK NA NA A1006 O HOH A1872 1555 1555 2.42
LINK NA NA A1006 O HOH A2314 1555 1555 2.51
LINK NA NA A1007 O HOH A1555 1555 1555 2.43
LINK NA NA A1007 O HOH A2295 1555 1555 2.36
LINK NA NA A1007 O HOH A2330 1555 1555 3.02
LINK NA NA A1007 O HOH A2508 1555 1555 2.20
LINK NA NA A1008 O HOH A1154 1555 1555 2.00
LINK NA NA A1008 O HOH A1219 1555 1555 3.17
LINK NA NA A1008 O HOH A1327 1555 1555 3.00
LINK NA NA A1008 O HOH A1535 1555 1555 3.11
LINK NA NA A1008 O HOH A1605 1555 1555 2.52
LINK NA NA A1008 O HOH A2314 1555 1555 3.08
LINK NA NA A1008 O HOH A2481 1555 1555 1.97
LINK NA NA A1009 O HOH A2262 1555 1555 2.39
LINK NA NA A1009 O HOH A2378 1555 1555 2.94
LINK NA NA A1009 O HOH A2400 1555 1555 2.18
LINK NA NA A1009 O HOH A2449 1555 1555 2.57
LINK NA NA A1010 O AHOH A1607 1555 1555 2.73
LINK NA NA A1010 O HOH A2249 1555 1555 2.56
LINK NA NA A1010 O HOH A2586 1555 1555 2.40
LINK NA NA A1011 O HOH A1293 1555 1555 2.22
LINK NA NA A1011 O HOH A1843 1555 1555 2.61
LINK NA NA A1011 O HOH A2225 1555 1555 2.56
LINK NA NA A1011 O HOH A2265 1555 1555 2.39
LINK NA NA A1011 O HOH A2783 1555 1555 2.17
CISPEP 1 GLU A 121 ALA A 122 0 1.07
SITE 1 AC1 4 HIS A 297 HIS A 301 GLU A 320 7ML A1002
SITE 1 AC2 13 GLU A 121 MET A 260 ALA A 262 GLU A 264
SITE 2 AC2 13 ARG A 293 HIS A 297 GLU A 298 HIS A 301
SITE 3 AC2 13 LYS A 319 GLU A 320 TYR A 381 ZN A1001
SITE 4 AC2 13 MLI A1012
SITE 1 AC3 6 SER A 332 ASP A 333 GLY A 335 HOH A1927
SITE 2 AC3 6 HOH A2214 HOH A2302
SITE 1 AC4 6 HIS A 771 PHE A 774 HOH A1322 HOH A1559
SITE 2 AC4 6 HOH A2247 HOH A2291
SITE 1 AC5 6 SER A 508 HOH A1882 HOH A2060 HOH A2145
SITE 2 AC5 6 HOH A2340 HOH A2806
SITE 1 AC6 7 GLU A 123 GLU A 371 HOH A1145 HOH A1497
SITE 2 AC6 7 HOH A1675 HOH A1872 HOH A2314
SITE 1 AC7 6 ASP A 452 TYR A 544 HOH A1555 HOH A2295
SITE 2 AC7 6 HOH A2330 HOH A2508
SITE 1 AC8 6 GLU A 371 HOH A1154 HOH A1327 HOH A1605
SITE 2 AC8 6 HOH A2314 HOH A2481
SITE 1 AC9 6 ASN A 67 THR A 91 HOH A2262 HOH A2378
SITE 2 AC9 6 HOH A2400 HOH A2449
SITE 1 AD1 6 ASN A 511 THR A 513 GLN A 517 HOH A1607
SITE 2 AD1 6 HOH A2249 HOH A2586
SITE 1 AD2 6 ASP A 452 HOH A1293 HOH A1843 HOH A2225
SITE 2 AD2 6 HOH A2265 HOH A2783
SITE 1 AD3 9 TYR A 376 THR A 377 LEU A 378 TYR A 381
SITE 2 AD3 9 GLU A 382 ARG A 825 7ML A1002 GOL A1038
SITE 3 AD3 9 HOH A1160
SITE 1 AD4 8 SER A 205 LYS A 577 LEU A 628 PHE A 629
SITE 2 AD4 8 ASP A 630 HOH A1103 HOH A1396 HOH A2492
SITE 1 AD5 9 ALA A 531 LEU A 532 TRP A 546 LEU A 551
SITE 2 AD5 9 ASP A 566 ALA A 567 SER A 570 HOH A1133
SITE 3 AD5 9 HOH A1175
SITE 1 AD6 11 GLY A 396 GLU A 397 GLU A 398 HOH A1169
SITE 2 AD6 11 HOH A1171 HOH A1223 HOH A1432 HOH A1437
SITE 3 AD6 11 HOH A1946 HOH A1952 HOH A2539
SITE 1 AD7 10 GLU A 123 TRP A 313 PHE A 314 VAL A 369
SITE 2 AD7 10 MET A 372 HOH A1145 HOH A1189 HOH A1239
SITE 3 AD7 10 HOH A1261 HOH A1719
SITE 1 AD8 4 THR A 393 GLU A 535 HOH A1214 HOH A2077
SITE 1 AD9 5 GLU A 627 PHE A 629 ASP A 630 ARG A 835
SITE 2 AD9 5 HOH A1119
SITE 1 AE1 6 THR A 393 LEU A 394 LEU A 395 GLY A 396
SITE 2 AE1 6 ASN A 507 HOH A1796
SITE 1 AE2 5 ASP A 28 LEU A 29 ASP A 30 LYS A 33
SITE 2 AE2 5 ARG A 171
SITE 1 AE3 6 ARG A 14 ALA A 15 PRO A 16 ASP A 17
SITE 2 AE3 6 HOH A2601 HOH A2779
SITE 1 AE4 4 ASP A 216 ALA A 254 SER A 273 HOH A1749
SITE 1 AE5 5 LEU A 617 LEU A 619 HOH A1578 HOH A1730
SITE 2 AE5 5 HOH A1840
SITE 1 AE6 4 GLU A 800 ASP A 801 HOH A1870 HOH A2464
SITE 1 AE7 4 ALA A 31 GLN A 32 HOH A1426 HOH A2004
SITE 1 AE8 5 GLU A 292 VAL A 670 HIS A 672 HOH A1167
SITE 2 AE8 5 HOH A1784
SITE 1 AE9 8 ARG A 681 GLN A 703 ALA A 707 ASN A 708
SITE 2 AE9 8 ASN A 709 ASP A 712 HOH A1333 HOH A1909
SITE 1 AF1 7 PHE A 704 LYS A 738 TRP A 739 HOH A1141
SITE 2 AF1 7 HOH A1307 HOH A1667 HOH A2123
SITE 1 AF2 6 TRP A 74 LYS A 75 HOH A1130 HOH A1397
SITE 2 AF2 6 HOH A1585 HOH A1876
SITE 1 AF3 8 LEU A 61 VAL A 62 TRP A 74 ARG A 669
SITE 2 AF3 8 GLU A 671 HOH A1155 HOH A1397 HOH A1973
SITE 1 AF4 6 ASP A 58 LEU A 59 ILE A 98 HOH A1274
SITE 2 AF4 6 HOH A1704 HOH A1992
SITE 1 AF5 5 ASP A 68 GLU A 69 ARG A 279 ASP A 281
SITE 2 AF5 5 HOH A1157
SITE 1 AF6 8 SER A 112 ALA A 115 PHE A 194 ASP A 216
SITE 2 AF6 8 ALA A 254 VAL A 255 ASP A 256 HOH A1158
SITE 1 AF7 10 MET A 368 PRO A 473 ASP A 474 ALA A 476
SITE 2 AF7 10 HOH A1122 HOH A1328 HOH A1359 HOH A1888
SITE 3 AF7 10 HOH A1919 HOH A2018
SITE 1 AF8 13 HIS A 11 ASP A 12 ARG A 468 THR A 469
SITE 2 AF8 13 LYS A 478 GLN A 479 HOH A1312 HOH A1590
SITE 3 AF8 13 HOH A1779 HOH A1788 HOH A1846 HOH A2158
SITE 4 AF8 13 HOH A2312
SITE 1 AF9 14 ARG A 293 VAL A 324 ASP A 327 GLN A 328
SITE 2 AF9 14 ASN A 344 GLU A 382 GOL A1038 HOH A1128
SITE 3 AF9 14 HOH A1160 HOH A1217 HOH A1269 HOH A1734
SITE 4 AF9 14 HOH A1823 HOH A1880
SITE 1 AG1 5 ASN A 623 GLY A 791 HOH A1129 HOH A1257
SITE 2 AG1 5 HOH A1634
SITE 1 AG2 6 TYR A 275 ARG A 293 MLI A1012 GOL A1036
SITE 2 AG2 6 HOH A1114 HOH A1160
SITE 1 AG3 10 VAL A 622 ALA A 638 THR A 755 SER A 792
SITE 2 AG3 10 ASN A 793 HOH A1179 HOH A1488 HOH A1606
SITE 3 AG3 10 HOH A1966 HOH A2033
CRYST1 120.827 120.827 170.628 90.00 90.00 120.00 P 31 2 1 6
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 0.008276 0.004778 0.000000 0.00000
SCALE2 0.000000 0.009557 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005861 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
