HEADER LIGASE 23-FEB-15 4YDQ
TITLE CRYSTAL STRUCTURE OF PROLYL-TRNA SYNTHETASE (PRS) FROM PLASMODIUM
TITLE 2 FALCIPARUM IN COMPLEX WITH HALOFUGINONE AND AMPPNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE--TRNA LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 254-746;
COMPND 5 SYNONYM: PROLYL-TRNA SYNTHETASE, PRORS, KATB, MANGANESE CATALASE;
COMPND 6 EC: 6.1.1.15;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: ISOLATE 3D7;
SOURCE 5 GENE: PRORS, PFL0670C;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM41
KEYWDS PROLYL-TRNA SYNTHETASE, COMPLEX, HALOFUGINONE, MALARIA, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.JAIN,M.YOGAVEL,A.SHARMA
REVDAT 2 08-NOV-23 4YDQ 1 SOURCE KEYWDS JRNL REMARK
REVDAT 2 2 1 LINK
REVDAT 1 20-MAY-15 4YDQ 0
JRNL AUTH V.JAIN,M.YOGAVEL,Y.OSHIMA,H.KIKUCHI,B.TOUQUET,M.A.HAKIMI,
JRNL AUTH 2 A.SHARMA
JRNL TITL STRUCTURE OF PROLYL-TRNA SYNTHETASE-HALOFUGINONE COMPLEX
JRNL TITL 2 PROVIDES BASIS FOR DEVELOPMENT OF DRUGS AGAINST MALARIA AND
JRNL TITL 3 TOXOPLASMOSIS
JRNL REF STRUCTURE V. 23 819 2015
JRNL REFN ISSN 0969-2126
JRNL PMID 25817387
JRNL DOI 10.1016/J.STR.2015.02.011
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX PHENIX.REFINE: 1.8.4_1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.82
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 53965
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2737
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 27.8178 - 6.2128 1.00 2666 124 0.1577 0.1852
REMARK 3 2 6.2128 - 4.9403 1.00 2616 138 0.1594 0.2091
REMARK 3 3 4.9403 - 4.3185 1.00 2591 133 0.1325 0.1621
REMARK 3 4 4.3185 - 3.9248 0.99 2562 154 0.1534 0.1952
REMARK 3 5 3.9248 - 3.6442 1.00 2580 138 0.1639 0.2214
REMARK 3 6 3.6442 - 3.4297 1.00 2547 147 0.1819 0.2191
REMARK 3 7 3.4297 - 3.2582 1.00 2560 146 0.1917 0.2331
REMARK 3 8 3.2582 - 3.1166 1.00 2563 153 0.1970 0.2516
REMARK 3 9 3.1166 - 2.9967 1.00 2571 134 0.2111 0.2297
REMARK 3 10 2.9967 - 2.8935 1.00 2582 133 0.2077 0.2789
REMARK 3 11 2.8935 - 2.8031 1.00 2552 142 0.2230 0.2759
REMARK 3 12 2.8031 - 2.7230 1.00 2581 130 0.2196 0.2701
REMARK 3 13 2.7230 - 2.6514 1.00 2586 122 0.2197 0.3001
REMARK 3 14 2.6514 - 2.5867 1.00 2556 138 0.2273 0.3020
REMARK 3 15 2.5867 - 2.5280 1.00 2548 128 0.2274 0.3675
REMARK 3 16 2.5280 - 2.4742 1.00 2574 131 0.2274 0.3261
REMARK 3 17 2.4742 - 2.4247 0.99 2563 152 0.2308 0.3167
REMARK 3 18 2.4247 - 2.3790 0.99 2523 135 0.2467 0.3119
REMARK 3 19 2.3790 - 2.3366 0.97 2511 127 0.2440 0.2784
REMARK 3 20 2.3366 - 2.2970 0.93 2396 132 0.2544 0.3057
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.78
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 : 0.010 8112
REMARK 3 ANGLE : 1.275 11039
REMARK 3 CHIRALITY : 0.047 1204
REMARK 3 PLANARITY : 0.007 1383
REMARK 3 DIHEDRAL : 15.626 2984
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 4YDQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207282.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : VARI MAX HR MIRRORS
REMARK 200 OPTICS : VARI MAX HR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54085
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.50100
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: 4TWA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 6.5, 2 % (V/V)
REMARK 280 TACSIMATE PH 5.0 AND 12 % (W/V) POLYETHYLENE GLYCOL 3,350.,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 44.46450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 250
REMARK 465 ALA A 251
REMARK 465 ILE A 332
REMARK 465 GLU A 333
REMARK 465 THR A 701
REMARK 465 ASN A 702
REMARK 465 SER A 703
REMARK 465 GLU A 704
REMARK 465 THR A 705
REMARK 465 THR A 706
REMARK 465 LEU A 707
REMARK 465 GLY B 250
REMARK 465 ALA B 251
REMARK 465 LYS B 327
REMARK 465 GLU B 328
REMARK 465 LYS B 329
REMARK 465 ASN B 330
REMARK 465 HIS B 331
REMARK 465 ILE B 332
REMARK 465 GLU B 333
REMARK 465 GLY B 334
REMARK 465 SER B 697
REMARK 465 LEU B 698
REMARK 465 ASN B 699
REMARK 465 GLN B 700
REMARK 465 THR B 701
REMARK 465 ASN B 702
REMARK 465 SER B 703
REMARK 465 GLU B 704
REMARK 465 THR B 705
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 LYS A 257 CD CE NZ
REMARK 470 LYS A 327 CG CD CE NZ
REMARK 470 GLU A 328 CG CD OE1 OE2
REMARK 470 LYS A 329 CG CD CE NZ
REMARK 470 ASN A 330 CG OD1 ND2
REMARK 470 ASP A 347 OD1 OD2
REMARK 470 GLU A 352 CG CD OE1 OE2
REMARK 470 ARG A 373 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 491 CG CD CE NZ
REMARK 470 LYS A 501 CE NZ
REMARK 470 TYR A 547 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 548 CG CD CE NZ
REMARK 470 THR A 550 OG1 CG2
REMARK 470 LYS A 604 CG CD CE NZ
REMARK 470 LYS A 647 CD CE NZ
REMARK 470 LYS A 690 CE NZ
REMARK 470 LYS A 691 CG CD CE NZ
REMARK 470 ASN A 699 CG OD1 ND2
REMARK 470 GLN A 700 CG CD OE1 NE2
REMARK 470 ASN A 726 CG OD1 ND2
REMARK 470 LYS A 728 CE NZ
REMARK 470 LYS B 257 CG CD CE NZ
REMARK 470 ILE B 259 CG1 CG2 CD1
REMARK 470 GLU B 260 CG CD OE1 OE2
REMARK 470 ASP B 347 OD1 OD2
REMARK 470 GLU B 352 CG CD OE1 OE2
REMARK 470 ARG B 373 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 393 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 395 CG CD OE1 NE2
REMARK 470 LYS B 491 CE NZ
REMARK 470 GLU B 497 OE1 OE2
REMARK 470 TYR B 547 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 548 CE NZ
REMARK 470 THR B 549 OG1 CG2
REMARK 470 THR B 550 OG1 CG2
REMARK 470 GLU B 552 CG CD OE1 OE2
REMARK 470 LYS B 560 CD CE NZ
REMARK 470 LYS B 604 CG CD CE NZ
REMARK 470 GLN B 607 CG CD OE1 NE2
REMARK 470 LYS B 625 CD CE NZ
REMARK 470 LYS B 626 CG CD CE NZ
REMARK 470 GLU B 627 CD OE1 OE2
REMARK 470 LYS B 650 CG CD CE NZ
REMARK 470 LYS B 690 CG CD CE NZ
REMARK 470 LYS B 691 CG CD CE NZ
REMARK 470 ARG B 695 CG CD NE CZ NH1 NH2
REMARK 470 THR B 706 OG1 CG2
REMARK 470 LEU B 707 CG CD1 CD2
REMARK 470 ASP B 719 OD1 OD2
REMARK 470 LYS B 728 CG CD CE NZ
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 OG SER B 661 OG SER B 663 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 TRP A 407 CB TRP A 407 CG -0.129
REMARK 500 TRP B 407 CB TRP B 407 CG -0.111
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 PRO B 725 C - N - CA ANGL. DEV. = 9.7 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 LYS A 329 -126.67 51.71
REMARK 500 THR A 359 166.50 173.84
REMARK 500 PHE A 399 -54.49 68.52
REMARK 500 TRP A 407 -178.33 -170.65
REMARK 500 ASP A 496 -164.79 -76.02
REMARK 500 THR A 513 -8.27 -59.46
REMARK 500 SER A 610 -168.12 -122.83
REMARK 500 LYS A 734 173.07 -57.94
REMARK 500 THR B 359 165.91 175.99
REMARK 500 PHE B 399 -54.23 61.02
REMARK 500 LYS B 491 60.18 62.52
REMARK 500 ASP B 525 -166.53 -128.26
REMARK 500 PRO B 725 -39.70 -27.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A 801 O1G
REMARK 620 2 ANP A 801 O2B 73.4
REMARK 620 3 HOH A 940 O 85.1 81.4
REMARK 620 4 HOH A1065 O 96.4 160.7 81.5
REMARK 620 5 HOH A1066 O 161.0 96.4 77.4 88.5
REMARK 620 6 HOH A1070 O 98.3 107.2 171.4 90.2 100.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP B 801 O2G
REMARK 620 2 HOH B1012 O 74.2
REMARK 620 3 HOH B1023 O 62.8 136.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HFG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ANP B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HFG B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TWA RELATED DB: PDB
REMARK 900 4TWA IS APO FORM OF SAME PROTIEN
REMARK 900 RELATED ID: 4HVC RELATED DB: PDB
REMARK 900 4HVC IS HUMAN PROLYL-TRNA SYNTHETASE IN COMPLEX WITH HALOFUGINONE
REMARK 900 AND AMPPNP
DBREF 4YDQ A 254 746 UNP Q8I5R7 SYP_PLAF7 254 746
DBREF 4YDQ B 254 746 UNP Q8I5R7 SYP_PLAF7 254 746
SEQADV 4YDQ GLY A 250 UNP Q8I5R7 EXPRESSION TAG
SEQADV 4YDQ ALA A 251 UNP Q8I5R7 EXPRESSION TAG
SEQADV 4YDQ MET A 252 UNP Q8I5R7 EXPRESSION TAG
SEQADV 4YDQ ALA A 253 UNP Q8I5R7 EXPRESSION TAG
SEQADV 4YDQ GLY B 250 UNP Q8I5R7 EXPRESSION TAG
SEQADV 4YDQ ALA B 251 UNP Q8I5R7 EXPRESSION TAG
SEQADV 4YDQ MET B 252 UNP Q8I5R7 EXPRESSION TAG
SEQADV 4YDQ ALA B 253 UNP Q8I5R7 EXPRESSION TAG
SEQRES 1 A 497 GLY ALA MET ALA ILE THR SER LYS LYS ILE GLU ASN PHE
SEQRES 2 A 497 SER ASP TRP TYR THR GLN VAL ILE VAL LYS SER GLU LEU
SEQRES 3 A 497 ILE GLU TYR TYR ASP ILE SER GLY CYS TYR ILE LEU ARG
SEQRES 4 A 497 PRO ALA ALA TYR TYR ILE TRP GLU CYS VAL GLN ALA PHE
SEQRES 5 A 497 PHE ASN LYS GLU ILE LYS LYS LEU ASN VAL GLU ASN SER
SEQRES 6 A 497 TYR PHE PRO LEU PHE VAL THR LYS ASN LYS LEU GLU LYS
SEQRES 7 A 497 GLU LYS ASN HIS ILE GLU GLY PHE SER PRO GLU VAL ALA
SEQRES 8 A 497 TRP VAL THR LYS TYR GLY ASP SER ASN LEU PRO GLU GLU
SEQRES 9 A 497 ILE ALA ILE ARG PRO THR SER GLU THR ILE MET TYR SER
SEQRES 10 A 497 VAL PHE PRO LYS TRP ILE ARG SER TYR ARG ASP LEU PRO
SEQRES 11 A 497 LEU LYS LEU ASN GLN TRP ASN THR VAL VAL ARG TRP GLU
SEQRES 12 A 497 PHE LYS GLN PRO THR PRO PHE ILE ARG THR ARG GLU PHE
SEQRES 13 A 497 LEU TRP GLN GLU GLY HIS THR ALA HIS LYS ASN GLU GLU
SEQRES 14 A 497 GLU ALA VAL LYS LEU VAL PHE ASP ILE LEU ASP LEU TYR
SEQRES 15 A 497 ARG ARG TRP TYR GLU GLU TYR LEU ALA VAL PRO ILE ILE
SEQRES 16 A 497 LYS GLY ILE LYS SER GLU GLY GLU LYS PHE GLY GLY ALA
SEQRES 17 A 497 ASN PHE THR SER THR ALA GLU ALA PHE ILE SER GLU ASN
SEQRES 18 A 497 GLY ARG ALA ILE GLN ALA ALA THR SER HIS TYR LEU GLY
SEQRES 19 A 497 THR ASN PHE ALA LYS MET PHE LYS ILE GLU PHE GLU ASP
SEQRES 20 A 497 GLU ASN GLU VAL LYS GLN TYR VAL HIS GLN THR SER TRP
SEQRES 21 A 497 GLY CYS THR THR ARG SER ILE GLY ILE MET ILE MET THR
SEQRES 22 A 497 HIS GLY ASP ASP LYS GLY LEU VAL LEU PRO PRO ASN VAL
SEQRES 23 A 497 SER LYS TYR LYS VAL VAL ILE VAL PRO ILE PHE TYR LYS
SEQRES 24 A 497 THR THR ASP GLU ASN ALA ILE HIS SER TYR CYS LYS ASP
SEQRES 25 A 497 ILE GLU LYS ILE LEU LYS ASN ALA GLN ILE ASN CYS VAL
SEQRES 26 A 497 TYR ASP ASP ARG ALA SER TYR SER PRO GLY TYR LYS PHE
SEQRES 27 A 497 ASN HIS TRP GLU LEU ARG GLY ILE PRO ILE ARG ILE GLU
SEQRES 28 A 497 VAL GLY PRO LYS ASP LEU GLN ASN ASN SER CYS VAL ILE
SEQRES 29 A 497 VAL ARG ARG ASP ASN ASN GLU LYS CYS ASN VAL LYS LYS
SEQRES 30 A 497 GLU SER VAL LEU LEU GLU THR GLN GLN MET LEU VAL ASP
SEQRES 31 A 497 ILE HIS LYS ASN LEU PHE LEU LYS ALA LYS LYS LYS LEU
SEQRES 32 A 497 ASP ASP SER ILE VAL GLN VAL THR SER PHE SER GLU VAL
SEQRES 33 A 497 MET ASN ALA LEU ASN LYS LYS LYS MET VAL LEU ALA PRO
SEQRES 34 A 497 TRP CYS GLU ASP ILE ALA THR GLU GLU GLU ILE LYS LYS
SEQRES 35 A 497 GLU THR GLN ARG LEU SER LEU ASN GLN THR ASN SER GLU
SEQRES 36 A 497 THR THR LEU SER GLY ALA MET LYS PRO LEU CYS ILE PRO
SEQRES 37 A 497 LEU ASP GLN PRO PRO MET PRO PRO ASN MET LYS CYS PHE
SEQRES 38 A 497 TRP SER GLY LYS PRO ALA LYS ARG TRP CYS LEU PHE GLY
SEQRES 39 A 497 ARG SER TYR
SEQRES 1 B 497 GLY ALA MET ALA ILE THR SER LYS LYS ILE GLU ASN PHE
SEQRES 2 B 497 SER ASP TRP TYR THR GLN VAL ILE VAL LYS SER GLU LEU
SEQRES 3 B 497 ILE GLU TYR TYR ASP ILE SER GLY CYS TYR ILE LEU ARG
SEQRES 4 B 497 PRO ALA ALA TYR TYR ILE TRP GLU CYS VAL GLN ALA PHE
SEQRES 5 B 497 PHE ASN LYS GLU ILE LYS LYS LEU ASN VAL GLU ASN SER
SEQRES 6 B 497 TYR PHE PRO LEU PHE VAL THR LYS ASN LYS LEU GLU LYS
SEQRES 7 B 497 GLU LYS ASN HIS ILE GLU GLY PHE SER PRO GLU VAL ALA
SEQRES 8 B 497 TRP VAL THR LYS TYR GLY ASP SER ASN LEU PRO GLU GLU
SEQRES 9 B 497 ILE ALA ILE ARG PRO THR SER GLU THR ILE MET TYR SER
SEQRES 10 B 497 VAL PHE PRO LYS TRP ILE ARG SER TYR ARG ASP LEU PRO
SEQRES 11 B 497 LEU LYS LEU ASN GLN TRP ASN THR VAL VAL ARG TRP GLU
SEQRES 12 B 497 PHE LYS GLN PRO THR PRO PHE ILE ARG THR ARG GLU PHE
SEQRES 13 B 497 LEU TRP GLN GLU GLY HIS THR ALA HIS LYS ASN GLU GLU
SEQRES 14 B 497 GLU ALA VAL LYS LEU VAL PHE ASP ILE LEU ASP LEU TYR
SEQRES 15 B 497 ARG ARG TRP TYR GLU GLU TYR LEU ALA VAL PRO ILE ILE
SEQRES 16 B 497 LYS GLY ILE LYS SER GLU GLY GLU LYS PHE GLY GLY ALA
SEQRES 17 B 497 ASN PHE THR SER THR ALA GLU ALA PHE ILE SER GLU ASN
SEQRES 18 B 497 GLY ARG ALA ILE GLN ALA ALA THR SER HIS TYR LEU GLY
SEQRES 19 B 497 THR ASN PHE ALA LYS MET PHE LYS ILE GLU PHE GLU ASP
SEQRES 20 B 497 GLU ASN GLU VAL LYS GLN TYR VAL HIS GLN THR SER TRP
SEQRES 21 B 497 GLY CYS THR THR ARG SER ILE GLY ILE MET ILE MET THR
SEQRES 22 B 497 HIS GLY ASP ASP LYS GLY LEU VAL LEU PRO PRO ASN VAL
SEQRES 23 B 497 SER LYS TYR LYS VAL VAL ILE VAL PRO ILE PHE TYR LYS
SEQRES 24 B 497 THR THR ASP GLU ASN ALA ILE HIS SER TYR CYS LYS ASP
SEQRES 25 B 497 ILE GLU LYS ILE LEU LYS ASN ALA GLN ILE ASN CYS VAL
SEQRES 26 B 497 TYR ASP ASP ARG ALA SER TYR SER PRO GLY TYR LYS PHE
SEQRES 27 B 497 ASN HIS TRP GLU LEU ARG GLY ILE PRO ILE ARG ILE GLU
SEQRES 28 B 497 VAL GLY PRO LYS ASP LEU GLN ASN ASN SER CYS VAL ILE
SEQRES 29 B 497 VAL ARG ARG ASP ASN ASN GLU LYS CYS ASN VAL LYS LYS
SEQRES 30 B 497 GLU SER VAL LEU LEU GLU THR GLN GLN MET LEU VAL ASP
SEQRES 31 B 497 ILE HIS LYS ASN LEU PHE LEU LYS ALA LYS LYS LYS LEU
SEQRES 32 B 497 ASP ASP SER ILE VAL GLN VAL THR SER PHE SER GLU VAL
SEQRES 33 B 497 MET ASN ALA LEU ASN LYS LYS LYS MET VAL LEU ALA PRO
SEQRES 34 B 497 TRP CYS GLU ASP ILE ALA THR GLU GLU GLU ILE LYS LYS
SEQRES 35 B 497 GLU THR GLN ARG LEU SER LEU ASN GLN THR ASN SER GLU
SEQRES 36 B 497 THR THR LEU SER GLY ALA MET LYS PRO LEU CYS ILE PRO
SEQRES 37 B 497 LEU ASP GLN PRO PRO MET PRO PRO ASN MET LYS CYS PHE
SEQRES 38 B 497 TRP SER GLY LYS PRO ALA LYS ARG TRP CYS LEU PHE GLY
SEQRES 39 B 497 ARG SER TYR
HET ANP A 801 31
HET HFG A 802 24
HET MG A 803 1
HET ANP B 801 31
HET HFG B 802 24
HET MG B 803 1
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETNAM HFG 7-BROMO-6-CHLORO-3-{3-[(2R,3S)-3-HYDROXYPIPERIDIN-2-
HETNAM 2 HFG YL]-2-OXOPROPYL}QUINAZOLIN-4(3H)-ONE
HETNAM MG MAGNESIUM ION
HETSYN HFG HALOFUGINONE
FORMUL 3 ANP 2(C10 H17 N6 O12 P3)
FORMUL 4 HFG 2(C16 H17 BR CL N3 O3)
FORMUL 5 MG 2(MG 2+)
FORMUL 9 HOH *333(H2 O)
HELIX 1 AA1 ASN A 261 SER A 273 1 13
HELIX 2 AA2 ARG A 288 LEU A 309 1 22
HELIX 3 AA3 LYS A 322 GLU A 326 1 5
HELIX 4 AA4 PHE A 335 GLU A 338 5 4
HELIX 5 AA5 SER A 360 SER A 366 1 7
HELIX 6 AA6 VAL A 367 ILE A 372 1 6
HELIX 7 AA7 SER A 374 LEU A 378 5 5
HELIX 8 AA8 ASN A 416 ALA A 440 1 25
HELIX 9 AA9 THR A 484 LYS A 491 1 8
HELIX 10 AB1 THR A 513 GLY A 524 1 12
HELIX 11 AB2 PRO A 532 SER A 536 5 5
HELIX 12 AB3 ASP A 551 ALA A 569 1 19
HELIX 13 AB4 SER A 582 ARG A 593 1 12
HELIX 14 AB5 GLY A 602 ASN A 608 1 7
HELIX 15 AB6 SER A 628 SER A 655 1 28
HELIX 16 AB7 SER A 661 SER A 663 5 3
HELIX 17 AB8 GLU A 664 LYS A 671 1 8
HELIX 18 AB9 ALA A 684 LEU A 698 1 15
HELIX 19 AC1 ASN B 261 SER B 273 1 13
HELIX 20 AC2 ARG B 288 LEU B 309 1 22
HELIX 21 AC3 LYS B 322 GLU B 326 1 5
HELIX 22 AC4 PHE B 335 GLU B 338 5 4
HELIX 23 AC5 SER B 360 SER B 366 1 7
HELIX 24 AC6 VAL B 367 ILE B 372 1 6
HELIX 25 AC7 SER B 374 LEU B 378 5 5
HELIX 26 AC8 ASN B 416 TYR B 438 1 23
HELIX 27 AC9 THR B 484 LYS B 491 1 8
HELIX 28 AD1 THR B 513 GLY B 524 1 12
HELIX 29 AD2 PRO B 532 SER B 536 5 5
HELIX 30 AD3 ASP B 551 ALA B 569 1 19
HELIX 31 AD4 SER B 582 ARG B 593 1 12
HELIX 32 AD5 GLY B 602 GLN B 607 1 6
HELIX 33 AD6 SER B 628 ASP B 654 1 27
HELIX 34 AD7 SER B 661 LYS B 671 1 11
HELIX 35 AD8 ALA B 684 LEU B 696 1 13
SHEET 1 AA1 2 ILE A 276 GLU A 277 0
SHEET 2 AA1 2 ILE A 286 LEU A 287 -1 O ILE A 286 N GLU A 277
SHEET 1 AA211 GLU A 312 ASN A 313 0
SHEET 2 AA211 LEU A 380 VAL A 389 1 O LYS A 381 N GLU A 312
SHEET 3 AA211 GLU A 404 HIS A 414 -1 O HIS A 411 N LEU A 382
SHEET 4 AA211 HIS A 505 THR A 512 -1 O HIS A 505 N HIS A 414
SHEET 5 AA211 ARG A 472 GLY A 483 -1 N HIS A 480 O SER A 508
SHEET 6 AA211 PHE A 459 ILE A 467 -1 N SER A 461 O SER A 479
SHEET 7 AA211 ILE A 444 ILE A 447 -1 N ILE A 444 O GLU A 464
SHEET 8 AA211 LYS A 712 PRO A 717 -1 O ILE A 716 N ILE A 447
SHEET 9 AA211 ARG A 738 GLY A 743 -1 O LEU A 741 N LEU A 714
SHEET 10 AA211 MET A 674 TRP A 679 -1 N TRP A 679 O ARG A 738
SHEET 11 AA211 ILE A 656 GLN A 658 1 N VAL A 657 O MET A 674
SHEET 1 AA3 6 PHE A 319 THR A 321 0
SHEET 2 AA3 6 SER A 348 ILE A 356 -1 O ALA A 355 N VAL A 320
SHEET 3 AA3 6 ALA A 340 TYR A 345 -1 N VAL A 342 O ILE A 354
SHEET 4 AA3 6 ALA B 340 TYR B 345 -1 O LYS B 344 N TRP A 341
SHEET 5 AA3 6 SER B 348 ILE B 356 -1 O ILE B 354 N VAL B 342
SHEET 6 AA3 6 PHE B 319 THR B 321 -1 N VAL B 320 O ALA B 355
SHEET 1 AA4 2 GLU A 493 GLU A 495 0
SHEET 2 AA4 2 LYS A 501 TYR A 503 -1 O GLN A 502 N PHE A 494
SHEET 1 AA5 5 CYS A 573 TYR A 575 0
SHEET 2 AA5 5 VAL A 540 PRO A 544 1 N ILE A 542 O VAL A 574
SHEET 3 AA5 5 ILE A 597 VAL A 601 1 O ILE A 599 N VAL A 541
SHEET 4 AA5 5 SER A 610 ARG A 615 -1 O VAL A 612 N GLU A 600
SHEET 5 AA5 5 LYS A 621 LYS A 625 -1 O CYS A 622 N ILE A 613
SHEET 1 AA6 2 ILE B 276 GLU B 277 0
SHEET 2 AA6 2 ILE B 286 LEU B 287 -1 O ILE B 286 N GLU B 277
SHEET 1 AA711 GLU B 312 ASN B 313 0
SHEET 2 AA711 LEU B 380 VAL B 389 1 O LYS B 381 N GLU B 312
SHEET 3 AA711 GLU B 404 HIS B 414 -1 O HIS B 411 N LEU B 382
SHEET 4 AA711 HIS B 505 THR B 512 -1 O TRP B 509 N GLY B 410
SHEET 5 AA711 ARG B 472 GLY B 483 -1 N HIS B 480 O SER B 508
SHEET 6 AA711 PHE B 459 ILE B 467 -1 N ALA B 463 O ALA B 476
SHEET 7 AA711 ILE B 444 ILE B 447 -1 N GLY B 446 O THR B 462
SHEET 8 AA711 LYS B 712 PRO B 717 -1 O ILE B 716 N ILE B 447
SHEET 9 AA711 ARG B 738 GLY B 743 -1 O LEU B 741 N LEU B 714
SHEET 10 AA711 MET B 674 TRP B 679 -1 N ALA B 677 O CYS B 740
SHEET 11 AA711 ILE B 656 GLN B 658 1 N VAL B 657 O MET B 674
SHEET 1 AA8 2 GLU B 493 GLU B 495 0
SHEET 2 AA8 2 LYS B 501 TYR B 503 -1 O GLN B 502 N PHE B 494
SHEET 1 AA9 5 CYS B 573 TYR B 575 0
SHEET 2 AA9 5 VAL B 540 PRO B 544 1 N ILE B 542 O VAL B 574
SHEET 3 AA9 5 ILE B 597 VAL B 601 1 O ILE B 599 N VAL B 543
SHEET 4 AA9 5 SER B 610 ARG B 615 -1 O VAL B 612 N GLU B 600
SHEET 5 AA9 5 LYS B 621 LYS B 625 -1 O CYS B 622 N ILE B 613
LINK O1G ANP A 801 MG MG A 803 1555 1555 1.90
LINK O2B ANP A 801 MG MG A 803 1555 1555 2.17
LINK MG MG A 803 O HOH A 940 1555 1555 2.36
LINK MG MG A 803 O HOH A1065 1555 1555 2.27
LINK MG MG A 803 O HOH A1066 1555 1555 2.00
LINK MG MG A 803 O HOH A1070 1555 1555 1.91
LINK O2G ANP B 801 MG MG B 803 1555 1555 2.15
LINK MG MG B 803 O HOH B1012 1555 1555 2.27
LINK MG MG B 803 O HOH B1023 1555 1555 2.53
CISPEP 1 LEU A 378 PRO A 379 0 1.67
CISPEP 2 LEU B 378 PRO B 379 0 2.61
SITE 1 AC1 19 ARG A 390 GLU A 392 LYS A 394 PHE A 399
SITE 2 AC1 19 ILE A 400 ARG A 401 THR A 402 PHE A 405
SITE 3 AC1 19 GLN A 475 ALA A 477 THR A 478 THR A 512
SITE 4 AC1 19 ARG A 514 HFG A 802 MG A 803 HOH A 940
SITE 5 AC1 19 HOH A1070 HOH A1071 HOH A1072
SITE 1 AC2 16 PHE A 335 VAL A 339 PRO A 358 THR A 359
SITE 2 AC2 16 GLU A 361 ARG A 390 TRP A 407 HIS A 411
SITE 3 AC2 16 PHE A 454 THR A 478 HIS A 480 TRP A 509
SITE 4 AC2 16 GLY A 510 ANP A 801 HOH A1046 HOH A1066
SITE 1 AC3 5 ANP A 801 HOH A 940 HOH A1065 HOH A1066
SITE 2 AC3 5 HOH A1070
SITE 1 AC4 21 ARG B 390 PHE B 399 ILE B 400 ARG B 401
SITE 2 AC4 21 THR B 402 PHE B 405 GLN B 475 ALA B 476
SITE 3 AC4 21 ALA B 477 THR B 478 THR B 512 ARG B 514
SITE 4 AC4 21 HFG B 802 MG B 803 HOH B 944 HOH B1012
SITE 5 AC4 21 HOH B1014 HOH B1023 HOH B1034 HOH B1035
SITE 6 AC4 21 HOH B1036
SITE 1 AC5 15 PHE B 335 VAL B 339 PRO B 358 THR B 359
SITE 2 AC5 15 GLU B 361 ARG B 390 TRP B 407 HIS B 411
SITE 3 AC5 15 PHE B 454 THR B 478 HIS B 480 TRP B 509
SITE 4 AC5 15 GLY B 510 ANP B 801 MG B 803
SITE 1 AC6 5 GLU B 338 ANP B 801 HFG B 802 HOH B1012
SITE 2 AC6 5 HOH B1023
CRYST1 81.026 88.929 86.295 90.00 96.71 90.00 P 1 21 1 4
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 0.012342 0.000000 0.001453 0.00000
SCALE2 0.000000 0.011245 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
