HEADER HYDROLASE/HYDROLASE INHIBITOR 19-MAY-15 4ZW6
TITLE X-RAY CRYSTAL STRUCTURE OF PFA-M1 IN COMPLEX WITH HYDROXAMIC ACID-
TITLE 2 BASED INHIBITOR 9Q
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: M1 FAMILY AMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 195 TO 1084;
COMPND 5 SYNONYM: PFA-M1;
COMPND 6 EC: 3.4.11.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 186763;
SOURCE 4 STRAIN: ISOLATE FCB1 / COLUMBIA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRCHIS-2B
KEYWDS M1 ALANYL-AMINOPEPTIDASE, PROTEASE, INHIBITOR, HYDROXAMIC ACID,
KEYWDS 2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.DRINKWATER,S.MCGOWAN
REVDAT 4 27-SEP-23 4ZW6 1 LINK
REVDAT 3 08-JAN-20 4ZW6 1 REMARK
REVDAT 2 27-SEP-17 4ZW6 1 JRNL REMARK
REVDAT 1 30-MAR-16 4ZW6 0
JRNL AUTH N.DRINKWATER,N.B.VINH,S.N.MISTRY,R.S.BAMERT,C.RUGGERI,
JRNL AUTH 2 J.P.HOLLERAN,S.LOGANATHAN,A.PAIARDINI,S.A.CHARMAN,
JRNL AUTH 3 A.K.POWELL,V.M.AVERY,S.MCGOWAN,P.J.SCAMMELLS
JRNL TITL POTENT DUAL INHIBITORS OF PLASMODIUM FALCIPARUM M1 AND M17
JRNL TITL 2 AMINOPEPTIDASES THROUGH OPTIMIZATION OF S1 POCKET
JRNL TITL 3 INTERACTIONS.
JRNL REF EUR.J.MED.CHEM. V. 110 43 2016
JRNL REFN ISSN 0223-5234
JRNL PMID 26807544
JRNL DOI 10.1016/J.EJMECH.2016.01.015
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.32
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 77491
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 3933
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 33.3251 - 5.7599 1.00 2810 169 0.1607 0.1770
REMARK 3 2 5.7599 - 4.5756 1.00 2711 150 0.1369 0.1526
REMARK 3 3 4.5756 - 3.9983 1.00 2702 127 0.1357 0.1723
REMARK 3 4 3.9983 - 3.6332 1.00 2664 154 0.1483 0.1870
REMARK 3 5 3.6332 - 3.3731 1.00 2669 119 0.1518 0.1595
REMARK 3 6 3.3731 - 3.1744 1.00 2639 146 0.1603 0.2166
REMARK 3 7 3.1744 - 3.0155 1.00 2639 130 0.1707 0.2087
REMARK 3 8 3.0155 - 2.8843 1.00 2626 139 0.1732 0.2143
REMARK 3 9 2.8843 - 2.7733 1.00 2628 144 0.1744 0.2200
REMARK 3 10 2.7733 - 2.6777 1.00 2634 146 0.1755 0.2219
REMARK 3 11 2.6777 - 2.5940 1.00 2614 126 0.1725 0.2043
REMARK 3 12 2.5940 - 2.5199 1.00 2622 149 0.1746 0.2005
REMARK 3 13 2.5199 - 2.4536 1.00 2597 152 0.1760 0.2216
REMARK 3 14 2.4536 - 2.3937 1.00 2642 126 0.1810 0.2340
REMARK 3 15 2.3937 - 2.3393 1.00 2596 127 0.1865 0.2431
REMARK 3 16 2.3393 - 2.2895 1.00 2621 141 0.1867 0.2274
REMARK 3 17 2.2895 - 2.2437 1.00 2607 138 0.1907 0.2435
REMARK 3 18 2.2437 - 2.2014 1.00 2600 126 0.1933 0.2691
REMARK 3 19 2.2014 - 2.1621 1.00 2607 145 0.1924 0.2775
REMARK 3 20 2.1621 - 2.1255 1.00 2581 144 0.1965 0.2436
REMARK 3 21 2.1255 - 2.0912 1.00 2573 160 0.2006 0.2286
REMARK 3 22 2.0912 - 2.0590 1.00 2629 136 0.2175 0.2621
REMARK 3 23 2.0590 - 2.0287 1.00 2561 164 0.2295 0.2819
REMARK 3 24 2.0287 - 2.0002 1.00 2611 128 0.2391 0.2885
REMARK 3 25 2.0002 - 1.9731 1.00 2595 124 0.2461 0.2509
REMARK 3 26 1.9731 - 1.9475 1.00 2588 138 0.2562 0.3122
REMARK 3 27 1.9475 - 1.9232 1.00 2565 151 0.2810 0.3422
REMARK 3 28 1.9232 - 1.9000 1.00 2627 134 0.2982 0.3314
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.78
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 : 0.008 7602
REMARK 3 ANGLE : 1.022 10299
REMARK 3 CHIRALITY : 0.041 1126
REMARK 3 PLANARITY : 0.005 1314
REMARK 3 DIHEDRAL : 13.464 2861
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): 92.6185 113.3785 128.8723
REMARK 3 T TENSOR
REMARK 3 T11: 0.1237 T22: 0.1428
REMARK 3 T33: 0.1140 T12: -0.0034
REMARK 3 T13: 0.0273 T23: 0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 0.5546 L22: 0.9750
REMARK 3 L33: 0.6602 L12: -0.2360
REMARK 3 L13: 0.1054 L23: 0.1767
REMARK 3 S TENSOR
REMARK 3 S11: -0.0857 S12: -0.0321 S13: 0.0140
REMARK 3 S21: 0.0513 S22: 0.0563 S23: -0.0256
REMARK 3 S31: -0.0554 S32: -0.0112 S33: 0.0300
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 4ZW6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SILICON 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77575
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 33.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 1.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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: 3EBG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% (V/V) PEG 8000, 10% (V/V)
REMARK 280 GLYCEROL, 0.1 M TRIS PH 8.5, 0.2 M MGCL2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 37.51500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.32000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.66000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.32000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.51500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.66000
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 GLU A 195
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 205 CD CE NZ
REMARK 470 LYS A 252 CD CE NZ
REMARK 470 ASN A 635 CG OD1 ND2
REMARK 470 GLU A 663 CD OE1 OE2
REMARK 470 LYS A 676 CE NZ
REMARK 470 GLU A 683 CG CD OE1 OE2
REMARK 470 LYS A 790 CG CD CE NZ
REMARK 470 HIS A 815 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 951 CD CE NZ
REMARK 470 LYS A1019 CD CE NZ
REMARK 470 LYS A1075 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 O HOH A 1206 O HOH A 1918 2.07
REMARK 500 O HOH A 1839 O HOH A 1895 2.08
REMARK 500 OE2 GLU A 850 O HOH A 1201 2.14
REMARK 500 O HOH A 1511 O HOH A 1957 2.16
REMARK 500 O HOH A 1744 O HOH A 1763 2.18
REMARK 500 O1 GOL A 1106 O HOH A 1202 2.18
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 311 -113.56 52.38
REMARK 500 GLU A 463 35.35 -88.46
REMARK 500 LEU A 475 -33.93 -131.84
REMARK 500 SER A 549 -71.89 -91.86
REMARK 500 SER A 706 -178.60 -68.03
REMARK 500 PHE A 736 72.57 54.87
REMARK 500 ASP A 974 31.52 -94.22
REMARK 500 VAL A 986 -55.14 -125.28
REMARK 500 LYS A 988 -129.76 49.06
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 A2034 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH A2035 DISTANCE = 6.60 ANGSTROMS
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 ZN A1102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 496 NE2
REMARK 620 2 HIS A 500 NE2 97.6
REMARK 620 3 GLU A 519 OE1 105.4 102.4
REMARK 620 4 4SY A1101 O 113.7 145.0 84.5
REMARK 620 5 4SY A1101 OAG 89.9 91.0 157.9 74.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1104 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 679 OE1
REMARK 620 2 HOH A1493 O 64.9
REMARK 620 3 HOH A1798 O 73.6 65.6
REMARK 620 4 HOH A1941 O 86.7 88.8 152.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1103 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1269 O
REMARK 620 2 HOH A1407 O 82.4
REMARK 620 3 HOH A1787 O 103.7 96.8
REMARK 620 4 HOH A2012 O 157.8 91.8 98.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1105 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1327 O
REMARK 620 2 HOH A1491 O 97.2
REMARK 620 3 HOH A1607 O 93.5 96.4
REMARK 620 4 HOH A1945 O 84.2 178.1 84.8
REMARK 620 5 HOH A2007 O 80.6 89.5 172.2 89.5
REMARK 620 6 HOH A2015 O 165.7 93.2 95.0 85.2 89.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4SY A 1101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 1112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1114
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EBG RELATED DB: PDB
REMARK 900 RELATED ID: 4ZW3 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZW5 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZW7 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZW8 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZX3 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZX4 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZX5 RELATED DB: PDB
REMARK 900 RELATED ID: 4ZX6 RELATED DB: PDB
DBREF 4ZW6 A 195 1084 UNP O96935 AMP1_PLAFQ 195 1084
SEQADV 4ZW6 GLN A 213 UNP O96935 ASN 213 ENGINEERED MUTATION
SEQADV 4ZW6 GLN A 223 UNP O96935 ASN 223 ENGINEERED MUTATION
SEQADV 4ZW6 PRO A 378 UNP O96935 HIS 378 ENGINEERED MUTATION
SEQADV 4ZW6 GLN A 501 UNP O96935 ASN 501 ENGINEERED MUTATION
SEQADV 4ZW6 GLN A 745 UNP O96935 ASN 745 ENGINEERED MUTATION
SEQADV 4ZW6 GLN A 795 UNP O96935 ASN 795 ENGINEERED MUTATION
SEQADV 4ZW6 GLN A 1069 UNP O96935 ASN 1069 ENGINEERED MUTATION
SEQRES 1 A 890 GLU PRO LYS ILE HIS TYR ARG LYS ASP TYR LYS PRO SER
SEQRES 2 A 890 GLY PHE ILE ILE ASN GLN VAL THR LEU ASN ILE ASN ILE
SEQRES 3 A 890 HIS ASP GLN GLU THR ILE VAL ARG SER VAL LEU ASP MET
SEQRES 4 A 890 ASP ILE SER LYS HIS ASN VAL GLY GLU ASP LEU VAL PHE
SEQRES 5 A 890 ASP GLY VAL GLY LEU LYS ILE ASN GLU ILE SER ILE ASN
SEQRES 6 A 890 ASN LYS LYS LEU VAL GLU GLY GLU GLU TYR THR TYR ASP
SEQRES 7 A 890 ASN GLU PHE LEU THR ILE PHE SER LYS PHE VAL PRO LYS
SEQRES 8 A 890 SER LYS PHE ALA PHE SER SER GLU VAL ILE ILE HIS PRO
SEQRES 9 A 890 GLU THR ASN TYR ALA LEU THR GLY LEU TYR LYS SER LYS
SEQRES 10 A 890 ASN ILE ILE VAL SER GLN CYS GLU ALA THR GLY PHE ARG
SEQRES 11 A 890 ARG ILE THR PHE PHE ILE ASP ARG PRO ASP MET MET ALA
SEQRES 12 A 890 LYS TYR ASP VAL THR VAL THR ALA ASP LYS GLU LYS TYR
SEQRES 13 A 890 PRO VAL LEU LEU SER ASN GLY ASP LYS VAL ASN GLU PHE
SEQRES 14 A 890 GLU ILE PRO GLY GLY ARG HIS GLY ALA ARG PHE ASN ASP
SEQRES 15 A 890 PRO PRO LEU LYS PRO CYS TYR LEU PHE ALA VAL VAL ALA
SEQRES 16 A 890 GLY ASP LEU LYS HIS LEU SER ALA THR TYR ILE THR LYS
SEQRES 17 A 890 TYR THR LYS LYS LYS VAL GLU LEU TYR VAL PHE SER GLU
SEQRES 18 A 890 GLU LYS TYR VAL SER LYS LEU GLN TRP ALA LEU GLU CYS
SEQRES 19 A 890 LEU LYS LYS SER MET ALA PHE ASP GLU ASP TYR PHE GLY
SEQRES 20 A 890 LEU GLU TYR ASP LEU SER ARG LEU ASN LEU VAL ALA VAL
SEQRES 21 A 890 SER ASP PHE ASN VAL GLY ALA MET GLU ASN LYS GLY LEU
SEQRES 22 A 890 ASN ILE PHE ASN ALA ASN SER LEU LEU ALA SER LYS LYS
SEQRES 23 A 890 ASN SER ILE ASP PHE SER TYR ALA ARG ILE LEU THR VAL
SEQRES 24 A 890 VAL GLY HIS GLU TYR PHE HIS GLN TYR THR GLY ASN ARG
SEQRES 25 A 890 VAL THR LEU ARG ASP TRP PHE GLN LEU THR LEU LYS GLU
SEQRES 26 A 890 GLY LEU THR VAL HIS ARG GLU ASN LEU PHE SER GLU GLU
SEQRES 27 A 890 MET THR LYS THR VAL THR THR ARG LEU SER HIS VAL ASP
SEQRES 28 A 890 LEU LEU ARG SER VAL GLN PHE LEU GLU ASP SER SER PRO
SEQRES 29 A 890 LEU SER HIS PRO ILE ARG PRO GLU SER TYR VAL SER MET
SEQRES 30 A 890 GLU ASN PHE TYR THR THR THR VAL TYR ASP LYS GLY SER
SEQRES 31 A 890 GLU VAL MET ARG MET TYR LEU THR ILE LEU GLY GLU GLU
SEQRES 32 A 890 TYR TYR LYS LYS GLY PHE ASP ILE TYR ILE LYS LYS ASN
SEQRES 33 A 890 ASP GLY ASN THR ALA THR CYS GLU ASP PHE ASN TYR ALA
SEQRES 34 A 890 MET GLU GLN ALA TYR LYS MET LYS LYS ALA ASP ASN SER
SEQRES 35 A 890 ALA ASN LEU ASN GLN TYR LEU LEU TRP PHE SER GLN SER
SEQRES 36 A 890 GLY THR PRO HIS VAL SER PHE LYS TYR ASN TYR ASP ALA
SEQRES 37 A 890 GLU LYS LYS GLN TYR SER ILE HIS VAL ASN GLN TYR THR
SEQRES 38 A 890 LYS PRO ASP GLU ASN GLN LYS GLU LYS LYS PRO LEU PHE
SEQRES 39 A 890 ILE PRO ILE SER VAL GLY LEU ILE ASN PRO GLU ASN GLY
SEQRES 40 A 890 LYS GLU MET ILE SER GLN THR THR LEU GLU LEU THR LYS
SEQRES 41 A 890 GLU SER ASP THR PHE VAL PHE ASN ASN ILE ALA VAL LYS
SEQRES 42 A 890 PRO ILE PRO SER LEU PHE ARG GLY PHE SER ALA PRO VAL
SEQRES 43 A 890 TYR ILE GLU ASP GLN LEU THR ASP GLU GLU ARG ILE LEU
SEQRES 44 A 890 LEU LEU LYS TYR ASP SER ASP ALA PHE VAL ARG TYR ASN
SEQRES 45 A 890 SER CYS THR ASN ILE TYR MET LYS GLN ILE LEU MET ASN
SEQRES 46 A 890 TYR ASN GLU PHE LEU LYS ALA LYS ASN GLU LYS LEU GLU
SEQRES 47 A 890 SER PHE GLN LEU THR PRO VAL ASN ALA GLN PHE ILE ASP
SEQRES 48 A 890 ALA ILE LYS TYR LEU LEU GLU ASP PRO HIS ALA ASP ALA
SEQRES 49 A 890 GLY PHE LYS SER TYR ILE VAL SER LEU PRO GLN ASP ARG
SEQRES 50 A 890 TYR ILE ILE ASN PHE VAL SER ASN LEU ASP THR ASP VAL
SEQRES 51 A 890 LEU ALA ASP THR LYS GLU TYR ILE TYR LYS GLN ILE GLY
SEQRES 52 A 890 ASP LYS LEU ASN ASP VAL TYR TYR LYS MET PHE LYS SER
SEQRES 53 A 890 LEU GLU ALA LYS ALA ASP ASP LEU THR TYR PHE ASN ASP
SEQRES 54 A 890 GLU SER HIS VAL ASP PHE ASP GLN MET ASN MET ARG THR
SEQRES 55 A 890 LEU ARG ASN THR LEU LEU SER LEU LEU SER LYS ALA GLN
SEQRES 56 A 890 TYR PRO ASN ILE LEU ASN GLU ILE ILE GLU HIS SER LYS
SEQRES 57 A 890 SER PRO TYR PRO SER ASN TRP LEU THR SER LEU SER VAL
SEQRES 58 A 890 SER ALA TYR PHE ASP LYS TYR PHE GLU LEU TYR ASP LYS
SEQRES 59 A 890 THR TYR LYS LEU SER LYS ASP ASP GLU LEU LEU LEU GLN
SEQRES 60 A 890 GLU TRP LEU LYS THR VAL SER ARG SER ASP ARG LYS ASP
SEQRES 61 A 890 ILE TYR GLU ILE LEU LYS LYS LEU GLU ASN GLU VAL LEU
SEQRES 62 A 890 LYS ASP SER LYS ASN PRO ASN ASP ILE ARG ALA VAL TYR
SEQRES 63 A 890 LEU PRO PHE THR ASN ASN LEU ARG ARG PHE HIS ASP ILE
SEQRES 64 A 890 SER GLY LYS GLY TYR LYS LEU ILE ALA GLU VAL ILE THR
SEQRES 65 A 890 LYS THR ASP LYS PHE ASN PRO MET VAL ALA THR GLN LEU
SEQRES 66 A 890 CYS GLU PRO PHE LYS LEU TRP ASN LYS LEU ASP THR LYS
SEQRES 67 A 890 ARG GLN GLU LEU MET LEU ASN GLU MET ASN THR MET LEU
SEQRES 68 A 890 GLN GLU PRO GLN ILE SER ASN ASN LEU LYS GLU TYR LEU
SEQRES 69 A 890 LEU ARG LEU THR ASN LYS
HET 4SY A1101 25
HET ZN A1102 1
HET MG A1103 1
HET MG A1104 1
HET MG A1105 1
HET GOL A1106 6
HET GOL A1107 6
HET GOL A1108 6
HET DMS A1109 4
HET DMS A1110 4
HET DMS A1111 4
HET DMS A1112 4
HET PO4 A1113 5
HET PO4 A1114 5
HETNAM 4SY TERT-BUTYL {(1S)-2-(HYDROXYAMINO)-1-[4-(1-METHYL-1H-
HETNAM 2 4SY PYRAZOL-4-YL)PHENYL]-2-OXOETHYL}CARBAMATE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 4SY C17 H22 N4 O4
FORMUL 3 ZN ZN 2+
FORMUL 4 MG 3(MG 2+)
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 10 DMS 4(C2 H6 O S)
FORMUL 14 PO4 2(O4 P 3-)
FORMUL 16 HOH *835(H2 O)
HELIX 1 AA1 LYS A 202 TYR A 204 5 3
HELIX 2 AA2 SER A 280 VAL A 283 5 4
HELIX 3 AA3 HIS A 297 ASN A 301 5 5
HELIX 4 AA4 GLY A 322 ILE A 326 5 5
HELIX 5 AA5 PRO A 381 PHE A 385 5 5
HELIX 6 AA6 LYS A 417 LYS A 421 5 5
HELIX 7 AA7 LEU A 422 GLY A 441 1 20
HELIX 8 AA8 ASN A 473 LEU A 475 5 3
HELIX 9 AA9 ASP A 484 HIS A 500 1 17
HELIX 10 AB1 ASP A 511 PHE A 513 5 3
HELIX 11 AB2 GLN A 514 LYS A 535 1 22
HELIX 12 AB3 VAL A 537 SER A 557 1 21
HELIX 13 AB4 SER A 570 TYR A 575 5 6
HELIX 14 AB5 THR A 576 ASP A 611 1 36
HELIX 15 AB6 THR A 616 ALA A 633 1 18
HELIX 16 AB7 ASN A 640 TYR A 642 5 3
HELIX 17 AB8 LEU A 643 GLN A 648 1 6
HELIX 18 AB9 THR A 747 ASP A 758 1 12
HELIX 19 AC1 ASP A 760 GLU A 789 1 30
HELIX 20 AC2 ASN A 800 GLU A 812 1 13
HELIX 21 AC3 ASP A 817 VAL A 825 1 9
HELIX 22 AC4 GLN A 829 ILE A 834 1 6
HELIX 23 AC5 ASN A 835 VAL A 837 5 3
HELIX 24 AC6 ASP A 841 LEU A 871 1 31
HELIX 25 AC7 LEU A 871 ASP A 876 1 6
HELIX 26 AC8 ASP A 888 ALA A 908 1 21
HELIX 27 AC9 ASN A 912 SER A 921 1 10
HELIX 28 AD1 TYR A 925 SER A 936 1 12
HELIX 29 AD2 ALA A 937 PHE A 939 5 3
HELIX 30 AD3 LYS A 941 LYS A 954 1 14
HELIX 31 AD4 ASP A 956 ARG A 969 1 14
HELIX 32 AD5 ASP A 974 VAL A 986 1 13
HELIX 33 AD6 ASN A 992 ASN A 1005 1 14
HELIX 34 AD7 ASN A 1006 HIS A 1011 1 6
HELIX 35 AD8 GLY A 1015 LYS A 1030 1 16
HELIX 36 AD9 ASN A 1032 LEU A 1039 1 8
HELIX 37 AE1 CYS A 1040 LEU A 1049 5 10
HELIX 38 AE2 ASP A 1050 GLN A 1066 1 17
HELIX 39 AE3 SER A 1071 THR A 1082 1 12
SHEET 1 AA1 2 HIS A 199 TYR A 200 0
SHEET 2 AA1 2 SER A 567 TYR A 568 -1 O TYR A 568 N HIS A 199
SHEET 1 AA2 8 LYS A 261 LYS A 262 0
SHEET 2 AA2 8 LYS A 252 ILE A 258 -1 N ILE A 258 O LYS A 261
SHEET 3 AA2 8 PHE A 288 ILE A 296 -1 O GLU A 293 N ASN A 254
SHEET 4 AA2 8 THR A 225 ILE A 235 -1 N LEU A 231 O PHE A 290
SHEET 5 AA2 8 PHE A 209 ILE A 220 -1 N ASN A 219 O ILE A 226
SHEET 6 AA2 8 ALA A 337 ASP A 346 1 O THR A 342 N ILE A 218
SHEET 7 AA2 8 ARG A 369 LYS A 380 -1 O PHE A 374 N VAL A 341
SHEET 8 AA2 8 ASP A 358 ILE A 365 -1 N VAL A 360 O ARG A 373
SHEET 1 AA3 3 LEU A 244 ASP A 247 0
SHEET 2 AA3 3 PHE A 275 ILE A 278 -1 O LEU A 276 N PHE A 246
SHEET 3 AA3 3 TYR A 269 TYR A 271 -1 N THR A 270 O THR A 277
SHEET 1 AA4 4 GLY A 306 SER A 310 0
SHEET 2 AA4 4 ILE A 313 GLN A 317 -1 O ILE A 313 N SER A 310
SHEET 3 AA4 4 VAL A 387 GLY A 390 -1 O ALA A 389 N ILE A 314
SHEET 4 AA4 4 VAL A 352 SER A 355 -1 N LEU A 354 O VAL A 388
SHEET 1 AA5 5 LEU A 392 ILE A 400 0
SHEET 2 AA5 5 LYS A 407 GLU A 415 -1 O LEU A 410 N ALA A 397
SHEET 3 AA5 5 ARG A 448 VAL A 454 1 O LEU A 451 N PHE A 413
SHEET 4 AA5 5 LEU A 467 ASN A 471 1 O PHE A 470 N VAL A 452
SHEET 5 AA5 5 ALA A 461 MET A 462 -1 N MET A 462 O ILE A 469
SHEET 1 AA6 2 THR A 508 LEU A 509 0
SHEET 2 AA6 2 THR A 614 ALA A 615 1 O ALA A 615 N THR A 508
SHEET 1 AA7 4 SER A 716 PHE A 721 0
SHEET 2 AA7 4 GLN A 666 TYR A 674 -1 N VAL A 671 O ASP A 717
SHEET 3 AA7 4 HIS A 653 ASP A 661 -1 N HIS A 653 O TYR A 674
SHEET 4 AA7 4 TYR A 741 GLU A 743 1 O TYR A 741 N VAL A 654
SHEET 1 AA8 3 THR A 708 LEU A 712 0
SHEET 2 AA8 3 ILE A 689 ILE A 696 -1 N VAL A 693 O THR A 708
SHEET 3 AA8 3 ILE A 729 LEU A 732 -1 O SER A 731 N GLY A 694
LINK NE2 HIS A 496 ZN ZN A1102 1555 1555 2.12
LINK NE2 HIS A 500 ZN ZN A1102 1555 1555 2.00
LINK OE1 GLU A 519 ZN ZN A1102 1555 1555 2.07
LINK OE1 GLU A 679 MG MG A1104 1555 1555 2.72
LINK O 4SY A1101 ZN ZN A1102 1555 1555 2.10
LINK OAG 4SY A1101 ZN ZN A1102 1555 1555 2.26
LINK MG MG A1103 O HOH A1269 1555 1555 2.57
LINK MG MG A1103 O HOH A1407 1555 1555 2.34
LINK MG MG A1103 O HOH A1787 1555 1555 2.15
LINK MG MG A1103 O HOH A2012 1555 1555 2.35
LINK MG MG A1104 O HOH A1493 1555 1555 2.36
LINK MG MG A1104 O HOH A1798 1555 1555 2.39
LINK MG MG A1104 O HOH A1941 1555 1555 2.73
LINK MG MG A1105 O HOH A1327 1555 1555 2.17
LINK MG MG A1105 O HOH A1491 1555 1555 2.21
LINK MG MG A1105 O HOH A1607 1555 1555 2.02
LINK MG MG A1105 O HOH A1945 1555 1555 2.30
LINK MG MG A1105 O HOH A2007 1555 1555 2.50
LINK MG MG A1105 O HOH A2015 1555 1555 2.20
CISPEP 1 GLU A 319 ALA A 320 0 -2.25
SITE 1 AC1 18 THR A 305 GLU A 319 VAL A 459 GLY A 460
SITE 2 AC1 18 ALA A 461 GLU A 463 ARG A 489 HIS A 496
SITE 3 AC1 18 GLU A 497 HIS A 500 GLU A 519 TYR A 575
SITE 4 AC1 18 TYR A 580 MET A1034 ZN A1102 GOL A1107
SITE 5 AC1 18 HOH A1243 HOH A1721
SITE 1 AC2 4 HIS A 496 HIS A 500 GLU A 519 4SY A1101
SITE 1 AC3 4 HOH A1269 HOH A1407 HOH A1787 HOH A2012
SITE 1 AC4 4 GLU A 679 HOH A1493 HOH A1798 HOH A1941
SITE 1 AC5 6 HOH A1327 HOH A1491 HOH A1607 HOH A1945
SITE 2 AC5 6 HOH A2007 HOH A2015
SITE 1 AC6 11 VAL A 459 GLY A 460 ASN A 471 ASN A 473
SITE 2 AC6 11 SER A 474 ARG A 489 ASN A 994 ARG A 997
SITE 3 AC6 11 HOH A1202 HOH A1252 HOH A1517
SITE 1 AC7 7 TYR A 575 TYR A 580 4SY A1101 HOH A1231
SITE 2 AC7 7 HOH A1253 HOH A1481 HOH A1777
SITE 1 AC8 6 TYR A 853 SER A 903 LEU A 904 DMS A1111
SITE 2 AC8 6 HOH A1669 HOH A1769
SITE 1 AC9 4 ASN A 573 HOH A1253 HOH A1295 HOH A1360
SITE 1 AD1 5 ASP A 758 SER A 759 ALA A 761 ARG A 764
SITE 2 AD1 5 HOH A1979
SITE 1 AD2 5 TYR A 853 THR A 900 SER A 903 LEU A 904
SITE 2 AD2 5 GOL A1108
SITE 1 AD3 3 SER A 822 TYR A 823 THR A 900
SITE 1 AD4 4 VAL A 245 ASP A 247 PHE A 275 HOH A1405
SITE 1 AD5 5 SER A 396 ALA A 397 THR A 398 GLU A 409
SITE 2 AD5 5 TYR A 411
CRYST1 75.030 109.320 118.640 90.00 90.00 90.00 P 21 21 21 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 0.013328 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009147 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008429 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
