HEADER HYDROLASE/HYDROLASE INHIBITOR 22-OCT-15 5EEI
TITLE CRYSTAL STRUCTURE OF DANIO RERIO HISTONE DEACETYLASE 6 CATALYTIC
TITLE 2 DOMAIN 2 IN COMPLEX WITH SAHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HDAC6 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN 2 (UNP RESIDUES 288-646);
COMPND 5 SYNONYM: HISTONE DEACETYLASE 6;
COMPND 6 EC: 3.5.1.98;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DANIO RERIO;
SOURCE 3 ORGANISM_COMMON: ZEBRAFISH;
SOURCE 4 ORGANISM_TAXID: 7955;
SOURCE 5 GENE: HDAC6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.HAI,D.W.CHRISTIANSON
REVDAT 6 27-SEP-23 5EEI 1 LINK
REVDAT 5 25-DEC-19 5EEI 1 REMARK
REVDAT 4 13-SEP-17 5EEI 1 REMARK
REVDAT 3 07-SEP-16 5EEI 1 JRNL
REVDAT 2 10-AUG-16 5EEI 1 JRNL
REVDAT 1 27-JUL-16 5EEI 0
JRNL AUTH Y.HAI,D.W.CHRISTIANSON
JRNL TITL HISTONE DEACETYLASE 6 STRUCTURE AND MOLECULAR BASIS OF
JRNL TITL 2 CATALYSIS AND INHIBITION.
JRNL REF NAT.CHEM.BIOL. V. 12 741 2016
JRNL REFN ESSN 1552-4469
JRNL PMID 27454933
JRNL DOI 10.1038/NCHEMBIO.2134
REMARK 2
REMARK 2 RESOLUTION. 1.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.3_1479
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) : 1.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 3 NUMBER OF REFLECTIONS : 170604
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.126
REMARK 3 R VALUE (WORKING SET) : 0.125
REMARK 3 FREE R VALUE : 0.148
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 8573
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 36.2717 - 4.0997 0.98 5760 306 0.1381 0.1431
REMARK 3 2 4.0997 - 3.2547 0.99 5766 290 0.1240 0.1311
REMARK 3 3 3.2547 - 2.8435 0.99 5754 279 0.1301 0.1452
REMARK 3 4 2.8435 - 2.5836 0.99 5681 293 0.1236 0.1411
REMARK 3 5 2.5836 - 2.3984 0.98 5649 295 0.1123 0.1265
REMARK 3 6 2.3984 - 2.2571 0.98 5617 313 0.1065 0.1233
REMARK 3 7 2.2571 - 2.1440 0.98 5627 288 0.1066 0.1344
REMARK 3 8 2.1440 - 2.0507 0.97 5562 291 0.1074 0.1319
REMARK 3 9 2.0507 - 1.9718 0.97 5560 302 0.1093 0.1340
REMARK 3 10 1.9718 - 1.9037 0.96 5532 301 0.1101 0.1379
REMARK 3 11 1.9037 - 1.8442 0.96 5480 301 0.1108 0.1413
REMARK 3 12 1.8442 - 1.7915 0.95 5439 309 0.1070 0.1358
REMARK 3 13 1.7915 - 1.7443 0.95 5417 294 0.1082 0.1515
REMARK 3 14 1.7443 - 1.7018 0.94 5402 279 0.1100 0.1468
REMARK 3 15 1.7018 - 1.6631 0.94 5400 270 0.1069 0.1636
REMARK 3 16 1.6631 - 1.6277 0.94 5363 292 0.1038 0.1599
REMARK 3 17 1.6277 - 1.5951 0.93 5421 257 0.1125 0.1469
REMARK 3 18 1.5951 - 1.5650 0.93 5271 283 0.1121 0.1440
REMARK 3 19 1.5650 - 1.5371 0.93 5323 302 0.1177 0.1710
REMARK 3 20 1.5371 - 1.5110 0.93 5263 276 0.1292 0.1652
REMARK 3 21 1.5110 - 1.4867 0.92 5278 285 0.1339 0.1756
REMARK 3 22 1.4867 - 1.4638 0.92 5284 262 0.1504 0.1954
REMARK 3 23 1.4638 - 1.4423 0.92 5181 279 0.1656 0.1945
REMARK 3 24 1.4423 - 1.4219 0.91 5291 259 0.1792 0.2302
REMARK 3 25 1.4219 - 1.4027 0.91 5142 315 0.1981 0.2408
REMARK 3 26 1.4027 - 1.3845 0.91 5226 267 0.2021 0.2376
REMARK 3 27 1.3845 - 1.3672 0.91 5174 274 0.2140 0.2347
REMARK 3 28 1.3672 - 1.3507 0.90 5184 274 0.2306 0.2590
REMARK 3 29 1.3507 - 1.3350 0.90 5171 280 0.2381 0.2673
REMARK 3 30 1.3350 - 1.3200 0.84 4813 257 0.2582 0.2982
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 5974
REMARK 3 ANGLE : 1.323 8137
REMARK 3 CHIRALITY : 0.079 882
REMARK 3 PLANARITY : 0.007 1066
REMARK 3 DIHEDRAL : 14.178 2230
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 5EEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214786.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.28184
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 170725
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.320
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 (%) : 95.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 1.17000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: PDB ENTRY 4CBT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 6.5, 0.2 M
REMARK 280 MAGNESIUM CHLORIDE, 25% PEG5000 MME, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 294K
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 41.77550
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 435
REMARK 465 ASN A 436
REMARK 465 ALA A 437
REMARK 465 GLY A 438
REMARK 465 GLY A 439
REMARK 465 SER A 440
REMARK 465 SER A 441
REMARK 465 SER B 435
REMARK 465 ASN B 436
REMARK 465 ALA B 437
REMARK 465 GLY B 438
REMARK 465 GLY B 439
REMARK 465 SER B 440
REMARK 465 SER B 441
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 ARG A 524 CD NE CZ NH1 NH2
REMARK 470 ARG B 524 CD NE CZ NH1 NH2
REMARK 470 LYS B 658 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 C ALA A 564 H VAL A 565 1.30
REMARK 500 C PRO B 467 H GLN B 468 1.31
REMARK 500 OE1 GLN A 728 O HOH A 2101 1.90
REMARK 500 O HOH A 2287 O HOH A 2382 2.17
REMARK 500 OE1 GLN A 560 O HOH A 2102 2.19
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 THR A 600 -84.39 -131.22
REMARK 500 TYR A 637 -53.58 -129.82
REMARK 500 LEU A 685 -63.80 -125.77
REMARK 500 GLU A 742 -112.68 -110.70
REMARK 500 THR B 600 -88.28 -130.63
REMARK 500 TYR B 637 -50.70 -130.32
REMARK 500 LEU B 685 -63.21 -125.34
REMARK 500 ALA B 694 60.18 61.10
REMARK 500 GLU B 742 -113.08 -111.30
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 B1194 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B1195 DISTANCE = 7.09 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 K A2002 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 610 O
REMARK 620 2 ASP A 610 OD1 71.3
REMARK 620 3 ASP A 612 O 98.9 96.5
REMARK 620 4 HIS A 614 O 164.1 93.0 79.8
REMARK 620 5 SER A 633 OG 85.0 110.4 152.6 103.6
REMARK 620 6 LEU A 634 O 76.7 141.7 68.0 116.7 86.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 612 OD1
REMARK 620 2 ASP A 612 OD2 53.6
REMARK 620 3 HIS A 614 ND1 100.7 154.4
REMARK 620 4 ASP A 705 OD2 107.4 89.1 99.2
REMARK 620 5 SHH A2004 O1 83.9 83.5 95.9 158.9
REMARK 620 6 SHH A2004 O2 156.4 111.9 92.5 89.4 75.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A2003 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 623 O
REMARK 620 2 ASP A 626 O 75.2
REMARK 620 3 VAL A 629 O 119.0 77.4
REMARK 620 4 TYR A 662 O 154.9 119.1 85.4
REMARK 620 5 HOH A2239 O 80.2 88.6 151.3 79.7
REMARK 620 6 HOH A2244 O 70.3 145.1 124.2 91.8 80.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 803 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 610 O
REMARK 620 2 ASP B 610 OD1 71.1
REMARK 620 3 ASP B 612 O 100.4 97.2
REMARK 620 4 HIS B 614 O 164.0 93.0 78.8
REMARK 620 5 SER B 633 OG 84.6 109.5 152.8 103.5
REMARK 620 6 LEU B 634 O 77.9 142.8 68.3 115.8 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 802 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 612 OD1
REMARK 620 2 ASP B 612 OD2 55.2
REMARK 620 3 HIS B 614 ND1 99.4 154.5
REMARK 620 4 ASP B 705 OD2 108.0 90.6 97.1
REMARK 620 5 SHH B 801 O1 85.8 85.8 94.4 160.1
REMARK 620 6 SHH B 801 O2 157.9 112.9 91.4 89.4 74.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 804 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 623 O
REMARK 620 2 ASP B 626 O 75.3
REMARK 620 3 VAL B 629 O 118.3 77.3
REMARK 620 4 TYR B 662 O 155.3 118.9 85.6
REMARK 620 5 HOH B 967 O 81.0 89.6 151.9 79.2
REMARK 620 6 HOH B1024 O 70.5 145.4 123.5 92.0 80.8
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 ZN A 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SHH A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 2010
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SHH B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 809
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5EDU RELATED DB: PDB
REMARK 900 RELATED ID: 5EEF RELATED DB: PDB
REMARK 900 RELATED ID: 5EEK RELATED DB: PDB
REMARK 900 RELATED ID: 5EEM RELATED DB: PDB
REMARK 900 RELATED ID: 5EEN RELATED DB: PDB
REMARK 900 RELATED ID: 5EF7 RELATED DB: PDB
REMARK 900 RELATED ID: 5EF8 RELATED DB: PDB
REMARK 900 RELATED ID: 5EFB RELATED DB: PDB
REMARK 900 RELATED ID: 5EFG RELATED DB: PDB
REMARK 900 RELATED ID: 5EFH RELATED DB: PDB
REMARK 900 RELATED ID: 5EFJ RELATED DB: PDB
REMARK 900 RELATED ID: 5EFK RELATED DB: PDB
REMARK 900 RELATED ID: 5EFN RELATED DB: PDB
DBREF 5EEI A 440 798 UNP A7YT55 A7YT55_DANRE 288 646
DBREF 5EEI B 440 798 UNP A7YT55 A7YT55_DANRE 288 646
SEQADV 5EEI SER A 435 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI ASN A 436 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI ALA A 437 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI GLY A 438 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI GLY A 439 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI SER B 435 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI ASN B 436 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI ALA B 437 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI GLY B 438 UNP A7YT55 EXPRESSION TAG
SEQADV 5EEI GLY B 439 UNP A7YT55 EXPRESSION TAG
SEQRES 1 A 364 SER ASN ALA GLY GLY SER SER PRO ILE THR GLY LEU VAL
SEQRES 2 A 364 TYR ASP GLN ARG MET MET LEU HIS HIS ASN MET TRP ASP
SEQRES 3 A 364 SER HIS HIS PRO GLU LEU PRO GLN ARG ILE SER ARG ILE
SEQRES 4 A 364 PHE SER ARG HIS GLU GLU LEU ARG LEU LEU SER ARG CYS
SEQRES 5 A 364 HIS ARG ILE PRO ALA ARG LEU ALA THR GLU GLU GLU LEU
SEQRES 6 A 364 ALA LEU CYS HIS SER SER LYS HIS ILE SER ILE ILE LYS
SEQRES 7 A 364 SER SER GLU HIS MET LYS PRO ARG ASP LEU ASN ARG LEU
SEQRES 8 A 364 GLY ASP GLU TYR ASN SER ILE PHE ILE SER ASN GLU SER
SEQRES 9 A 364 TYR THR CYS ALA LEU LEU ALA ALA GLY SER CYS PHE ASN
SEQRES 10 A 364 SER ALA GLN ALA ILE LEU THR GLY GLN VAL ARG ASN ALA
SEQRES 11 A 364 VAL ALA ILE VAL ARG PRO PRO GLY HIS HIS ALA GLU LYS
SEQRES 12 A 364 ASP THR ALA CYS GLY PHE CYS PHE PHE ASN THR ALA ALA
SEQRES 13 A 364 LEU THR ALA ARG TYR ALA GLN SER ILE THR ARG GLU SER
SEQRES 14 A 364 LEU ARG VAL LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY
SEQRES 15 A 364 ASN GLY THR GLN HIS ILE PHE GLU GLU ASP ASP SER VAL
SEQRES 16 A 364 LEU TYR ILE SER LEU HIS ARG TYR GLU ASP GLY ALA PHE
SEQRES 17 A 364 PHE PRO ASN SER GLU ASP ALA ASN TYR ASP LYS VAL GLY
SEQRES 18 A 364 LEU GLY LYS GLY ARG GLY TYR ASN VAL ASN ILE PRO TRP
SEQRES 19 A 364 ASN GLY GLY LYS MET GLY ASP PRO GLU TYR MET ALA ALA
SEQRES 20 A 364 PHE HIS HIS LEU VAL MET PRO ILE ALA ARG GLU PHE ALA
SEQRES 21 A 364 PRO GLU LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA
SEQRES 22 A 364 ARG GLY ASP PRO LEU GLY GLY PHE GLN VAL THR PRO GLU
SEQRES 23 A 364 GLY TYR ALA HIS LEU THR HIS GLN LEU MET SER LEU ALA
SEQRES 24 A 364 ALA GLY ARG VAL LEU ILE ILE LEU GLU GLY GLY TYR ASN
SEQRES 25 A 364 LEU THR SER ILE SER GLU SER MET SER MET CYS THR SER
SEQRES 26 A 364 MET LEU LEU GLY ASP SER PRO PRO SER LEU ASP HIS LEU
SEQRES 27 A 364 THR PRO LEU LYS THR SER ALA THR VAL SER ILE ASN ASN
SEQRES 28 A 364 VAL LEU ARG ALA HIS ALA PRO PHE TRP SER SER LEU ARG
SEQRES 1 B 364 SER ASN ALA GLY GLY SER SER PRO ILE THR GLY LEU VAL
SEQRES 2 B 364 TYR ASP GLN ARG MET MET LEU HIS HIS ASN MET TRP ASP
SEQRES 3 B 364 SER HIS HIS PRO GLU LEU PRO GLN ARG ILE SER ARG ILE
SEQRES 4 B 364 PHE SER ARG HIS GLU GLU LEU ARG LEU LEU SER ARG CYS
SEQRES 5 B 364 HIS ARG ILE PRO ALA ARG LEU ALA THR GLU GLU GLU LEU
SEQRES 6 B 364 ALA LEU CYS HIS SER SER LYS HIS ILE SER ILE ILE LYS
SEQRES 7 B 364 SER SER GLU HIS MET LYS PRO ARG ASP LEU ASN ARG LEU
SEQRES 8 B 364 GLY ASP GLU TYR ASN SER ILE PHE ILE SER ASN GLU SER
SEQRES 9 B 364 TYR THR CYS ALA LEU LEU ALA ALA GLY SER CYS PHE ASN
SEQRES 10 B 364 SER ALA GLN ALA ILE LEU THR GLY GLN VAL ARG ASN ALA
SEQRES 11 B 364 VAL ALA ILE VAL ARG PRO PRO GLY HIS HIS ALA GLU LYS
SEQRES 12 B 364 ASP THR ALA CYS GLY PHE CYS PHE PHE ASN THR ALA ALA
SEQRES 13 B 364 LEU THR ALA ARG TYR ALA GLN SER ILE THR ARG GLU SER
SEQRES 14 B 364 LEU ARG VAL LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY
SEQRES 15 B 364 ASN GLY THR GLN HIS ILE PHE GLU GLU ASP ASP SER VAL
SEQRES 16 B 364 LEU TYR ILE SER LEU HIS ARG TYR GLU ASP GLY ALA PHE
SEQRES 17 B 364 PHE PRO ASN SER GLU ASP ALA ASN TYR ASP LYS VAL GLY
SEQRES 18 B 364 LEU GLY LYS GLY ARG GLY TYR ASN VAL ASN ILE PRO TRP
SEQRES 19 B 364 ASN GLY GLY LYS MET GLY ASP PRO GLU TYR MET ALA ALA
SEQRES 20 B 364 PHE HIS HIS LEU VAL MET PRO ILE ALA ARG GLU PHE ALA
SEQRES 21 B 364 PRO GLU LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA
SEQRES 22 B 364 ARG GLY ASP PRO LEU GLY GLY PHE GLN VAL THR PRO GLU
SEQRES 23 B 364 GLY TYR ALA HIS LEU THR HIS GLN LEU MET SER LEU ALA
SEQRES 24 B 364 ALA GLY ARG VAL LEU ILE ILE LEU GLU GLY GLY TYR ASN
SEQRES 25 B 364 LEU THR SER ILE SER GLU SER MET SER MET CYS THR SER
SEQRES 26 B 364 MET LEU LEU GLY ASP SER PRO PRO SER LEU ASP HIS LEU
SEQRES 27 B 364 THR PRO LEU LYS THR SER ALA THR VAL SER ILE ASN ASN
SEQRES 28 B 364 VAL LEU ARG ALA HIS ALA PRO PHE TRP SER SER LEU ARG
HET ZN A2001 1
HET K A2002 1
HET K A2003 1
HET SHH A2004 37
HET GOL A2005 6
HET GOL A2006 6
HET EDO A2007 4
HET CL A2008 1
HET CL A2009 1
HET MG A2010 2
HET CL A2011 1
HET SHH B 801 37
HET ZN B 802 1
HET K B 803 1
HET K B 804 1
HET GOL B 805 6
HET GOL B 806 6
HET CL B 807 1
HET CL B 808 1
HET EDO B 809 4
HETNAM ZN ZINC ION
HETNAM K POTASSIUM ION
HETNAM SHH OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETSYN SHH SAHA
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 K 4(K 1+)
FORMUL 6 SHH 2(C14 H20 N2 O3)
FORMUL 7 GOL 4(C3 H8 O3)
FORMUL 9 EDO 2(C2 H6 O2)
FORMUL 10 CL 5(CL 1-)
FORMUL 12 MG MG 2+
FORMUL 23 HOH *644(H2 O)
HELIX 1 AA1 GLN A 450 HIS A 455 5 6
HELIX 2 AA2 PRO A 467 LEU A 480 1 14
HELIX 3 AA3 LEU A 482 CYS A 486 5 5
HELIX 4 AA4 THR A 495 ALA A 500 1 6
HELIX 5 AA5 SER A 504 SER A 514 1 11
HELIX 6 AA6 GLU A 515 MET A 517 5 3
HELIX 7 AA7 LYS A 518 GLU A 528 1 11
HELIX 8 AA8 GLU A 537 THR A 558 1 22
HELIX 9 AA9 ASN A 587 ILE A 599 1 13
HELIX 10 AB1 GLY A 616 GLU A 624 1 9
HELIX 11 AB2 GLU A 638 ALA A 641 5 4
HELIX 12 AB3 SER A 646 ASN A 650 5 5
HELIX 13 AB4 LEU A 656 ARG A 660 5 5
HELIX 14 AB5 GLY A 674 LEU A 685 1 12
HELIX 15 AB6 LEU A 685 ALA A 694 1 10
HELIX 16 AB7 THR A 718 MET A 730 1 13
HELIX 17 AB8 SER A 731 GLY A 735 5 5
HELIX 18 AB9 ASN A 746 LEU A 762 1 17
HELIX 19 AC1 LYS A 776 ALA A 791 1 16
HELIX 20 AC2 TRP A 794 ARG A 798 5 5
HELIX 21 AC3 ASP B 449 HIS B 455 5 7
HELIX 22 AC4 PRO B 467 LEU B 480 1 14
HELIX 23 AC5 LEU B 482 CYS B 486 5 5
HELIX 24 AC6 THR B 495 ALA B 500 1 6
HELIX 25 AC7 SER B 504 SER B 514 1 11
HELIX 26 AC8 GLU B 515 MET B 517 5 3
HELIX 27 AC9 LYS B 518 ASP B 527 1 10
HELIX 28 AD1 GLU B 537 THR B 558 1 22
HELIX 29 AD2 ASN B 587 ILE B 599 1 13
HELIX 30 AD3 GLY B 616 GLU B 624 1 9
HELIX 31 AD4 GLU B 638 ALA B 641 5 4
HELIX 32 AD5 SER B 646 ASN B 650 5 5
HELIX 33 AD6 LEU B 656 ARG B 660 5 5
HELIX 34 AD7 GLY B 674 LEU B 685 1 12
HELIX 35 AD8 LEU B 685 ALA B 694 1 10
HELIX 36 AD9 THR B 718 MET B 730 1 13
HELIX 37 AE1 SER B 731 GLY B 735 5 5
HELIX 38 AE2 ASN B 746 LEU B 762 1 17
HELIX 39 AE3 LYS B 776 ALA B 791 1 16
HELIX 40 AE4 TRP B 794 ARG B 798 5 5
SHEET 1 AA1 8 HIS A 487 ARG A 488 0
SHEET 2 AA1 8 THR A 444 TYR A 448 1 N THR A 444 O HIS A 487
SHEET 3 AA1 8 ASN A 563 ILE A 567 1 O ASN A 563 N GLY A 445
SHEET 4 AA1 8 VAL A 737 LEU A 741 1 O ILE A 739 N ALA A 566
SHEET 5 AA1 8 LEU A 697 ALA A 702 1 N VAL A 700 O ILE A 740
SHEET 6 AA1 8 VAL A 606 ASP A 610 1 N LEU A 607 O LEU A 699
SHEET 7 AA1 8 VAL A 629 ARG A 636 1 O ILE A 632 N ASP A 610
SHEET 8 AA1 8 ASN A 663 TRP A 668 1 O VAL A 664 N TYR A 631
SHEET 1 AA2 8 HIS B 487 ARG B 488 0
SHEET 2 AA2 8 THR B 444 VAL B 447 1 N THR B 444 O HIS B 487
SHEET 3 AA2 8 ASN B 563 ALA B 566 1 O ASN B 563 N GLY B 445
SHEET 4 AA2 8 VAL B 737 LEU B 741 1 O ILE B 739 N ALA B 566
SHEET 5 AA2 8 LEU B 697 ALA B 702 1 N VAL B 700 O ILE B 740
SHEET 6 AA2 8 VAL B 606 ASP B 610 1 N LEU B 607 O LEU B 699
SHEET 7 AA2 8 VAL B 629 ARG B 636 1 O ILE B 632 N ASP B 610
SHEET 8 AA2 8 ASN B 663 TRP B 668 1 O VAL B 664 N TYR B 631
LINK O ASP A 610 K K A2002 1555 1555 2.81
LINK OD1 ASP A 610 K K A2002 1555 1555 2.72
LINK OD1 ASP A 612 ZN ZN A2001 1555 1555 2.03
LINK OD2 ASP A 612 ZN ZN A2001 1555 1555 2.65
LINK O ASP A 612 K K A2002 1555 1555 2.54
LINK ND1 HIS A 614 ZN ZN A2001 1555 1555 2.14
LINK O HIS A 614 K K A2002 1555 1555 2.73
LINK O PHE A 623 K K A2003 1555 1555 2.69
LINK O ASP A 626 K K A2003 1555 1555 2.90
LINK O VAL A 629 K K A2003 1555 1555 2.66
LINK OG SER A 633 K K A2002 1555 1555 2.73
LINK O LEU A 634 K K A2002 1555 1555 2.70
LINK O TYR A 662 K K A2003 1555 1555 2.81
LINK OD2 ASP A 705 ZN ZN A2001 1555 1555 1.99
LINK O PHE A 793 MG A MG A2010 1555 1555 2.87
LINK ZN ZN A2001 O1 SHH A2004 1555 1555 2.07
LINK ZN ZN A2001 O2 SHH A2004 1555 1555 2.16
LINK K K A2003 O HOH A2239 1555 1555 2.68
LINK K K A2003 O HOH A2244 1555 1555 3.00
LINK O ASP B 610 K K B 803 1555 1555 2.81
LINK OD1 ASP B 610 K K B 803 1555 1555 2.70
LINK OD1 ASP B 612 ZN ZN B 802 1555 1555 2.08
LINK OD2 ASP B 612 ZN ZN B 802 1555 1555 2.58
LINK O ASP B 612 K K B 803 1555 1555 2.56
LINK ND1 HIS B 614 ZN ZN B 802 1555 1555 2.16
LINK O HIS B 614 K K B 803 1555 1555 2.75
LINK O PHE B 623 K K B 804 1555 1555 2.70
LINK O ASP B 626 K K B 804 1555 1555 2.89
LINK O VAL B 629 K K B 804 1555 1555 2.65
LINK OG SER B 633 K K B 803 1555 1555 2.71
LINK O LEU B 634 K K B 803 1555 1555 2.70
LINK O TYR B 662 K K B 804 1555 1555 2.82
LINK OD2 ASP B 705 ZN ZN B 802 1555 1555 1.97
LINK O1 SHH B 801 ZN ZN B 802 1555 1555 2.02
LINK O2 SHH B 801 ZN ZN B 802 1555 1555 2.19
LINK K K B 804 O HOH B 967 1555 1555 2.70
LINK K K B 804 O HOH B1024 1555 1555 3.00
CISPEP 1 ARG A 569 PRO A 570 0 -2.53
CISPEP 2 PHE A 643 PRO A 644 0 9.54
CISPEP 3 ARG B 569 PRO B 570 0 -5.86
CISPEP 4 PHE B 643 PRO B 644 0 7.09
SITE 1 AC1 4 ASP A 612 HIS A 614 ASP A 705 SHH A2004
SITE 1 AC2 5 ASP A 610 ASP A 612 HIS A 614 SER A 633
SITE 2 AC2 5 LEU A 634
SITE 1 AC3 6 PHE A 623 ASP A 626 VAL A 629 TYR A 662
SITE 2 AC3 6 HOH A2239 HOH A2244
SITE 1 AC4 16 PRO A 464 SER A 531 HIS A 573 HIS A 574
SITE 2 AC4 16 PHE A 583 ASP A 612 HIS A 614 PHE A 643
SITE 3 AC4 16 ASP A 705 LEU A 712 TYR A 745 ZN A2001
SITE 4 AC4 16 GOL A2005 GOL A2006 HOH A2229 HOH A2284
SITE 1 AC5 2 SHH A2004 HOH A2115
SITE 1 AC6 8 ALA A 641 PHE A 642 PHE A 643 ASN A 645
SITE 2 AC6 8 SHH A2004 HOH A2108 HOH A2227 HOH A2284
SITE 1 AC7 1 ASN A 784
SITE 1 AC8 3 ARG A 481 LEU A 483 SER A 484
SITE 1 AC9 3 ASN A 785 ARG A 788 HOH A2277
SITE 1 AD1 3 TYR A 662 PHE A 793 TRP A 794
SITE 1 AD2 2 ARG A 476 EDO B 809
SITE 1 AD3 14 PRO B 464 SER B 531 HIS B 573 HIS B 574
SITE 2 AD3 14 PHE B 583 ASP B 612 HIS B 614 PHE B 643
SITE 3 AD3 14 ASP B 705 LEU B 712 TYR B 745 ZN B 802
SITE 4 AD3 14 HOH B 953 HOH B1072
SITE 1 AD4 4 ASP B 612 HIS B 614 ASP B 705 SHH B 801
SITE 1 AD5 5 ASP B 610 ASP B 612 HIS B 614 SER B 633
SITE 2 AD5 5 LEU B 634
SITE 1 AD6 6 PHE B 623 ASP B 626 VAL B 629 TYR B 662
SITE 2 AD6 6 HOH B 967 HOH B1024
SITE 1 AD7 3 ARG B 601 ARG B 605 GLU B 696
SITE 1 AD8 4 ASN A 746 SER A 749 ARG B 476 GLU B 479
SITE 1 AD9 1 CL B 808
SITE 1 AE1 2 ARG B 601 CL B 807
SITE 1 AE2 6 ARG A 476 GLU A 479 CL A2011 GLY B 709
SITE 2 AE2 6 ASN B 746 SER B 749
CRYST1 54.790 83.551 86.806 90.00 98.09 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 0.018252 0.000000 0.002594 0.00000
SCALE2 0.000000 0.011969 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011636 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
