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HEADER HYDROLASE 27-JUL-23 8Q03
TITLE METAGENOMIC LIPASE ORF30
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORF30;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ORF30;
COMPND 7 CHAIN: C;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PHAT2;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 9 ORGANISM_TAXID: 256318;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PHAT2
KEYWDS LIPASE, ESTERASE, METAGENOMIC, ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RANGEL PEREIRA,A.BALAN,M.HYVONEN
REVDAT 1 07-AUG-24 8Q03 0
JRNL AUTH M.RANGEL PEREIRA,A.BALAN,M.HYVONEN
JRNL TITL LIPASES ISOLATED FROM METAGENOMIC LIBRARIES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 159155
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 8017
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 46.6700 - 4.6000 0.94 5624 294 0.1522 0.1682
REMARK 3 2 4.6000 - 3.6500 1.00 5778 317 0.1198 0.1548
REMARK 3 3 3.6500 - 3.1900 1.00 5751 313 0.1337 0.1476
REMARK 3 4 3.1900 - 2.9000 1.00 5776 292 0.1470 0.1779
REMARK 3 5 2.9000 - 2.6900 1.00 5680 295 0.1494 0.1777
REMARK 3 6 2.6900 - 2.5300 1.00 5708 297 0.1445 0.1832
REMARK 3 7 2.5300 - 2.4000 1.00 5718 306 0.1386 0.1731
REMARK 3 8 2.4000 - 2.3000 1.00 5709 291 0.1296 0.1605
REMARK 3 9 2.3000 - 2.2100 1.00 5694 334 0.1251 0.1814
REMARK 3 10 2.2100 - 2.1300 1.00 5693 302 0.1342 0.1683
REMARK 3 11 2.1300 - 2.0700 1.00 5661 294 0.1378 0.1811
REMARK 3 12 2.0700 - 2.0100 1.00 5672 336 0.1337 0.1896
REMARK 3 13 2.0100 - 1.9600 1.00 5664 317 0.1367 0.1708
REMARK 3 14 1.9600 - 1.9100 1.00 5635 298 0.1364 0.1857
REMARK 3 15 1.9100 - 1.8600 1.00 5786 275 0.1337 0.1796
REMARK 3 16 1.8600 - 1.8300 1.00 5612 298 0.1328 0.2037
REMARK 3 17 1.8300 - 1.7900 1.00 5694 313 0.1466 0.2126
REMARK 3 18 1.7900 - 1.7500 1.00 5631 291 0.1570 0.2149
REMARK 3 19 1.7500 - 1.7200 1.00 5715 281 0.1783 0.2343
REMARK 3 20 1.7200 - 1.6900 0.97 5482 294 0.2018 0.2725
REMARK 3 21 1.6900 - 1.6700 0.90 5160 239 0.1836 0.2215
REMARK 3 22 1.6700 - 1.6400 0.85 4758 249 0.1862 0.2403
REMARK 3 23 1.6400 - 1.6200 0.79 4480 249 0.1920 0.2455
REMARK 3 24 1.6200 - 1.5900 0.73 4133 228 0.1969 0.2444
REMARK 3 25 1.5900 - 1.5700 0.68 3831 209 0.2084 0.3072
REMARK 3 26 1.5700 - 1.5500 0.63 3635 172 0.2149 0.2764
REMARK 3 27 1.5500 - 1.5300 0.58 3304 173 0.2373 0.2736
REMARK 3 28 1.5300 - 1.5100 0.53 3009 156 0.2541 0.3028
REMARK 3 29 1.5100 - 1.5000 0.50 2797 155 0.2947 0.3433
REMARK 3 30 1.5000 - 1.4800 0.42 2348 149 0.3816 0.3982
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.169
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.774
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.58
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 : 0.006 7686
REMARK 3 ANGLE : 0.714 10448
REMARK 3 CHIRALITY : 0.076 1082
REMARK 3 PLANARITY : 0.007 1409
REMARK 3 DIHEDRAL : 11.766 2810
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 8Q03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-AUG-23.
REMARK 100 THE DEPOSITION ID IS D_1292131974.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 159190
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 46.670
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 200 DATA REDUNDANCY : 15.00
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.1400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.96800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.200
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.1 M BICINE,
REMARK 280 PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 91.18800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.87100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 91.18800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.87100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 BIOMT1 2 -1.000000 0.000000 0.000000 -36.47167
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 130.36327
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 NH2 ARG C 240 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 765 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 -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 LYS A 4
REMARK 465 MET B -8
REMARK 465 SER B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 LYS B 4
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ALA C 3
REMARK 465 LYS C 4
REMARK 465 THR C 5
REMARK 465 PRO C 6
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 O2 GOL A 401 O HOH A 501 1.82
REMARK 500 O HOH C 535 O HOH C 700 1.82
REMARK 500 O HOH A 792 O HOH C 661 1.84
REMARK 500 O HOH B 720 O HOH B 783 1.88
REMARK 500 O HOH A 769 O HOH A 771 1.89
REMARK 500 O HOH A 849 O HOH C 816 1.90
REMARK 500 O HOH C 717 O HOH C 781 1.94
REMARK 500 O HOH C 705 O HOH C 764 1.97
REMARK 500 O HOH A 749 O HOH A 877 1.99
REMARK 500 O HOH C 767 O HOH C 805 2.02
REMARK 500 O HOH A 820 O HOH A 881 2.04
REMARK 500 O HOH C 839 O HOH C 842 2.05
REMARK 500 O HOH B 551 O HOH B 772 2.05
REMARK 500 O HOH B 794 O HOH B 806 2.05
REMARK 500 OD1 ASN A 250 O HOH A 502 2.05
REMARK 500 OE1 GLU A 158 O HOH A 503 2.06
REMARK 500 O HOH A 795 O HOH A 847 2.06
REMARK 500 O HOH B 759 O HOH B 846 2.08
REMARK 500 O HOH C 767 O HOH C 772 2.08
REMARK 500 O HOH A 505 O HOH B 772 2.09
REMARK 500 O HOH A 632 O HOH A 813 2.09
REMARK 500 O HOH A 840 O HOH A 859 2.10
REMARK 500 O THR A 5 O HOH A 504 2.10
REMARK 500 O HOH C 802 O HOH C 841 2.12
REMARK 500 O HOH A 780 O HOH A 874 2.13
REMARK 500 O HOH A 771 O HOH A 876 2.13
REMARK 500 O HOH A 578 O HOH A 828 2.14
REMARK 500 OH TYR A 248 O HOH A 505 2.15
REMARK 500 O HOH A 753 O HOH A 773 2.15
REMARK 500 O HOH C 720 O HOH C 830 2.16
REMARK 500 O HOH C 622 O HOH C 806 2.16
REMARK 500 O HOH B 565 O HOH B 674 2.16
REMARK 500 NH1 ARG A 52 O HOH A 506 2.17
REMARK 500 OH TYR C 248 O HOH C 501 2.18
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 CZ ARG C 240 NH2 ARG C 240 2556 1.34
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 109 40.08 -148.77
REMARK 500 SER A 170 -116.50 62.44
REMARK 500 SER A 170 -120.93 61.87
REMARK 500 PHE A 199 59.60 31.44
REMARK 500 MET A 206 106.75 84.53
REMARK 500 VAL A 219 -58.09 75.78
REMARK 500 GLN B 109 40.52 -147.37
REMARK 500 SER B 170 -122.13 63.62
REMARK 500 SER B 170 -118.11 58.57
REMARK 500 PHE B 199 60.67 31.11
REMARK 500 MET B 206 105.70 84.17
REMARK 500 VAL B 219 -60.71 71.43
REMARK 500 GLN C 109 39.78 -150.49
REMARK 500 SER C 170 -119.51 61.37
REMARK 500 SER C 170 -117.86 61.51
REMARK 500 PHE C 199 60.75 31.57
REMARK 500 MET C 206 104.62 83.25
REMARK 500 VAL C 219 -60.29 75.15
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 A 896 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B 855 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH B 856 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH C 842 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH C 843 DISTANCE = 6.84 ANGSTROMS
DBREF 8Q03 A -8 322 PDB 8Q03 8Q03 -8 322
DBREF 8Q03 B -8 322 PDB 8Q03 8Q03 -8 322
DBREF 8Q03 C 1 322 PDB 8Q03 8Q03 1 322
SEQRES 1 A 331 MET SER HIS HIS HIS HIS HIS HIS SER MET THR ALA LYS
SEQRES 2 A 331 THR PRO LEU ASP PRO ALA LEU PHE ARG PRO ASP ALA ILE
SEQRES 3 A 331 SER ASP GLU THR ARG GLY ILE ASN ASP PHE ILE ILE LYS
SEQRES 4 A 331 ALA PHE GLU ALA VAL PRO GLU TRP TRP GLU ILE GLY ALA
SEQRES 5 A 331 ALA THR VAL ARG GLU ALA ARG ALA ARG GLY GLU GLY GLY
SEQRES 6 A 331 PHE PRO LEU PRO PRO LYS SER GLU ARG ALA ARG THR ILE
SEQRES 7 A 331 GLU ILE GLU GLY LYS GLY GLY HIS LYS VAL PRO LEU ARG
SEQRES 8 A 331 ILE ILE ALA PRO GLU SER PRO LYS GLY VAL TYR LEU HIS
SEQRES 9 A 331 ILE HIS GLY GLY GLY TRP VAL LEU GLY ALA CYS ASP GLN
SEQRES 10 A 331 GLN ASP PRO MET LEU GLU ARG ILE ALA GLN ASN ALA GLY
SEQRES 11 A 331 LEU ALA CYS VAL SER VAL GLU TYR ARG LEU ALA PRO GLU
SEQRES 12 A 331 HIS PRO TYR PRO ALA GLY PRO ASP ASP CYS GLU ALA ALA
SEQRES 13 A 331 ALA LEU TRP LEU VAL LYS ASN ALA LYS LYS GLU PHE GLY
SEQRES 14 A 331 THR GLU VAL LEU THR ILE GLY GLY GLU SER ALA GLY GLY
SEQRES 15 A 331 HIS LEU SER ALA VAL THR LEU LEU ARG MET ARG ASP ARG
SEQRES 16 A 331 HIS GLY TYR LYS GLY PHE LYS GLY ALA ASN LEU VAL PHE
SEQRES 17 A 331 GLY ALA PHE ASP MET SER MET SER PRO SER GLN ARG VAL
SEQRES 18 A 331 PHE GLY ASN GLU ARG LEU VAL LEU ARG THR VAL ASP ILE
SEQRES 19 A 331 GLN LYS PHE GLY ASP ALA PHE LEU PRO ASN GLY GLU ASP
SEQRES 20 A 331 ARG ARG ASP PRO ASP ILE SER PRO LEU TYR ALA ASN LEU
SEQRES 21 A 331 HIS ASP MET PRO PRO ALA LEU PHE THR VAL GLY THR ARG
SEQRES 22 A 331 ASP ALA LEU VAL ASP ASP THR LEU PHE MET HIS ALA ARG
SEQRES 23 A 331 TRP ILE ALA ALA GLY ASN GLU ALA GLU LEU GLY VAL PHE
SEQRES 24 A 331 PRO GLY GLY ALA HIS GLY PHE VAL ALA PHE PRO GLY GLU
SEQRES 25 A 331 ILE ALA ARG ALA ALA ASN ALA GLN ALA ASP ALA PHE LEU
SEQRES 26 A 331 ARG ARG VAL THR GLY GLN
SEQRES 1 B 331 MET SER HIS HIS HIS HIS HIS HIS SER MET THR ALA LYS
SEQRES 2 B 331 THR PRO LEU ASP PRO ALA LEU PHE ARG PRO ASP ALA ILE
SEQRES 3 B 331 SER ASP GLU THR ARG GLY ILE ASN ASP PHE ILE ILE LYS
SEQRES 4 B 331 ALA PHE GLU ALA VAL PRO GLU TRP TRP GLU ILE GLY ALA
SEQRES 5 B 331 ALA THR VAL ARG GLU ALA ARG ALA ARG GLY GLU GLY GLY
SEQRES 6 B 331 PHE PRO LEU PRO PRO LYS SER GLU ARG ALA ARG THR ILE
SEQRES 7 B 331 GLU ILE GLU GLY LYS GLY GLY HIS LYS VAL PRO LEU ARG
SEQRES 8 B 331 ILE ILE ALA PRO GLU SER PRO LYS GLY VAL TYR LEU HIS
SEQRES 9 B 331 ILE HIS GLY GLY GLY TRP VAL LEU GLY ALA CYS ASP GLN
SEQRES 10 B 331 GLN ASP PRO MET LEU GLU ARG ILE ALA GLN ASN ALA GLY
SEQRES 11 B 331 LEU ALA CYS VAL SER VAL GLU TYR ARG LEU ALA PRO GLU
SEQRES 12 B 331 HIS PRO TYR PRO ALA GLY PRO ASP ASP CYS GLU ALA ALA
SEQRES 13 B 331 ALA LEU TRP LEU VAL LYS ASN ALA LYS LYS GLU PHE GLY
SEQRES 14 B 331 THR GLU VAL LEU THR ILE GLY GLY GLU SER ALA GLY GLY
SEQRES 15 B 331 HIS LEU SER ALA VAL THR LEU LEU ARG MET ARG ASP ARG
SEQRES 16 B 331 HIS GLY TYR LYS GLY PHE LYS GLY ALA ASN LEU VAL PHE
SEQRES 17 B 331 GLY ALA PHE ASP MET SER MET SER PRO SER GLN ARG VAL
SEQRES 18 B 331 PHE GLY ASN GLU ARG LEU VAL LEU ARG THR VAL ASP ILE
SEQRES 19 B 331 GLN LYS PHE GLY ASP ALA PHE LEU PRO ASN GLY GLU ASP
SEQRES 20 B 331 ARG ARG ASP PRO ASP ILE SER PRO LEU TYR ALA ASN LEU
SEQRES 21 B 331 HIS ASP MET PRO PRO ALA LEU PHE THR VAL GLY THR ARG
SEQRES 22 B 331 ASP ALA LEU VAL ASP ASP THR LEU PHE MET HIS ALA ARG
SEQRES 23 B 331 TRP ILE ALA ALA GLY ASN GLU ALA GLU LEU GLY VAL PHE
SEQRES 24 B 331 PRO GLY GLY ALA HIS GLY PHE VAL ALA PHE PRO GLY GLU
SEQRES 25 B 331 ILE ALA ARG ALA ALA ASN ALA GLN ALA ASP ALA PHE LEU
SEQRES 26 B 331 ARG ARG VAL THR GLY GLN
SEQRES 1 C 322 MET SER ALA LYS THR PRO LEU ASP PRO ALA LEU PHE ARG
SEQRES 2 C 322 PRO ASP ALA ILE SER ASP GLU THR ARG GLY ILE ASN ASP
SEQRES 3 C 322 PHE ILE ILE LYS ALA PHE GLU ALA VAL PRO GLU TRP TRP
SEQRES 4 C 322 GLU ILE GLY ALA ALA THR VAL ARG GLU ALA ARG ALA ARG
SEQRES 5 C 322 GLY GLU GLY GLY PHE PRO LEU PRO PRO LYS SER GLU ARG
SEQRES 6 C 322 ALA ARG THR ILE GLU ILE GLU GLY LYS GLY GLY HIS LYS
SEQRES 7 C 322 VAL PRO LEU ARG ILE ILE ALA PRO GLU SER PRO LYS GLY
SEQRES 8 C 322 VAL TYR LEU HIS ILE HIS GLY GLY GLY TRP VAL LEU GLY
SEQRES 9 C 322 ALA CYS ASP GLN GLN ASP PRO MET LEU GLU ARG ILE ALA
SEQRES 10 C 322 GLN ASN ALA GLY LEU ALA CYS VAL SER VAL GLU TYR ARG
SEQRES 11 C 322 LEU ALA PRO GLU HIS PRO TYR PRO ALA GLY PRO ASP ASP
SEQRES 12 C 322 CYS GLU ALA ALA ALA LEU TRP LEU VAL LYS ASN ALA LYS
SEQRES 13 C 322 LYS GLU PHE GLY THR GLU VAL LEU THR ILE GLY GLY GLU
SEQRES 14 C 322 SER ALA GLY GLY HIS LEU SER ALA VAL THR LEU LEU ARG
SEQRES 15 C 322 MET ARG ASP ARG HIS GLY TYR LYS GLY PHE LYS GLY ALA
SEQRES 16 C 322 ASN LEU VAL PHE GLY ALA PHE ASP MET SER MET SER PRO
SEQRES 17 C 322 SER GLN ARG VAL PHE GLY ASN GLU ARG LEU VAL LEU ARG
SEQRES 18 C 322 THR VAL ASP ILE GLN LYS PHE GLY ASP ALA PHE LEU PRO
SEQRES 19 C 322 ASN GLY GLU ASP ARG ARG ASP PRO ASP ILE SER PRO LEU
SEQRES 20 C 322 TYR ALA ASN LEU HIS ASP MET PRO PRO ALA LEU PHE THR
SEQRES 21 C 322 VAL GLY THR ARG ASP ALA LEU VAL ASP ASP THR LEU PHE
SEQRES 22 C 322 MET HIS ALA ARG TRP ILE ALA ALA GLY ASN GLU ALA GLU
SEQRES 23 C 322 LEU GLY VAL PHE PRO GLY GLY ALA HIS GLY PHE VAL ALA
SEQRES 24 C 322 PHE PRO GLY GLU ILE ALA ARG ALA ALA ASN ALA GLN ALA
SEQRES 25 C 322 ASP ALA PHE LEU ARG ARG VAL THR GLY GLN
HET GOL A 401 14
HET BUA A 402 6
HET SO4 A 403 5
HET SO4 A 404 5
HET GOL B 401 14
HET BUA B 402 6
HET SO4 B 403 5
HET SO4 B 404 5
HET SO4 B 405 5
HET SO4 B 406 5
HET SO4 B 407 5
HET GOL C 401 14
HET BUA C 402 6
HET SO4 C 403 5
HET SO4 C 404 5
HET SO4 C 405 5
HET SO4 C 406 5
HET SO4 C 407 5
HET SO4 C 408 5
HETNAM GOL GLYCEROL
HETNAM BUA BUTANOIC ACID
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 BUA 3(C4 H8 O2)
FORMUL 6 SO4 13(O4 S 2-)
FORMUL 23 HOH *1095(H2 O)
HELIX 1 AA1 ASP A 8 ILE A 17 5 10
HELIX 2 AA2 SER A 18 PHE A 32 1 15
HELIX 3 AA3 GLU A 37 GLY A 42 1 6
HELIX 4 AA4 GLY A 42 ARG A 52 1 11
HELIX 5 AA5 GLN A 109 GLY A 121 1 13
HELIX 6 AA6 PRO A 138 GLY A 160 1 23
HELIX 7 AA7 SER A 170 GLY A 188 1 19
HELIX 8 AA8 SER A 207 PHE A 213 1 7
HELIX 9 AA9 ARG A 221 LEU A 233 1 13
HELIX 10 AB1 SER A 245 ALA A 249 5 5
HELIX 11 AB2 LEU A 267 ALA A 281 1 15
HELIX 12 AB3 GLY A 296 PHE A 300 5 5
HELIX 13 AB4 GLY A 302 THR A 320 1 19
HELIX 14 AB5 ASP B 8 ILE B 17 5 10
HELIX 15 AB6 SER B 18 ALA B 34 1 17
HELIX 16 AB7 GLU B 37 GLY B 42 1 6
HELIX 17 AB8 GLY B 42 ARG B 52 1 11
HELIX 18 AB9 GLN B 109 GLY B 121 1 13
HELIX 19 AC1 PRO B 138 GLY B 160 1 23
HELIX 20 AC2 SER B 170 GLY B 188 1 19
HELIX 21 AC3 SER B 207 PHE B 213 1 7
HELIX 22 AC4 ARG B 221 LEU B 233 1 13
HELIX 23 AC5 SER B 245 ALA B 249 5 5
HELIX 24 AC6 LEU B 267 ALA B 281 1 15
HELIX 25 AC7 GLY B 296 PHE B 300 5 5
HELIX 26 AC8 GLY B 302 THR B 320 1 19
HELIX 27 AC9 ASP C 8 ILE C 17 5 10
HELIX 28 AD1 SER C 18 ALA C 34 1 17
HELIX 29 AD2 GLU C 37 GLY C 42 1 6
HELIX 30 AD3 GLY C 42 ARG C 52 1 11
HELIX 31 AD4 GLN C 109 GLY C 121 1 13
HELIX 32 AD5 PRO C 138 GLY C 160 1 23
HELIX 33 AD6 SER C 170 GLY C 188 1 19
HELIX 34 AD7 SER C 207 PHE C 213 1 7
HELIX 35 AD8 ARG C 221 LEU C 233 1 13
HELIX 36 AD9 SER C 245 ALA C 249 5 5
HELIX 37 AE1 LEU C 267 ALA C 281 1 15
HELIX 38 AE2 GLY C 296 PHE C 300 5 5
HELIX 39 AE3 GLY C 302 THR C 320 1 19
SHEET 1 AA1 8 ARG A 67 GLU A 72 0
SHEET 2 AA1 8 LYS A 78 ILE A 84 -1 O ILE A 83 N ARG A 67
SHEET 3 AA1 8 ALA A 123 VAL A 127 -1 O CYS A 124 N ILE A 84
SHEET 4 AA1 8 VAL A 92 ILE A 96 1 N TYR A 93 O ALA A 123
SHEET 5 AA1 8 LEU A 164 GLU A 169 1 O THR A 165 N LEU A 94
SHEET 6 AA1 8 ALA A 195 VAL A 198 1 O ASN A 196 N ILE A 166
SHEET 7 AA1 8 ALA A 257 ARG A 264 1 O LEU A 258 N LEU A 197
SHEET 8 AA1 8 ALA A 285 ALA A 294 1 O GLU A 286 N ALA A 257
SHEET 1 AA2 8 ARG B 67 GLU B 72 0
SHEET 2 AA2 8 LYS B 78 ILE B 84 -1 O ILE B 83 N ARG B 67
SHEET 3 AA2 8 ALA B 123 VAL B 127 -1 O CYS B 124 N ILE B 84
SHEET 4 AA2 8 VAL B 92 ILE B 96 1 N TYR B 93 O ALA B 123
SHEET 5 AA2 8 LEU B 164 GLU B 169 1 O THR B 165 N LEU B 94
SHEET 6 AA2 8 ALA B 195 VAL B 198 1 O ASN B 196 N ILE B 166
SHEET 7 AA2 8 ALA B 257 ARG B 264 1 O LEU B 258 N ALA B 195
SHEET 8 AA2 8 ALA B 285 ALA B 294 1 O GLY B 288 N PHE B 259
SHEET 1 AA3 8 ARG C 67 GLU C 72 0
SHEET 2 AA3 8 LYS C 78 ILE C 84 -1 O ILE C 83 N ARG C 67
SHEET 3 AA3 8 ALA C 123 VAL C 127 -1 O CYS C 124 N ILE C 84
SHEET 4 AA3 8 VAL C 92 ILE C 96 1 N TYR C 93 O ALA C 123
SHEET 5 AA3 8 LEU C 164 GLU C 169 1 O THR C 165 N LEU C 94
SHEET 6 AA3 8 ALA C 195 VAL C 198 1 O ASN C 196 N ILE C 166
SHEET 7 AA3 8 ALA C 257 ARG C 264 1 O LEU C 258 N ALA C 195
SHEET 8 AA3 8 ALA C 285 ALA C 294 1 O GLY C 288 N PHE C 259
CISPEP 1 ALA A 132 PRO A 133 0 0.96
CISPEP 2 TYR A 137 PRO A 138 0 5.51
CISPEP 3 ALA B 132 PRO B 133 0 0.10
CISPEP 4 TYR B 137 PRO B 138 0 6.63
CISPEP 5 ALA C 132 PRO C 133 0 6.19
CISPEP 6 TYR C 137 PRO C 138 0 5.46
CRYST1 182.376 45.742 135.369 90.00 105.63 90.00 C 1 2 1 8
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 0.005483 0.000000 0.001534 0.00000
SCALE2 0.000000 0.021862 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007671 0.00000
TER 2475 GLN A 322
TER 4961 GLN B 322
TER 7405 GLN C 322
MASTER 388 0 19 39 24 0 0 6 8481 3 125 77
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