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HEADER HYDROLASE 27-JAN-21 7E04
TITLE CRYSTAL STRUCTURE OF BOMGL, A MONOACYLGLYCEROL LIPASE FROM MARINE
TITLE 2 BACILLUS SP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CYTOBACILLUS OCEANISEDIMINIS;
SOURCE 3 ORGANISM_TAXID: 665099;
SOURCE 4 GENE: BBV17_11975;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIPASE, MONOACYLGLYCEROL, MARINE BACTERIAL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.H.WANG,J.WANG,D.M.LAN
REVDAT 1 02-FEB-22 7E04 0
JRNL AUTH Y.H.WANG,J.WANG,D.M.LAN
JRNL TITL CRYSTAL STRUCTURE OF BOMGL, A MONOACYLGLYCEROL LIPASE FROM
JRNL TITL 2 MARINE BACILLUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1_4122
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) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 72775
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3564
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 23.1400 - 3.6500 1.00 3044 164 0.1574 0.1394
REMARK 3 2 3.6500 - 2.9000 1.00 2885 159 0.1622 0.1958
REMARK 3 3 2.9000 - 2.5300 1.00 2818 172 0.1715 0.1678
REMARK 3 4 2.5300 - 2.3000 1.00 2807 149 0.1661 0.1934
REMARK 3 5 2.3000 - 2.1400 1.00 2826 132 0.1586 0.1680
REMARK 3 6 2.1400 - 2.0100 1.00 2794 152 0.1614 0.1715
REMARK 3 7 2.0100 - 1.9100 1.00 2782 141 0.1609 0.1470
REMARK 3 8 1.9100 - 1.8300 1.00 2772 147 0.1654 0.1943
REMARK 3 9 1.8300 - 1.7600 1.00 2784 118 0.1681 0.1649
REMARK 3 10 1.7600 - 1.7000 1.00 2778 139 0.1719 0.1821
REMARK 3 11 1.7000 - 1.6400 1.00 2753 146 0.1672 0.1821
REMARK 3 12 1.6400 - 1.6000 1.00 2771 140 0.1631 0.1721
REMARK 3 13 1.6000 - 1.5500 1.00 2741 138 0.1616 0.1686
REMARK 3 14 1.5500 - 1.5200 1.00 2766 144 0.1637 0.1749
REMARK 3 15 1.5200 - 1.4800 1.00 2729 131 0.1692 0.2161
REMARK 3 16 1.4800 - 1.4500 1.00 2733 163 0.1737 0.1876
REMARK 3 17 1.4500 - 1.4200 1.00 2762 125 0.1717 0.1885
REMARK 3 18 1.4200 - 1.3900 1.00 2743 145 0.1883 0.1974
REMARK 3 19 1.3900 - 1.3700 1.00 2749 125 0.1895 0.2036
REMARK 3 20 1.3700 - 1.3500 1.00 2725 140 0.1968 0.2208
REMARK 3 21 1.3500 - 1.3200 1.00 2725 150 0.2012 0.2314
REMARK 3 22 1.3200 - 1.3000 1.00 2710 148 0.2084 0.2256
REMARK 3 23 1.3000 - 1.2900 0.99 2716 149 0.2403 0.2468
REMARK 3 24 1.2900 - 1.2700 0.98 2694 116 0.2754 0.3225
REMARK 3 25 1.2700 - 1.2500 0.95 2604 131 0.3268 0.3447
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) : 0.121
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.49
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 : 0.005 1989
REMARK 3 ANGLE : 0.834 2698
REMARK 3 CHIRALITY : 0.078 306
REMARK 3 PLANARITY : 0.006 344
REMARK 3 DIHEDRAL : 5.178 272
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 7E04 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-21.
REMARK 100 THE DEPOSITION ID IS D_1300020510.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-20
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72862
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 27.750
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 30.70
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 28.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.28
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.92500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHENIX
REMARK 200 STARTING MODEL: 5XKS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM ACETATE TETRAHYDRATE,
REMARK 280 0.1 M SODIUM CACODYLATE TRIHYDRATE PH 6.5, 20% (W/V) PEG 8000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.00667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.00333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.50500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 19.50167
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 97.50833
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.00667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 39.00333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 19.50167
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 58.50500
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 97.50833
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 407 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 744 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 1
REMARK 465 SER A 2
REMARK 465 GLN A 253
REMARK 465 GLY A 254
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 GLU A 3 CG CD OE1 OE2
REMARK 470 GLU A 20 CG CD OE1 OE2
REMARK 470 GLU A 112 CG CD OE1 OE2
REMARK 470 GLU A 135 CG CD OE1 OE2
REMARK 470 LYS A 153 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 O HOH A 587 O HOH A 680 1.78
REMARK 500 O HOH A 676 O HOH A 702 1.94
REMARK 500 O HOH A 555 O HOH A 704 1.96
REMARK 500 O HOH A 401 O HOH A 653 1.96
REMARK 500 O HOH A 420 O HOH A 516 1.99
REMARK 500 O HOH A 449 O HOH A 707 2.02
REMARK 500 O HOH A 707 O HOH A 749 2.05
REMARK 500 O HOH A 478 O HOH A 734 2.07
REMARK 500 O HOH A 716 O HOH A 730 2.07
REMARK 500 O HOH A 707 O HOH A 708 2.08
REMARK 500 O HOH A 636 O HOH A 707 2.09
REMARK 500 O HOH A 502 O HOH A 719 2.10
REMARK 500 O HOH A 469 O HOH A 707 2.11
REMARK 500 O HOH A 642 O HOH A 733 2.12
REMARK 500 O HOH A 586 O HOH A 667 2.13
REMARK 500 O HOH A 435 O HOH A 707 2.15
REMARK 500 O HOH A 442 O HOH A 690 2.15
REMARK 500 O HOH A 654 O HOH A 664 2.16
REMARK 500 N GLU A 3 O HOH A 401 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 609 O HOH A 690 8566 1.93
REMARK 500 O HOH A 570 O HOH A 690 10666 1.98
REMARK 500 O HOH A 566 O HOH A 649 10666 1.99
REMARK 500 O HOH A 658 O HOH A 704 7555 2.02
REMARK 500 O HOH A 678 O HOH A 690 8566 2.03
REMARK 500 O HOH A 614 O HOH A 614 10666 2.13
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 30 -7.76 71.70
REMARK 500 THR A 60 -82.59 -129.45
REMARK 500 SER A 97 -113.43 63.95
REMARK 500 GLU A 124 114.17 -161.54
REMARK 500 GLU A 193 68.22 -116.49
REMARK 500 TYR A 223 -149.93 -98.77
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 752 DISTANCE = 6.01 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301
DBREF1 7E04 A 1 254 UNP A0A1S1YN08_9BACI
DBREF2 7E04 A A0A1S1YN08 1 254
SEQADV 7E04 TYR A 127 UNP A0A1S1YN0 ASP 127 CONFLICT
SEQRES 1 A 254 MET SER GLU LYS TYR PRO ILE ILE GLU GLY ALA GLU PRO
SEQRES 2 A 254 PHE TYR TYR GLU GLY ASN GLU ILE GLY ILE LEU VAL SER
SEQRES 3 A 254 HIS GLY PHE THR GLY SER THR GLN SER MET ARG PRO LEU
SEQRES 4 A 254 GLY GLU ALA TYR ALA ASN ALA GLY TYR THR VAL CYS GLY
SEQRES 5 A 254 PRO ARG LEU ARG GLY HIS GLY THR HIS TYR GLU GLU MET
SEQRES 6 A 254 GLU THR THR THR TYR GLN ASP TRP ILE HIS SER VAL GLU
SEQRES 7 A 254 GLU GLY TYR GLN TRP LEU LYS GLU ARG CYS SER THR ILE
SEQRES 8 A 254 PHE VAL THR GLY LEU SER MET GLY GLY THR LEU THR LEU
SEQRES 9 A 254 TYR MET ALA GLU LYS TYR PRO GLU ILE LYS GLY ILE ILE
SEQRES 10 A 254 PRO ILE ASN ALA ALA ILE GLU ILE SER TYR MET GLU ALA
SEQRES 11 A 254 ALA ALA SER LEU GLU ASP VAL ARG PHE LEU ASP ALA ILE
SEQRES 12 A 254 GLY SER ASP ILE LYS ASN PRO ASP ILE LYS GLU LEU ALA
SEQRES 13 A 254 TYR GLU LYS THR PRO VAL LYS SER ILE GLY GLU ILE THR
SEQRES 14 A 254 GLU LEU MET LYS LYS VAL LYS GLY ASP LEU GLU LYS VAL
SEQRES 15 A 254 ASN CYS PRO ALA LEU ILE PHE VAL SER LYS GLU ASP HIS
SEQRES 16 A 254 VAL VAL PRO PRO SER ASN SER GLN GLU ILE TYR SER SER
SEQRES 17 A 254 ILE LYS SER ALA ALA LYS GLU LEU VAL THR LEU ASP ASN
SEQRES 18 A 254 SER TYR HIS VAL ALA THR LEU ASP ASN ASP GLN ASP ILE
SEQRES 19 A 254 ILE ILE GLU ARG THR LEU HIS PHE LEU GLN ARG VAL LEU
SEQRES 20 A 254 GLU THR SER SER LEU GLN GLY
HET GOL A 301 14
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *352(H2 O)
HELIX 1 AA1 SER A 32 SER A 35 5 4
HELIX 2 AA2 MET A 36 ALA A 46 1 11
HELIX 3 AA3 HIS A 61 GLU A 66 1 6
HELIX 4 AA4 THR A 69 GLU A 86 1 18
HELIX 5 AA5 SER A 97 TYR A 110 1 14
HELIX 6 AA6 ILE A 125 ALA A 132 1 8
HELIX 7 AA7 VAL A 162 ASP A 178 1 17
HELIX 8 AA8 LEU A 179 VAL A 182 5 4
HELIX 9 AA9 PRO A 198 ILE A 209 1 12
HELIX 10 AB1 ASP A 231 THR A 249 1 19
SHEET 1 AA1 5 PHE A 14 TYR A 16 0
SHEET 2 AA1 5 THR A 49 GLY A 52 -1 O GLY A 52 N PHE A 14
SHEET 3 AA1 5 ILE A 21 SER A 26 1 N VAL A 25 O CYS A 51
SHEET 4 AA1 5 THR A 90 LEU A 96 1 O THR A 90 N GLY A 22
SHEET 5 AA1 5 GLY A 115 ILE A 119 1 O ILE A 119 N GLY A 95
SHEET 1 AA2 2 PHE A 139 ASP A 141 0
SHEET 2 AA2 2 LYS A 159 PRO A 161 -1 O THR A 160 N LEU A 140
SHEET 1 AA3 2 ALA A 186 SER A 191 0
SHEET 2 AA3 2 LYS A 214 LEU A 219 1 O VAL A 217 N ILE A 188
SITE 1 AC1 10 PHE A 29 GLY A 31 SER A 97 GLY A 144
SITE 2 AC1 10 GLU A 154 HIS A 224 VAL A 225 HOH A 460
SITE 3 AC1 10 HOH A 508 HOH A 521
CRYST1 87.280 87.280 117.010 90.00 90.00 120.00 P 65 2 2 12
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 0.011457 0.006615 0.000000 0.00000
SCALE2 0.000000 0.013230 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008546 0.00000
TER 1944 LEU A 252
MASTER 373 0 1 10 9 0 3 6 2301 1 14 20
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