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HEADER HYDROLASE 23-MAR-23 8OIM
TITLE CRYSTAL STRUCTURE OF THE LIPASE SPL FROM SPHINGOMONAS SP. HXN-200
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS SP.;
SOURCE 3 ORGANISM_TAXID: 28214;
SOURCE 4 GENE: LH19_08550;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA HYDROLASE, LIPASE, SPL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MOKOS,K.GRUBER,B.DANIEL
REVDAT 1 03-APR-24 8OIM 0
JRNL AUTH E.ZUKIC,D.MOKOS,B.DANIEL,M.WEBER,N.STIX,K.DITRICH,
JRNL AUTH 2 C.WILLRODT,K.GRUBER,W.KROUTIL
JRNL TITL AMIDE FORMATION OF (HETERO)AROMATIC ESTERS AND PRIMARY
JRNL TITL 2 AMINES IN BUFFER CATALYZED BY SERINE HYDROLASES: AN ASP NEXT
JRNL TITL 3 TO SER OF THE CATALYTIC TRIAD OF SERINE HYDROLASES IS
JRNL TITL 4 CRUCIAL FOR ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0403
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.6
REMARK 3 NUMBER OF REFLECTIONS : 44805
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.153
REMARK 3 FREE R VALUE TEST SET COUNT : 2309
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2941
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4674
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.02900
REMARK 3 B22 (A**2) : 1.90200
REMARK 3 B33 (A**2) : -0.96200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.50700
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.162
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.699
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4798 ; 0.015 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 4476 ; 0.001 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6560 ; 2.037 ; 1.658
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10326 ; 0.641 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 616 ; 6.966 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 38 ; 8.198 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 704 ;15.415 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 722 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5716 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1036 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1006 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 23 ; 0.138 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2369 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 304 ; 0.184 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2470 ; 3.776 ; 2.915
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2470 ; 3.760 ; 2.914
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3084 ; 4.704 ; 5.214
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3085 ; 4.705 ; 5.216
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2328 ; 6.051 ; 3.536
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2329 ; 6.050 ; 3.538
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3476 ; 8.644 ; 6.165
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3477 ; 8.643 ; 6.166
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 314 NULL
REMARK 3 1 A 6 A 314 NULL
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 8OIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-23.
REMARK 100 THE DEPOSITION ID IS D_1292128967.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033210
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44854
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 42.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 8.92
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 42.05
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.05300
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MG/ML SPL, INDEX SCREEN CONDITION 78
REMARK 280 (0.2 M AMMONIUM ACETATE, 0.1 M BIS-TRIS, 25% PEG 3350), PH 5.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.48300
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLN A -2
REMARK 465 ASP A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ASP A 3
REMARK 465 SER A 4
REMARK 465 THR A 5
REMARK 465 ALA A 315
REMARK 465 MET B -13
REMARK 465 GLY B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 SER B -3
REMARK 465 GLN B -2
REMARK 465 ASP B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASP B 3
REMARK 465 SER B 4
REMARK 465 THR B 5
REMARK 465 ALA B 315
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 HH11 ARG A 10 HG SER A 292 1.20
REMARK 500 HG1 THR B 279 H ILE B 280 1.35
REMARK 500 HH11 ARG B 60 O HOH B 407 1.59
REMARK 500 O HOH A 564 O HOH A 576 2.12
REMARK 500 O HOH B 401 O HOH B 532 2.14
REMARK 500 OD2 ASP B 202 O HOH B 401 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 275 CD GLU B 275 OE1 0.083
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 ARG A 77 69.93 -154.75
REMARK 500 ARG A 80 158.33 -47.09
REMARK 500 ASP A 98 -159.60 -162.90
REMARK 500 PRO A 131 33.80 -96.87
REMARK 500 SER A 159 -111.85 65.27
REMARK 500 TYR A 188 66.25 27.89
REMARK 500 LEU A 208 -57.02 73.87
REMARK 500 ARG B 77 67.72 -151.19
REMARK 500 ALA B 82 113.32 -35.73
REMARK 500 ASP B 98 -166.07 -162.58
REMARK 500 PRO B 131 35.44 -99.83
REMARK 500 SER B 159 -113.77 59.50
REMARK 500 TYR B 188 57.34 31.73
REMARK 500 LEU B 208 -59.99 71.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 51 0.09 SIDE CHAIN
REMARK 500 ARG B 254 0.08 SIDE CHAIN
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 577 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH A 578 DISTANCE = 6.43 ANGSTROMS
DBREF1 8OIM A 1 315 UNP A0A0N7I173_SPHMC
DBREF2 8OIM A A0A0N7I173 1 315
DBREF1 8OIM B 1 315 UNP A0A0N7I173_SPHMC
DBREF2 8OIM B A0A0N7I173 1 315
SEQADV 8OIM MET A -13 UNP A0A0N7I17 INITIATING METHIONINE
SEQADV 8OIM GLY A -12 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM SER A -11 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM SER A -10 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS A -9 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS A -8 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS A -7 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS A -6 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS A -5 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS A -4 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM SER A -3 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM GLN A -2 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM ASP A -1 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM PRO A 0 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM ILE A 120 UNP A0A0N7I17 VAL 120 CONFLICT
SEQADV 8OIM MET B -13 UNP A0A0N7I17 INITIATING METHIONINE
SEQADV 8OIM GLY B -12 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM SER B -11 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM SER B -10 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS B -9 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS B -8 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS B -7 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS B -6 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS B -5 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM HIS B -4 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM SER B -3 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM GLN B -2 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM ASP B -1 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM PRO B 0 UNP A0A0N7I17 EXPRESSION TAG
SEQADV 8OIM ILE B 120 UNP A0A0N7I17 VAL 120 CONFLICT
SEQRES 1 A 329 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 329 PRO MET THR ASP SER THR THR HIS TYR THR ARG PRO ASP
SEQRES 3 A 329 VAL ALA ALA PHE LEU ALA PHE LEU ASN ALA GLN GLU GLY
SEQRES 4 A 329 PRO LYS MET GLU GLU MET PRO PRO ALA GLY ALA ARG GLU
SEQRES 5 A 329 MET MET ARG VAL MET GLY GLN LEU ALA ASP VAL PRO ARG
SEQRES 6 A 329 GLY GLU ILE ALA LYS VAL GLU ASP ARG MET ILE PRO GLY
SEQRES 7 A 329 PRO ASP GLY ASP ILE PRO ILE ARG LEU TYR ASP ASN ARG
SEQRES 8 A 329 PRO ASP ARG GLU ALA GLY PRO VAL MET VAL PHE TYR HIS
SEQRES 9 A 329 GLY GLY GLY TRP VAL ILE GLY ASP LEU GLU THR HIS ASP
SEQRES 10 A 329 PRO TYR CYS ALA GLU ALA ALA ARG ILE LEU ASP MET PRO
SEQRES 11 A 329 VAL ILE ALA ILE ASP TYR ARG LEU ALA PRO GLU HIS PRO
SEQRES 12 A 329 PHE PRO ALA ALA PRO ILE ASP CYS GLU ALA ALA THR ARG
SEQRES 13 A 329 TRP VAL ALA ASP ASN ILE ALA CYS THR GLY LEU VAL LEU
SEQRES 14 A 329 SER GLY ASP SER ALA GLY GLY ASN LEU THR ILE VAL THR
SEQRES 15 A 329 ALA LEU ALA LEU ARG ASP GLU PRO ALA ALA LYS PRO VAL
SEQRES 16 A 329 ILE ALA ILE HIS PRO ILE TYR PRO ALA VAL THR THR HIS
SEQRES 17 A 329 ASN ASP TRP GLN SER TYR ARG ASP PHE GLY GLU GLY HIS
SEQRES 18 A 329 LEU LEU THR GLU GLY SER MET THR TRP PHE GLY ASN HIS
SEQRES 19 A 329 TYR ALA ALA ASP PRO ALA ASP ARG ARG ALA ALA PRO ILE
SEQRES 20 A 329 ASP PHE PRO ALA ASP GLY LEU PRO PRO THR LEU LEU ILE
SEQRES 21 A 329 THR ALA SER LEU ASP PRO LEU ARG ASP GLN GLY ARG ALA
SEQRES 22 A 329 TYR ALA ALA LYS LEU ILE GLU ALA GLY VAL PRO THR THR
SEQRES 23 A 329 TYR ARG GLU ALA LYS GLY THR ILE HIS GLY TYR ILE CYS
SEQRES 24 A 329 LEU ALA GLN GLY ILE PRO SER ALA LYS ASP ASP ILE ARG
SEQRES 25 A 329 GLY ALA LEU THR VAL LEU LYS ALA ILE VAL ALA GLU ALA
SEQRES 26 A 329 THR GLY ALA ALA
SEQRES 1 B 329 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 329 PRO MET THR ASP SER THR THR HIS TYR THR ARG PRO ASP
SEQRES 3 B 329 VAL ALA ALA PHE LEU ALA PHE LEU ASN ALA GLN GLU GLY
SEQRES 4 B 329 PRO LYS MET GLU GLU MET PRO PRO ALA GLY ALA ARG GLU
SEQRES 5 B 329 MET MET ARG VAL MET GLY GLN LEU ALA ASP VAL PRO ARG
SEQRES 6 B 329 GLY GLU ILE ALA LYS VAL GLU ASP ARG MET ILE PRO GLY
SEQRES 7 B 329 PRO ASP GLY ASP ILE PRO ILE ARG LEU TYR ASP ASN ARG
SEQRES 8 B 329 PRO ASP ARG GLU ALA GLY PRO VAL MET VAL PHE TYR HIS
SEQRES 9 B 329 GLY GLY GLY TRP VAL ILE GLY ASP LEU GLU THR HIS ASP
SEQRES 10 B 329 PRO TYR CYS ALA GLU ALA ALA ARG ILE LEU ASP MET PRO
SEQRES 11 B 329 VAL ILE ALA ILE ASP TYR ARG LEU ALA PRO GLU HIS PRO
SEQRES 12 B 329 PHE PRO ALA ALA PRO ILE ASP CYS GLU ALA ALA THR ARG
SEQRES 13 B 329 TRP VAL ALA ASP ASN ILE ALA CYS THR GLY LEU VAL LEU
SEQRES 14 B 329 SER GLY ASP SER ALA GLY GLY ASN LEU THR ILE VAL THR
SEQRES 15 B 329 ALA LEU ALA LEU ARG ASP GLU PRO ALA ALA LYS PRO VAL
SEQRES 16 B 329 ILE ALA ILE HIS PRO ILE TYR PRO ALA VAL THR THR HIS
SEQRES 17 B 329 ASN ASP TRP GLN SER TYR ARG ASP PHE GLY GLU GLY HIS
SEQRES 18 B 329 LEU LEU THR GLU GLY SER MET THR TRP PHE GLY ASN HIS
SEQRES 19 B 329 TYR ALA ALA ASP PRO ALA ASP ARG ARG ALA ALA PRO ILE
SEQRES 20 B 329 ASP PHE PRO ALA ASP GLY LEU PRO PRO THR LEU LEU ILE
SEQRES 21 B 329 THR ALA SER LEU ASP PRO LEU ARG ASP GLN GLY ARG ALA
SEQRES 22 B 329 TYR ALA ALA LYS LEU ILE GLU ALA GLY VAL PRO THR THR
SEQRES 23 B 329 TYR ARG GLU ALA LYS GLY THR ILE HIS GLY TYR ILE CYS
SEQRES 24 B 329 LEU ALA GLN GLY ILE PRO SER ALA LYS ASP ASP ILE ARG
SEQRES 25 B 329 GLY ALA LEU THR VAL LEU LYS ALA ILE VAL ALA GLU ALA
SEQRES 26 B 329 THR GLY ALA ALA
FORMUL 3 HOH *360(H2 O)
HELIX 1 AA1 ARG A 10 ALA A 22 1 13
HELIX 2 AA2 LYS A 27 MET A 31 5 5
HELIX 3 AA3 PRO A 32 ASP A 48 1 17
HELIX 4 AA4 HIS A 102 ASP A 114 1 13
HELIX 5 AA5 PRO A 131 ILE A 148 1 18
HELIX 6 AA6 SER A 159 GLU A 175 1 17
HELIX 7 AA7 TRP A 197 GLY A 204 1 8
HELIX 8 AA8 THR A 210 ALA A 222 1 13
HELIX 9 AA9 ALA A 231 PHE A 235 5 5
HELIX 10 AB1 LEU A 253 ALA A 267 1 15
HELIX 11 AB2 GLY A 282 LEU A 286 5 5
HELIX 12 AB3 SER A 292 GLY A 313 1 22
HELIX 13 AB4 ARG B 10 ALA B 22 1 13
HELIX 14 AB5 LYS B 27 MET B 31 5 5
HELIX 15 AB6 PRO B 32 ASP B 48 1 17
HELIX 16 AB7 HIS B 102 ASP B 114 1 13
HELIX 17 AB8 PRO B 131 ILE B 148 1 18
HELIX 18 AB9 SER B 159 GLU B 175 1 17
HELIX 19 AC1 TRP B 197 GLY B 204 1 8
HELIX 20 AC2 THR B 210 ALA B 222 1 13
HELIX 21 AC3 ALA B 231 PHE B 235 5 5
HELIX 22 AC4 LEU B 253 ALA B 267 1 15
HELIX 23 AC5 GLY B 282 LEU B 286 5 5
HELIX 24 AC6 SER B 292 GLY B 313 1 22
SHEET 1 AA1 6 LYS A 56 GLY A 64 0
SHEET 2 AA1 6 GLY A 67 ASP A 75 -1 O LEU A 73 N GLU A 58
SHEET 3 AA1 6 VAL A 117 ILE A 120 -1 O VAL A 117 N TYR A 74
SHEET 4 AA1 6 PRO A 84 TYR A 89 1 N MET A 86 O ILE A 118
SHEET 5 AA1 6 GLY A 152 ASP A 158 1 O VAL A 154 N VAL A 87
SHEET 6 AA1 6 VAL A 181 ILE A 187 1 O ILE A 187 N GLY A 157
SHEET 1 AA2 4 THR A 243 ALA A 248 0
SHEET 2 AA2 4 THR A 271 ALA A 276 1 O ALA A 276 N THR A 247
SHEET 3 AA2 4 THR B 271 ALA B 276 -1 O TYR B 273 N THR A 271
SHEET 4 AA2 4 THR B 243 ALA B 248 1 N THR B 247 O ALA B 276
SHEET 1 AA3 6 LYS B 56 ILE B 62 0
SHEET 2 AA3 6 ILE B 69 ASP B 75 -1 O ILE B 71 N ARG B 60
SHEET 3 AA3 6 VAL B 117 ILE B 120 -1 O ALA B 119 N ARG B 72
SHEET 4 AA3 6 PRO B 84 TYR B 89 1 N MET B 86 O ILE B 118
SHEET 5 AA3 6 GLY B 152 ASP B 158 1 O VAL B 154 N VAL B 87
SHEET 6 AA3 6 VAL B 181 ILE B 187 1 O ILE B 187 N GLY B 157
CISPEP 1 ALA A 125 PRO A 126 0 3.00
CISPEP 2 PHE A 130 PRO A 131 0 2.21
CISPEP 3 ALA B 125 PRO B 126 0 0.10
CISPEP 4 PHE B 130 PRO B 131 0 1.81
CRYST1 60.812 88.966 65.627 90.00 96.41 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 0.016444 0.000000 0.001848 0.00000
SCALE2 0.000000 0.011240 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015334 0.00000
TER 4631 ALA A 314
TER 9262 ALA B 314
MASTER 378 0 0 24 16 0 0 6 5034 2 0 52
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