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HEADER HYDROLASE 08-JUL-20 7CIP
TITLE MICROBIAL HORMONE-SENSITIVE LIPASE E53 WILD TYPE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;
SOURCE 3 ORGANISM_TAXID: 1044;
SOURCE 4 GENE: EH31_02760;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K-12
KEYWDS ESTERASE, MICROBIAL HORMONE-SENSITIVE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.YANG,Z.LI,X.XU,J.LI
REVDAT 1 14-JUL-21 7CIP 0
JRNL AUTH X.YANG
JRNL TITL MICROBIAL HORMONE-SENSITIVE LIPASE E53 WILD TYPE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 203688
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) : 0.176
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 439
REMARK 3 SOLVENT ATOMS : 1433
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.03
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.71
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 7CIP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1300017675.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 80
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 : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
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 : 203688
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.752
REMARK 200 RESOLUTION RANGE LOW (A) : 48.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.1900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 4YPV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.5, PEG, AMMONIUM SULFATE,
REMARK 280 DIOXANE, PEG 1000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
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,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
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 35.28800
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.53950
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 35.28800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 110.53950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 C1 NPO D1421 LIES ON A SPECIAL POSITION.
REMARK 375 C4 NPO D1421 LIES ON A SPECIAL POSITION.
REMARK 375 OH NPO D1421 LIES ON A SPECIAL POSITION.
REMARK 375 N1 NPO D1421 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 744 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1010 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D1661 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 THR A 2
REMARK 465 ASP A 3
REMARK 465 THR A 313
REMARK 465 ALA A 314
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASP B 3
REMARK 465 THR B 313
REMARK 465 ALA B 314
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ASP C 3
REMARK 465 THR C 313
REMARK 465 ALA C 314
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ASP D 3
REMARK 465 THR D 313
REMARK 465 ALA D 314
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 THR A 4 OG1 CG2
REMARK 470 GLU A 76 CG CD OE1 OE2
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 GLU A 204 CG CD OE1 OE2
REMARK 470 THR B 4 OG1 CG2
REMARK 470 THR C 4 OG1 CG2
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 THR D 4 OG1 CG2
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 DMS A 414 O HOH A 501 1.72
REMARK 500 OE1 GLU C 280 O HOH C 901 1.75
REMARK 500 O HOH B 949 O HOH B 965 1.96
REMARK 500 O1 EDO A 412 O HOH A 502 1.97
REMARK 500 O HOH D 1716 O HOH D 1772 1.97
REMARK 500 O1 EDO A 405 O HOH A 503 2.04
REMARK 500 O HOH D 1699 O HOH D 1723 2.05
REMARK 500 O HOH C 951 O HOH C 1146 2.05
REMARK 500 O HOH C 908 O HOH C 1015 2.06
REMARK 500 O2 NPO B 620 O HOH B 701 2.06
REMARK 500 O HOH A 787 O HOH A 839 2.08
REMARK 500 O HOH A 775 O HOH A 871 2.10
REMARK 500 O HOH B 880 O HOH B 949 2.11
REMARK 500 O HOH C 1067 O HOH C 1108 2.12
REMARK 500 O HOH A 853 O HOH A 861 2.13
REMARK 500 O2 EDO B 605 O HOH B 702 2.14
REMARK 500 O ARG A 151 O HOH A 504 2.15
REMARK 500 O HOH A 503 O HOH A 795 2.15
REMARK 500 O HOH A 765 O HOH A 766 2.16
REMARK 500 O DMS C 820 O HOH C 902 2.16
REMARK 500 OE1 GLU D 280 O HOH D 1501 2.16
REMARK 500 O HOH C 1211 O HOH C 1221 2.17
REMARK 500 O HOH A 721 O HOH A 813 2.17
REMARK 500 O HOH C 1203 O HOH C 1259 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 ASP A 96 -163.97 -165.36
REMARK 500 SER A 162 -127.01 62.18
REMARK 500 LEU A 186 137.05 -172.50
REMARK 500 PHE A 191 59.10 27.04
REMARK 500 VAL A 211 -69.44 68.14
REMARK 500 ASP B 96 -161.84 -166.58
REMARK 500 SER B 162 -125.42 64.05
REMARK 500 PHE B 191 63.82 29.41
REMARK 500 VAL B 211 -68.65 69.36
REMARK 500 ASP C 96 -160.80 -167.60
REMARK 500 SER C 162 -116.18 54.49
REMARK 500 PHE C 191 62.25 26.71
REMARK 500 VAL C 211 -70.13 68.63
REMARK 500 ASP D 96 -158.59 -166.96
REMARK 500 SER D 162 -121.14 56.01
REMARK 500 LEU D 186 140.23 -172.73
REMARK 500 PHE D 191 62.48 28.96
REMARK 500 VAL D 211 -60.22 57.68
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 901 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B1024 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B1025 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH C1295 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH C1296 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH D1811 DISTANCE = 6.66 ANGSTROMS
DBREF1 7CIP A 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CIP A A0A074MDU6 1 314
DBREF1 7CIP B 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CIP B A0A074MDU6 1 314
DBREF1 7CIP C 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CIP C A0A074MDU6 1 314
DBREF1 7CIP D 1 314 UNP A0A074MDU6_ERYLO
DBREF2 7CIP D A0A074MDU6 1 314
SEQRES 1 A 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 A 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 A 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 A 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 A 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 A 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 A 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 A 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 A 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 A 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 A 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 A 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 A 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 A 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 A 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 A 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 A 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 A 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 A 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 A 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 A 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 A 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 A 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 A 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 A 314 THR ALA
SEQRES 1 B 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 B 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 B 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 B 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 B 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 B 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 B 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 B 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 B 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 B 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 B 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 B 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 B 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 B 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 B 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 B 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 B 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 B 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 B 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 B 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 B 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 B 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 B 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 B 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 B 314 THR ALA
SEQRES 1 C 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 C 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 C 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 C 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 C 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 C 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 C 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 C 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 C 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 C 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 C 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 C 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 C 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 C 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 C 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 C 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 C 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 C 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 C 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 C 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 C 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 C 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 C 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 C 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 C 314 THR ALA
SEQRES 1 D 314 MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA
SEQRES 2 D 314 PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU
SEQRES 3 D 314 ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL
SEQRES 4 D 314 ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU
SEQRES 5 D 314 ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY
SEQRES 6 D 314 ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG
SEQRES 7 D 314 GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY
SEQRES 8 D 314 PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS
SEQRES 9 D 314 THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA
SEQRES 10 D 314 VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA
SEQRES 11 D 314 ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA
SEQRES 12 D 314 SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL
SEQRES 13 D 314 ILE PRO ILE GLY ASP SER ALA GLY GLY ASN ALA THR ILE
SEQRES 14 D 314 VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL
SEQRES 15 D 314 PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER
SEQRES 16 D 314 ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU
SEQRES 17 D 314 GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP
SEQRES 18 D 314 THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE
SEQRES 19 D 314 PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE
SEQRES 20 D 314 VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY
SEQRES 21 D 314 ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP
SEQRES 22 D 314 VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE
SEQRES 23 D 314 THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP
SEQRES 24 D 314 LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY
SEQRES 25 D 314 THR ALA
HET GOL A 401 6
HET EDO A 402 4
HET 6NA A 403 8
HET EDO A 404 4
HET EDO A 405 4
HET DMS A 406 4
HET DMS A 407 4
HET CCN A 408 3
HET CCN A 409 3
HET CCN A 410 3
HET CCN A 411 3
HET EDO A 412 4
HET CCN A 413 3
HET DMS A 414 4
HET DMS A 415 4
HET D8F A 416 17
HET 6NA A 417 8
HET CCN A 418 3
HET SO4 A 419 5
HET SO4 A 420 5
HET EDO B 601 4
HET EDO B 602 4
HET EDO B 603 4
HET DIO B 604 6
HET EDO B 605 4
HET EDO B 606 4
HET CCN B 607 3
HET EDO B 608 4
HET CCN B 609 3
HET CCN B 610 3
HET DMS B 611 4
HET DMS B 612 4
HET CCN B 613 3
HET CCN B 614 3
HET BUA B 615 6
HET DMS B 616 4
HET DMS B 617 4
HET CCN B 618 3
HET GOL B 619 6
HET NPO B 620 10
HET NPO B 621 10
HET DMS B 622 4
HET D8F B 623 17
HET EDO B 624 4
HET EDO C 801 4
HET GOL C 802 6
HET EDO C 803 4
HET EDO C 804 4
HET EDO C 805 4
HET EDO C 806 4
HET CCN C 807 3
HET CCN C 808 3
HET GOL C 809 6
HET 6NA C 810 8
HET CCN C 811 3
HET EDO C 812 4
HET GOL C 813 6
HET GOL C 814 6
HET EDO C 815 4
HET GOL C 816 6
HET D8F C 817 17
HET EDO C 818 4
HET DMS C 819 4
HET DMS C 820 4
HET NA C 821 1
HET GOL D1401 6
HET EDO D1402 4
HET CCN D1403 3
HET EDO D1404 4
HET EDO D1405 4
HET EDO D1406 4
HET CCN D1407 3
HET CCN D1408 3
HET DMS D1409 4
HET GOL D1410 6
HET CCN D1411 3
HET 6NA D1412 8
HET DMS D1413 4
HET EDO D1414 4
HET CCN D1415 3
HET CCN D1416 3
HET CCN D1417 3
HET 6NA D1418 8
HET CCN D1419 3
HET CCN D1420 3
HET NPO D1421 10
HET EDO D1422 4
HET D8F D1423 17
HETNAM GOL GLYCEROL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM 6NA HEXANOIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CCN ACETONITRILE
HETNAM D8F (4-NITROPHENYL) HEXANOATE
HETNAM SO4 SULFATE ION
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM BUA BUTANOIC ACID
HETNAM NPO P-NITROPHENOL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 GOL 9(C3 H8 O3)
FORMUL 6 EDO 25(C2 H6 O2)
FORMUL 7 6NA 5(C6 H12 O2)
FORMUL 10 DMS 13(C2 H6 O S)
FORMUL 12 CCN 24(C2 H3 N)
FORMUL 20 D8F 4(C12 H15 N O4)
FORMUL 23 SO4 2(O4 S 2-)
FORMUL 28 DIO C4 H8 O2
FORMUL 39 BUA C4 H8 O2
FORMUL 44 NPO 3(C6 H5 N O3)
FORMUL 69 NA NA 1+
FORMUL 93 HOH *1433(H2 O)
HELIX 1 AA1 ARG A 8 ALA A 22 1 15
HELIX 2 AA2 THR A 30 ASP A 46 1 17
HELIX 3 AA3 HIS A 100 ASP A 112 1 13
HELIX 4 AA4 PRO A 129 SER A 144 1 16
HELIX 5 AA5 SER A 145 GLY A 150 5 6
HELIX 6 AA6 SER A 162 LYS A 178 1 17
HELIX 7 AA7 SER A 200 PHE A 206 1 7
HELIX 8 AA8 THR A 213 LYS A 225 1 13
HELIX 9 AA9 PHE A 234 GLY A 238 5 5
HELIX 10 AB1 ILE A 256 ALA A 270 1 15
HELIX 11 AB2 SER A 285 ILE A 289 5 5
HELIX 12 AB3 SER A 295 GLY A 312 1 18
HELIX 13 AB4 ARG B 8 ALA B 22 1 15
HELIX 14 AB5 THR B 30 ASP B 46 1 17
HELIX 15 AB6 HIS B 100 ASP B 112 1 13
HELIX 16 AB7 PRO B 129 SER B 144 1 16
HELIX 17 AB8 SER B 145 GLY B 150 5 6
HELIX 18 AB9 SER B 162 LYS B 178 1 17
HELIX 19 AC1 SER B 200 PHE B 206 1 7
HELIX 20 AC2 THR B 213 LYS B 225 1 13
HELIX 21 AC3 PHE B 234 GLY B 238 5 5
HELIX 22 AC4 ILE B 256 ALA B 270 1 15
HELIX 23 AC5 SER B 285 ILE B 289 5 5
HELIX 24 AC6 PRO B 294 GLY B 312 1 19
HELIX 25 AC7 ARG C 8 ALA C 22 1 15
HELIX 26 AC8 THR C 25 MET C 29 5 5
HELIX 27 AC9 THR C 30 ASP C 46 1 17
HELIX 28 AD1 HIS C 100 ASP C 112 1 13
HELIX 29 AD2 PRO C 129 SER C 144 1 16
HELIX 30 AD3 SER C 162 LYS C 178 1 17
HELIX 31 AD4 SER C 200 PHE C 206 1 7
HELIX 32 AD5 THR C 213 LYS C 225 1 13
HELIX 33 AD6 PHE C 234 GLY C 238 5 5
HELIX 34 AD7 ILE C 256 ALA C 270 1 15
HELIX 35 AD8 SER C 285 ILE C 289 5 5
HELIX 36 AD9 SER C 295 GLY C 312 1 18
HELIX 37 AE1 ARG D 8 ALA D 22 1 15
HELIX 38 AE2 THR D 30 ASP D 46 1 17
HELIX 39 AE3 HIS D 100 ASP D 112 1 13
HELIX 40 AE4 PRO D 129 SER D 144 1 16
HELIX 41 AE5 SER D 145 GLY D 150 5 6
HELIX 42 AE6 SER D 162 LYS D 178 1 17
HELIX 43 AE7 SER D 200 PHE D 206 1 7
HELIX 44 AE8 THR D 213 LYS D 225 1 13
HELIX 45 AE9 PHE D 234 GLY D 238 5 5
HELIX 46 AF1 ILE D 256 ALA D 270 1 15
HELIX 47 AF2 SER D 285 ILE D 289 5 5
HELIX 48 AF3 SER D 295 GLY D 312 1 18
SHEET 1 AA1 6 VAL A 54 GLY A 62 0
SHEET 2 AA1 6 GLY A 65 ASP A 73 -1 O LEU A 71 N ARG A 56
SHEET 3 AA1 6 VAL A 115 VAL A 118 -1 O VAL A 115 N TYR A 72
SHEET 4 AA1 6 GLY A 81 TYR A 87 1 N ILE A 84 O VAL A 116
SHEET 5 AA1 6 ALA A 153 ASP A 161 1 O ILE A 157 N VAL A 83
SHEET 6 AA1 6 VAL A 188 ILE A 190 1 O ILE A 190 N GLY A 160
SHEET 1 AA2 4 THR A 246 ALA A 251 0
SHEET 2 AA2 4 VAL A 274 MET A 279 1 O VAL A 275 N VAL A 248
SHEET 3 AA2 4 VAL B 274 MET B 279 -1 O TYR B 276 N VAL A 274
SHEET 4 AA2 4 THR B 246 ALA B 251 1 N VAL B 248 O VAL B 275
SHEET 1 AA3 6 VAL B 54 CYS B 60 0
SHEET 2 AA3 6 ILE B 67 ASP B 73 -1 O ILE B 67 N CYS B 60
SHEET 3 AA3 6 VAL B 115 VAL B 118 -1 O VAL B 115 N TYR B 72
SHEET 4 AA3 6 GLY B 81 TYR B 87 1 N ILE B 84 O VAL B 116
SHEET 5 AA3 6 ALA B 153 ASP B 161 1 O ILE B 157 N VAL B 83
SHEET 6 AA3 6 VAL B 188 ILE B 190 1 O ILE B 190 N GLY B 160
SHEET 1 AA4 6 VAL C 54 PRO C 61 0
SHEET 2 AA4 6 ASP C 66 ASP C 73 -1 O ILE C 67 N CYS C 60
SHEET 3 AA4 6 VAL C 115 VAL C 118 -1 O VAL C 115 N TYR C 72
SHEET 4 AA4 6 GLY C 81 TYR C 87 1 N ILE C 84 O VAL C 116
SHEET 5 AA4 6 ALA C 153 ASP C 161 1 O ILE C 157 N VAL C 83
SHEET 6 AA4 6 VAL C 188 ILE C 190 1 O ILE C 190 N GLY C 160
SHEET 1 AA5 4 THR C 246 ALA C 251 0
SHEET 2 AA5 4 VAL C 274 MET C 279 1 O MET C 279 N THR C 250
SHEET 3 AA5 4 VAL D 274 MET D 279 -1 O TYR D 276 N VAL C 274
SHEET 4 AA5 4 THR D 246 ALA D 251 1 N VAL D 248 O VAL D 275
SHEET 1 AA6 6 VAL D 54 CYS D 60 0
SHEET 2 AA6 6 ILE D 67 ASP D 73 -1 O ILE D 67 N CYS D 60
SHEET 3 AA6 6 VAL D 115 VAL D 118 -1 O VAL D 115 N TYR D 72
SHEET 4 AA6 6 GLY D 81 TYR D 87 1 N ILE D 84 O VAL D 116
SHEET 5 AA6 6 ALA D 153 ASP D 161 1 O ILE D 157 N VAL D 83
SHEET 6 AA6 6 VAL D 188 ILE D 190 1 O ILE D 190 N GLY D 160
LINK NA NA C 821 O HOH C1119 1555 1555 2.47
CISPEP 1 ALA A 123 PRO A 124 0 1.14
CISPEP 2 PHE A 128 PRO A 129 0 3.31
CISPEP 3 ALA B 123 PRO B 124 0 1.33
CISPEP 4 PHE B 128 PRO B 129 0 5.19
CISPEP 5 ALA C 123 PRO C 124 0 1.17
CISPEP 6 PHE C 128 PRO C 129 0 2.64
CISPEP 7 ALA D 123 PRO D 124 0 0.93
CISPEP 8 PHE D 128 PRO D 129 0 7.02
CRYST1 70.576 129.838 221.079 90.00 90.00 90.00 P 21 2 21 16
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 0.014169 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007702 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004523 0.00000
TER 2278 GLY A 312
TER 4568 GLY B 312
TER 6854 GLY C 312
TER 9144 GLY D 312
MASTER 397 0 88 48 32 0 0 611012 4 440 100
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