HEADER TRANSFERASE 22-MAY-19 5QQT
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF HUMAN ALAS2A
TITLE 2 IN COMPLEX WITH Z2856434834
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5-AMINOLEVULINATE SYNTHASE, ERYTHROID-SPECIFIC,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: B, A;
COMPND 5 SYNONYM: ALAS-E,5-AMINOLEVULINIC ACID SYNTHASE 2,DELTA-ALA SYNTHASE
COMPND 6 2,DELTA-AMINOLEVULINATE SYNTHASE 2;
COMPND 7 EC: 2.3.1.37;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALAS2, ALASE, ASB;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS SGC - DIAMOND I04-1 FRAGMENT SCREENING, PANDDA, XCHEMEXPLORER,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.A.BEZERRA,W.FOSTER,H.BAILEY,L.SHRESTHA,T.KROJER,R.TALON,J.BRANDAO-
AUTHOR 2 NETO,A.DOUANGAMATH,B.B.NICOLA,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,
AUTHOR 3 C.BOUNTRA,P.E.BRENNAN,W.W.YUE
REVDAT 2 06-MAR-24 5QQT 1 REMARK
REVDAT 1 07-AUG-19 5QQT 0
JRNL AUTH G.A.BEZERRA,W.FOSTER,H.BAILEY,L.SHRESTHA,T.KROJER,R.TALON,
JRNL AUTH 2 J.BRANDAO-NETO,A.DOUANGAMATH,B.B.NICOLA,F.VON DELFT,
JRNL AUTH 3 C.H.ARROWSMITH,A.EDWARDS,C.BOUNTRA,P.E.BRENNAN,W.W.YUE
JRNL TITL PANDDA ANALYSIS GROUP DEPOSITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 80.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 62.0
REMARK 3 NUMBER OF REFLECTIONS : 65558
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3339
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) : 1.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 200
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 2.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 9
REMARK 3 BIN FREE R VALUE : 0.4870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6605
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 248
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : -0.15000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.06000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.160
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.112
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.561
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7327 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 6410 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9704 ; 1.535 ; 1.632
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14820 ; 1.352 ; 1.568
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 899 ; 6.674 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 365 ;27.408 ;21.397
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1113 ;16.038 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;18.059 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 891 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8187 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1631 ; 0.001 ; 0.020
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): 3606 ; 1.562 ; 2.188
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3605 ; 1.561 ; 2.187
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4459 ; 2.420 ; 3.265
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 : MASK
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 THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5QQT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-19.
REMARK 100 THE DEPOSITION ID IS D_1001402290.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68893
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.674
REMARK 200 RESOLUTION RANGE LOW (A) : 71.513
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 6HRH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 0.2 M MAGNESIUM
REMARK 280 CHLORIDE, 20% PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 62.99500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.31650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 62.99500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 54.31650
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 B 119
REMARK 465 GLY B 120
REMARK 465 HIS B 121
REMARK 465 HIS B 122
REMARK 465 HIS B 123
REMARK 465 HIS B 124
REMARK 465 HIS B 125
REMARK 465 HIS B 126
REMARK 465 SER B 127
REMARK 465 SER B 128
REMARK 465 GLY B 129
REMARK 465 VAL B 130
REMARK 465 ASP B 131
REMARK 465 LEU B 132
REMARK 465 GLY B 133
REMARK 465 THR B 134
REMARK 465 GLU B 135
REMARK 465 ASN B 136
REMARK 465 GLU B 183
REMARK 465 ALA B 184
REMARK 465 SER B 185
REMARK 465 VAL B 186
REMARK 465 ALA B 187
REMARK 465 ASP B 549
REMARK 465 VAL B 550
REMARK 465 SER B 551
REMARK 465 VAL B 552
REMARK 465 ALA B 553
REMARK 465 ALA B 554
REMARK 465 CYS B 555
REMARK 465 ASN B 556
REMARK 465 PHE B 557
REMARK 465 GLY B 579
REMARK 465 PRO B 580
REMARK 465 GLN B 581
REMARK 465 TYR B 582
REMARK 465 VAL B 583
REMARK 465 THR B 584
REMARK 465 THR B 585
REMARK 465 TYR B 586
REMARK 465 ALA B 587
REMARK 465 MET A 119
REMARK 465 GLY A 120
REMARK 465 HIS A 121
REMARK 465 HIS A 122
REMARK 465 HIS A 123
REMARK 465 HIS A 124
REMARK 465 HIS A 125
REMARK 465 HIS A 126
REMARK 465 SER A 127
REMARK 465 SER A 128
REMARK 465 GLY A 129
REMARK 465 VAL A 130
REMARK 465 ASP A 131
REMARK 465 LEU A 132
REMARK 465 GLY A 133
REMARK 465 THR A 134
REMARK 465 GLU A 135
REMARK 465 ASN A 136
REMARK 465 SER A 182
REMARK 465 GLU A 183
REMARK 465 ALA A 184
REMARK 465 SER A 185
REMARK 465 VAL A 186
REMARK 465 ALA A 187
REMARK 465 ASP A 549
REMARK 465 VAL A 550
REMARK 465 SER A 551
REMARK 465 VAL A 552
REMARK 465 ALA A 553
REMARK 465 ALA A 554
REMARK 465 CYS A 555
REMARK 465 GLY A 579
REMARK 465 PRO A 580
REMARK 465 GLN A 581
REMARK 465 TYR A 582
REMARK 465 VAL A 583
REMARK 465 THR A 584
REMARK 465 THR A 585
REMARK 465 TYR A 586
REMARK 465 ALA A 587
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 GLN B 147 CG CD OE1 NE2
REMARK 470 ARG B 150 NE CZ NH1 NH2
REMARK 470 LYS B 152 CE NZ
REMARK 470 GLN B 210 CG CD OE1 NE2
REMARK 470 GLU B 214 CG CD OE1 OE2
REMARK 470 GLU B 245 CD OE1 OE2
REMARK 470 LYS B 311 CD CE NZ
REMARK 470 LYS B 316 CG CD CE NZ
REMARK 470 LYS B 320 CG CD CE NZ
REMARK 470 ARG B 404 NE CZ NH1 NH2
REMARK 470 GLU B 441 CG CD OE1 OE2
REMARK 470 LYS B 455 CD CE NZ
REMARK 470 LYS B 488 CE NZ
REMARK 470 LYS B 496 CG CD CE NZ
REMARK 470 GLN B 527 CG CD OE1 NE2
REMARK 470 LYS B 535 CG CD CE NZ
REMARK 470 LEU B 545 CG CD1 CD2
REMARK 470 GLN B 548 CG CD OE1 NE2
REMARK 470 CYS B 558 SG
REMARK 470 ARG B 559 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 146 CG OD1 OD2
REMARK 470 MET A 154 SD CE
REMARK 470 LYS A 166 CE NZ
REMARK 470 LYS A 189 CG CD CE NZ
REMARK 470 LYS A 312 CE NZ
REMARK 470 LYS A 316 CE NZ
REMARK 470 GLU A 441 CG CD OE1 OE2
REMARK 470 LYS A 455 CG CD CE NZ
REMARK 470 GLN A 459 CD OE1 NE2
REMARK 470 LEU A 460 CG CD1 CD2
REMARK 470 LYS A 488 CG CD CE NZ
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 GLN A 527 CG CD OE1 NE2
REMARK 470 GLU A 530 CG CD OE1 OE2
REMARK 470 GLU A 534 CG CD OE1 OE2
REMARK 470 LEU A 545 CG CD1 CD2
REMARK 470 GLN A 548 CG CD OE1 NE2
REMARK 470 ARG A 559 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 577 CG OD1 ND2
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 B 817 O HOH B 829 1.56
REMARK 500 O3P PLP B 601 O HOH B 701 1.93
REMARK 500 OE1 GLN B 349 O HOH B 702 2.06
REMARK 500 NH1 ARG B 303 O HOH B 703 2.11
REMARK 500 OE2 GLU B 242 O HOH B 704 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ARG B 170 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG A 368 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 368 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
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 TYR B 138 -133.60 -127.10
REMARK 500 ASP B 146 -78.69 -31.98
REMARK 500 ALA B 174 45.29 -143.44
REMARK 500 PRO B 176 40.40 -99.34
REMARK 500 VAL B 221 -70.60 -96.77
REMARK 500 ILE B 229 76.44 -114.90
REMARK 500 LYS B 391 -108.10 -119.40
REMARK 500 CYS B 395 -132.11 -116.65
REMARK 500 SER B 402 -169.89 -163.46
REMARK 500 PHE B 419 47.88 -94.55
REMARK 500 TYR A 138 69.52 -113.05
REMARK 500 ALA A 174 48.49 -144.50
REMARK 500 PRO A 176 42.15 -106.13
REMARK 500 VAL A 221 -80.83 -95.75
REMARK 500 ILE A 229 74.29 -114.65
REMARK 500 THR A 329 -70.91 -84.05
REMARK 500 LYS A 391 -106.99 -116.07
REMARK 500 CYS A 395 -133.25 -112.04
REMARK 500 SER A 402 -166.31 -165.79
REMARK 500 PHE A 419 42.09 -98.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PLP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NT7 A 602
DBREF 5QQT B 143 578 UNP P22557 HEM0_HUMAN 145 580
DBREF 5QQT A 143 578 UNP P22557 HEM0_HUMAN 145 580
SEQADV 5QQT MET B 119 UNP P22557 INITIATING METHIONINE
SEQADV 5QQT GLY B 120 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS B 121 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS B 122 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS B 123 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS B 124 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS B 125 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS B 126 UNP P22557 EXPRESSION TAG
SEQADV 5QQT SER B 127 UNP P22557 EXPRESSION TAG
SEQADV 5QQT SER B 128 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLY B 129 UNP P22557 EXPRESSION TAG
SEQADV 5QQT VAL B 130 UNP P22557 EXPRESSION TAG
SEQADV 5QQT ASP B 131 UNP P22557 EXPRESSION TAG
SEQADV 5QQT LEU B 132 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLY B 133 UNP P22557 EXPRESSION TAG
SEQADV 5QQT THR B 134 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLU B 135 UNP P22557 EXPRESSION TAG
SEQADV 5QQT ASN B 136 UNP P22557 EXPRESSION TAG
SEQADV 5QQT LEU B 137 UNP P22557 EXPRESSION TAG
SEQADV 5QQT TYR B 138 UNP P22557 EXPRESSION TAG
SEQADV 5QQT PHE B 139 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLN B 140 UNP P22557 EXPRESSION TAG
SEQADV 5QQT SER B 141 UNP P22557 EXPRESSION TAG
SEQADV 5QQT MET B 142 UNP P22557 EXPRESSION TAG
SEQADV 5QQT VAL B 221 UNP P22557 ALA 223 CONFLICT
SEQADV 5QQT GLY B 579 UNP P22557 EXPRESSION TAG
SEQADV 5QQT PRO B 580 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLN B 581 UNP P22557 EXPRESSION TAG
SEQADV 5QQT TYR B 582 UNP P22557 EXPRESSION TAG
SEQADV 5QQT VAL B 583 UNP P22557 EXPRESSION TAG
SEQADV 5QQT THR B 584 UNP P22557 EXPRESSION TAG
SEQADV 5QQT THR B 585 UNP P22557 EXPRESSION TAG
SEQADV 5QQT TYR B 586 UNP P22557 EXPRESSION TAG
SEQADV 5QQT ALA B 587 UNP P22557 EXPRESSION TAG
SEQADV 5QQT MET A 119 UNP P22557 INITIATING METHIONINE
SEQADV 5QQT GLY A 120 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS A 121 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS A 122 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS A 123 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS A 124 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS A 125 UNP P22557 EXPRESSION TAG
SEQADV 5QQT HIS A 126 UNP P22557 EXPRESSION TAG
SEQADV 5QQT SER A 127 UNP P22557 EXPRESSION TAG
SEQADV 5QQT SER A 128 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLY A 129 UNP P22557 EXPRESSION TAG
SEQADV 5QQT VAL A 130 UNP P22557 EXPRESSION TAG
SEQADV 5QQT ASP A 131 UNP P22557 EXPRESSION TAG
SEQADV 5QQT LEU A 132 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLY A 133 UNP P22557 EXPRESSION TAG
SEQADV 5QQT THR A 134 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLU A 135 UNP P22557 EXPRESSION TAG
SEQADV 5QQT ASN A 136 UNP P22557 EXPRESSION TAG
SEQADV 5QQT LEU A 137 UNP P22557 EXPRESSION TAG
SEQADV 5QQT TYR A 138 UNP P22557 EXPRESSION TAG
SEQADV 5QQT PHE A 139 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLN A 140 UNP P22557 EXPRESSION TAG
SEQADV 5QQT SER A 141 UNP P22557 EXPRESSION TAG
SEQADV 5QQT MET A 142 UNP P22557 EXPRESSION TAG
SEQADV 5QQT VAL A 221 UNP P22557 ALA 223 CONFLICT
SEQADV 5QQT GLY A 579 UNP P22557 EXPRESSION TAG
SEQADV 5QQT PRO A 580 UNP P22557 EXPRESSION TAG
SEQADV 5QQT GLN A 581 UNP P22557 EXPRESSION TAG
SEQADV 5QQT TYR A 582 UNP P22557 EXPRESSION TAG
SEQADV 5QQT VAL A 583 UNP P22557 EXPRESSION TAG
SEQADV 5QQT THR A 584 UNP P22557 EXPRESSION TAG
SEQADV 5QQT THR A 585 UNP P22557 EXPRESSION TAG
SEQADV 5QQT TYR A 586 UNP P22557 EXPRESSION TAG
SEQADV 5QQT ALA A 587 UNP P22557 EXPRESSION TAG
SEQRES 1 B 469 MET GLY HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP
SEQRES 2 B 469 LEU GLY THR GLU ASN LEU TYR PHE GLN SER MET PHE SER
SEQRES 3 B 469 TYR ASP GLN PHE PHE ARG ASP LYS ILE MET GLU LYS LYS
SEQRES 4 B 469 GLN ASP HIS THR TYR ARG VAL PHE LYS THR VAL ASN ARG
SEQRES 5 B 469 TRP ALA ASP ALA TYR PRO PHE ALA GLN HIS PHE SER GLU
SEQRES 6 B 469 ALA SER VAL ALA SER LYS ASP VAL SER VAL TRP CYS SER
SEQRES 7 B 469 ASN ASP TYR LEU GLY MET SER ARG HIS PRO GLN VAL LEU
SEQRES 8 B 469 GLN ALA THR GLN GLU THR LEU GLN ARG HIS GLY VAL GLY
SEQRES 9 B 469 ALA GLY GLY THR ARG ASN ILE SER GLY THR SER LYS PHE
SEQRES 10 B 469 HIS VAL GLU LEU GLU GLN GLU LEU ALA GLU LEU HIS GLN
SEQRES 11 B 469 LYS ASP SER ALA LEU LEU PHE SER SER CYS PHE VAL ALA
SEQRES 12 B 469 ASN ASP SER THR LEU PHE THR LEU ALA LYS ILE LEU PRO
SEQRES 13 B 469 GLY CYS GLU ILE TYR SER ASP ALA GLY ASN HIS ALA SER
SEQRES 14 B 469 MET ILE GLN GLY ILE ARG ASN SER GLY ALA ALA LYS PHE
SEQRES 15 B 469 VAL PHE ARG HIS ASN ASP PRO ASP HIS LEU LYS LYS LEU
SEQRES 16 B 469 LEU GLU LYS SER ASN PRO LYS ILE PRO LYS ILE VAL ALA
SEQRES 17 B 469 PHE GLU THR VAL HIS SER MET ASP GLY ALA ILE CYS PRO
SEQRES 18 B 469 LEU GLU GLU LEU CYS ASP VAL SER HIS GLN TYR GLY ALA
SEQRES 19 B 469 LEU THR PHE VAL ASP GLU VAL HIS ALA VAL GLY LEU TYR
SEQRES 20 B 469 GLY SER ARG GLY ALA GLY ILE GLY GLU ARG ASP GLY ILE
SEQRES 21 B 469 MET HIS LYS ILE ASP ILE ILE SER GLY THR LEU GLY LYS
SEQRES 22 B 469 ALA PHE GLY CYS VAL GLY GLY TYR ILE ALA SER THR ARG
SEQRES 23 B 469 ASP LEU VAL ASP MET VAL ARG SER TYR ALA ALA GLY PHE
SEQRES 24 B 469 ILE PHE THR THR SER LEU PRO PRO MET VAL LEU SER GLY
SEQRES 25 B 469 ALA LEU GLU SER VAL ARG LEU LEU LYS GLY GLU GLU GLY
SEQRES 26 B 469 GLN ALA LEU ARG ARG ALA HIS GLN ARG ASN VAL LYS HIS
SEQRES 27 B 469 MET ARG GLN LEU LEU MET ASP ARG GLY LEU PRO VAL ILE
SEQRES 28 B 469 PRO CYS PRO SER HIS ILE ILE PRO ILE ARG VAL GLY ASN
SEQRES 29 B 469 ALA ALA LEU ASN SER LYS LEU CYS ASP LEU LEU LEU SER
SEQRES 30 B 469 LYS HIS GLY ILE TYR VAL GLN ALA ILE ASN TYR PRO THR
SEQRES 31 B 469 VAL PRO ARG GLY GLU GLU LEU LEU ARG LEU ALA PRO SER
SEQRES 32 B 469 PRO HIS HIS SER PRO GLN MET MET GLU ASP PHE VAL GLU
SEQRES 33 B 469 LYS LEU LEU LEU ALA TRP THR ALA VAL GLY LEU PRO LEU
SEQRES 34 B 469 GLN ASP VAL SER VAL ALA ALA CYS ASN PHE CYS ARG ARG
SEQRES 35 B 469 PRO VAL HIS PHE GLU LEU MET SER GLU TRP GLU ARG SER
SEQRES 36 B 469 TYR PHE GLY ASN MET GLY PRO GLN TYR VAL THR THR TYR
SEQRES 37 B 469 ALA
SEQRES 1 A 469 MET GLY HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP
SEQRES 2 A 469 LEU GLY THR GLU ASN LEU TYR PHE GLN SER MET PHE SER
SEQRES 3 A 469 TYR ASP GLN PHE PHE ARG ASP LYS ILE MET GLU LYS LYS
SEQRES 4 A 469 GLN ASP HIS THR TYR ARG VAL PHE LYS THR VAL ASN ARG
SEQRES 5 A 469 TRP ALA ASP ALA TYR PRO PHE ALA GLN HIS PHE SER GLU
SEQRES 6 A 469 ALA SER VAL ALA SER LYS ASP VAL SER VAL TRP CYS SER
SEQRES 7 A 469 ASN ASP TYR LEU GLY MET SER ARG HIS PRO GLN VAL LEU
SEQRES 8 A 469 GLN ALA THR GLN GLU THR LEU GLN ARG HIS GLY VAL GLY
SEQRES 9 A 469 ALA GLY GLY THR ARG ASN ILE SER GLY THR SER LYS PHE
SEQRES 10 A 469 HIS VAL GLU LEU GLU GLN GLU LEU ALA GLU LEU HIS GLN
SEQRES 11 A 469 LYS ASP SER ALA LEU LEU PHE SER SER CYS PHE VAL ALA
SEQRES 12 A 469 ASN ASP SER THR LEU PHE THR LEU ALA LYS ILE LEU PRO
SEQRES 13 A 469 GLY CYS GLU ILE TYR SER ASP ALA GLY ASN HIS ALA SER
SEQRES 14 A 469 MET ILE GLN GLY ILE ARG ASN SER GLY ALA ALA LYS PHE
SEQRES 15 A 469 VAL PHE ARG HIS ASN ASP PRO ASP HIS LEU LYS LYS LEU
SEQRES 16 A 469 LEU GLU LYS SER ASN PRO LYS ILE PRO LYS ILE VAL ALA
SEQRES 17 A 469 PHE GLU THR VAL HIS SER MET ASP GLY ALA ILE CYS PRO
SEQRES 18 A 469 LEU GLU GLU LEU CYS ASP VAL SER HIS GLN TYR GLY ALA
SEQRES 19 A 469 LEU THR PHE VAL ASP GLU VAL HIS ALA VAL GLY LEU TYR
SEQRES 20 A 469 GLY SER ARG GLY ALA GLY ILE GLY GLU ARG ASP GLY ILE
SEQRES 21 A 469 MET HIS LYS ILE ASP ILE ILE SER GLY THR LEU GLY LYS
SEQRES 22 A 469 ALA PHE GLY CYS VAL GLY GLY TYR ILE ALA SER THR ARG
SEQRES 23 A 469 ASP LEU VAL ASP MET VAL ARG SER TYR ALA ALA GLY PHE
SEQRES 24 A 469 ILE PHE THR THR SER LEU PRO PRO MET VAL LEU SER GLY
SEQRES 25 A 469 ALA LEU GLU SER VAL ARG LEU LEU LYS GLY GLU GLU GLY
SEQRES 26 A 469 GLN ALA LEU ARG ARG ALA HIS GLN ARG ASN VAL LYS HIS
SEQRES 27 A 469 MET ARG GLN LEU LEU MET ASP ARG GLY LEU PRO VAL ILE
SEQRES 28 A 469 PRO CYS PRO SER HIS ILE ILE PRO ILE ARG VAL GLY ASN
SEQRES 29 A 469 ALA ALA LEU ASN SER LYS LEU CYS ASP LEU LEU LEU SER
SEQRES 30 A 469 LYS HIS GLY ILE TYR VAL GLN ALA ILE ASN TYR PRO THR
SEQRES 31 A 469 VAL PRO ARG GLY GLU GLU LEU LEU ARG LEU ALA PRO SER
SEQRES 32 A 469 PRO HIS HIS SER PRO GLN MET MET GLU ASP PHE VAL GLU
SEQRES 33 A 469 LYS LEU LEU LEU ALA TRP THR ALA VAL GLY LEU PRO LEU
SEQRES 34 A 469 GLN ASP VAL SER VAL ALA ALA CYS ASN PHE CYS ARG ARG
SEQRES 35 A 469 PRO VAL HIS PHE GLU LEU MET SER GLU TRP GLU ARG SER
SEQRES 36 A 469 TYR PHE GLY ASN MET GLY PRO GLN TYR VAL THR THR TYR
SEQRES 37 A 469 ALA
HET PLP B 601 16
HET PLP A 601 16
HET NT7 A 602 18
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETNAM NT7 N-(2,3-DIMETHYLPHENYL)-2-(MORPHOLIN-4-YL)ACETAMIDE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 3 PLP 2(C8 H10 N O6 P)
FORMUL 5 NT7 C14 H20 N2 O2
FORMUL 6 HOH *248(H2 O)
HELIX 1 AA1 SER B 144 ASP B 159 1 16
HELIX 2 AA2 GLY B 201 ARG B 204 5 4
HELIX 3 AA3 HIS B 205 GLY B 220 1 16
HELIX 4 AA4 SER B 233 HIS B 247 1 15
HELIX 5 AA5 SER B 257 LEU B 273 1 17
HELIX 6 AA6 HIS B 285 GLY B 296 1 12
HELIX 7 AA7 ASP B 306 LYS B 316 1 11
HELIX 8 AA8 PRO B 339 TYR B 350 1 12
HELIX 9 AA9 GLY B 371 ASP B 376 1 6
HELIX 10 AB1 ILE B 378 ILE B 382 5 5
HELIX 11 AB2 THR B 403 ALA B 414 1 12
HELIX 12 AB3 ALA B 414 PHE B 419 1 6
HELIX 13 AB4 PRO B 424 GLY B 440 1 17
HELIX 14 AB5 GLY B 440 ARG B 464 1 25
HELIX 15 AB6 ASN B 482 GLY B 498 1 17
HELIX 16 AB7 SER B 525 GLY B 544 1 20
HELIX 17 AB8 SER B 568 GLY B 576 1 9
HELIX 18 AB9 SER A 144 ASP A 159 1 16
HELIX 19 AC1 GLY A 201 ARG A 204 5 4
HELIX 20 AC2 HIS A 205 GLY A 220 1 16
HELIX 21 AC3 SER A 233 GLN A 248 1 16
HELIX 22 AC4 SER A 257 LEU A 273 1 17
HELIX 23 AC5 HIS A 285 GLY A 296 1 12
HELIX 24 AC6 ASP A 306 LYS A 316 1 11
HELIX 25 AC7 PRO A 339 TYR A 350 1 12
HELIX 26 AC8 GLY A 371 ASP A 376 1 6
HELIX 27 AC9 ILE A 378 ILE A 382 5 5
HELIX 28 AD1 THR A 403 ALA A 414 1 12
HELIX 29 AD2 ALA A 414 PHE A 419 1 6
HELIX 30 AD3 PRO A 424 GLY A 440 1 17
HELIX 31 AD4 GLY A 440 ARG A 464 1 25
HELIX 32 AD5 ASN A 482 GLY A 498 1 17
HELIX 33 AD6 SER A 525 VAL A 543 1 19
HELIX 34 AD7 ASN A 556 ARG A 560 5 5
HELIX 35 AD8 SER A 568 GLY A 576 1 9
SHEET 1 AA1 4 THR B 167 ARG B 170 0
SHEET 2 AA1 4 PHE B 177 PHE B 181 -1 O GLN B 179 N ASN B 169
SHEET 3 AA1 4 LYS B 189 VAL B 193 -1 O VAL B 191 N ALA B 178
SHEET 4 AA1 4 ILE B 499 TYR B 500 1 O TYR B 500 N SER B 192
SHEET 1 AA2 7 SER B 251 PHE B 255 0
SHEET 2 AA2 7 GLY B 398 SER B 402 -1 O GLY B 398 N PHE B 255
SHEET 3 AA2 7 ILE B 384 THR B 388 -1 N GLY B 387 O TYR B 399
SHEET 4 AA2 7 LEU B 353 ASP B 357 1 N VAL B 356 O ILE B 384
SHEET 5 AA2 7 LYS B 323 GLU B 328 1 N VAL B 325 O PHE B 355
SHEET 6 AA2 7 GLU B 277 ASP B 281 1 N TYR B 279 O ILE B 324
SHEET 7 AA2 7 ALA B 298 PHE B 302 1 O PHE B 300 N ILE B 278
SHEET 1 AA3 3 ILE B 476 ARG B 479 0
SHEET 2 AA3 3 LEU B 515 LEU B 518 -1 O LEU B 518 N ILE B 476
SHEET 3 AA3 3 ALA B 503 ILE B 504 -1 N ILE B 504 O LEU B 515
SHEET 1 AA4 4 VAL A 168 ARG A 170 0
SHEET 2 AA4 4 PHE A 177 HIS A 180 -1 O GLN A 179 N ASN A 169
SHEET 3 AA4 4 LYS A 189 VAL A 193 -1 O LYS A 189 N HIS A 180
SHEET 4 AA4 4 ILE A 499 TYR A 500 1 O TYR A 500 N SER A 192
SHEET 1 AA5 7 SER A 251 PHE A 255 0
SHEET 2 AA5 7 GLY A 398 SER A 402 -1 O GLY A 398 N PHE A 255
SHEET 3 AA5 7 ILE A 384 THR A 388 -1 N GLY A 387 O TYR A 399
SHEET 4 AA5 7 LEU A 353 ASP A 357 1 N THR A 354 O ILE A 384
SHEET 5 AA5 7 LYS A 323 GLU A 328 1 N VAL A 325 O PHE A 355
SHEET 6 AA5 7 GLU A 277 ASP A 281 1 N TYR A 279 O ALA A 326
SHEET 7 AA5 7 ALA A 298 PHE A 302 1 O ALA A 298 N ILE A 278
SHEET 1 AA6 3 ILE A 476 ARG A 479 0
SHEET 2 AA6 3 LEU A 515 LEU A 518 -1 O LEU A 518 N ILE A 476
SHEET 3 AA6 3 ALA A 503 ILE A 504 -1 N ILE A 504 O LEU A 515
CISPEP 1 TYR B 175 PRO B 176 0 3.03
CISPEP 2 TYR B 506 PRO B 507 0 5.08
CISPEP 3 TYR A 175 PRO A 176 0 9.03
CISPEP 4 TYR A 506 PRO A 507 0 4.85
SITE 1 AC1 16 PHE A 419 THR A 420 THR A 421 SER B 257
SITE 2 AC1 16 CYS B 258 PHE B 259 ASN B 262 HIS B 285
SITE 3 AC1 16 GLU B 328 SER B 332 ASP B 357 HIS B 360
SITE 4 AC1 16 THR B 388 LYS B 391 GLY B 397 HOH B 701
SITE 1 AC2 16 SER A 257 CYS A 258 PHE A 259 ASN A 262
SITE 2 AC2 16 HIS A 285 GLU A 328 SER A 332 ASP A 357
SITE 3 AC2 16 VAL A 359 HIS A 360 THR A 388 LYS A 391
SITE 4 AC2 16 GLY A 397 HOH A 701 THR B 420 THR B 421
SITE 1 AC3 6 HIS A 348 GLN A 349 ALA A 352 GLN B 140
SITE 2 AC3 6 SER B 141 MET B 142
CRYST1 125.990 108.633 75.808 90.00 109.38 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 0.007937 0.000000 0.002792 0.00000
SCALE2 0.000000 0.009205 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013983 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
